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Q03073
MSQPSISKSMTIGESGLAVVFAATAFLCVIAAAKALDAPFAFHAALSAAASVAAVFCIVNRYFERPAALPPAEINGRPNYNMGPIKFSSFMAMFWGIAGFLVGLIIASQLAWPALNFDLPWISFGRLRPLHTSAVIFAFGGNVLIATSFYVVQKSCRVRLAGDLAPWFVVVGYNFFILVAGTGYLLGVTQSKEYAEPEWYADLWLTIVWVVYLLVFLATIIKRKEPHIFVANWFYLAFIVTIAVLHLGNNPALPVSAFGSKSYVAWGGIQDAMFQWWYGHNAVGFFLTAGFLAIMYYFIPKRAERPIYSYRLSIIHFWALIFLYIWAGPHHLHYTALPDWTQTLGMTFSIMLWMPSWGGMINGLMTLSGAWDKLRTDPVLRMLVVSVAFYGMSTFEGPMMSIKVVNSLSHYTDWTIGHVHSGALGWVGFVSFGALYCLVPWAWNRKGLYSLKLVNWHFWVATLGIVLYISAMWVSGILQGLMWRAYTSLGFLEYSFIETVEAMHPFYIIRAAGGGLFLIGALIMAYNLWMTVRVGEAEVQMPVALQPAE
Cofactor: Binds 1 copper ion per subunit, denoted as copper B. Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O Location Topology: Multi-pass membrane protein Sequence Mass (Da): 61273 Sequence Length: 549 Pathway: Energy metabolism; oxidative phosphorylation. Subcellular Location: Cell membrane EC: 7.1.1.9
Q05572
MKHTVEMVVLSVGAFLALVGAGLAQDRLFGAHMWVLFFALLAGTLVLMRRVDFRPAVAGHPGRRREYFDEVVKYGVVATVFWGVVGFLVGVVVALQLAFPELNVEPWFNFGRVRPLHTSAVIFAFGGNALIATSFYVVQRTSRARLFGGDLGWFVFWGYQLFIVLAASGYLLGITQSREYAEPEWYVDLWLTIVWVAYLVAFLGTIMKRKEPHIYVANWFYLAFIVTIAMLHVVNNLAVPVSFLGSKSYSAFSGVQDALTQWWYGHNAVGFFLTAGFLAMMYYFIPKQVNRPVYSYRLSIIHFWAIIFMYIWAGPHHLHYTALPDWAQTLGMVFSIMLWMPSWGGMINGLMTLSGAWDKIRTDPVVRMMVMAVAFYGMATFEGPMMSIKTVNSLSHYTDWTIGHVHSGALGWNGLITFGAIYYLVPKLWNRERLYSVRMVNWHFWLATLGIVVYAAVMWVAGIQQGLMWREYDDQGFLVYSFAETVAAMFPYYVMRAAGGALFLAGALLMAFNVTMTILGRVRDEEPIFGAAPLPAPAE
Cofactor: Binds 1 copper ion per subunit, denoted as copper B. Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B. Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O Location Topology: Multi-pass membrane protein Sequence Mass (Da): 60869 Sequence Length: 539 Pathway: Energy metabolism; oxidative phosphorylation. Subcellular Location: Cell membrane EC: 7.1.1.9
A8HZ17
MSTSHESHHAPVDGAGGPSTTGHEWDGIQELNNPLPRWWLWTFYATIIWAFGYWVAYPAWPLVSNYTSGVLGWNSRSAVVEQISDLQKLRAASSAKLANVPLEDIEKNPELLSLARAEGKVAFADNCAPCHGAGGGGAKGFPNLNDDDWLWGGTLAQIQQTITHGIRSGDDEGHQGNMLAFGSILSKADISNVADYVRSLSGAAPGDTPAAKKGAEIFAANCATCHGENGKGNQELGSKNLTDGIWLYGGDKATIVQTITNGRGGVMPAWGPRLSPTTIKALTVYVHTLGGGQ
Cofactor: Binds 2 heme C groups per subunit. Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subunit where oxygen reduction takes place. The complex also functions as a proton pump (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 30980 Sequence Length: 293 Pathway: Energy metabolism; oxidative phosphorylation. Subcellular Location: Cell inner membrane
Q03075
MTDHSEFDSVSGKTTTGHEWDGIKELNTPLPRWWVICFYLTIVWAIGYWIVYPAWPLISSNTTGLFGYSSRADVAVELANLEKIRGDKMAALGAASLADVEKDPALLALARAKGKTVFGDNCAPCHGSGGAGAKGFPNLNDDDWLWGGTLDQIMQTIQFGARSGHAKTHEGQMLAFGKDGVLKGDEIVTVANYVRSLSGLPTRKGYDAAKGEKIFVENCVACHGDGGKGNQEMGAPNLTDKIWLYGSDEAALIETISQGRAGVMPAWEGRLDPSTIKAMAVYVHSLGGGK
Cofactor: Binds 2 heme C groups per subunit. Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subunit where oxygen reduction takes place. The complex also functions as a proton pump. Location Topology: Single-pass membrane protein Sequence Mass (Da): 31024 Sequence Length: 290 Pathway: Energy metabolism; oxidative phosphorylation. Subcellular Location: Cell inner membrane
P0AEM2
MSESVQSNSAVLVHFTLKLDDGTTAESTRNNGKPALFRLGDASLSEGLEQHLLGLKVGDKTTFSLEPDAAFGVPSPDLIQYFSRREFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEA
Function: PPIases accelerate the folding of proteins. Substrate specificity carried out with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide', where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln (By similarity). Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Mass (Da): 16081 Sequence Length: 149 EC: 5.2.1.8
P21863
MTDQVLAEQRIGQNTEVTLHFALRLENGDTVDSTFDKAPATFKVGDGNLLPGFEAALFGFKAGDKRTLQILPENAFGQPNPQNVQIIPRSQFQNMDLSEGLLVIFNDAANTELPGVVKAFDDAQVTIDFNHPLAGKTLTFDVEIIDVKAL
Function: PPIases accelerate the folding of proteins. Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Mass (Da): 16373 Sequence Length: 150 EC: 5.2.1.8
P44760
MLKIQKLSIAALMVSAVISGQVFAEDNTFDEKAASYAVGTLMGSQMKDLVDSHKEVIKYDNARILDGLKDALEGKVDVRKDEKIQKTLESIEAKLVAASKAKAESIAKQAKEEGDKFRAEFAKGKDVKTTQSGLMYKIESAGKGDTIKSTDTVKVHYTGKLPNGKVFDSSVERGQPVEFQLDQVIKGWTEGLQLVKKGGKIQFVIAPELGYGEQGAGASIPPNSTLIFDVEVLDVNPKSEK
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Mass (Da): 26125 Sequence Length: 241 EC: 5.2.1.8
P30417
MLQATCARIARRFVWRNRMPRRLFIGLFLLPLPLFAAPPKDELAYAVGARLGMRLQQEMPGLELSELLLGLRQAYRGEALEIPPERIEQLLLQHENATTETPRTTPAEARFLANEKARFGVRELTGGVLVSELRRGQGNGIGAATQVHVRYRGLLADGQVFDQSESAEWFALDSVIEGWRTALRAMPVGARWRVVIPSAQAYGHEGAGDLIPPDAPLVFEIDLLGFR
Function: PPIases accelerate the folding of proteins. Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Sequence Mass (Da): 25278 Sequence Length: 227 EC: 5.2.1.8
P40466
MSVTSREQKFSGKYSSYTAQDRQGLVNAVTCVLSSSSDPVAVSSDYSNSLSIAREVNAYAKIAGCDWTYYVQKLEVTIGRNTDSLNLNAVPGTVVKKNIDIDLGPAKIVSRKHAAIRFNLESGSWELQIFGRNGAKVNFRRIPTGPDSPPTVLQSGCIIDIGGVQMIFILPEQETIISDYCLNHLMPKLLSTYGTNGNNNPLLRNIIEGSTYLREQRLQEEARLQQLDHLHTPLSSSSDVNPIGDPHGDTIMMEEDEEDENYTRGGIRPNTYTSSSNNAVTNGNVPHIENPSDLSLDENRYIKPPQSYASMITQAILSTPEGSISLADIYKFISDNYAFYRFSQMAWQNSVRHNLSLNKAFEKVPKRAGQQGKGMNWKISDEVRRDFLNKWNAGKLSKIRRGASVTRQLQLHMSKFGEIPAPESSSIDPRGIKAQKVKKSLQATSSILGESAPQLQRTQLTGQISTTTSMDVTTNANVNNSSLS
Function: Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle . The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave of cell cycle regulated gene expression in the M/G1 phase interval . Involved in HMRa silencing . FKH1 and FKH2 associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing . Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation . FKH1 and FKH2 function also in controlling yeast cell morphology by preventing preudohyphal growth . Acts as a rate-limiting replication origin activator via its interactin with the origin recognition complex (ORC) . Plays a transcription-independent role in recombination donor preference during mating-type switching through binding to the recombination enhancer (RE), a 700-bp cis-acting element that controls recombination along the left arm of chromosome III . Sequence Mass (Da): 53490 Sequence Length: 484 Domain: The phosphothreonine-binding FHA domain is required for the interaction with MPH1 and controlling recombination donor preference during mating-type switching. Subcellular Location: Nucleus
O60129
MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSPSSPVPLLAKKREGSPSLPIPILPKMKDTSIPAAEPASSTTSARDQTPSTPKDVGSPSTAETSAEEKQMETYKTPTHAALSDIISTHDYALDANSASQTKKAAFGSPIGSSTYPTSSPAPFWKYVAVPNPHDWPQVGSYDTISPYRNPVNSHLIYSQIQQSSPKKIDEQLHDLQGVDLVNGFEGISSWRESMVNKLRSSVSDSPTMNLANSNSKSSPVAVQRVSTLPQASANKQAKEMESKMSNSPTQKSKTEENNQAVRAILDASATMEKQYDLHRLPTPTSQTESASVPQIANPPNSQNLVKEKSPQQYIQVPQSNVKSSA
Function: Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Binds, cooperatively with mcm1, the CLB cluster regulatory elements throughout the cell cycle. Regulates the periodic transcription of cdc15 and spo12. Required for the correct timing, positioning and contraction of the division septum. PTM: Phosphorylated. Occurs periodically during mitosis. Sequence Mass (Da): 71174 Sequence Length: 642 Subcellular Location: Nucleus
P41813
MSSSNFNEMNELNMTQTNYGSTKYTAQHHQGVINAIISSLTAPDQPTTVSLQYSNDKNMATEIQAYAKLSGPNWTYYVKDLEVSIGRNTDPLNSALQENSDGVKNSYRVNIDLGPAKVVSRKHAIIKYNMNIGGWELHILGRNGAKVNFQRTHNGPNNPPIRLSSGTLLDIGGTQMMFILPDSDPVVAPICIEHLMPNLINMFGLEGNNNPLLRDIIKQSNYAKQRQLTSNQQIKGFKLYGSGGNAPFGSGANLGPSEQGIFNNNNNSKNKNGYFTSINPNYTASTTTSNTINPQAASPQGPPNTIIAANFVDSYKSSNAYPQALDFTSDLSHDENRNVKPPHSYATMITQAILSSPEGVISLADIYKYISSNYAYYRFAKSGWQNSIRHNLSLNKAFEKVPRRPNEPGKGMKWRISESYQQEFLNKWNTGKVGKIRRGSSVARQLQLHMAKFNSLPMEMDYRLSLNMAQPPKRQLQSHNVLEPSNNNIIEGFVQHVPSKGNLPASQQSQPPVSHQNQSQQPPPQEQRQEIQFTFADTQNRNIALARPIKTPQLQAPNSNANLNQNNMKEYKESLHPPAISISQMNRQSPNNALVSFTNACANSKIINNISDSADKSTNNNGGTKMNLPAISTSSLDENGNLEPTTTTSSGNSNSVPQTGTTTSSLAANSLRLSQPYDTLLRSPTKAFHITAMEAYTPERGSANRARSPLHSNSNNTNNNGANNSNLQTSGMENKQTGLVLDSNVLKSMESNNDNRRLTPSTSKSQNVKSSPGVWNLLQFSSTNNTPAADSGGNKRGFSINPDIKAKENENATSEKDSDSNSNDLETKDINSSPLKNQGGSTANAKELILDTDGAKISIINN
Function: Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle . The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave of cell cycle regulated gene expression in the M/G1 phase interval . Involved in HMRa silencing . FKH1 and FKH2 associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing . Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation . FKH1 and FKH2 function also in controlling yeast cell morphology by preventing preudohyphal growth . Acts as a rate-limiting replication origin activator via its interactin with the origin recognition complex (ORC) . Sequence Mass (Da): 94374 Sequence Length: 862 Domain: The FHA domain is necessary for the interaction with NDD1. Subcellular Location: Nucleus
D4B388
MLLYYILVALWATVTYAKSFSEDISEMPELSEMSSYLNQTPEAKDVLDQQKNVTLLALENSAFRDFVGQGEGNDNQSSSNSSLLRGIFSYQLVKGLHNSEQITTTPQFSPTELNDAGFTNVSSGQIVQLVEKDGKDYAISGLNDNSTIIKPGVDVENGVIHVIDRPLTLPQSVTATLQAANLTSFQGALQRGNAVSNANDPKDITLFAPRNLGFQRIGTAFENISAEDLGQIANYHIVKGKVLYSPDLTDADHPTYADKDLHISTVDGRSYVNSARVESTNLLVNNGVIHVISDVLNPNNDTAKPVPNADPPPPAFENANPVSTDPLTDGIPSPTSVIPLPGITSGGEGGGGGGGESTAPPSPTATVTETQSGGGGGGGGGAGGGPGPTATNTPQPGAAATERAKAGLAAVVGLGVVLINA
Function: May be a cell surface adhesion protein. Location Topology: Lipid-anchor Sequence Mass (Da): 43547 Sequence Length: 421 Subcellular Location: Cell membrane
Q30SL9
MIRNFLLFFMPIYAILFLSGCTANLSDPEIDFEPPAYVEEMPSKEDNKDFTSVGSVFGQGENPLFSDHKAMHVNDIVTVIISENTQSSNSGSKQISESDSLNLGGGAFTSAGTNSAVNSAVSKLNGIANLGFGSTSDSAYKGQGSATKDASFTTTVSARIVKVLQNGNYFISGKREILVDNQKQIIQIGGVIRPYDIDQGNRINSSQMSEAKILYKTQGDVERATDRGWGTKIIQSVWPF
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 25958 Sequence Length: 240 Subcellular Location: Cell outer membrane
Q2LT21
MNILIQNRLIFLFLILWLWTGCATKPDFTAGEQPLDLTVRPEALPVRGSIWPGESASNMLFADKKARYINDIVTILINEASQGGNKATTNTSRDSDSAAGIDAFWGLDQSILSRNVNMGSKIKIGGSSSSTLKGTGNTTRGGQLKGTVTARVVRVLDNGNLVIEGRRQLTINEEDQYLIISGIIRPEDITTENCIFSQYIADARIVYAGKGIINDKMRPGWATRIVDWVWPF
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 25534 Sequence Length: 232 Subcellular Location: Cell outer membrane
Q3A5F4
MRTWAVLPILLMLVGCVTQRIVEPQPHSAPIAARQVQPEQPQAPGSLWTEGRGSLFRDNKARRVGDIVTVAIYEQASASKQASTATGRSSSMSAGLTNLFGIEGNIGNLNKFIDPTSLIDTSYENAFDGSGSTSRKEDLVATLTAQVIEELPNGNLCIAGGKTVTVNREDQIILLEGIIRPEDISARNVVSSKHILDAKIAYTGKGVISDKQRPGWMTRVLDHIWPF
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 24595 Sequence Length: 227 Subcellular Location: Cell outer membrane
B5YIX2
MRKLILISLCIFFLASCSELQEVRDIKNAGMPPKYYPEPPQTQVASEGSLWRNKASLYEDKKARRVNDLVTILINESTSAQKTASTTASRDSSTNYGLDTFFGMNTDFNIHNLPLINGFYKAGNVFSPSVKGSATSDFKGDGDTARTGKITGTITAKVVEVLPNGNLVIESRKEVIVNNEKEILVLRGIIRPDDISQSNTILSQYVADAQIYLVGEGTLGDKQSQGWLVRFLDKIWPF
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 26318 Sequence Length: 238 Subcellular Location: Cell outer membrane
Q3SIE4
MKTTRAIAMLGLLLGLAACGTTPSTIVERPTTARPQAPAAVPATNGAIYQAATYRPLFEDRRARHVGDVLTIVINERTRAGKEASSSASKTSAVDASVGGVAKLPLKMFQGLGINAEASAEYEDESALDSSNTFSGNVTVTVIEVLPNGNLVVAGEKQIGLDKGTEYIRLSGVVQPDTIQAGNTVSSAKVADARIEYRSSAKFDKAEVMNWLGRFFLSFIPL
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 23434 Sequence Length: 222 Subcellular Location: Cell outer membrane
A5F678
MAAMKRLLASSLLILLSGCSLMQPPIESAETIQGTTTVDAVEGDKSESNSGLTDALRNRTDPVAGDPAWAPIHPKGKPEHYAAETGSLFNLASSSSMYDDSKPRGVGDIITVTLNESTKAAKSADADLNKKNDASMDPLAVGGKDLTIGDYNFSYALKNDNKFSGSAAANQSNSMSGSITVEVIEVLANGNLVIRGEKWLTLNTGDEYIRLSGTIRPDDIDFDNTIASNRISNARIQYSGTGTNQDMQEPGFLARFFNVSL
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 27790 Sequence Length: 261 Subcellular Location: Cell outer membrane
Q7M7T1
MSGFLLVTLVAALYSGCSVADPQISFKPPEYVEEMPAREVEESFGNAGSLFGQGDNPLFADRRAMKLNDLVTVIINETASASSSGKKDLSETSSSTMNGPSVTFGGPSQSIGNAVNKLNNFTSFGLSTGNNNSTFAGSGTQQRQESFTTTVSARIIKVMENGNYFIEGGREILINGEKQIMRLTGVIRPYDIGRNNTINSRYIADAKIMYETQGEIKKSTEKGWGTKVLESVWPF
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 25442 Sequence Length: 235 Subcellular Location: Cell outer membrane
Q3BU05
MSRLPSLSRLCLAIACSALLGGCVAAGDVRPFAELAPIVPVVAPVAQPTAGAIYAAGPSLNLYGDRRARDVGDLLTVNLVESTTASSTANTSISKKDATTMGAPTLLGAPLTVGGLNVLENSTSGDRSFAGKGNTAQSNRMQGSVTVTVMQRLPNGNLVIQGQKNLRLTQGDELVQVQGIVRAADIAPDNTVPSSKVADARIAYGGRGAIAQSNAMGWLSRFFNSRLSPY
Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. Location Topology: Lipid-anchor Sequence Mass (Da): 23697 Sequence Length: 230 Subcellular Location: Cell outer membrane
P21184
MALTVNTNIASLNTQRNLNNSSASLNTSLQRLSTGSRINSAKDDAAGLQIANRLTSQVNGLNVATKNANDGISLAQTAEGALQQSTNILQRMRDLSLQSANGSNSDSERTALNGEVKQLQKELDRISNTTTFGGRKLLDGSFGVASFQVGSAANEIISVGIDEMSAESLNGTYFKADGGGAVTAATASGTVDIAIGITGGSAVNVKVDMKGNETAEQAAAKIAAAVNDANVGIGAFSDGDTISYVSKAGKDGSGAITSAVSGVVIADTGSTGVGTAAGVTPSATAFAKTNDTVAKIDISTAKGAQSAVLVIDEAIKQIDAQRADLGAVQNRFDNTINNLKNIGENVSAARGRIEDTDFAAETANLTKNQVLQQAGTAILAQANQLPQSVLSLLR
Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. PTM: Phosphorylated on tyrosine residue(s). Sequence Mass (Da): 40066 Sequence Length: 394 Subcellular Location: Secreted
P72151
MALTVNTNIASLNTQRNLNASSNDLNTSLQRLTTGYRINSAKDDAAGLQISNRLSNQISGLNVATRNANDGISLAQTAEGALQQSTNILQRIRDLALQSANGSNSDADRAALQKEVAAQQAELTRISDTTTFGGRKLLDGSFGTTSFQVGSNAYETIDISLQNASASAIGSYQVGSNGAGTVASVAGTATASGIASGTVNLVGGGQVKNIAIAAGDSAKAIAEKMDGAIPNLSARARTVFTADVSGVTGGSLNFDVTVGSNTVSLAGVTSTQDLADQLNSNSSKLGITASINDKGVLTITSATGENVKFGAQTGTATAGQVAVKVQGSDGKFEAAAKNVVAAGTAATTTIVTGYVQLNSPTAYSVSGTGTQASQVFGNASAAQKSSVASVDISTADGAQNAIAVVDNALAAIDAQRADLGAVQNRFKNTIDNLTNISENATNARSRIKDTDFAAETAALSKNQVLQQAGTAILAQANQLPQAVLSLLR
Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. PTM: Phosphorylated on tyrosine residue(s). Sequence Mass (Da): 49242 Sequence Length: 488 Subcellular Location: Secreted
O67241
MDKLREYLNLLKERFNALTPVQKALAVGIPLLLLSLGAVALIYLSQENYTVLYTGLSPDDLNAVVTELDKEGVKYKISPDGRTIYVPENVARELRLKLAAKGVPRKGIVGYELFDKSGIVLSRFQQLVNFKRAIEGELAKTIMSLDCVEFARVHIVLPEKSLFIREEEEAKASVFLKLKPGCELTPEQVKAIRNLVSGSVENLKPSQVVVVDDKGRDLTAYLDEEFKTNASQLKVKREFEKSLERKLQKTLEEVFGYGKVKVNVSAELDFSSMKKREELYDPDLTAVVSEQKKKERTTSTRAQGIPGTQANIPPATGRQGGGELITERKESITNYEVSKREIYFEDKTIKVKRISVGLVIDKDVKVNTEELKNLIIASAGLDPKRGDQVSIVSVPFVKPTVVAEKPKVPTYVYVAVALVSLVILGLVAFGLVKLLRRRPPAPTPAPAVPGVPPTVEEVRKKTPYEELLEIAKQEPEKVAMVLKKWLKEG
Function: The M ring may be actively involved in energy transduction. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 54450 Sequence Length: 489 Subcellular Location: Cell inner membrane
P23447
MNRTLMQMKNKTSEFWKNRSKLQKILMVSALAAIIIIGIIISVFASNSKMAPLYKDLSAEEAGQIKEELDAKKVPNELSNGGTVISVPEDQVDSLKVQMAAEGLPKTGSIDYSFFGQNAGFGLTDNEFDMVKVKATQTELSNLINEMDGIKNSKVMINLPKDAVFVGEEQSAASASIVLQIQPGYTLDQSQINGLYHLVSKSVPNLKEDNIVIMDQNSTYYDKSDSDAGSYADSYSSQQGIKSQVEKDIQKHVQSLLGTMMGQDKVVVSVTADIDFTKENRTEDIVEPVDKENMEGIAVSAEKVSETYQGDGAANGGTAGTGEEDVTNYKADGENTESGNYEKNSNKINYEVNRIHKEIAESPYKVRDLGIQVMVEPPDAKNTASLSTERQDDIQKILSTVVRTSLDKDETQNQNLSDADINNKIVVSVQPFDGKVNLDTNTEESSGIPLWAYIVGGVLIAAIIVLIIMLIRKKRAQEDEFEEYEYEVPQEPINLPDINEEENETAESVRRKQLEKMAKDKPEDFAKLLRSWLAED
Function: The M ring may be actively involved in energy transduction. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 59300 Sequence Length: 536 Subcellular Location: Cell membrane
Q44912
MSKFFTNFFVSAKGIFKKASTVQKIALGLIIFFVILALVFLIGFSTKSQSIALFGVEIKDQYLLDRISQRLDRENVKYFLSSDGRIYLDDEKLAKKMRAILVREELVPVHMDPWALFDIDRWTITDFERSINLRRSITRAVEQHIVALDDVDAVSVNLVMPEKALFKESQEPVKASVRITPRPGSDIITNRKKVEGLVKLIQYAIEGLESDNIAIVDNSGTILNDFSNLDGIDRIDLAEKERKLKLKYEAMLRGEIDSALSKVLSVDRFMIARVNVKLDTSKETTESKEYAPIELQSQDPKASYNTRKVSDSTIISSQTQKKEYQGQGYSPWGPPGQEGNTPPEYQDLSDITGKYNESQEIKNVALNEKKSTSEKEPARIVGVSLGIFVDGIWNFVYDEKGDFVIENGMRKREYKPMALEEIKNIEDVLQSSFEYKPERGDSITVRNISFDRMNEFREIDENYFASERFKYFLFIASIVFSLLILVFTIFFAISRELERRRRLREEELAKQAHLRRQQALMDGGDDIGVDDVVGGIREGDELQSNAELLAREKPEDVAKLIRTWLLKNA
Function: The M ring may be actively involved in energy transduction. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 65133 Sequence Length: 569 Subcellular Location: Cell inner membrane
Q8YDM4
MAVVWMQQNFQQLIEQLKGTLGKLGARKLIALGLVGAALMGAILYTSIYLGRPSYETLYVGLSRDDVNRMGLALGEAGIPFDVKSDGSSILVPIGKAENARMYLAEKGLPTSNNAGYELFDNMGSLGLTSFMQEITRVRALEGEIARTIQAIRGVKAARVHIVLAEKGSFRRGDQKPSASVVIRAEGGFSAESAQSIRQLVAAAVPSLDASSVTVLDTNGHLLASAGEGANGAALMTASLEQQVASHVDDSIRKALAPYLGLGHFQTSVQAALDTDRRQTKETTYDPESRVERSVRVVRESGDSRNNRNDNATGVEQNIPQEQIQNRNGESSTEKTDRREELTNYEVNSMTVSTVSDGYSIKRLSIAVVIDQARLLQTAGTTPPPANFVDQQITKIRDLVATAAGLNTNRGDVINVTAVNFLDSAGADMEPVSAPWTDTLLRQSGSYANALAILAAVGLLIWFGLRPLLRDQNVKPAGTEVAIREAGEVATPNFIGGAESVGEGVQAVIGGPAAYADQMKTSLSDLRQRMRMPAKLRLEQMIEMDEERVAAVLKQWIHETASGREADPAKASAMPELKAA
Function: The M ring may be actively involved in energy transduction (By similarity). The flagellum is required to cause a persistent disease in a murine model of infection. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 62161 Sequence Length: 580 Subcellular Location: Cell inner membrane
P54466
MDPSTLMILAIVAVAIIVLAVFFTFVPVMLWISALAAGVKISIFTLVGMRLRRVIPNRVVNPLIKAHKAGLNVGTNQLESHYLAGGNVDRVVNALIAAQRANIELTFERCAAIDLAGRDVLEAVQMSVNPKVIETPFIAGVAMDGIEVKAKARITVRANIERLVGGAGEETIVARVGEGIVSTIGSSDNHKKVLENPDMISQTVLGKGLDSGTAFEILSIDIADVDIGKNIGAILQTDQAEADKNIAQAKAEERRAMAVAQEQEMRARVEEMRAKVVEAEAEVPLAMAEALREGNIGVMDYMNIKNIDADTEMRDSFGKLTKDPSDEDRKS
Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes . Flotillins are thought to be important factors in membrane fluidity, especially during periods of rapid growth in rich media (Probable). Whether specific proteins are associated with FMMs is controversial; in one study FloT rafts have been shown to include proteins involved in adaptation to stationary phase, while FloA-FloT rafts include proteins involved in differentation including sporulation, biofilm formation and DNA uptake competence . Another (more finely resolved) study only showed association of NfeD2 with FloT rafts of all the proteins examined . Involved in spatial organization of membranes, perhaps recruiting proteins to specific membrane regions . Simultaneous overexpression of both FloA and FloT leads to defects in cell division and differentiation, in part caused by stabilization of FtsH and its subsequent increased ability to degrade proteins. Cells make more biofilm, are about half as long, have less EzrA and more frequent Z-rings . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 35641 Sequence Length: 331 Domain: The last 95 residues are required for correct localization . The C-terminus determines the oligomerization state of the protein; there are many small foci for FloA. Swapping with the C-terminus of FloT leads to fewer large foci . N-terminally tagged, purified protein lacking the first 10 residues oligomerizes, with 12mer to about 50mer complexes found . Subcellular Location: Cell membrane
B8DZW4
MNLIWGFLILILVLIFLGVFFSFVPLGLWISALAAGVSIRITDLIGMRLRRVPPGVIINSLIKAHKAGLSEVTLDKLEAHYLAGGNVDKVVNALIAAQRAGIPLTFEKAAAIDLAGRDVLEAVQMSVNPKVIETPVVAAVAKDGIELKAKARVTVRANIERLVGGAGEATIIARVGEGIVTTIGSAESYKEVLENPDSISKTVLAKGLDAGTAFEIVSIDIADVDVGNNVGARLKMDQAEADMRIAQAQAESRRALAIAREQEMKALTQEMRARLIEAEKEVPLAIAEALRSGKIGVLDYYTLKNIIADTAMREAISKLGQKEEEGRKD
Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity. Location Topology: Single-pass membrane protein Sequence Mass (Da): 35210 Sequence Length: 329 Subcellular Location: Cell membrane
Q9WZP3
MADQYHEPVSELTGKDRDFVRALNSLKEEIEAVAWYHQRVVTTKDETVRKILEHNRDEEMEHAAMLLEWLRRNMPGWDEALRTYLFTDKPITEIEEETSGGSENTGGDLGIRKL
Function: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like protein that probably stores iron in the encapsulin nanocompartment. Sequence Mass (Da): 13289 Sequence Length: 114 Domain: The C-terminal 15-30 residues (cargo loading-peptide, CLP, or targeting peptide) are sufficient to target this protein to the nanocompartment in vivo, while the C-terminal 5 residues suffice in vitro. Subcellular Location: Encapsulin nanocompartment
P9WQL7
MTALNRAVASARVGTEVIRVRGLTFRYPKAAEPAVRGMEFTVGRGEIFGLLGPSGAGKSTTQKLLIGLLRDHGGQATVWDKEPAEWGPDYYERIGVSFELPNHYQKLTGYENLRFFASLYAGATADPMQLLAAVGLADDAHTLVGKYSKGMQMRLPFARSLINDPELLFLDEPTSGLDPVNARKIKDIIVDLKARGRTIFLTTHDMATADELCDRVAFVVDGRIVALDSPTELKIARSRRRVRVEYRGDGGGLETAEFGMDGLADDPAFHSVLRNHHVETIHSREASLDDVFVEVTGRQLT
Function: Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c involved in fluoroquinolones export. Confers resistance to ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and sparfloxacin. Probably responsible for energy coupling to the transport system. Location Topology: Peripheral membrane protein Sequence Mass (Da): 33100 Sequence Length: 301 Subcellular Location: Cell membrane EC: 7.6.2.-
P9WJB2
MRAISSLAGPRALAAFGRNDIRGTYRDPLLVMLVIAPVIWTTGVALLTPLFTEMLARRYGFDLVGYYPLILTAFLLLTSIIVAGALAAFLVLDDVDAGTMTALRVTPVPLSVFFGYRAATVMVVTTIYVVATMSCSGILEPGLVSSLIPIGLVAGLSAVVTLLLILAVANNKIQGLAMVRALGMLIAGLPCLPWFISSNWNLAFGVLPPYWAAKAFWVASDHGTWWPYLVGGAVYNLAIVWVLFRRFRAKHA
Function: Part of the ABC transporter complex involved in fluoroquinolones export. Probably responsible for the translocation of the substrate across the membrane (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 27144 Sequence Length: 252 Subcellular Location: Cell membrane
P9WJB0
MTRLVPALRLELTLQVRQKFLHAAVFSGLIWLAVLLPMPVSLRPVAEPYVLVGDIAIIGFFFVGGTVFFEKQERTIGAIVSTPLRFWEYLAAKLTVLLAISLFVAVVVATIVHGLGYHLLPLVAGIVLGTLLMLLVGFSSSLPFASVTDWFLAAVIPLAIMLAPPVVHYSGLWPNPVLYLIPTQGPLLLLGAAFDQVSLAPWQVGYAVVYPIVCAAGLCRAAKALFGRYVVQRSGVL
Function: Part of the ABC transporter complex involved in fluoroquinolones export. Probably responsible for the translocation of the substrate across the membrane (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 25576 Sequence Length: 237 Subcellular Location: Cell membrane
Q6FRT6
MNYLHNFKDTLFVDLLEVLNIVTIGEEHVNQLNLSGDASLSASSESSNMSFNSGSEENSQEKSVEDLEKQNCEINIHKNSDKEADTKKDPFLVTFNGEDDPLMPYNWSTNKKALIIIQTMLLTCVNYMGSSIYTPGQLEIQNEFHVGHVVGTLNLSLYVLGYGLGPIVFSPLTEISSIGRLPVYMITFFLFTMLQIGCALAPNFAGLVILRFITGVLCSPALSTGGATLGDIVSQNYLALVLGLWSIGAVAAPVLAPLLGASMVVAKDWRWIFWLLFFCCCATMLLLTFFFPETSSDTVLHRKAARIRKLTGDNRYYTEKEREEAQLPKKQFLIETLYRPFSMMITEPIVLAFDLYIALCYGAFYLFFEAFPIVFGGIYHFTLVEQGLAYFGFCVGCIFAYIILLVFSIKVAAKRFANNTFTPETTLILAMCIGWCIPLALFMFGWTAKVHWILPIISEVFFVLGCFNIFQASFSYLAICYPKYVASVFAGNGFARSSFAAAFPLFGQAMYNNLGTKNYPVAWGSSLVGFFTIGLWVIPFVLYKYGPSLRSMSKYNR
Function: Multidrug transporter that confers resistance to 5-flucytosine (5-FC) and clotrimazole . Confers also resistance to benomyl, but not 4-nitroquinoline-N-oxide, cycloheximide, or fluconazole . Plays direct roles in extrusion of 5-flucytosine and clotrimazole . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 62260 Sequence Length: 557 Subcellular Location: Cell membrane
P38124
MVYTSTYRHTIVVDLLEYLGIVSNLETLQSAREDETRKPENTDKKECKPDYDIECGPNRSCSESSTDSDSSGSQIEKNDPFRVDWNGPSDPENPQNWPLLKKSLVVFQIMLLTCVTYMGSSIYTPGQEYIQEEFHVGHVVATLNLSLYVLGYGLGPIIFSPLSETARYGRLNLYMVTLFFFMIFQVGCATVHNIGGLIVMRFISGILCSPSLATGGGTVADIISPEMVPLVLGMWSAGAVAAPVLAPLLGAAMVDAKNWRFIFWLLMWLSAATFILLAFFFPETQHHNILYRRALKLRKETGDDRYYTEQDKLDREVDARTFLINTLYRPLKMIIKEPAILAFDLYIAVAYGCFYLFFEAFPIVFVGIYHFSLVEVGLAYMGFCVGCVLAYGLFGILNMRIIVPRFRNGTFTPEAFLIVAMCVCWCLPLSLFLFGWTARVHWILPVISEVFFVLAVFNIFQATFAYLATCYPKYVASVFAGNGFCRASFACAFPLFGRAMYDNLATKNYPVAWGSSLVGFLTLGLAIIPFILYKYGPSLRTRSSYTEE
Function: Probable efflux transporter. Confers resistance to the azole derivative fluconazole (FCZ). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 61629 Sequence Length: 548 Subcellular Location: Membrane
Q9HNW1
MGIPLRIDARSTALVAVGGAVGAVLRYTVAQAIAGPLGTLAANAAGSLALGALAYEAAATDSVLSADAHTLLGTGCLSAFTTYSTFAVQTAGLAPRWMAANVATTYALGFAGVLVGRAIAATARGDRR
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12595 Sequence Length: 128 Subcellular Location: Cell membrane
Q5FKD1
MNFLLAGIGASIGAMLRYAITNYGKKHWEWIGNKFSNLPTPTLFINLTGAFILGFIFGIKTNVFIYAIVGTGVLGGYTTFSTMNTELVELYKSKNYRGFIFYALSSYLGGLILVFVGYYLAILF
Function: Fluoride-specific ion channel . Important for reducing fluoride concentration in the cell, thus reducing its toxicity (By similarity). Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13786 Sequence Length: 124 Subcellular Location: Cell membrane
Q88ZT7
MKKIIAITGFAMLGGGLREGLSLLVTWPQHFWITCLINIVGAFVLSLITNLLPARLPVSEDIVIGMSVGFVGSFTTFSTFTFETLQSFQSGHSVLALSYVAASLGLGLLAGLAGNFLSTYWLPKEEF
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13647 Sequence Length: 127 Subcellular Location: Cell membrane
Q38ZE4
MTILLVGLGAALGAILRYQLTRIGNHIASEFPLMTFLINLTGSFCLGWLTGSQLSQPVTLFLGVGVLGGYTTFSTLNSELSQLWFRRRYHIFFGYWLLTYGLGLLVAAAGFYAGL
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12601 Sequence Length: 115 Subcellular Location: Cell membrane
Q6AHI4
MSRRSSFPVHLHGRSMLLVFVGGALGTAARALLSAAAPTVAVISVITFVINVIGAFVLGWLLESLALRGPDEGRRRDVRLFAGTGVLGGFTTYSAFAVDTDGLIVASNVGGGILYAAATIAIGAAAYLAGIALGAAIGCRRGVSA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 14588 Sequence Length: 145 Subcellular Location: Cell membrane
Q1WS51
MIEVQNVKLGTLISVFFFGMIGGTLRYLLSLKLASTGTILVNLIGSFCLAFLTYYVIERQKLPAWLSTGLGTGMVGAFTTFSTFTVDILGLSTFTDATFYLLISVVGGFLLAYTGMILGIKLGKVGDRR
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13940 Sequence Length: 129 Subcellular Location: Cell membrane
Q8Y5I0
MYFLYVGVFGALGGMCRYAMNLWLGGGDFPSATLAVNLIGCFLLAFLMRFLAEKSRVSLVLLNGIGTGFIGAFTTFSAFSVDTIQLVQSGAWLFAVSYVLASFIGGLIMVKFGRMLSNKLLNRGEHRVG
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13952 Sequence Length: 129 Subcellular Location: Cell membrane
Q8TIQ4
MPSQDKEIDKIFLIGAGGFLGAVCRFLLCELVEGQLGILSVNVIGSFMLGMIMYDTEYLGFIGPKGKIAFGTGFMGAFTTFSTFAVQSFSLPFIPALGNISANIFLTLTGVFFGRSVIKALSSREI
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13496 Sequence Length: 126 Subcellular Location: Cell membrane
Q2FLB7
MEHLILVGIGGAVGAMLRFELSKLRPVRSIPLGTALVNIIGSSLFGCVVFSRSPGDIFYLVDVGILGGFTTFSTFSFETFRMFEEQDYQTMVLNISINLIGSLIGVLLSFILVTLILTGG
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12952 Sequence Length: 120 Subcellular Location: Cell membrane
Q2RL34
MAWLYVGCGGIAGTLARFLLSRWLGNRVRGTWPLGTLFVNLSGAFLLGLLLALPQGRLPANVTLALGTGFVGAYTTFSTFTYETVTMIGDGEGKRALAYSLGSILGGLLLAWLGWLAAGSLF
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12831 Sequence Length: 122 Subcellular Location: Cell membrane
P63865
MTASTALTVAIWIGVMLIGGIGSVLRFLVDRSVARRLARTFPYGTLTVNITGAALLGFLAGLALPKDAALLAGTGFVGAYTTFSTWMLETQRLGEDRQMVSALANIVVSVVLGLAAALLGQWIAQI
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13167 Sequence Length: 126 Subcellular Location: Cell membrane
P61393
MTTVAVWVGVALIGGVGSVLRFVVDGAVARRASRPFPLGTLVVNLSGAALLGFLGGLALSREAALLAGTAFVGAYTTFSTWMLETQRLGEERQLRAALANIVVSVVLGGAAAFIGQQLAQLV
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12484 Sequence Length: 122 Subcellular Location: Cell membrane
Q8FMR6
MQVSIPVCYPCPSFPQTRPFAGDGRKFGRVDSGFMPKLWEGLSVGAGAAVGACARLALTMQFGEGLWPILAINMLGSFLMGRYRPGPFWGTGVLGGFTTFSAFAVVLVDVPLPHAVAYLTVTVVSCVAAWLMGNRWSA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 14676 Sequence Length: 138 Subcellular Location: Cell membrane
A9KG69
MNVLLIFLGCGAGGVARYGVSNLMYLLMGKQFPIGTLIVNITGSLLMGILFIFILERLSGNIQLWRSLLLIGFLGGYTTFSSFSIETFNLIEAGHYFGAALNVLLSVALCIAGAWLGVLIGRQL
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13334 Sequence Length: 124 Subcellular Location: Cell inner membrane
Q8VM97
MGPLGFVAVGVGAAAGAWLRWGFAVLWNAINPALPYGTLAANLLGGYLVGLAVGFFDTHAGLPPEWRLLAITGFLGGLTTFSTFSSEVVANLIAGDYGWAGLHLLLHLGGSLLLTAFGLWTYRLLA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13116 Sequence Length: 126 Subcellular Location: Cell inner membrane
Q11UI4
MLHFILVLVGGAIGSGSRYLLSLHITRTYPGTFPYSTFAVNIIGCLLIGIIYGLAERFQLAVHWRLFLATGLCGGFTTFSAFAYENILLLQNGNYTAFTVNTLGSCMFGFTAVFLGVMLTKISI
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13503 Sequence Length: 124 Subcellular Location: Cell inner membrane
Q3Z6F1
MGEILLLAAGGALGAVSRYGLNNLTVKLLGDSFPYGTLIVNCLGCFVLGFLMQWGFSSDSHNTHLKLMLTAGFLGAFTTFSTFSYETLDCFKNGDYFNGFSNILANVLLGLLMVFIGAYLGSLLKQNSGT
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13915 Sequence Length: 130 Subcellular Location: Cell membrane
Q9RXX0
MSFPLWLWLALGGAVGAVCRQAAVLLLAPLVARTGFPAAVLLINVLGSFLLGLTLALTGRGVWPEAVRMTFGTGVLGAFTTFSTFSTELDGLLLRGQGGLALAYAALSVGLGLTAAVAGRVLGARL
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 12784 Sequence Length: 126 Subcellular Location: Cell membrane
Q6AP26
MDPVMGIIAVALGGAVGSLARYAIALGTQKIAHAFPFGTFIANLAGCLFIGLLWSFFEKIHISHTFRLFLFTGLLGGLTTFSTFSRETYGFFETGEYWQGFGYLFLSISLGLAMVAVGFFISHKFLLR
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 14037 Sequence Length: 128 Subcellular Location: Cell inner membrane
Q72BN6
MHRFVLVATGGIFGSLARYVLSGVAQKLTTSSFPYGTVLVNLLGSLLFGLVWGILENRITFAPEARLLLLTGFMGSLTTFSTLTYEGMVLLQSHMWLQAALYIVGQTVAGIMLVWFGAGLGRLV
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13401 Sequence Length: 124 Subcellular Location: Cell inner membrane
Q01QP2
MKYLLIALGGGTGSLARYLLGTAITSRVGARFPIGTMVVNVSGCFAIGLAMTLLTERLQPHPYWRLALVVGFLGGYTTFSSFEWETYAAVREGGFWIGLANVLGSVTLGYAAVWFGALLARR
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13097 Sequence Length: 122 Subcellular Location: Cell inner membrane
A9GIP6
MERWFWIGLGGAAGTLARYGLSTWCQQRFGAEFPYGTLAVNVIGSFLLGAIGEIAATTELLSPTLRLSLSTGVMGGFTTYSSFNNETIRLIEYKSWAAGLANIAITLVVCLLAGVLGMVVARRLIAG
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13495 Sequence Length: 127 Subcellular Location: Cell inner membrane
Q1GRB2
MNSLFPVMVGGAVGAGARHLVGQAMLARFGPGFPWWTLSVNIVGSLAMGLLIGLLARSGTGGETTRLFVGVGMLGGFTTFSSFSMEFWLLFERGQSVQAGLYVVASVVGALLACGAGMILIRQLPA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13024 Sequence Length: 126 Subcellular Location: Cell inner membrane
Q30TB5
MSWQTILAIGSGGFIGAVLRAYFNGIISHKMPHDIPFGTLGVNLVGSFIMGILIAYFMYSTIFSLHVKSFLSTGVLGALTTYSTFAIESFLLLNSGHIALALANISLNAFGSILMAGGGFYIIKLSLRA
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13713 Sequence Length: 129 Subcellular Location: Cell inner membrane
A6Q9S3
MQPYLLLAVGTGGFVGAILRFLISGWVQRLSPTLFPVGTLSVNVLGSFIIGFLALYFESVVAPHQKALVITGMLGALTTFSTFSLETVTMLQGGLWGRVVTNITLNVFLCVVATMLGMMLFKRLYG
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13593 Sequence Length: 126 Subcellular Location: Cell inner membrane
B2V9L9
MEKYLVIAVGGSIGAILRYLTGVYSAKFFGTWLPYGTLIVNVVGSFILSFFMILFLEKLSLDPLWRLFVAVGFCGSYTTLSSITYETLSIVMDGDYVRALLNIALNFGLSFLSAFAGIVLARML
Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Catalytic Activity: fluoride(in) = fluoride(out) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 13646 Sequence Length: 124 Subcellular Location: Cell inner membrane
Q00045
MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGIWPENNPAGVASPASDIKGKYVQSVTVANGVVTAQMKSDGVNKEIKNKKLSLWARREAGSVKWFCGQPVTRDNAGTDAVTADTTGKDKEIDTKHLPSTCRCFQIGSVKWFCGQPVTRDNAGTDAVTADTTGKDKEIDTKHLPSTCRDKSSAE
Function: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation, resistance to neutrophil mediated killing, twitching motility as well as transformation. Mediates the attachment and the formation of bacterial microcolonies on host epithelial cells. Mechanistically, pili retractation induces host NF-kappa-B activation in infected cells, which is temporally associated with the formation of gonococcal microcolonies. Location Topology: Single-pass membrane protein Sequence Mass (Da): 23021 Sequence Length: 214 Subcellular Location: Fimbrium
Q50228
MKTIVKLDLDKKPWEQDGQIHNRWHPDLPMIAMVKPGDEFRVECMDWTGGQIGNNDSANDVRDVDLTQVHYLSGPIGVEGAEPGDLMVVDILDVGTFDDSQWGFNGLFAKENGGGFLTDHFPEASKTIWDFHGVYTTSRHVPKVRYAGIMHPGLIGCLPSKELLDTWNKREGDLIATDPDRVPPLACPPTSQSAVMGRLSGDAAKKAAAEGARTVPPRDHGGNCDIKNLTKGSRVYFPVYVKDGGLSMGDLHFSQGDGEITFCGAIEMAGYLDIKVGLIKDGVKKYGIKNPVFQPSPITPTYRDYMIFEGISVDEAGKQHYLDVHIAYRQACLNAIEYLKKFGYSGEQAVSILGTAPVEGHISGIVDIPNACATLWIPTEIFEFDIRPNADGPKIMVPPGVDVSFTS
Function: Hydrolyzes formamide with the production of ammonia which can be used as a source of nitrogen for growth. Also acts, more slowly, on acetamide, propanamide and butanamide. Catalytic Activity: formamide + H2O = formate + NH4(+) Sequence Mass (Da): 44466 Sequence Length: 407 EC: 3.5.1.49
Q9URY7
MAPRTIVKVDLNKPAWEQPNLHNRWHPDIPFAESIDEGETVKIECLDWTGGQIKNDDSAEDIKNVDLTRIHYLSGPFEIKGAEPGDVLVVEIQDVQPLENQPWGYSGIFAKENGGGFLDEHYPKAAKAVFDFEGIFCSSRHIPGVRFPGLIHPGIIGTAPSKEILAEWNRREGALVAENPHSTHVMAQLPNASYAFAGILADEKLSATVASEGARTIPGRPENGGNCDIKNLSRGSKVFLPVHVPGAKLSIGDLHFSQGDGEISFCGAIEMAGSITIKCKILKNGISDLAMKSPMYLPGPVEPHFSPSRYLTFEGFSVDESGKQHYLCTTTAYRQTCLRVIEYFRRFGYNDYQLYLLLSCAPIQGHVAGIVDIPNSCTTIGVPMDIFEFDVSPNGKAKIIDLGSCAFANS
Function: Hydrolyzes formamide with the production of ammonia which can be used as a source of nitrogen for growth. May also act on acetamide, propanamide and butanamide (By similarity). Catalytic Activity: formamide + H2O = formate + NH4(+) Sequence Mass (Da): 44793 Sequence Length: 410 Subcellular Location: Cytoplasm EC: 3.5.1.49
Q48943
MTEGVLINENEVESKLEAVIKPGSFTGENAGEMAEVILIPKKAIDIKLEADVITPDSFAGKSAEEIGKLSVWQGPKTYPLSEFFEVTGNGGSSAAETLIRIKGDAMRIKRIGESMSAGKIEIEGSAGMHVGTGMKGGELVVYGDADSWAGMEMTGGLLHIKGNAGDHVGCAYRGKWHGMKGGRIVIEGSARHQLGGGMDGGEILVEGDVKSFCGIRQNGGLIFVKGSALRGVGAEMAGGTIVIGGKIERFSPGFEFVSMENSITSGEVELIGEFKKFTGDYAISKRAKGALYVVADTNPEL
Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can use N-furfurylformamide, formamide, N-methylformamide, and formate as substrates. This enzyme is oxygen-labile. Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin] Sequence Mass (Da): 31551 Sequence Length: 301 Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3. EC: 1.2.7.12
O27002
MGFVLVPKSDFQIPLEADTIRPDLFEGLDLDEIRSLQVYEGNIKRPLGEFFEIAETPHADQLIRIDGDVSRVKYIGSGMKSGKIIINGDVGLQLGCEMKGGEIEVNGNVSSWIGMEMHGGTIKINGNAGDYVGCAYRGEWRGMKGGKIIIQGNAGNNIGGGMMAGEIYIGGDAGNFCGIRMNGGEITVRGDAGRAPGAEMVSGIIKIHGRISSLLPGFKEISTFKEDGSLMILFKGDLSEKNPEGNLYINYNKNLHILENETDEGRVITKKGIKVIYNSGSTIREGQIIKGGNKLTDDYIDECARCCISPEDYKLLGEPENVVVSSHGNEVVLRAVEDPGIQMGTIFIPRGIWANVLTPPYTESTGSPMYKGVPVYLRKASQGERILSAEELVEEYGVGK
Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile. Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin] Sequence Mass (Da): 43288 Sequence Length: 400 Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3. EC: 1.2.7.12
P10552
MGIALMFLLALYQMQSAIHSEIIDTPNYAGNSLQDADSEVSPSQDNDLVDALLGNDQTERAELEFRHPISVIGIDYSKNAVVLHFQKHGRKPRYKYDPELEAKRRSVQDNFMHFGKRQAEQLPPEGSYAGSDELEGMAKRAAMDRYGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRTPAEDFMRFGRTPAEDFMRFGRSDNFMRFGRSPHEELRSPKQDFMRFGRPDNFMRFGRSAPQDFVRSGKMDSNFIRFGKSLKPAAPESKPVKSNQGNPGERSPVDKAMTELFKKQELQDQQVKNGAQATTTQDGSVEQDQFFGQ
Function: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs. PTM: This precursor includes 13 peptides that have FMRF or related sequences at their C-termini, and other putative neuropeptides. Sequence Mass (Da): 40100 Sequence Length: 347 Subcellular Location: Secreted
Q08325
MLAAAKYRNLDPAFVERLAQEAAERFRDRGQAVKYAKRKLHQAFGAFVAGTPAQAVAACVAKIAAGAEPKEAGREAMRAHASSAERVDWLEPFYERVAQWCGPASSVIDLACGLNPLAVPWMALAPGATYACYDVDRTMAEALRALGTVYPVRVNAAAVDLVAAVPAAGVDVALVLKTLTTVEQQRGGRRVAEYRRELTAVQHHSDGARSLSGRRGYADDPDAIVQRAVHGTGYEVVDEAAFGTEALYHLVPLAGTAGRPAPAEGAAEPGATRPVVDVPATARPDADRVDPTG
Function: Specifically methylates the N(7) position of guanine 1405 in 16S rRNA (By similarity). Confers resistance to aminoglycosides. Catalytic Activity: guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine Sequence Mass (Da): 30922 Sequence Length: 293 EC: 2.1.1.179
P50264
MNTVSPAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNESSKIVTLANSTNEFVEIVRNAENLDELDSMLEREDSQKHTSVTCWSQPLFFVNLSKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSEDVIDGMRPIENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMVVAMSNGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLK
Cofactor: Binds 1 FAD per subunit. Function: Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance. Catalytic Activity: H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine Sequence Mass (Da): 57806 Sequence Length: 508 EC: 1.5.3.17
P15488
MLKIKYLLIGLSLSAMSSYSLAAAGPTLTKELALNVLSPAALDATWAPQDNLTLSNTGVSNTLVGVLTLSNTSIDTVSIASTNVSDTSKNGTVTFAHETNNSASFATTISTDNANITLDKNAGNTIVKTTNGSQLPTNLPLKFITTEGNEHLVSGNYRANITITSTIK
Function: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. PTM: A longer minor form, starting at amino acid 15, has been detected by amino acid sequencing. This is probably due to alternative processing of the signal peptide. Sequence Mass (Da): 17492 Sequence Length: 168 Subcellular Location: Fimbrium
Q2FZK3
MKFNKVKLVIHACVLLFIIISIALIFHRLQTKTHSIDPIHKETKLSDNEKYLVDRNKEKVAPSKLKEVYNSKDPKYKKIDKYLQSSLFNGSVAIYENGKLKMSKGYGYQDFEKGIKNTPNTMFLIGSAQKFSTGLLLKQLEEEHKININDPVSKYLPWFKTSKPIPLKDLMLHQSGLYKYKSSKDYKNLDQAVKAIQKRGIDPKKYKKHMYNDGNYLVLAKVIEEVTGKSYAENYYTKIGDPLKLQHTAFYDEQPFKKYLAKGYAYNSTGLSFLRPNILDQYYGAGNLYMTPTDMGKLITQIQQYKLFSPKITNPLLHEFGTKKYPDEYRYGFYAKPTLNRLNGGFFGQVFTVYYNDKYVVVLALNVKGNNEVRIKHIYNDILKQNKPYNTKGVIVQ
Function: Catalyzes the liberation of D-alanyl moieties present on wall teichoic acid (WTA) and lipoteichoic acid (LTA) (By similarity). Affects the methicillin resistance level and autolysis in the presence of Triton X-100 as well as the cell wall structure . Catalytic Activity: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n D-alanine. Location Topology: Peripheral membrane protein Sequence Mass (Da): 46067 Sequence Length: 397 Subcellular Location: Cell membrane EC: 3.1.1.103
B5Y7I0
MKIAFFSSGTFGLPVLEELKKENHEIVLITKVDAPSGRGLKLQPSPPAVVAEALQIPIVKVNSLKNDFIEWYFSQGFDVAIVVDFGFYIPKQLFQADKPVMVNIHPSLLPKYRGPNPIRRAICSGELETGVTLIKISEKMDEGDIYLQERVLIDPDDDYVSLTPKLQHVSMELLKKFFLELKQGNLRAFPQLGDPSYAPKFTPDELWIDWQKPAHDIQNQVRALADVGAKTTLGSKLVKIFKVRISGMEDSLPPGHYVAEKESLYVGTGQGSLEILSLQQEGRKKQDAASFVKGLREKEGVFGG
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 33894 Sequence Length: 304 EC: 2.1.2.9
Q4JVI0
MKIVFAGTPEPAAVALEHLIADERIEVVAVVTQPDAKRGRGRSLRPSKVAEVAEEAAIPTYKWPSLKAGTESGDEARAVLGDLAAQGVTAAAVVAYGNLIPKDILDVFEHGWVNLHYSLLPRWRGAAPVQAALAAGDETTGASIFRIEEGLDTGPVAAQLTQKIGLEDTADDLLASLTYAGRELLADTLVAMDEGKAELSGQDDAQATHAPKIHPADAQIDWSQPAEVIQRVARAHTPAPGAWTLLDGQRYKIGMLLPSDPADVAELGPGEVVASPKKVFVGTGTGPLEITRIQPPGKKMMEAAAWARGQQELLAGRPTFSARETGE
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 34489 Sequence Length: 327 EC: 2.1.2.9
Q6A8H1
MRLLFAGTPDVAVPTLTALVADPRHEVAAVLTRPDAAVGRHRTPRPCPVAKAAEELGIPAIKATSVKSGEGHDAITSLDADVAVVVAYGGLIPADLLAVPRHGWINLHFSLLPRWRGAAPIQRAIMAGDEETGACVFQLVESLDAGPVYRTMTVPIGPMTTAGELLDELAHTATPLVIEALEDIEAGVEPTPQSVEGVTIAPQIHPDDVRVTVTAAAQEIDNLVRGVSPTPGAWAELDGKRFKILRTRCLEAGDGVPSTVATAQPGQLVATRKQLFLGTGSQPLELLQVQAFGKRAMSGADWARGADIDAGTRLR
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 33096 Sequence Length: 315 EC: 2.1.2.9
B2A2K2
MRTIFMGTPDFSVPFIEAIARSTHNLNLVVTQPDRRKGRGKELQPPPAKRKAEELGIDVFQPESIHNNYAYQILSDIEPHLIVTAAYGQILPRKILDLPRIKAINVHASLLPEYRGAAPIHRAVMDGKEQTGVTIMEMCDKMDAGDILNYESVDIGKTDTTGDVYKQIITVGPQLLIETMDLLEKNQVTPLKQDENQVSYAPKLKKEDEYLDFSKYTNTEVFNRVRGLNPWPGAFTKFEGKRLKIWETKVHNSSSFNSNSKPGEIIEINQQGPVVKCCQGSVILTKIQPSGKKAMTGEQFIRGYDIKSGIQLE
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 35185 Sequence Length: 313 EC: 2.1.2.9
Q9K1K6
MKVIFAGTPDFAAAALRAVAAAGFEIPLVLTQPDRPKGRGMQLTAPPVKQAALELGLRVEQPEKLRNNAEALQMLKEVEADVMVVAAYGLILPQEVLDTPKHGCLNIHASLLPRWRGAAPIQRAIEAGDAETGVCIMQMDIGLDTGDVVSEHRYAIQPTDTANEVHDALMEIGAAAVVADLQQLQSKGRLNAVKQPEEGVTYAQKLSKEEARIDWSKSAAVIERKIRAFNPVPAAWVEYQGKPMKIRRAEVVAQQGAAGEVLSCSADGLVVACGENALKITELQPAGGRRMNIAAFAAGRHIEAGAKL
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 32901 Sequence Length: 308 EC: 2.1.2.9
Q820J7
MRIIFAGTPDFAARALEELQKAGLDIVLTLTQPDRPAGRGMKMQASPVKILAQQYDIPLLQPETLKSSDIQAQLATFKPDVMIVAAYGLLLPEAVLRIPRHGCINIHASLLPRWRGAAPIQRALLEGDTETGISIMQMNQGLDTGAVLLKRSLPIEPYDTTATLHDKLADLGGKCIVEALTLLDQGRLISEPQNEVDACYAAKIRKIEAEIDWTCDAAYIDRMIRTFDPHPGAFTHLQGNTIKLWQARIVSHVNHNSSHQAGKIITVDPDGIVVACGRDALSIDILQKAGGKKLTAAQFLAGHPLHPGESFHKATQDNQGASET
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 35217 Sequence Length: 324 EC: 2.1.2.9
Q3J6T9
MAAPPHILFAGTPVFAAIILRRLLEAKYHIGAVYTQPDRPSGRGRRPTPSPVKDIAITHQLPLYQPATLKDKGSQAQLAALAPDLMVVAAYGLILPATVLQIPPLGCINVHASLLPRWRGAAPIQRALLAGDKVTGISIMQMDAGLDTGPVVHTARYPIHPKDTAATVHDQLAELGAEALLQCLPSLLEKKANIATLQDESQACYAPKIRKEEAWLDWSQPAVLLERQVRAFNPWPVAQTQIGGKTLRVWSAAALAQTANALPGTLLAVHKTGIDVATGNGTLRLLEVQLAGKRVMTVQDYLNAHTLTPGIVLVKNPGKAKSP
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 34554 Sequence Length: 323 EC: 2.1.2.9
A6Q4C9
MRIVFMGTPDYATTILEGLLEKFEVVGVFTQPDKPVGRKQVVTPPHVKKFLIEKNVDIPIFQPSTLKSEEVYEQLHTLAPDFIVVAAYGQILPKEILQLAPCINLHASLLPKYRGASPIQHALLNGDTVTGVTAMLMDEGLDTGDILAYDVIDIQNSDNAITLFEKLSHLAKELTPKVLQSFENIAPIAQHDVDASYCKKIRKQDGQIRFSDAKVIWNKYRAFIVWPGIFLENGLKLKEIDLVETDNTHEEGKILEISDAGVVVGCRRGSICIKSVQPPSKKAMEAVAYLRGKRLKVGDTFF
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 33628 Sequence Length: 302 EC: 2.1.2.9
Q827P7
MKLVFAGTPEVAVPALDALIASGRHEVAAVVTRPDAPAGRGRRLVASPVAQRAEEAGIEVLKPVKPRDEEFLARLREIAPDCCPVVAYGALLPRVALDIPAHGWVNLHFSLLPAWRGAAPVQHSIMAGDEITGASTFLIEEGLDSGPVFGTVTEEIRPTDTSGDLLTRLAFAGSGLLVATMDGVEEGKLKAVPQPADGITLAPKITVENAHVDWSTPALRVDRVVRGCTPAPGAWTVFRGERLKLIQVVPVPERTDLAPGALSVGKNNVYVGTGSYAVELLWVQAQGKKPMRAADWARGVRITDGEPLGA
Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet) Sequence Mass (Da): 32764 Sequence Length: 310 EC: 2.1.2.9
O29370
MRVALLGGTGNLGKGLALRLATLGHEIVVGSRREEKAEAKAAEYRRIAGDASITGMKNEDAAEACDIAVLTIPWEHAIDTARDLKNILREKIVVSPLVPVSRGAKGFTYSSERSAAEIVAEVLESEKVVSALHTIPAARFANLDEKFDWDVPVCGDDDESKKVVMSLISEIDGLRPLDAGPLSNSRLVESLTPLILNIMRFNGMGELGIKFL
Function: Catalyzes the reversible reduction of NADP(+) by F420H(2). In this reaction the proS hydrogen at C5 of F420 is transferred into the proS position at C4 of NADPH. Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n) Sequence Mass (Da): 22865 Sequence Length: 212 EC: 1.5.1.40
Q58896
MKIAILGGTGDQGFGLALRLAKNNKIIIGSRKKEKAEEAAKKAKEILKQRGIEADIIGLENKDAAKEGDVVILSLPYEYTLSTIKQLKEELKGKIVVSIGVPLATAIGDKPTRLLFPPDGSVAEMVQNVLKESKVVSAFQNVCHAVLEDLDNPVDCDILVCGNDEEAKKVVIDLANQIDGVRAIDCGNLEKSRIIEAITPLLIGLNIKYKSKGTGIRITNLEI
Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions. Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n) Sequence Mass (Da): 24068 Sequence Length: 223 EC: 1.5.1.40
P80951
MKVGIMGGTGNIGEGLARRIXIGGKYDVMIKGRDKA
Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. In M.organophilum, an alcohol-fermenting methanogen containing an NADP-dependent alcohol dehydrogenase, is probably involved in the regeneration of F420H(2) required for CO(2) reduction to methane. Thus, during growth on alcohol and CO(2), the F420-dependent NADP reductase probably has the function of coupling the NADP-dependent oxidation of the alcohol to the aldehyde with the F420-dependent reduction of CO(2) to methane. Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n) Sequence Mass (Da): 3775 Sequence Length: 36 EC: 1.5.1.40
D9PVP5
MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE
Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions. Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n) Sequence Mass (Da): 23448 Sequence Length: 224 EC: 1.5.1.40
Q9FKW6
MAAAISAAVSLPSSKSSSLLTKISSVSPQRIFLKKSTVCYRRVVSVKAQVTTDTTEAPPVKVVKESKKQEEGIVVNKFKPKNPYTGRCLLNTKITGDDAPGETWHIVFTTEGEVPYREGQSIGVIPEGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDGGEIVKGVCSNFLCDLKPGDEAKITGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEEHEDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKNPDNFRLDFAVSREQTNEKGEKMYIQTRMAEYAEELWELLKKDNTFVYMCGLKGMEKGIDDIMVSLAAKDGIDWLEYKKQLKRSEQWNVEVY
Function: Plays a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. PTM: May form interchain disulfide bonds with LIR1. Location Topology: Peripheral membrane protein Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin] Sequence Mass (Da): 40326 Sequence Length: 360 Pathway: Energy metabolism; photosynthesis. Subcellular Location: Plastid EC: 1.18.1.2
Q9M0V6
MALSTTPSQMSVALPTRIDGSSRSMIKVQSISFTDKSWGPPLLRLDSKSRSLGVKKRSTICMSLQQSSKSKVLVTPLELEDPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIASTRYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVAPYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWEQKLTQLRKNKQWHVEVY
Function: Maintains the supply of reduced ferredoxin under non-photosynthetic conditions. Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin] Sequence Mass (Da): 42396 Sequence Length: 378 Subcellular Location: Plastid EC: 1.18.1.2
Q9S9P8
MSHSAVSQAGAVSVSIENQRSLRRSVFKQNNSISFNSKSWSSSLALNQKTTSIRDGKRYPSTTICMSVQQTSSSKVTVSPIELEDPKDPPLNLYKPKESYTAKIVSVERVVGPKAPGETCHIVIDHDGNLPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIASTRYGDFFDGKTASLCVRRAVYYDPETGKEDPSKNGVCSNFLCDSKPGDKIQITGPSGKVMLLPESDPNATHIMIATGTGVAPYRGYLRRMFMENVPNKTFSGLAWLFLGVANTDSLLYDEEFTKYLKDHPDNFRFDKALSREEKNKKGGKMYVQDKIEEYSDEIFKLLDNGAHIYFCGLKGMMPGIQDTLKRVAEERGESWDLKLSQLRKNKQWHVEVY
Function: Maintains the supply of reduced ferredoxin under non-photosynthetic conditions. Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin] Sequence Mass (Da): 42789 Sequence Length: 382 Subcellular Location: Plastid EC: 1.18.1.2
P46908
MNFLSVRPSDSDLISSDLYELLESISTKRKMEKHTYLFREGMDAEELYLIQSGLIEIGKLTSDGKDLTLRICQKHDIVGELTLFTEEPRYMLSAKVLEDGEVLVINKNKLEKELIQNGALTFEFMKWMSTHLRKIQSKIRDLLLHGKKGALYSTLIRLSNSYGVERSDGILINIVLTNQDLAKFCAAARESVNRMLGDLRKKGVISIDESGKIILHKRDYLRCEIECENCPLEICNID
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Function: It is involved in the activation of genes necessary for anaerobic respiration. Sequence Mass (Da): 27218 Sequence Length: 238 Domain: The cysteine cluster which is probably involved in the coordination of the [4Fe-4S] cluster is located at the C-terminal part of the protein. Subcellular Location: Cytoplasm
Q46158
CEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLDVFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISR
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Function: It is involved in the activation of genes necessary for anaerobic respiration. It probably also activates genes involved in the production of virulence factors. Sequence Mass (Da): 10704 Sequence Length: 92 Subcellular Location: Cytoplasm
Q54CY5
MNKILLKRQILYNLPKYFKNNIPYTITINKSNQFINNNCKNNNNNFRKLNFTTTTTTTTTAPITNNKPKSNMLYSPKDRSYEEAVNALLTLQSNQTVIISWTKERRDNKEESAKFLMEEMRNYCKTLSIDLERESIIHVAGTKGKGSTCAITESIIREQGFSTGLFTSPHLISPRERIRINGEMISKEMFSQYFWNCWDLLIKDYQTQLPNFFRYLTLMALKIFQDEAIQCTILEVGIGGRMDSTNVFPKPMVTGISALGYDHQNLLGNTLAEIALEKAGIMKVGIPIFTVSSQLPEAINVLIDHSNKVKSPLSIVPSIDQYTISSGGGNNNNNKIESIGLKGTHQLENASLAIALANCWFKKQTFKDVNEIFNSENHKQYNYETNNYNVTQFTPLLKSIELGLKNCEWAGRAQHFTNPSHFPNMDFYLDGAHTVESSIVMLNWWKSIVNTTTTTTTTTTTTTTNNNDDDTIHILIFNSTGGRNPTSFLTPIIQSIDNKEIPIFNKSIIPNIIIEKPIDKKYYINEIIQSNQSSTATTTPIPDNAAVKQTTEIKESSTWEDFVVECYDKLSKKSHPCITADSIESSIEIAKELSENGTKNVKVLITGSLYLVGGVLKVLLKEKSFN
Function: Conversion of folates to polyglutamate derivatives. Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate Sequence Mass (Da): 70637 Sequence Length: 626 Pathway: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. EC: 6.3.2.17
P08192
MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKALPKNGRVLAVIGMLHDKDIAGTLAWLKSVVDDWYCAPLEGPRGATAEQLLEHLGNGKSFDSVAQAWDAAMADAKAEDTVLVCGSFHTVAHVMEVIDARRSGGK
Cofactor: Binds 2 Mg(2+) ions per subunit. Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives. Catalytic Activity: 7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate Sequence Mass (Da): 45406 Sequence Length: 422 Domain: The N-terminal domain alone (residues 1-287) is sufficient to bind both tetrahydrofolate and dihydropteroate with the same affinity as the intact enzyme, but is not able to bind ATP and has no enzymatic activity. Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. EC: 6.3.2.12
P43775
MNNMQLKATSPLAEWLSYLEKSHFKPIDLGLDRIKSVAEKLDLLHPVPYVITVGGTNGKGTTCRLLETILLNHGLRVGVYSSPHLLRYNERVRIQNQDLPDEAHTASFAFIDENKTESLTYFEFSTLSALHLFKQAKLDVVILEVGLGGRLDATNIVDSHLAVITSIDIDHTDFLGDTREAIAFEKAGIFRENCPVVIGEPNVPQTMLDQAEKLHCQVARRDVDWLFEQNAENWQWQNKKVRLENLPFCQIPLANAATVLAAVQYLPFDISEQTLRKSLQEVELVGRFQAIKTDKREKLADYLGVPVETLPTIIVDVGHNPHAAKYLSEKLTALKRSIEGKMIAVCGMLKDKDANGVFEHLTPIIDEWHCVTLGGYRGQSGDELVEKLKSHFPNIQATSDNSVMDGVCTALKSAVKNDVVLVFGSFHTVAEFWAVVE
Cofactor: Binds 2 Mg(2+) ions per subunit. Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives. Catalytic Activity: 7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate Sequence Mass (Da): 48826 Sequence Length: 437 Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. EC: 6.3.2.12
Q05932
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRDPAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEEQASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSPPKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
Cofactor: A monovalent cation. K(+) is most effective, followed by NH4(+) and Rb(+). Na(+), Li(+) and Cs(+) are ineffective. Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis. Unsubstituted reduced folates are the preferred substrates. Metabolizes methotrexate (MTX) to polyglutamates. Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate Sequence Mass (Da): 64609 Sequence Length: 587 Pathway: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. Subcellular Location: Mitochondrion inner membrane EC: 6.3.2.17
I6Y0R5
MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQLDGDAVRAGFAAVTSPGRLERMRSAPTVFIDAAHNPAGASALAQTLAHEFDFRFLVGVLSVLGDKDVDGILAALEPVFDSVVVTHNGSPRALDVEALALAAGERFGPDRVRTAENLRDAIDVATSLVDDAAADPDVAGDAFSRTGIVITGSVVTAGAARTLFGRDPQ
Cofactor: Binds 2 Mg(2+) ions per subunit. Function: Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu) . Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives (By similarity). Catalytic Activity: 7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate Sequence Mass (Da): 50779 Sequence Length: 487 Domain: Is folded into two distinct domains, an N-terminal ATPase domain and a C-terminal Rossmann-fold domain, which are joined by a flexible linker. Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. EC: 6.3.2.12
P36001
MDDISGRQTLPRINRLLEHVGNPQDSLSILHIAGTNGKETVSKFLTSILQHPGQQRQRVLIGRYTTSSLLNAKEEDISINNEAISLIEYSRIEKELIEADSSLKLQCNNLELLTSVALVYFAKKNCQWCIIETGLAGKQDPGSIIAGQSRVCCAITNVGISDEAFLCKFLSQITESSTNKAIFLLDGSNDEFVRNTITKRCHDVGCPLEITDPSLRDYNVHTDTWGTLEVRLPYSEEEYQIFNLRVAIAVLDFLSKEKKVCISKDQLSQGLISVDWPRSLHRLDYCYESTSGKKIALLLDNANNAKAARNLACHLRTTYGDTPLTFVIAITTGKKVSPLLDPLIRPQDYVIVTRFGSVVGMPWIQSLEPVNLLAFIKNRYTRNVNMQPDLQSVWTFLETSGLKTIVPVIVCGSLYICKELLRLHNCHLPV
Function: Conversion of folates to polyglutamate derivatives. Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate Sequence Mass (Da): 48143 Sequence Length: 430 Pathway: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. Subcellular Location: Mitochondrion EC: 6.3.2.17
A2RVV7
MLMIARKALASAHTKAFRLATRDVHCFSSILVSPPLVSLDLPENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIISEVGKMKKAVGKVPGLAVVLVGEQRDSQTYVRNKIKACEETGIKSVLAELPEDCTEGQIISVLRKFNEDTSIHGILVQLPLPQHLNESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRTGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEHITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSSCEFGYRLVGDVCYEEALGVASAITPVPGGVGPMTITMLLCNTLEAAKRIFL
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 38048 Sequence Length: 352 Pathway: One-carbon metabolism; tetrahydrofolate interconversion. Subcellular Location: Mitochondrion
Q24ZZ6
MTQILNAKPVVQAMKENLRQEVAALQAEGKAPTLGIIRVGSRPDDVYYENNIIKNCETIGIATKTYPLDLNISMEEFTAVMTQVNDDPSVHGIMLFRPLPPQLDEEVIKHLISADKDIDCMSPLNLEKVFEGDMSGLLPCTPAAVMAILRHYEIELKGANAVVMGRSLVVGKPLSMMLLQDNATVTICHSRTRNLPEVAKNADIVIAAMGRARMIDDNYVAENSIVIDVGINDAGDGKICGDVDYDAVVDKVKAITPVPGGVGSVTTTILLNNLVRACKSQ
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 30399 Sequence Length: 281 Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Q2JCX4
MRMLDGRSMAAEIGRYVVDEAERLAAAGVTPTLAVVLPTADPAAYSYAEIIERTAGKVGVHCVLHEPKGEPAAILDTIDTVAADPTVHGIIVQTPLPGGLTSREVGEHIPTAKDVDGMNPSSLGRLALGLPSFAPATAAAVVEILTRARIPMSGARVCVIGRGPVVGKPVSLLLLAEDATVTICHSRTKGLVSIAHEADIIVSATGHPRLVGAGFVRPGAAVIDVGTVVTETGQVGDVDAAAVSSVAGALTPVPGGVGPVTTMLLLRNTIRAARAA
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 27948 Sequence Length: 276 Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Q74GN1
MNLLDGKKCAESLVAEIARKVAGYTESGLRTPHMTIILVGEHAPSESYVKSKIATSGLAGFESTLLRFPETIRESELLAKIKEVNEDPTTDGLIVQLPLPKHINQQHVINAIAPEKDIDGFHPANFGRMTLGQKAFRPATAYGICKLLQFYEVPVKAKHCVVIGRSNIVGKPISIMLSNDFDIGNATVTLTHIETPRELLLDETRRADIVIVAVGIPGFVTADMVKDGVVLIDVGINRLESGKIVGDVDFENVAQKCSWITPVPGGVGRMTVAALMINTLMAYQNNFNLA
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 31486 Sequence Length: 290 Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Q47IX6
MTAQIIDGKALAEELRQGFKARVEALTAKGHKPGLVVILVGADPASEVYVRNKVNGCLAIGMHSEKITYDATIDQATVLNKIAELNADPNIHGILVQLPLPKHFDEEAVLEAISAEKDVDGFHAENVGALAQGNPRFIPCTPYGVMKMFEKGNVDLTGKEAVVIGRSNIVGKPMALLLINAGATVTVCNSRTKDLKFHTSRADILVAAVGKPKFVTGDMVKPGAVVIDVGINRLPDGKLCGDVDFASCLEVAGQITPVPGGVGPMTITMLLANTIEAAERKAGL
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 29895 Sequence Length: 284 Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Q3Z8K6
MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLVK
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH Sequence Mass (Da): 31283 Sequence Length: 296 Pathway: One-carbon metabolism; tetrahydrofolate interconversion.