ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q92QZ0 | MSETSIGPVALTMGDPAGIGPDITLSVWAKRADRPTPPFLYVGDPALLAARAKLLGQTVPICETDCPGAVAAFRQALPVWPVRSPAPVIPGNPDAANASAVTDAIDTAVRLVLAGEASALATNPISKAVLYEAGFRFPGHTEYLADLAARATGVAALPVMMLAGPKLRAVPVTIHIPLKDVPAALTPDLIYETCTITAADLRSRFGLPAPRLAIAGLNPHAGEGGALGREDDAVIRPVIDRLRAEGLDVVGPLPADTMFHDRARETYDVAICMYHDQALIPAKALGFDDSVNVTLGLPFIRTSPDHGTAFSLAGKGIARE... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
Q7UMZ2 | MTDANQTRPKLAITMGDAAGIGPEISLRVWDSPEVQSQGYPLLFGDAAIYHRAAKKLGCDCPGTISLAEFLDMPKQSIPSDAPHGVIVDCGKLTTEELGSFTPGKFSAATGRASYQSVTDAIDAAVSGHVDAIVTGPIQKEAWHQAGIDFPGHTELLADRAGRAVQGEPADVRMMLASDTIACVLETIHIPLADVASQLNTESLVRTINLAGETVQRRNQNRGSLLPPRIAVCGLNPHAGENGLFSHQEEEQIILPAIEAARQSGWTIEGPLSPDTAFTPAMRERIDIYVCMYHDQGLIPLKALSFDDAVNVTLGLPIIR... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(... |
B0TKZ7 | MKILADENMPYVQQLFGDLGTIETVNGRELTPEQVKDADVLLVRSVTKVDQALLAENNRLKFVGSATIGTDHIDLDYLASHNIPFSNAPGCNATAVGEFAFIAMLELAQRFNSPLKGKVVGIVGAGNTGTAVVKCLEAYGIEVLLNDPLLEQSGDPRDFVSLDTLIEKCDVISLHVPITKTGEHKTWYLFDEQRLNSLAENTWLVNCCRGEVIDNRALIKFKQQRDDVKVVLDVWEGEPNPMPELVPYVEFCTPHIAGYSLEGKARGTYILYQKLAEVLQISADKQMESLLPALWSERVLVQEISDERALLQLARFVYDL... | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 42181
Sequence Length: 376
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate b... |
Q8ECR2 | MKIVVDENMPYVEPLFGDLGEIIPVNGRTLTPEQVQDADVLLVRSVTRVNAALLEANQKLKFVGSATIGTDHVDLAYLATRGIVFSNAPGCNATAVGEFAFIAMLELAARFNSPLRGKVVGIVGAGNTGSATAKCLEAFGIKVLLNDPIKEAEGDPRDFVSLETLLQEADIISLHVPITRTGEHKTLHLFDEARLMSLKANIWLINCCRGDVIDNQALIKVKQQRDDLKLVLDVWEGEPNPMPELVPFAEFATPHIAGYSLEGKARGTFMLYQKLCELLAIPATKGLSDLLPRFNIKAVELEQLPDEKALLQLARFVYDL... | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 41503
Sequence Length: 376
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate b... |
Q56731 | KLKDKTVGIVGAGNTGSAVAKCLQAYGVTVLLHDPVIQDSDPRDFISLDELIACCDVISLHVPITKTGEHKTWYLFDEARLNSLKQGTWLLNCCRGEVIDNQALIKVKLERPDIKLVLDVWEGEPNPMHELIPLVELATPHIAGYSLEGKARGTFMLYQKLMQVLGKDADKSMTALLPSLWSVQLDVESIPDQKSLLQLARFIYDLRDDDELFRKTILDDSSKNPQVNSLNNNGFDLMRKNHLHRREFSALRLVNTGHSDVNWLTNLGFSGIGQ | Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Catalytic Activity: 4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + H(+) + NADH
Sequence Mass (Da): 30717
Sequence Length: 274
Pathway: Cofactor biosynthesis; pyridoxine 5'-phosphate b... |
Q2GFR2 | MIKKDPIELFDLWYNEVLAVSLQDKKDPTAMVLATCSKDLKPSARVVLLKKYSDQGFVFFTNMNSRKGKEMAENPSVALVFDWSRISKQVRIEGRIKMLPCNDADEYYASRPRGSQIGAWCSKQSSVLENREDFVELIKEMTIKFHEKPIPRPDYWVGIVVVPMLMEFWQEGLNRIHTRYQYTRDSNNMDKWNVVSLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 23296
Sequence Length: ... |
Q2N6B2 | MQSEESIMTDLATSEIPETDPFALFAEWMEEARASELNDPNAMALATATPDGAPSVRMVLLKDHGPQGFTFYTNAESRKGEEIRANAQTALLFHWKSLRRQIRVEGPVREVAPEVADAYFHSRARESQLGAVASDQSRPLEDRRVFVDRFRAAQERFDEGEVERPAYWTGFTVTPQRIEFWCDRPNRLHDRRLFTLSGAGDALSWTSTLLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24124
Sequence Length: ... |
A6H098 | MKDLSNYRKSYEKSELLETNIPEDPITLFKKWFHEVEDFGGIEEVNAMTVSSIGLDGFPKARVVLLKQFTYEGFIFYTNYDSEKGRAIANNPNICLSFFWHSLERQIIIKGKVKKIAENLSDGYFESRPNGSKLGAIVSNQSEVIASRMILEEKLKQLEDNCVGKEILRPKNWGGYIVEPQEVEFWQGRPNRLHDRIRYKLSADFYWKIERLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24921
Sequence Length: ... |
Q2JGW9 | MGGPDPDVPDLDVPDPALLRQGYRAGRLEPEHLAPTWVEQFAAWFIDAATPGVGVPEANAAVFATASAAGRPSARTVLLKGFDQRGFVIYTNYASRKGREATENPFGSLVFPWYALERQVVVIGSIERVSRAETERYFQSRPHGSQLGAWASHQSTIIESRTVLDDRAAELAARWPEGTRVPTPEFWGGLRIVPDTVEFWQGRADRLHDRLRYRRVSVPADGGGTDSLAVADPDATGVRVGDAGGGDAGGGVPTAAEDLWVVERLAP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 28842
Sequence Length: ... |
Q0BVM8 | MSMDSDAKSPFQTAELAFDDPFAAFSQWMEDARGAEPNDPNAMTLATASPSGVPSARIVLLRSVDAAEHPERGFVFFTNTESRKGVEIAANPQVALLFHWKSLGRQIRIEGKAIPVAVEEAESYFHTRPRISRLGARASDQSRPLPDRKTLQKRVEEEEARYPGDDIPRPAYWSGYRVTPTVIEFWQQMPFRLHDRLVFRRQGKNWGQEKLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24261
Sequence Length: ... |
P44909 | MELHNIRDEYTKRVLSQHDCHENPISQFEQWQKEAIHAQVNEPTAMNIATVDEQGRPNSRMVLLKEVNEQGFVFFTNYLSRKGGCIEHNPYVALTFFWPELERQVRIEGKAVKIPAEQSDKYFATRPYTSRIGAWASEQSAVISNYKSLLAKAALVAAKHPLNVPRPDYWGGYLVVPETVEFWQGRPSRLHDRIRYRKESDNWIRERLSP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 24500
Sequence Length: ... |
Q9RNP3 | MTQDPHKMFDEWMDEAKKAETDDPTAMALATASKQAFPCVRMMLLKGHTKDGFVFFTNLGSRKGHELLENPVATLLFHWKKLRRQVRIEGAATLISDEEADAYFATRARKSQLGAWASEQSRPLPARDVFEKRIADIEARYEGKDVPRPPYWTGFRVSPIRMEFWNDREFRLHERELFTLNDGRWQSEFLYP | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic Activity: H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) + pyridoxal 5'-phosphate
Sequence Mass (Da): 22486
Sequence Length: ... |
P25906 | MSSNTFTLGTKSVNRLGYGAMQLAGPGVFGPPRDRHVAITVLREALALGVNHIDTSDFYGPHVTNQIIREALYPYSDDLTIVTKIGARRGEDASWLPAFSPAELQKAVHDNLRNLGLDVLDVVNLRVMMGDGHGPAEGSIEASLTVLAEMQQQGLVKHIGLSNVTPTQVAEARKIAEIVCVQNEYNIAHRADDAMIDALAHDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENMAAEKLHLSEEVLSTLDGISRE | Function: Catalyzes the NAD(P)H-dependent reduction of pyridoxal to pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize pyridoxine or pyridoxamine . Has Kemp eliminase activity towards the non-physiological substrate 5-nitrobenzisoxazole, producing 4-nitro-2-cyanophenol; this activity is not conside... |
Q8UDU5 | MPAKLSVNLNAIAMLRNRRDLPWPDVAHFGQIALSAGASGLTVHPRPDQRHIRFSDLPVLRALIDDRFPGAEFNIEGYPTEDFLVLCEKTQPEQVTLVPDDPSQATSDHGWDFRKHAVFLKDVVGRLKAGGMRVSLFADGDGEREPVELAAETGAARIELYTGPYGGCFDDTQKADLLVEKLGQTADHAAALGLAVNAGHDLTVANLPKLMKRIPNLAEVSIGHGLTADAMEYGMAETVRRFCQACGQRNS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
B2URE7 | MLLGVNIDHIATLRQARYATMLDSFNVEPSVLDAAYAAQRGGADSITLHVRGDRRHMQDADALSVRESVALPLNLEMGNTPEMVDFALRLKPDYICMVPEKREEITTEGGLDAVFHEKDLAPTMARMADNGIQVSLFIDPEVPQVEAAARLGAPMIELHTGCFANHSGRERTEELARLKRAAELAHSLGIQVNAGHGINYQNLEQLLAGVPYLHELNIGHTIVSRALFVGMEQAVREMRQAIDRLS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q21XM2 | MTTKLSVNLNKVALVRNTRHLGIPSVTRAATLCLQAGANGITVHPRPDERHIRTDDVRDLALLMQAWPDREFNIEGNPLHNLMDVVHGLVEKKLPVHQVTFVPDSEGQFTSDHGWNFPGDASRLRPLIAQAHAWGLRVSLFMDADPAAMAGAQAVGADRVELYTEPYAAAWGTAQQTPQLARFAETARAALKLGLGVNAGHDLNRDNLSAFIQAVPGVAEVSIGHALIADALELGYSATVQAYLRCIAQGRS | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q3V7J9 | MQLGVNVDHVATLRNLRSTAYPDVVRIASKAVECGADFITVHLREDRRHIRDGDVFALKKHLAVPLNLEMAATREMLEIAKKVAPRYVCLVPEKREEITTESGVDAKGMFEILAPVVSDLRQSGIGVTLFIEPEKEQVDYAKKLCADKVELHVGAYCLSKSQGELERIANAAAYSHEQGMECHAGHGIDYGTAATIATIRHVSALNVGHFLICESLLHGVGSAVRNMKKIILEQRHNA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q5P083 | MIELGVNIDHVATLRQARRTWEPDPAWAAMEAHLGGADGITVHLREDRRHIQDEDVRRLRELTQVKLNLEMAATDEMVGIACALRPEMAMLVPEGRHEVTTEGGLDVLAQEGRLKDVVARLADAGIVTSVFIDAELGQVEAAARIGARVCEIHTGPYAHAFHAAGRDPQSAAVVDEIDKVRRAGEAIRALGMRFNAGHALNYYNVQPIARLPEVRELHIGHAIVSRSVFTGLRDAVREMKRLMREAAGVGR | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q82SJ7 | MIALGVNIDHVATVRQARGTTYPSPVEAALVAEVAGADAITLHLREDRRHIQENDVVILRDRLKTRMNLESAVTEEMIAFACRIKPHDICLVPERREELTTEGGLDVIRHFQQVSVACKRLAEAGIRVSLFVDAQAGQIDAAVEAGAPVIELHTGRYADAATPEMQQVELETIRTMAAYAFGRGLQVNAGHGLHYENTVQIAAIPELSELNIGHAIVARALFVGFAEAVREMKALLQQARA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q2Y865 | MIKLGVNIDHVATLRQARGTTYPDPIEAALIAESAGADAITLHLREDRRHIQDRDVEILRGALKTRMNLESAVTDEMIGFALRIKPHDICLVPERREELTTEGGLDVARHFEQVQRACHRLAEAGIRVSLFVDAEPAQIDASVEAGAPVIEIHTGHYADAQTTDEQQGELERVRAAVSKGLNHGLTVNAGHGLHYLNVQAIAAIPGVSELNIGHAIVARALFVGFERAVREMKNLMLEACK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
A6Q3Y6 | MKLGVNIDHIAVLREARKINDPDPIEALPIVKRAGADQITIHLREDRRHINDFDAKRIIEYSSLPVNMECSIDPDIIDIVAQLKPHRATLVPEKREEVTTEGGLDVIGQYERISDAIEKLKANEIDVSLFIDPDIEIIAACADTGADMVELHTGEYANIYAMLYSNLSKTPHSIKSLELSRKELQEKLSIAIGDLENAAIYAAKSGLLVAAGHGLNYQNVGTIAAMANIIELNIGQSIIARSIWDGLFEAVRKMKEIIDEAGHCH | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q3SRB0 | MSSSQSLRLGVNVDHVATIRNARGGDRPDVVRIALAAIAAGADGITAHLREDRRHIRDSDMARLKAEIEKPLNFEMAATAEMQGIALATQPHAVCLVPERREELTTEGGLDAAGQYNALAPFIAKLNDAGIRVSLFIAADPRQIEAAAKLRAPVIEIHTGGWCDAVVEGDSGKADAEWRRIVEGAALARSVGLEVHAGHGLDYATAETIAALPEITELNIGYFMMGEALLVGIAETVRTMRAAMDRGRATLKTRTA | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
B1ZNA6 | MILLGVNIDHCATLRQARYRQAEATAGGPIEPDPVTLALAAERAGADGITVHLREDRRHIQERDVWRLRESIATRLNFEMACTPAMTQLALKLKPESVCLVPENRQEITTEGGLDVTAQRDRVRACVEAMNAAGIQASLFIDPDEQQIELAAQLHAPCVELHTGAYASSYPQPTSRTKEFQRLRMGAARAHELGLIVNAGHGINYVNIAEVRTLPHLHELNIGHSIISRALFTGIDEAVREMKVRMNP | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q4FLS6 | MKRLGVNIDHVATVRNARGSFHPDPFTIAKHVIKCGAHSVTIHLREDRRHIKDSDVVKICKSRKIITNLEISLNKEIIDIALKNRPNFICIVPEKRKEVTTEGGLNLIKNKKKIKSIISLFNKKSIRTSLFIDPNLKDIKIAKELNATCVELHTGKISNLIKENKSYKNEYLKIKKCSELGVKLGIEVHAGHGLDYKTTSILSKIKEITEFNIGHFIIGESLTHGLKKTITIFKEITNK | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
C0QU74 | MRLGVNIDHIATVREARKTYEPDPVKGAIIARDAGADQITFHLREDRRHIQDSDVEKLRAVITEIPLNMEMAATEEMKQIAIRIKPDRVTIVPEKREEITTEGGLDVVSMTDYLREFIKELKDNGINVATFVDPVEEQIKASMEVGADAVEIHTGEYANARSDKERDNEIFRIKKAAVYGRSLGLKVFAGHGLTYTNVQPVAEIEEIEELNIGHSIIANAIFLGLDEAVRKMKKLINEVRRKDIRV | Function: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic Activity: 1-deoxy-D-xylulose 5-phosphate + 3-am... |
Q9WYU4 | MEIKKGTWIIKKGFAEMFKGGVIMDVTSAEQAKIAEEAGAVAVMALERVPADIRKEGGVARMASIAKIREIMEAVSIPVMAKVRIGHIAEAKILEELGVDFIDESEVLTPADDRFHINKHEFKVPFVCGARDLGEALRRIAEGAAMIRTKGEAGTGNVVEAVKHMRRVMEQIKQVTKMEDEELVAYGKEIGAPVELLREVKRLGRLPVVNFAAGGVATPADAALMMMLGADGVFVGSGIFKSKDPRKMAKAMVLAVTYWDNPRILLKISEDIGEPMRGLDVEELEVRMQERGW | Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G... |
Q73WF2 | MSAPRIGVLALQGDTREHLAALREAGAESMPVRRRGELEAVDGLVIPGGESTTMSHLLKDLDLLEPLRGLLADGLPAYGACAGMILLASEILDAGAGGREALPLRAIDMTVRRNAFGRQVDSFEGDIAFAGLDGPVRAVFIRAPWVERAGDGVEVLARAAGHVVAVAGIEPDA | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
A0QWH0 | MTAHVGVLALQGDTREHLAALREAGAEASTVRRLSELAAVDALVIPGGESTAISHLLREFDLLEPLRARIAEGMPCYGSCAGMILLATEIADAGVPGRAAVPLKGIDMTVRRNAFGRQVDSFEGDIDFVGLDTPVHAVFIRAPWVERIGPDVEVLARADDHIVAVRQGPMFATAFHPEVTGDRRIHKLFVDSL | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
Q3IU60 | MLKAGVIAVQGDVAEHADAIRRAADRHGEDCTVESIRSAGVVPECDLLLLPGGESTTISRLLAEEGIDEEIEAFAAAGKPLLATCAGLIVASRDAKDDRVSTLDILDVSVDRNAFGRQKDSFEAAIDVEGLDEPFPAVFIRAPLIDEVDAAVETLAAVDDRPVAVRQDNVVGTSFHPELTDDSRIHGLAFFS | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
A9A4S0 | MSAKIGILAIQGDVAENVSSLVASIADLNQDATVHVVKTPEEISAMDGLVIPGGESTTIGQLSLVNGSQKVIKQKVESGMPVLGICAGMVLLASNATDRVVGKTEQPLFDFLDIELERNSFGRQRESFEANVSMDSIGISNYNGVFIRAPAISSTSDDIEVLAKLNEKIVAIKKGNIIGTSFHPELTDDLAVHKYFVNLVKETKQ | Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
Catalytic Activity: aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutam... |
L7N697 | MSFVFAVPEMVAATASDLASLGAALSEATAAAAIPTTQVLAAAADEVSAAIAELFGAHGQEFQALSAQASAFHDRFVRALSAAAGWYVDAEAANAALVDTAATGASELGSGGRTALILGSTGTPRPPFDYMQQVYDRYIAPHYLGYAFSGLYTPAQFQPWTGIPSLTYDQSVAEGAGYLHTAIMQQVAAGNDVVVLGFSQGASVATLEMRHLASLPAGVAPSPDQLSFVLLGNPNNPNGGILARFPGLYLQSLGLTFNGATPDTDYATTIYTTQYDGFADFPKYPLNILADVNALLGIYYSHSLYYGLTPEQVASGIVLP... | Function: Esterase that hydrolyzes short to medium chain fatty acid esters with the highest specific activity for p-nitrophenyl caproate (pNPC6). Has lower activity with p-nitrophenyl caprylate (pNPC8) and p-nitrophenyl butyrate (pNPC4). Has weak activity with p-nitrophenyl caprate (pNPC10) and p-nitrophenyl laurate (p... |
Q9SRQ3 | MANSHTDDLDELLDSALDDFKDLNLSHQRNQREAQEEEEKKRKEETVLLPSGVQGLGMGLPDMRSKKRGKQKVSKEDHVAEALDKLREQTRETVKGLESISSKQLPASDDDGMVEDFLKQFEDLAGSKDLESIVETMMQQLLSKDILHEPMKELGARYPKWLKENEASLSKEDYKRYSQQYKLIEELNAVYENEPNNSSKIMEIMQKMQECGQPPSDIVKEIDPGFDFASLGQISPEMLESSPNCCIM | Function: Contributes to morphology determination of peroxisomes, but not to import of peroxisomal matrix proteins . Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs) . Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the ... |
Q94EI3 | MANDTHTDDLDELLDSALDDFKDLNLTQRNGGVKKEEGDKKETESLPSGVQGLGMGLPDMRSKKKGKKKIAKEDHVTEALDKLREQTRETVKGLESLSSKQQPTGSDDAMVEDWIKQFENLTGSNDLESIVDTMMQQLLSKDILHEPMKEIGARYPKWLEEHESSLNKEEFDRYSRQYELIKELNLVYENEPNNSTKIMEIMQKMQECGQPPSDIVQEMDPGFDFASLGQMSPDMLESSPNCCVM | Function: Contributes to morphology determination of peroxisomes, but not to import of peroxisomal matrix proteins. Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the pe... |
Q9BGL8 | MSLCGPLNLSLAGEATPCAEPGAPNASAWPPSGRASASPALPIFSMTLGAVSNVLALALLAQAAGRLRRRRSAATFLLFVASLLATDLAGHVIPGALVLRLYAAGRSPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTRPLLHAARVSAARARLALAVLAALALAVALLPLARVGRYELQYPGTWCFIGLRPAGGWRQALLAGLFAGLGLAALLAALVCNTLSGLALLRARWRRRRSRRRPQACGPDGRRHWGARAPRSASASSSSSVASVPGGSPGRGSARRARAHDVEMVGQLVGIMVVSCICWSPLLVLVVL... | Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues (By ... |
P34995 | MSPCGPLNLSLAGEATTCAAPWVPNTSAVPPSGASPALPIFSMTLGAVSNLLALALLAQAAGRLRRRRSAATFLLFVASLLATDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTRPLLHAARVSVARARLALAAVAAVALAVALLPLARVGRYELQYPGTWCFIGLGPPGGWRQALLAGLFASLGLVALLAALVCNTLSGLALLRARWRRRSRRPPPASGPDSRRRWGAHGPRSASASSASSIASASTFFGGSRSSGSARRARAHDVEMVGQLVGIMVVSCICWSPMLVLVALA... | Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues.
PTM... |
P35375 | MSPCGLNLSLADEAATCATPRLPNTSVVLPTGDNGTSPALPIFSMTLGAVSNVLALALLAQVAGRMRRRRSAATFLLFVASLLAIDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTQPLIHAARVSVARARLALAVLAAMALAVALLPLVHVGRYELQYPGTWCFISLGPRGGWRQALLAGLFAGLGLAALLAALVCNTLSGLALLRARWRRRRSRRFRKTAGPDDRRRWGSRGPRLASASSASSITSATATLRSSRGGGSARRVHAHDVEMVGQLVGIMVVSCICWSPLLVLV... | Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues.
PTM... |
P37868 | MSFHHRVFKLSALSLALFSHLSFASTDSELNLDFLQGMSAIPSVLKSGSDFPAGQYYVDVIVNQENVGKARLSITPQEESANALCLSPEWLKAAGVPVRLEGYASTLNAAGQCYVLSRNPYTRVDFSYGSQSLVFSIPQSFLVGKTDPSRWDYGVPAARLKYSANASQTSGQSTSAYANADLMVNLGRWVLASNMSASRYADGSGEFTARDITLSTAISQVQGDLLLGKSQTRSALFSDFGFYGAALRSNSNMLPWEARGYAPLITGVANSTSRVTISQNGYAVYSKVVPPGPYQLDDVRSVGNGDLVVTVEDASGHKTT... | Function: Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86370
Sequence Length: 802
Subcellular Location: Cell outer membrane
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Q86TG7 | MTERRRDELSEEINNLREKVMKQSEENNNLQSQVQKLTEENTTLREQVEPTPEDEDDDIELRGAAAAAAPPPPIEEECPEDLPEKFDGNPDMLAPFMAQCQIFMEKSTRDFSVDRVRVCFVTSMMTGRAARWASAKLERSHYLMHNYPAFMMEMKHVFEDPQRREVAKRKIRRLRQGMGSVIDYSNAFQMIAQDLDWNEPALIDQYHEGLSDHIQEELSHLEVAKSLSALIGQCIHIERRLARAAAARKPRSPPRALVLPHIASHHQVDPTEPVGGARMRLTQEEKERRRKLNLCLYCGTGGHYADNCPAKASKSSPAGK... | Function: Retrotransposon-derived protein that binds its own mRNA and self-assembles into virion-like capsids . Forms virion-like extracellular vesicles that encapsulate their own mRNA and are released from cells, enabling intercellular transfer of PEG10 mRNA . Binds its own mRNA in the 5'-UTR region, in the region nea... |
Q7TN75 | MAAAGGSSNCPPPPPPPPPNNNNNNNTPKSPGVPDAEDDDERRHDELPEDINNFDEDMNRQFENMNLLDQVELLAQSYSLLDHLDDFDDDDEDDDFDPEPDQDELPEYSDDDDLELQGAAAAPIPNFFSDDDCLEDLPEKFDGNPDMLGPFMYQCQLFMEKSTRDFSVDRIRVCFVTSMLIGRAARWATAKLQRCTYLMHNYTAFMMELKHVFEDPQRREAAKRKIRRLRQGPGPVVDYSNAFQMIAQDLDWTEPALMDQFQEGLNPDIRAELSRQEAPKTLAALITACIHIERRLARDAAAKPDPSPRALVMPPNSQTD... | Function: Retrotransposon-derived protein that binds its own mRNA and self-assembles into virion-like capsids . Forms virion-like extracellular vesicles that encapsulate their own mRNA and are released from cells, enabling intercellular transfer of PEG10 mRNA . Binds its own mRNA in the 5'-UTR region, in the region nea... |
P15922 | MKVITFSRRSALASIVATCLMSTPALAATAQAPQKLQIPTLSYDDHSVMLVWDTPEDTSNITDYQIYQNGQLIGLASQNNDKNSPAKPYISAFYKSDAANFHHRIVLQNAKVDGLKAGTDYQFTVRTVYADGTTSNDSNTVTTTTTAVPKVINITQYGAKGDGTTLNTSAIQKAIDACPTGCRIDVPAGVFKTGALWLKSDMTLNLLQGATLLGSDNAADYPDAYKIYSYVSQVRPASLLNAIDKNSSAVGTFKNIRIVGKGIIDGNGWKRSADAKDELGNTLPQYVKSDNSKVSKDGILAKNQVAAAVATGMDTKTAYS... | Function: Contributes significantly to bacterial utilization of polygalacturonate and the induction of pectate lyase in the presence of extracellular pectic polymers.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-2) + alpha-D-galacturonosyl-(1->4)-D-galacturonate
Seque... |
Q9C660 | MTTPAQAPREEVSLSPSLASPPLMALPPPQPSFPGDNATSPTREPTNGNPPETTNTPAQSSPPPETPLSSPPPEPSPPSPSLTGPPPTTIPVSPPPEPSPPPPLPTEAPPPANPVSSPPPESSPPPPPPTEAPPTTPITSPSPPTNPPPPPESPPSLPAPDPPSNPLPPPKLVPPSHSPPRHLPSPPASEIPPPPRHLPSPPASERPSTPPSDSEHPSPPPPGHPKRREQPPPPGSKRPTPSPPSPSDSKRPVHPSPPSPPEETLPPPKPSPDPLPSNSSSPPTLLPPSSVVSPPSPPRKSVSGPDNPSPNNPTPVTDNS... | Function: Could be involved in the negative regulation of root growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 80856
Sequence Length: 762
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9SGY7 | MDKVQQQADLFGKTISPFVASQPTNVGGFTDQKIIGGSETTQPPATSPPSPPSPDTQTSPPPATAAQPPPNQPPNTTPPPTPPSSPPPSITPPPSPPQPQPPPQSTPTGDSPVVIPFPKPQLPPPSLFPPPSLVNQLPDPRPNDNNILEPINNPISLPSPPSTPFSPPSQENSGSQGSPPLSSLLPPMLPLNPNSPGNPLQPLDSPLGGESNRVPSSSSSPSPPSLSGSNNHSGGSNRHNANSNGDGGTSQQSNESNYTEKTVIGIGIAGVLVILFIAGVFFVRRKQKKGSSSPRSNQYLPPANVSVNTEGFIHYRQKPG... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77549
Sequence Length: 718
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9ZUE0 | MSDLGESPSSSPPAPPADTAPPPETPSENSALPPVDSSPPSPPADSSSTPPLSEPSTPPPDSQLPPLPSILPPLTDSPPPPSDSSPPVDSTPSPPPPTSNESPSPPEDSETPPAPPNESNDNNPPPSQDLQSPPPSSPSPNVGPTNPESPPLQSPPAPPASDPTNSPPASPLDPTNPPPIQPSGPATSPPANPNAPPSPFPTVPPKTPSSGPVVSPSLTSPSKGTPTPNQGNGDGGGGGGGYQGKTMVGMAVAGFAIMALIGVVFLVRRKKKRNIDSYNHSQYLPHPNFSVKSDGFLYGQDPGKGYSSGPNGSMYNNSQQ... | Function: Regulates the auxin-related MAX (More Axillary Growth) pathway during the shoot branching.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76302
Sequence Length: 720
Subcellular Location: Cell membrane
E... |
Q9CAL8 | MSDSPTSSPPAPSADSAPPPDTSSDGSAAPPPTDSAPPPSPPADSSPPPALPSLPPAVFSPPPTVSSPPPPPLDSSPPPPPDLTPPPSSPPPPDAPPPIPIVFPPPIDSPPPESTNSPPPPEVFEPPPPPADEDESPPAPPPPEQLPPPASSPQGGPKKPKKHHPGPATSPPAPSAPATSPPAPPNAPPRNSSHALPPKSTAAGGPLTSPSRGVPSSGNSVPPPANSGGGYQGKTMAGFAIAGFAVIALMAVVFLVRRKKKRNIDAYSDSQYLPPSNFSIKSDGFLYGQNPTKGYSGPGGYNSQQQSNSGNSFGSQRGGG... | Function: Regulates negatively root hairs elongation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75372
Sequence Length: 710
Subcellular Location: Cell membrane
EC: 2.7.11.1
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O65530 | MSLSPSSSPAPATSPPAMSLPPADSVPDTSSPPAPPLSPLPPPLSSPPPLPSPPPLSAPTASPPPLPVESPPSPPIESPPPPLLESPPPPPLESPSPPSPHVSAPSGSPPLPFLPAKPSPPPSSPPSETVPPGNTISPPPRSLPSESTPPVNTASPPPPSPPRRRSGPKPSFPPPINSSPPNPSPNTPSLPETSPPPKPPLSTTPFPSSSTPPPKKSPAAVTLPFFGPAGQLPDGTVAPPIGPVIEPKTSPAESISPGTPQPLVPKSLPVTTSYHRSSAGFLFGGVIVGALLLILLGLLFVFYRATRNRNNNSSSAHHQS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77397
Sequence Length: 731
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9C821 | MSTDTIPSLSSPPAPEFPSTTPDTATSPAPSQPSIIGPSSLAPFPETTTNIDGGSRNVALTGLITGVVLGATFVLLGVCIFVCFYKRKKRKLKKKKKEDIEASINRDSLDPKDDSNNLQQWSSSEIGQNLFTYEDLSKATSNFSNTNLLGQGGFGYVHRGVLVDGTLVAIKQLKSGSGQGEREFQAEIQTISRVHHRHLVSLLGYCITGAQRLLVYEFVPNKTLEFHLHEKERPVMEWSKRMKIALGAAKGLAYLHEDCNPKTIHRDVKAANILIDDSYEAKLADFGLARSSLDTDTHVSTRIMGTFGYLAPEYASSGKL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55659
Sequence Length: 509
Subcellular Location: Cell membrane
EC: 2.7.11.1
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P94449 | MKRFCLWFAVFSLLLVLLPGKAFGAVDFPNTSTNGLLGFAGNAKNEKGISKASTTGGKNGQIVYIQSVNDLKTHLGGSTPKILVLQNDISASSKTTVTIGSNKTLVGSYAKKTLKNIYLTTSSASGNVIFQNLTFEHSPQINGNNDIQLYLDSGINYWIDHVTFSGHSYSASGSDLDKLLYVGKSADYITISNSKFANHKYGLILGYPDDSQHQYDGYPHMTIANNYFENLYVRGPGLMRYGYFHVKNNYSNNFNQAITIATKAKIYSEYNYFGKGSEKGGILDDKGTGYFKDTGSYPSLNKQTSPLTSWNPGSNYSYRV... | Function: Catalyzes the depolymerization of pectins of methyl esterification degree from 13 to 75%, with an endo mode of action. Cannot degrade polygalacturonate. Also displays protopectinase activity, i.e. releases pectin from protopectin.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ... |
Q48677 | MELFDKVKALTEIQATSGFEGPVRDYLKARMVELGYQPEFDGLGGIFVTKASKVENAPRIMVAAHMDEVGFMVSSIKADGTFRVVPLGGWNPLVVSGQRFTLFTRTGKKIPVVTGGLPPHLLRGTGVTPQIPAISDIIFDGAFENAAEAAEFGIAQGDLIIPETETILSANGKNIISKAWDNRYGCLMILELLEFLADKELPVTLIIGANVQEEVGLRGAKVSTTKFNPDLFFAVDCSPASDTFGDDNGRLGEGTTLRFFDPGHIMLPGMKNFLLDTANHAKVKTQVYMAKGGTDAGAAHLANGGVPSTTIGVVARYIHS... | Cofactor: Binds 2 divalent metal cations per subunit.
Catalytic Activity: Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.
Sequence Mass (Da): 38324
Sequence Length: 355
EC: 3.4.11.7
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Q01972 | MVVFSQVTVALTCFSAIASAAAVRQEPPQGFTVNQVQKAVPGTRTVNLPGLYANALVKYGATVPATVHAAAVSGSAITTPEADDVEYLTPVTIGSSTLNLDFDTGSADLWVFSSELTSSQQSGHDVYNVGSLGTKLSGASWSISYGDGSSASGDVYKDTVTVGGVKATGQAVEAAKKISSQFLQDKNNDGLLGMAFSSINTVSPTPQKTFFDTVKSSLGEPLFAVTLQGTGRPWHLRFGYIDSDKYTGTLAYADVDDSDGFWSFTADSYKIGTGAAGKSITGIADTGTTLLLLDSSIVTGLLQEGYPGSQNSSSAGGYIF... | Function: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positio... |
Q9GMY7 | MKWLLLLSLVALSECYIYKVPLVKKKSLRKNLMEQGLLQDYLKTHSINPASKYLKEAASMMATQPLENYMDMEYFGTIGIGTPPQEFTVIFDTGSSNLWVPSVYCSSPACSNHNRFNPQQSSTYQGTNQKLSVAYGTGSMTGILGYDTVQVGGITDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSIASSGATPVFDNIWNQGLVSQDLFSVYLSSNDQGGSVVMFGGIDSSYFTGNLNWVPLSSETYWQITVDSITMNGQVIACSGSCQAIVDTGTSLLSGPTNAIASIQGYIGASQNANGEMVVSCSAINTLPNIVF... | Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Catalytic Activity: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala... |
P13636 | FIIKVPLVKKKSLRKNLKEHGLLKDFLKKHSPNPASKYFPQEAAVMATQPLENYMDMEYF | Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Catalytic Activity: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala... |
Q8SQ41 | MKIQVLVLVCLHLSEGVERIILKKGKSIRQVMEERGVLETFLRNHPKVDPAAKYLFNNDAVAYEPFTNYLDSYYFGEISIGTPPQNFLILFDTGSSNLWVPSTYCQSQACSNHNRFNPSRSSTYQSSEQTYTLAYGFGSLTVLLGYDTVTVQNIVIHNQLFGMSENEPNYPFYYSYFDGILGMAYSNLAVDNGPTVLQNMMQQGQLTQPIFSFYFSPQPTYEYGGELILGGVDTQFYSGEIVWAPVTREMYWQVAIDEFLIGNQATGLCSQGCQGIVDTGTFPLTVPQQYLDSFVKATGAQQDQSGNFVVNCNSIQSMPT... | Function: Hydrolyzes various peptides including beta-endorphin, insulin B chain, dynorphin A, and neurokinin A, with high specificity for the cleavage of the Phe-Xaa bonds.
Catalytic Activity: Degradation of gelatin, little activity on hemoglobin. Specificity on B chain of insulin more restricted than that of pepsin A.... |
Q55E60 | MSVHPRNQGKDDCCEKTHLDSQYSPGYYWLGNNTLKVPLVLHKENRQRLVSQILSKHKDQVKENSFILLESGKSTMQYDTDHEPLFKQERYFFWTFGSDIPDCFGIVGLDEQATSILCIPKLPAEYATWMGEIRSKEYYKSIFLVDQVLYVDEMMDYLKSKNASTIYTILGTNTDSGSTFVEPQYPGLRETFNVNNTLLFPEIAECRVIKSPKEVEVIRYCVDASVSAHKHVMRKVKVGLKEYQCESEFLHHVYNEWGCRNVGYTCICAANKNSAVLHYGHAGEPNSATISENGFCLFDMGAEYHSYTADITCSFPATGK... | Cofactor: Binds 2 manganese ions per subunit.
Function: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position.
Catalytic Activity: H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline
Sequence Mass (Da): 56426
Sequence Length: 501
EC... |
P15288 | MSELSQLSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVGNILIRKPATAGMENRKPVVLQAHLDMVPQKNNDTVHDFTKDPIQPYIDGEWVKARGTTLGADNGIGMASALAVLADENVVHGPLEVLLTMTEEAGMDGAFGLQGNWLQADILINTDSEEEGEIYMGCAGGIDFTSNLHLDREAVPAGFETFKLTLKGLKGGHSGGEIHVGLGNANKLLVRFLAGHAEELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDVLKSLVNTYQEILKNELAEKEKNLALLLDSVANDKAALIAKSRDTF... | Cofactor: Binds 2 Zn(2+) ions per subunit. Can also use Co(2+).
Function: Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas s... |
P12955 | MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAM... | Cofactor: Binds 2 manganese ions per subunit.
Function: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position . The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro... |
Q11136 | MASTVRPSFSLGNETLKVPLALFALNRQRLCERLRKNGAVQAASAVVLQGGEEMQRYCTDTSIIFRQESFFHWAFGVVESGCYGVIDVDTGKSTLFVPRLPDSYATWMGKIHSKEYFKEKYAVDDVQYTDEIASVLTSRNPSVLLTLRGVNTDSGSVCREASFEGISKFNVNNTILHPEIVECRVFKTDMELEVLRYTNRISSEAHREVMKAVKVGMKEYEMESLFQHYCYSRGGMRHTSYTCICCSGENAAVLHYGHAGAPNDRTIKDGDICLFDMGGEYYCFASDITCSFPANGKFTEDQKAIYEAVLRSCRTVMSTM... | Cofactor: Binds 2 manganese ions per subunit.
Function: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro,... |
O53896 | MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGA... | Function: Required for virulence . Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone . Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks . May utilize its PDZ domain to recogniz... |
Q5I0D7 | MASTVRPSFSLGNETLKVPLALFALNRQRLCERLRKNGAVQAGSAVVLQGGEEMQRYCTDTSIIFRQESFFHWAFGVIESGCYGVIDVDTGKSTLFVPRLPASYATWMGKIHSKEHFKEKYAVDDVQYADEIASVLTSRNPSVLLTLRGVNTDSGNVCREASFEGISKFTVNNTILHPEIVECRVFKTDMELEVLRYTNRISSEAHREVMKAVKVGMKEYEMESLFQHYCYSKGGMRHTSYTCICCSGENAAVLHYGHAGAPNDRTIKDGDICLFDMGGEYYCFASDITCSFPANGKFTDDQKAIYEAVLRSCRTVMSTM... | Cofactor: Binds 2 manganese ions per subunit.
Function: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro,... |
Q9VYH3 | MASARNLLLLSSSRLHGHGYLEHARGQLEDLFKSANVKTVLFVPYALRDHDKYTATVRDALQPWGFNVEGLHTKPDREQALREAQAIFVGGGNTFVLLRSLYEMKLLDPIRELVLQRGLPYVGSSAGTNVATRSIHTTNDMPVAYPPSFEALALVPFNINPHYLDPEAGSRHKGETRDERLEEFVAYHGLPVLGLREGTSVRVQGEKAILLGDRNAKLFKADGGTEELAPLADLTFLLQK | Function: Hydrolyzes dipeptides containing N-terminal aspartate residues.
Catalytic Activity: Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Sequence Mass (Da): 26598
Sequence Length: 240
Subcellular L... |
Q835J5 | MYENLLPRFLRYVKTETRSDATSTTTPSTQTQVAFAQTLKKELEELGMSDVIYNETNGFVIATLPSNVEKDVRSIGFIAHMDTADFNAVNVSPQIVENYDGESTIPLDKEGKFTLNTKDFPNLKNYRGETLITTDGTTLLGADDKSGIAEIMTAMEYLINHPEIKHGTIRVAFGPDEEIGVGADKFDVAQFNVDFAYTMDGGPVGELQFETFNAAQAEITIQGKNVHPGTAKNTMINALQLGIDFHNALPADEVPEKTAGEEGFYHLAAFAGTPEEATMTYIIRDHNREIFEARKAKIKEIQQTLNAPFDEERIKVDLFD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Cleaves the N-terminal amino acid of tripeptides.
Catalytic Activity: Release of the N-terminal residue from a tripeptide.
Sequence Mass (Da): 45400
Sequence Length: 409
Subcellular Location: Cytoplasm
EC: 3.4.11.4
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P86063 | NYPTQDSTMDKTFANNL | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P86007 | VVSCADILTLAAR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
P85434 | ELVTLSGAHTIGQAR | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might ... |
P86066 | GQNFTSDKDLYTDSR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P80679 | QLNATFYSGTCPNASAIVRSTIQQAFQSDTRIGASLIRLHFHDCFVDGCDASILLDDSGSIQSEKNAGPNANSARGFNVVDNIKTALENTCPGVVSCSDILALASEASVSLTGGPSWTVLLGRRDSLTANLAGANSAIPSPFEGLSNITSKFSAVGLNTNDLVALSGAHTFGRARCGVFNNRLFNFSGTNGPDPTLNSTLLSSLQQLCPQNGSASTITNLDLSTPDAFDNNYFANLQSNNGLLQSDQELFSTLGSATIAVVTSFASNQTLFFQAFAQSMINMGNISPLTGSNGEIRLDCKKVDGS | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P84752 | VNQIGSVTESIEAVKAALVSHGAGVAVVGRKINLAGGPSYTVELGRFDGLVSRALYGLSKLPELGTHGLTLICISWALRVMSNVHDFFVHVAAKVESIHQYIESMRYGSLSPTIFDNYSKDCMIAHGAAHFLKXRPPDPAETRGGAVADNGSGAVARMPTLEEYGTNLTKLAEEGKANFDAAMVKLKNFSFILMFGVLGTIISFCLISSGAVLLLKHHVFPDSNINPSSGAAITSGVRGDLRAYVVAYLDPSRTSFTVDNAIYGEIRRTVLAWLIDSGTLQLSEKVLALVLTMVAATVLGVAKSMIKMGQIEVLTGTQGE... | PTM: Partially N-glycosylated.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 38444
Sequence Length: 361
Subcellular Location: Secreted
EC: 1.11.1.7
|
O04795 | MASFMKQLSLVLSFIALALAGCAVYQNTQTAMKDQLKVTPTWLDNTLKSTNLLSLGLGKPSGGKLGDEACVFSAVKEVVVAAINAEARMGASLIRLFFHDCFVDGCDAGLLLNDTATFTGEQTAAGNNNSVRGFAVIEQAKQNVKTQMPDMSVSCADILSIAARDSFEKFSGSTYTVTLGRKDARTANFTGANTQLVGPNENLTSQLTKFAAKGFNGTEMVALLGSHTIGFARCPLLCISTFINPARVSTLNCNCSGTVNATGLVGLDPTPTTWDQRYFSDVVNDQGLLFSDNELLKGNTTNAAVRRYRDAMGAFLTDFA... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P84753 | VEMACPGKVSCLGDKAITVLSENNPLTGTKGEIRMGDGFNVEEEIEKVLEQVGKTTFDVALYASGSWKKPQPLAVMVATLAVMQVRDVVWLSALAMACRLLMDTFAEKYFLQPVLQPSYELFKNAGSNMDGTVTSFDNIYYKTNSWASPLSIRGGYPMHSTSNMGSQIYQDNPVANCLDLSSLDLANR | PTM: Partially N-glycosylated.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 20592
Sequence Length: 188
Subcellular Location: Secreted
EC: 1.11.1.7
|
Q7DBF7 | MNLYGIFGAGSYGRETIPILNQQIKQECGSDYALVFVDDVLAGKKVNGFEVLSTNCFLKAPYLKKYFNVAIANDKIRQRVSESILLHGVEPITIKHPNSVVYDHTMIGSGAIISPFVTISTNTHIGRFFHANIYSYVAHDCQIGDYVTFAPGAKCNGYVVIEDNAYIGSGAVIKQGVPNRPLIIGAGAIIGMGAVVTKSVPAGITVCGNPAREMKRSPTSI | Function: Catalyzes the transfer of an acetyl residue from acetyl-CoA onto GDP-perosamine to form GDP-N-acetyl-perosamine.
Catalytic Activity: acetyl-CoA + GDP-alpha-D-perosamine = CoA + GDP-N-acetyl-alpha-D-perosamine + H(+)
Sequence Mass (Da): 23742
Sequence Length: 221
Pathway: Bacterial outer membrane biogenesis; L... |
P14650 | MRTLGAMAVMLVVMGTAIFLPFLLRSRDILGGKTMTSHVISVVETSQLLVDNAVYNTMKRNLKKRGVLSPAQLLSFSKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILATIANLSGCLPFMLPPRCPDTCLANKYRPITGVCNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSRTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDAST... | Cofactor: Binds 1 Ca(2+) ion per heterodimer.
Function: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).
Catalytic Activity: 2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O
PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. He... |
P16147 | EPGPSSDLTTLTTKFAAKGLTPSDLTVLSGGHTIGQSECQFFKTRIYNDTNIDTNFATSRQANCPFSAGGETNLAPLDSLTPNRFDNNYYKDLVSNRGLLHSDQVLFNGGSQDTLVRTYSTNNVKFFSDFAAAIVKMSKISPLTGIAGEIRKNCRVIN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
Q02200 | MNTPTQSFRAKAAIFSLLLLSCMQCHAQLSATFYDNTCPNALNTIRTSVRQAISSERRMAASLIRLHFHDCFVQGCDASILLDETPSIESEKTALPNLGSARGFGIIEDAKREVEKICPGVVSCADILTVAARDASAAVGGPSWTVKLGRRDSTTASKTLAETDLPGPFDPLNRLISSFASKGLSTRDMVALSGAHTIGQAQCFLFRDRIYSNGTDIDAGFASTRRRQCPQEGENGNLAPLDLVTPNQFDNNYFKNLIQKKGLLQSDQVLFNGGSTDNIVSEYSNSARAFSSDFAAAMIKMGDISPLSGQNGIIRKVCGS... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
P15984 | ALRGFGVIDSIKTQIEAICNQTVSCADILTVAARDSVVALGGPSWTVPLGRRDSIDANEAEANSDLPGFNSSRSELEAAF | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
Q17062 | MNNMDGSENNAKVSDSAYSNSCSNSQSRRSHSSKSTHSGSNSSGSSGYGGQPSTSSSSNDLSDQKKEKELKKKKQVETLMPDTQIEVECRPEEDVINIPSEEGGAADDVLVPSPKQTLQTDNDIADIEVAIPDTNNDKEEAIVYNTSLINPGTACPFGRPALSNCNGFSCVISMHDGVVLYATASLTSTLGFPKDMWVGRSFIDFVHPRDRNTFASQITNELAIPKIVSLTEETDQTMENPGSTMVCRIRRYRGLSCGFSVKNTTTAYLPFLLKFKFKNVNEDKGNVIYLVIQAVPFFSAFKTSNEVLAKTVSFVIRHSA... | Function: Involved in the generation of biological rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the tim-per complex. Light induces the degradation of tim, which promotes elimination of per. Nuclear activity of the heterodimer coordinatively regulates per and tim transcript... |
P28314 | MKLSLLSTFAAVIIGALALPQGPGGGGSVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDAIGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTVEALRAVGINHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGNTVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVFDTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACRWQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAV... | Cofactor: Binds 2 calcium ions per subunit.
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 37640
Sequence Length: 363
Subcellular Location: Secreted
EC: 1.11.1.7
|
P84714 | VVSCADITALAARQGLFTSDQDLYTDSRMGQLNVLTGTQGEIR | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
B0BYQ1 | MVEPLLAGIVLGLVPVTLAGLFVAAWQQYKRGEEVG | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Location Topology: Single-pass membran... |
Q85FK3 | MVEALLSGIVLGLIPITLAGLFVTAYLQYRRGDQLDIR | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Location Topology: Single-pass membran... |
B0YPP7 | MVEALLSGIVPGLIPITLAGSFVIAYLQYRRGDQLDL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Location Topology: Single-pass membran... |
A6MM54 | MPTITSYFGFLLAASTITPALFIGLSKIRLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
Q8M9Y3 | MISILTYFGILFGILTITVIIFVALNKIQLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
Q1ACI4 | MFTVISYLSLLFISFLFALTLFIVLNKIELI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
Q19V67 | MFTAISYLGILVGALLFVTITFLTLRTIQLL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
P50369 | MIFDFNYIHIFMLTITSYVGLLIGALVFTLGIYLGLLKVVKLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
P56306 | MVTIFSYIALLLSALVITLTCYIGLLKIKLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
A7M915 | MPTITSYFCLLLAALTLTLALFIGLSKRQLI | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6... |
P0C1D4 | MLAEGEPAIVQIGWAATCVMFSFSLSLVVWGRSGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3727
Sequence Length: 35
Subcellular Location: Plastid
|
Q4VZP0 | MDMVSLAWAALMVVFTFSLSLVVWGRSGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3188
Sequence Length: 29
Subcellular Location: Plastid
|
A7M8Z4 | MNIDIVSMAWAALMVVFTFSLSLVIWGRSGL | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3429
Sequence Length: 31
Subcellular Location: Plastid m... |
Q9TLR6 | MNISLVDLTWACLMVSFTVSLALVVWARNGF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3458
Sequence Length: 31
Subcellular Location: Plastid
|
O94516 | MKPLAYYEDQLLKDEKSFLKVTEIERLLSYAAYLLPAEFRDDQLKSQTITSILLLLHQFHTGLLFRKIAELPKTEQAILKSERTQYLEYFRKKNPSFEKVSELLYFLNISTFPIELVISKYNPSRQYDSVLFLESVKFLLRVHIMWTTGGDLPLSNPVLQRDFNVKTFIHLHKKYSNSGSAVVLKNSKKVVPRLNTVNSSLDFLQNRTPRLSSILPDEIFTKRLPNLRIFSNFIKVCRPLIYMLFMWHWKRKQKSSSLKVRPWGPWIVAFVFEVISQLIDRRCESATSSRQGFGLERRTNQSQFQHFVVWAFTQGRFYDE... | Function: Involved in the biogenesis of peroxisomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43105
Sequence Length: 364
Subcellular Location: Peroxisome membrane
|
P87200 | MNKYLVPPPQANRTVTNLDLLINNLRGSSTPGAAEVDTRDILQRIVFILPTIKNPLNLDLVIKEIINSPRLLPPLIDLHDYQQLTDAFRATIKRKALVTDPTISFEAWLETCFQVITRFAGPGWKKLPLLAGLILADYDISADGPTLERKPGFPSKLKHLLKREFVTTFDQCLSIDTRNRSDATKWVPVLACISIAQVYSLLGDVAINYRRFLQVGLDLIFSNYGLEMGTALARLHAESGGDATTAGGLIGKKLKEPVVALLNTFAHIASSCIVHVDIDYIDRIQNKIILVCENQAETWRILTIESPTVMHHQESVQYLK... | Function: Involved in peroxisome biosynthesis. Required for the import of a subset of matrix proteins into peroxisomes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75532
Sequence Length: 671
Subcellular Location: Peroxisome membrane
|
P40155 | MTSINSFPRNIDWPSNIGIKKIEGTNPTVNAIKGLLYNGGSIYAFLYFVIAMFVEPTLQKQYQQRNDFSLFVLLRLRRIIAQLQKRLVMTPVSSLGFNEQNNFVERSTQTSDDNIIREDNSHWAEMIYQLQNMKQELQYFNRSSGQPSESIDDFVFQIKMVTDQVELTDRSRAFSNKSRNIIQGIREIKGWFVNGQVPR | Function: Component of the peroxisomal translocation machinery with PEX13 and PEX14. Interacts indirectly with the PTS1 receptor (PAS10/PEX5) and directly binds to PEX14. Required for import of both PTS1 and PTS2 proteins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23169
Sequence Length: 199
Sub... |
P38855 | MNSNRCQTNEVNKFISSTEKGPFTGRDNTLSFNKIGSRLNSPPILKDKIELKFLQHSEDLNQSRSYVNIRPRTLEDQSYKFEAPNLNDNETSWAKDFRYNFPKNVEPPIENQIANLNINNGLRTSQTDFPLGFYSQKNFNIASFPVVDHQIFKTTGLEHPINSHIDSLINAEFSELEASSLEEDVHTEEENSGTSLEDEETAMKGLASDIIEFCDNNSANKDVKERLNSSKFMGLMGSISDGSIVLKKDNGTERNLQKHVGFCFQNSGNWAGLEFHDVEDRIA | Function: Involved in peroxisome biogenesis and the import of peroxisomal matrix proteins that contain the peroxisomal targeting sequence PTS2 . Required for peroxisomal targeting of PEX7 and growth on oleate .
PTM: Ubiquitinated in a UBC4/UBC5 dependent manner.
Location Topology: Peripheral membrane protein
Sequence M... |
Q3SZD1 | MAAAEGDGGVRAEADRELEELLESALDDFDKAKPSPAPPPTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDATSQQEFTSCLKETLSGLAKNATDLQNSGMSEEELTKAMEGLGMDEGDGEGTILPIMQSIMQNLLSRDVLYPSLKEITEKYPEWLRAHRDSLPPEQFEKYQEQHSVMGKICEQFEAETPTDSEATQKARFEVVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGANGEQCLIM | Function: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome me... |
P40855 | MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM | Function: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome me... |
Q8VCI5 | MAAAEEGCGVGVEDDRELEELLESALDDFDKAKPSPEHAPTISAPDASGPQKRAPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDASSQQEFTSCLKETLSGLAKNATELQNSGMSEEELMKAMEGLGMDEGDGEASILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHQDSTPPEQFEKYQQQHSVMVKICEQFEAETPTDSEATQRARFEAMLDLMQQLQALGHPPKELAGEMPPGLNFDLDALNLSGPPGANGEQCLIM | Function: Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome me... |
Q07418 | MNENEYDNFDDLDDLLDEDPTKLDEAEPDDVQAKGSVYNDSENKEKNAESKDSDGVQVANESEEDPELKEMMVDLQNEFANLMKNNGNENNVKTEDFNKLISALEEAAKVPHQQMEQGCSSLKSNSTDKGTVNGSNPGFKNIVSNTLDRLKENGNKVDTSLAEETKESQRSGQNNNIDDILSQLLDQMVASGGKESAENQFDLKDGEMDDAITKILDQMTSKEVLYEPMKEMRSEFGVWFQENGENEEHKEKIGTYKRQFNIVDEIVNIYELKDYDELKHKDRVTELLDELEQLGDSPIRSANSPLKHGNEEEELMKMLE... | Function: Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maint... |
Q8EVH2 | MKKIAILTSGGDASTMNKCLSTFITYASKYNCEVVFVKNGYKGIYDNEFVKPDYTETKSWWSLPGTKIYSSRFPEILDEQVRKQMVDNLHKNSIDTLVVIGGDGSYKGARLLSKSGIKVIGLPGTIDNDIASTSYSIGFDTSLNAIVNSIKEIKSCMDSHANVAMIEIMGRHCIDLTVFAGIATEADIIITPESFYTPQQLLAKINEKRKTNSRGIIILYVELLLGTENIPTVEEYIKYIQANSKESVKKNILGYLQRGGNPTAMDMIRASLMTEHALKMISENQYNKIIGVDEFKVVSYDLETAINMKNPSRKDLIDKF... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35983
Sequence Length: 322
Pathway: Carbohydrate degra... |
Q601D3 | MSKKIGILTSGGDAPGMNSAISFLAKSALSLGFEPYLIFDGYSGIIARKILPAKNFPYNGISSFGGTAIGSSRFPEFKKEEVQNKAVEILSEIGISSLVVVGGDGTYNGGYKLHLKGIKVIALPGTIDNDIQFTDYTIGFDTALNTIVETIDKLRDTANSHRRCFVVEVMGRHCQDLALYSAIATGSEILITNTNILTPEEVSQRVLEQFAKGKPSVIVTITENILPNLKEFAAKIEELTKISTRSLEVGHTQRGGRPSAFDRILAAKMAMKAMELINQDKSGLAISYLDGKIQTFDIAKVVSKPVRKTNDLVLEINKIN... | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34961
Sequence Length: 322
Pathway: Carbohydrate degra... |
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