ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A368NPV3 | MTSISELLLEAAGIMAVGMIFVFLFLSLLVVGVKLLARFAGGPEPLTANATPPPQTTGVSPDVVAAISAAVHKYRNTTKD | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8298
Location Topology: Single-pass membrane protein
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A0A1F3D7E1 | MKTGKGSAIKLGVTGGIGSGKTSVCRVFSVLGIPVFSADTVAREVMDIDTGIILRINTIVGKNLYSDGSLDRNELAKLIFNNKKLLEKVNSLVHPVVFSRFREWEKKQLTPYVIMEAAILFESGGSEVVDRIITVVAPIEERVGRVIHRSDLTREQVMERMRNQMSDSDRIKHSDYVIQNSENDMIIPSVLRIHEDILKMVNSRV | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
K1X9I7 | MFSTLSNPRQGALQLLNFALVLSTAFMMWKGLSVISDSPSPIVVVLSGSMEPAFQRGDLLILWNRNWLEPETGVGEIVVYNVKGKDIPIVHRVVRKFGTGEHAKLLTKGDNNDADDTELYARGQDYLERKDIIGSVVAYIPFVGYVTIMLSEHPWLKTVMLGIMGLVVKYNEQSQTDIREIVVTGRKKQVLQSIQALSRSRSLSAPASALAERAMIDPLSLCLANMPHISKPVQRYIYPSRLDSSPHSLSFLFIFPSAIPSRLIPSHPTFNSAAISLVSSHIKPSHGPTLHLTSSHLSSLPPLPTPKRPQHRPRYPSPSP... | Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-hel... |
A0A914DU86 | MERKPLLSSSQLTPSSIPSNAPGSSLSTARAIGSDRRTTGETSDDDMVRLCNEQYGSVSGEDYAAVVAEAIRAINNGIFPERIAQGSSGSYFVKNLRGEKIGVFKPKNEEPYGQLNPKWIKWLHKLFFPCCFGRSCLVPNQVGFNCIDKSDVHKVSTIKYPSSLNFTIF | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
EC: 2.7.1.67
Subcellular Location: Membrane
Sequence Length: 169
Sequence Mass (Da): 18615
Location Topology: Peripheral membrane protein
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A0A564W9I5 | MTDALAPIDSEEFAALMRAVGPFEPAPRLAVGVSGGPDSLALALLAADWVRARHGSLSALIVDHGLRPEAGDEARLTRAWLHARGIQGEILRWEGAKPTSGIPAHARDARYRLLLERCRRMGIVHLLLGHHAFDQTETVLMRLFGGSGIEGLAGILPIRYTPLTRMVRPLLPIDPARLRATLTARGQAWLEDPTNADQAYTRARFRRALSAFPEAMGIRDELARLRASAVQATEGLDAAIDDGFARCCEIDRLGFAWVDEDALATVPEEVAWRLLARVLCGIGGTTWPAATSSVRALRGRILSRAGRPSGSLGRCRLLRR... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A7X5SAN1 | VVVSACEQSGRARIPTVAAPHGLQDAAQASDPQALRLTLDPHGAHRLGSLVLDAQPHVIVAIGPEGGWSPRDRATLADTGFSGLQLGPRILRTETAGLAAIAALQSRFGDL | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A191ZE06 | MIHPTAIISPEAKLDPSVVVGPYVVVEGAVEIGAGTKIDSHSILKGPCRIGRDNHVFSHVIIGEIPQDLKFRGEESSVEIGDRNQIREFSTIHRGTQGGGGVTRIGSDNLVMAYAHIAHDCTLGEHVILANAASLAGHVSVGDFAILGGFAVAHQFCRIGAHAFIGGFSKLSKDVPPFVMADGARARSVGLNKEGLKRRNFSSETINLLSRAFRQLVKKQGDEKVWAEFDEAAKGDAALAQMLAFIRMSERGITR | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 1/6.
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the ... |
A0A2S0KL73 | MKRKILHVDMNNFYASVELLDKPELRDKPVIVGGDESSRHGIVLAKNEIAKRYGIKTAETLYQARKKCPNLVVLPSHHDLYREYSRKAKAIYLEYSDRVQSFGPDEAWIDVSHRPESGLEIAKTIQNRILKELGLTVSVGVSWNKTFAKMGSDYKKPFAITVIDENNYQEILWPLPVETFLFVGSKTAERLKTIGIDTIGELAKVDPVYISKYLGKNGMSLVKNARGEDEDPVLSQDEQGPAKSIGAMRTTSKDLSSLEEISKLFSILAEEVEARLAAENMRTRTLRIYVRDNKFNNYTRQKALERAISTKTELTKAALD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A1Q2SPY7 | MSTPIWLLVGLGNPGSQYAQSRHNVGFWWVENLARELGARFKPEAKFFGDYARMSWCGHDILLLKPTTFMNHSGQAVLALLSYYQIPPQQLCIIHDDLDLPSGVARLKREGGHGGHNGLRDIINRLGLKHFLRLRLGIGHPGNGQDVVGYVLSRPSVADQLAIEVAITAGIKILPEVLAGEVEKAMHRLHSAV | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 193
Sequence Mass (Da): 21270
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A0A9D9YJK4 | MKYLGIDYGSKKVGFAQSDDEGRLAFPLMISPNDDALLGDTVELIRAMKITDVVIGESVDGHGKLNPIAKEARKFGLSLEQVVDVRIAFEKEWYSTVEARKQPGKEGSHEVDDQAAAIVLQRHLDKINGPGVASEETYEEGDDSDSTPDSW | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 151
Sequence Mass (Da): 16566
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A0A1J4XCC3 | MMIGITGNIGSGKSTAAQLFAKYGFVIIDSDNIVHDLLRHDPEVIKAVKSHFSAAILNSEMNIDRKKLGDIVFNNEEDLKFLEQLLHPKVRAHWLELAKQSPQQKYIVEVPLLFEKGYEADFDKTICVIADEESTHSRLSKRGLSVSEMNLRLSKFLSIDEKMKRADIVLFNNSTLDILKEQVDLCVNHIINK | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A2G6CFN0 | MSTRRLRPSKKKSCRSDLRSRQGRDVFKRKAKDAPAQVSADTGTDGGADGAVEDGPRHVAIIMDGNGRWAQARGRPRLFGHHAGAKRVREIVEACPDYGVKYLTIFAFSTENWKRTQTEVAGLMSLFRRYIRREAEDLKAENVRVRFIGDRFKLDAELRKLMDELEALTAECDRVHLTIAMNYGGRDEVGRAIRRMAEDVAAGKLRPEDVGEDTLPHYLDTHVLPDPDLVIRTSGEARISNFLLWQSAYAEYEFIDTLWPDFTREIFGEVLQRYGARDRRFGGVKP | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 286
Sequence Mass (Da): 32573
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A0A914CZ19 | MILVSLESLNLQLFIDTQIIGIGCKDFNTDIRVSQEANKYQDILLFDYTESYYNVSRKIFGYLRYVYDYCPNVKCVLKGDSDAIINLSGMEKLCEVLPDQQHLMTGRIVHFEPDRIPWAKHYVPFFVWPDNYPPFTLGFSYLLSDRRITVAYLKI | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 155
Sequence Mass (Da): 18182
Location Topology: Single-pass type II membrane protein
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A0A914EDF7 | MRWRNIIFKWRPLLLIVAVIYTILIIPSWFSSSLDETKDEPRLAQGVNPKLKLGRKSSNNSKLTIDHSAELMKIKPETEAPKKLINVKPDLKPSAQLETNNEQPEMVVASEKFVFKLNYRGQSLAIEEVLTHPDMPKLKERVTFSPDLAKSNRTKILIWDSGFGQQNLGGCPEWNCEVISGAGNLASADVVVIQSPSFTIKKEPHQLFVYYSQESPRNSASLGQGPPGYFNTMFGFRHDTVGGSPYGYTVKLAPESRRTGEIVDKKLVMGKSKGATWFVSHCSTQSHREEYVRELQKYFQVDIYGQCGTMRCAKGDNCEN... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 490
Sequence Mass (Da): 55918
Location Topology: Single-pass type II membrane protein
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A0A914DYU8 | MSNKLVLYSCWTSSCSFRARIALALKNLDYELKCINLQKGEQKRQEYLAINPNGMVPTLIHNGKVFSDSMAIIEYLDEKFPQPYKFLPEDSESRAIVRALSYSITTNVQPLHCLRVRNYHGQGNKQKADEWARYWIQIGNEAIERTLEKTAGKYAYGNSLTMADICIPPHVFNARDKFGIDMSSYPTISRLDKNLSGMQEIQGAHPTKQPDCNQ | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Length: 214
Sequence Mass (Da): 24429
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A0A3N4Z6U7 | MTGALQPWHWIVLIAVILLLFGSTRLPGLAKSVGQSMKIFKREINELRSDGDDDTKQDTATTDDTKKNETTATNGGVSKGDDAPKA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 86
Sequenc... |
A0A914E239 | MYHGMAYLMSGYSIVTRMLKILKEKTPFFISENYRRFMENVIFAGDVRVAAGIRIQDIGGYNCCGRQMRFWCDDLSKYVKVPITFENYNMSVEEGWNLMQKWIDTDTCEAISSQYQSLLPVILIWTKYYGNNFTVAQRLPSCPYQCIYTNDQNFRDHANAVVFHIRDLNVQHLPEPQLDSYKVFFNMESPPHTHLHFNELPSDYFNLSMTYRVDSDVYCPYGSMNSITIKTKENNVFTDEEVDSLISKKRLPILYLVSNCKSRSGREWYAEKLKNFINITQLGKCNNKSCDQNCEHEQIEQHYFYLAFENSICNDYVTEK... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 438
Sequence Mass (Da): 51819
Location Topology: Single-pass type II membrane protein
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A0A659SDZ3 | MKQTWRWYGPNDPVTLSDVRQAGATGVVTALHHIPNGEIWSVDEIQKRKAIVEEAGLEWSVVESVPIHEDIKTHTGQYDLWIKNYQQTLRNLAQCGIYTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFELHILKRPGAEADYTAEEIAQAERRFATMSEEDKARLTRNIIAGLPGAEDGLSRLHLSEPTGRR | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 200
Sequence Mass (Da): 22783
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A0A8T3VR48 | MVDGKTMILGVIGDPIEHTFSPAMQNAGLDALNLNYIYLPFHVKPNGLKECIEGAKAMGIQGLNVTIPHKTNVMKHLDEIDQVASMIGAVNTIQFIFDENNESSNQNNEINVTTKGFNTDGYGCLRAINEKTSINKKKVTITGAGGAARAVAFQIASSGIDELSILNRNFTKAESLANDLRSNLSNAGIDISINSCEMDYLKKELDSSDIFIDTTPIGMYPNVNDKPIASADMLHEGLVVNDIVYTPMETSLIKEAKKANAQVVYGYEMLLYQGIRSFEIWLGRDAPADVMEKALLDVLGI | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A3N1HLD9 | MTAAEVGGAGAAGGPLRLGTRRSPLARAQSEMVAERLRATSGRAVVLVEVTTQGDVDRAPLRQIGGTGVFVAALREALLEGRVDLAVHSFKDLPTAPAPGLVLAAVPPREDPRDVLVGAGGAGLGDLPVGARVGTGSPRRAAQLRALGLGLDVVDVRGNVDTRVGFVTSGRLDAVVLASAGLRRLGRHDEVTDVLDVDQVLPAPAQGALALECRADDDATAQACAALDDPAARAATTAERALLAALEAGCSAPVGALARPAAGEGGGLLELVAVVAATDGSRVLRRSVRGDEAEAAELGRRLAAELLADGAADLVADGAP... | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 442
Sequence Mass (Da): 43315
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A0A920GPM6 | MNGNLMSDLRKVIIDETELEVDGSMTLIQACEEAGIEIPRFCYHERLSIAGNCRMCLVEIVGGPPKPAASCAMQVRDLRPGPEGQPPVVKTSSPMVKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAMAYGVDFSRFREAKRASDDLDLGPLVETHMTRCISCTRCVRFTTEVAGASQMGQTGRGEDSEITSYLGETLESNLQGNIIDLCPVGALTSKPYSFTARPWELTKTETIDVMDALGCNIRVDTKGREVMRIMPRNHDGINEEWISDKSRFVWDGLRRQRLDTPYIREKGKLRAATWSETLAKAKTEIKNKK... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic ... |
A0A963TDZ8 | SRANINCSIDESLERFEPIISAANVRKVKVRGYISCVTDCPYDGVVAPDKVAWVAARLRDMGCYEISLGDTVGVGTPQRARDMVDTVATKVPIDRLAAHFHDTYGQALANLLAVLELGVSVIDSSVAGLGGCPYAKGAAGNVATEDVLYMLHGLGIETGVDLKAVAAAGWEICGHLGRAPVSKVSLALGAGEDDGNGAGA | Pathway: Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1.
EC: 4.1.3.4
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA
Sequence Length: 200
Sequence Mass (Da): 20654
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E6YI67 | MADTFFFTPSRRLTVADVVKLTGAKLLNPEFSNTVINTLSSVESAGEGSLVFIENRKFSDALLGSSAVAVFCTSDIVFKVPESIAILVTSTPQRDFAQVGRILFPTSVKPTPWFGQREISPHAHIHSSAKLEDDVCVEAGAVIGRNVEIGSGTLISSTAVIGENCRIGRDCYIAPKVTVQYSLIGDRVYIYPGVCIGQDGFGYVRSAICVEKIPHLGRVIIQDGVEIGANTTIDRGTFDDTIIGEGSKIDNLVQIAHNVKIGRYCLIAAQCGIAGSTSVGDMSQLGGSVGIADHITIGEGVQIAAGSGVMNDIPDGEKWG... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.... |
A0A2H6EWC3 | MTKSKKKMFDFEAGEILLIAKPIGWTSFDVVNKLKKALKIKKVGHTGTLDPFAAGLLIVLTGRKTKESAAFQQLPKTYRGILELGKTTDTLDIEGKTTETKPVPDLTKEHVEKVLKSFMGESLQVPPVYSALKIRGERAYKLARRNKPVHLEPRKIEIYAIQLLDFLGDKIYFQVNCSKGTYIRSLGRDIAERLETVGYIKALVRTQIGQYSLDDAVDVNEFIDSVGQKDH | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 231
Sequence Mass (Da): 25983
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K4IN05 | MALISLKGVTKIYPRGSRPALDNISLDVNRGDFVFLVGASGSGKTTLLRLLLREEEATEGEIRVAGNDLRRLRNREIPGYRRSIGFVFQDYKLLNNKTVWQNVAFTLEVIGARRSTIKTLVPQVLKTVGLTGKEHNYPHELSGGEAQRVALARAYVNNPEILLADEPTGNLDPTTSLGIMEVLDAINRTGTTVVMATHNEEIVNSMRKRVVELHTGRIVRDEVHGSYDSSRFFPDAEVAARSHHAIGDPDDGDALDRVREAGVGGRRPVQVVVQEGNSLATEPIADGAKGARQVVQAAAEAVNQGQYGDEGIARLAKSMH... | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 601
Sequence Mass (Da): 65093
Location Topology: Peripheral membrane protein
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A0A3C2D343 | MQKKLSFFLSAISGILLSLPWIFPGQSWTLFFAFCPLLFAEDQLARQKDGRISQLYLPAFLTFLIWNLLSTWWIAHVSLVGMLLITELNATVMASVWWSSQLVSRKLGLASSTFSLIVFWLAFEFVQHNWAIPWPWLTLGNGFANSVEIVQWYEFTGILGGSLWILLSNFLVYSTIKNFIQRSSFLKSIKFAGLALLVVIIPLFGSLYLYANYTEKGKLLEVLILQPNIDPYKEKFSGMSSEEQINRLLALAESNLTGSVKLVVAPETAWPPLWEDSIFTQNQSLIPLSEIIQSYPEVNFIVGAITQRKFGDERVISETA... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A2D9YF74 | MYNRNFMRIAINLAKKNIGNTGINPSVACLIEKDNHIIGIGLTGESGRPHAEYNAMSKCKDQIKGSTVYVTMEPCSHEGATPSCARILAEAGVAKVVSPIMDPNPVVNGKGFEILKNSGVEVFIDKEHNEKAKRIIEGFSKKILTGKPFVTLKLASSLDGKIALNSGKSKWISGVESRRKTQLLRYRNDAIMVGSKTFIEDNPELSIRENFGRNNQPIRVLLSSDCKILPKGKIFDTLKSQKTIIFTGYKGKKNWSDWEKAGANLIQVKSTKNSLDLHAVLYQLGSMGISNLLVEGGANLSASLLNENLLDRIIIFYSGR... | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino... |
A0A7X5N2D9 | MERADAAVALSRQVEKKRTTLRGRTQINLFFEPSTRTQSSFELAGKRLGADVMNMSVASSSVKKGETLIDTAATLNAMRPDIIVVRHESAGAVHLLARKVDCAVVNAGDGAHEHPTQALLDALTIRRNKGRIEGLQVAICGDVLHSRVARSNIILLQAMGARVRLIAPSTLLPSGIERFGVEVFTDMRKGLAGCDIVMMLRLQRERMNGSFVPSVKEYFRYFGLDAEKLALAKPDALVMHPGPMNRGV | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 248
Sequence Mass (Da): 27074
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H8MPR6 | MNTLTVFRLGRVEYEDGLKLMHLFGEARLQERIGDALLLLEHPPVLTLGRAAKRENITATDARLSEEGVEVFDTNRGGDVTYHGPGQVVGYPILLLPPERRDVRRYVRDVERGLIQTLAAFGLTAGAIPKWPGVWLGQEGSPDARKIGAIGVHLSRWLTTHGFALNVNTNLEHFQLIVPCGIREAGVTSMQRELGHPVSVPDVEEVLAREFTQVFDAQRVDGTVDLRTVSVAVMHGRGLEARVLLLRRTPERGGFWQTVTGRLEPGESPVEAARREVAEETGLQLPVVDLAYRHAFALGDALPPKLVEEHGFTVHAAPDT... | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
H8MTT4 | MKKTPLVTEISKEFTFEAAHRLPNVPEGHKCSRVHGHSYRIEITLRGPVHPQFGWIVDFAELNAAWQPLHAQLDHRLLNDVPGLENPTSELLAAWLFERVNVPGTTVARIRVAETCTSSCTVYAQEG | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 127
Sequence Mass (Da): 14253
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A0A2M8D1E9 | MYSVKVETRFSSSHHLTGYEGNCSRLHGHNWRVVVEVAGSKLNEIGMLVDFTQLKGKLDEIARELDHIVLNDHPYFQSSGLNPTAENLASFFYSSLQGNFGDNRVLRVEVYETEDSVAAYVPD | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 123
Sequence Mass (Da): 13866
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A0A8C4SCB7 | YQSLHQKCTLLVEYLCYKGSTFHRVVKNFMIQGGDFTEGNGRGGESIYGGYFEDENFVLKHDRAFLLSMANRGKDTNGSQFFIILLSYSVHVVFGLIISGFEVIKQIENLKTDAASRPYADVRVIDCGQLITKSANDGKYCSL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 143
Sequence Mass (Da): 16039
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A0A0C3AK39 | MSGIVLSINAGSSSLKVSLFAPTFDGPKHLATCNVSSIGAEGTSFSSTSKAVSEEEKGMNNVQDHDSALQHILRHLFRTTTSQEDITHVCHRVVHGGEYKEHIKIDTDALHHLEALTELAPLHNASAVALIRSCLKQLPNTMSIAWFDTTFHQSIPSHIYTFPIDQELAKKYGLRKYGFHGISYSFIVRNVAEFLKKPTFTTNLIILHLGSGASACCVKNGQSLDTSMSLTPLAGLPGATRSGSIDPNAILHLMKKSQTSIYDAETVLNKKSGWKSLTQTSSFGDIVESDEASKRLAFDIFVDRILDFVGAYYVKLGGQV... | Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
EC: 2.7.2.1
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Length: 403
Sequence Mass (Da): 44163
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A0A8C4XH73 | MPRRKRCRLMVCRLRCVVLTAPLALFVMLVTLLDPLSTKYEENKHEFYEHVSPRFVDLEEILQDEVQMDKDGLSSWSSFREDQLLVVHSDGKLSTHDGKRGNYKMLKTTVQKKVDSWVLTLGKTTSPMHVTVNELGAESPARMLRVREVPNELLSLRRKLPDLRHTLCPVNHDISKLPTTSIIICFHNEALSTLLRTVYSILETVPKSLLQEVILVDDLSQQAYLKTTLSEYISRLERVKLIRSNKRVGVIGGRLLGAARASGDVLVFMDSHCECPRGWLEPLLTQIADDRHRVVAPVLDVIDLKSFQYLQMIDQQRGVI... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 621
Sequence Mass (Da): 71015
Location Topology: Single-pass type II membrane protein
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A0A8C4RHU2 | LLPNIILINCLHSPHNLKCSLLTSERQQTRAPEYTVLGLSDKILLFRHHLDSENILHRLMGNDIIQDGDLIEVILSASLHLRPHILAVHSYRTPTFCHHCGEMLWGLVRQGLKCEGCGLDFHKRCAFRIPNDCSQAKRRCGSSISLFPMSLNQSTMLKSNMSLKQPSWTGHTIWVDHRRQVSIEVPHTFQIHTYKRPTVCQFCHRLLKGLFRQGLQCRDCKFNCHRRCQQRVPNNCVGEKSSSNDQASDRSQFQTAMLQTNGTTPAIPQNHMAPCPCFSNNIPLMRIVQSVRQTKRKSSTVIKESWMVHYTCQDSLRKRH... | Catalytic Activity: ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
EC: 2.7.11.13
Subcellular Location: Membrane
Sequence Length: 723
Sequence Mass (Da): 83661
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H8MPP5 | MIPFRETYRDIPLYSPAKKPCRVDLSDNTNLFGAPPSADRVLREEGFLRLARYPAGYAPDLKRAVAAYAGVAVENVTTGCGSDDVIDCALRAFLEPGDAVAFPDPTFVMVPMFARLSALKPVPVPLRSDHGLDVDGLLATGAKLIYVCTPNNPTGTVASRAALERLVDSASGVVLVDQAYVEFTRGGDFLDLARTRPNVLVTRTMSKAFGLAGLRVGWGVGAPSLVAEVEKARGPYKHTALGEAVAVAALTDDVAWMEACAAEAVVNRERLRGALKALGLEPLPSEGNFLLVPVPEARQVGEALRERNVNVRVFEGLTGV... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 345
Sequence Mass (Da): 36724
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A0A291IRG0 | MIKRPRGTSDIYGRRMEILSYVTEVFHEVLEKANYHEIVTPTFEAKELFVRSVGETSDVVSKEMYDFQDKKGRDLVLRPEGTAGVVRALIENKLYVLNNLPLKLFYQESMYRYERPQAGRQRQFNQLGIETFGADDVKQDLEIIVVAMDILKALQLDTRANIHINYLVNGEERVKYTEALRTYLKSFNDLCSDCQIRIEKNPLRALDCKIDGAKFTDAPVMSDYLKPEDQTRFDDLVELLKQMGYQTTIDANLVRGLDYYTGCVFEIKYDSQINKDQLTLIGGGRYNNLVQELGGPSTPAAGFGLGIERLLDILENEEIN... | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 421
Sequence Mass (Da): 48180
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A0A2M8D1I8 | MKLIDVLSKHKTSFLLLYAGLLLPVILLFYFFKPMVISGSSMYPTFHNNDHIVVDKFNGYISTLKRGDVIVFFSPIDENRLLVKRIIGLPGDVIAIRNGSVLLNGKLLREPYTNHRSESYETIPAFLIPDDSVFVLGDNRLVSADSREWGAVDKSRIYGKYILKLRN | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 19006
Location Topology: Single-pass type II membrane protein
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A0A2M8D3R1 | MKFKILFVVLLTAGAVYYIYPPKEKINLGLDLQGGIHMVLQVEMKDAMKAELDNSKSNLERILKDEKVDVKQVKANPEQLKIMVTGVSEDKVEKTEKIFDDYMSRFNVSDDGAGDYTLSFKGAEVKEIRKQAMRQALITIHNRVDAYGVSEPIIQRQGLESNRIVVELPGLDDPTRVKKSLSEPGWLEWRLLAAPNSFKSKEDILAANNGKIPDGTAIFPSEPSANGGIVWYLVKDRVELNGNDIKTARRSSDQFGSPTVAFTLNQAGVSKFSRVTTEHRGERLAIILDKKVVSAPSINEPINTPNAQITGHFTIDESED... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 516
Sequence Mass (Da): 56748
Location... |
A0A5C5XL89 | MQNVTTISEVRQILHEVRRSGKSIGCVPTMGALHEGHLSLIEVAVEQSDFVVVTIFVNPTQFAPHEDLSKYPRPLERDLKLCTEAGASLVFHPSAEEMYAKDSQISVTVGSLADCWEGASRPDHFDGVATVVTKLFNVVQPDLAFFGAKDYQQQSIIRAMCRDLDIPVKIVTCPTIREESGLALSSRNVYLSDQEREIAVHISQALLRARERYADAEWSLEQLRKTLRQELNETGGLELDYATIVDPTTLEEVLEKQNTMVALIAARVGTTRLIDNMELSLKS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-... |
F4NSF3 | MSEFLVKKLGWLFVAFTTALITFVPVTTYVFIFERWFAYHQERNIFVWLAPFYISVLFIYINYYLGCSTDPGRVLRDYDPTNGLNAKTCSTGEEQVKPKSTVKTRKQTSKGHDGVDLVYVSNLLEVITALTATGAFYEWIITFQDLSASSNILFGWFIGKCSGPWLNNCIGHNNIPHFIRFLCSVTMASLSCLVLLGLRVWDLIKYQNSLSKLYSTGGSFRSNVVVFYTPPADDKEIIFMLVNLVILFALLFSVGILSIWQLFYVAYNVTTIESMENGKIDELMRRGKIPNTYVYPYTLSVFRNFQAVFGQRWYLWWMPA... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 496
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 56648
Location Topology: Multi-pass membrane protein
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A0A545TZD5 | MLTGYSAELRRIAIYAALCVAIGLITGYLVWALIIGGVLYLTWIFWQIRRLDQWLTLSRKHPQSPPDASGIWGDIFDNIYRLQQRHRKEKRRLQQVISRMHETTAAFADGVVVVDSRGNIEWWNKSAELLLGLQQQDSGHPLVNYVRNPRFINYFDSGDYRLPVDMPSARESDKRLQYQINSFGQGERLIVVRDVTRLYRLEAMRKDFVANVSHELRTPLTVIRGYLETLGDSQDLSSVWQRALLQMQQQSERMTALINDLITLSTLETDDPERDQRCIAVEPMLMMIRTDAEAFSGDKGHRVTLDCEANAYIHGSEKEL... | Function: Member of the two-component regulatory system PhoR/PhoB involved in the phosphate regulon genes expression. PhoR may function as a membrane-associated protein kinase that phosphorylates PhoB in response to environmental signals.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phos... |
A0A1H1N3E6 | MSTPLGELARANGLHLHDAASPAEQARLMADFVLEALARALHERGHASLAVSGGRSPAAFFKRLNESELDWEEVTLTLADERWVPQDDPESNAGLVQRSMPNVFARAHWVPLYRGLDPHKDAAAVSTDIERLLPLDVLVLGVGADGHTASLFPVGDHLLENLRSDAPALCQAVPAADQRLPRLTLTGAVLQRARVRLLQVNGGEKQAVVARAFNAEPREMPVAAFLQPPMDIFYAPNHEEPHEPG | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A964T821 | MPSLKALGPGPALQAVAAAAPPSPSAPEAGDTAAPADAGRETAPDRVPAAESGAAEADAPRRAATEPPRHLDFVPALDGQVPARGRGGVRRFLGKAAGVSLGLALVVAAVGIWIGRDLPFGFVNGGPGAAATVLAAADGSPVAPVSAPLAAGDLPDDLANAVLVAVDRQFFDQNGIDFSGVWSVVWSGLVGRSGEETGSLAQQLSRSAFIAKDASLKRRLQEAVLTAALEWRLDRRAILSRFLDGASFGNAAIGVRSAARIYFDKDVADLDLPESAFLAGLLGAPPGFDPRGADAAEAVRRANGVIDGMRGQGFVAPDRA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
H8MMZ2 | MRARPGALQVGSFRGVPIRVHVSLLVALPLLALSFGGALQQAAETADVPPGALSGHPWAWGLAVAVGLFLSVLLHEMAHTLYALRHGGEVHGITLMIVGGVSELAEVPKRPRDEAVMALVGPLTSLGLAAFLGALTWLVHGLGMFQVQFALFTLAMLNAVLGGFNLLPAFPMDGGRIVRAALTPRLGLLRATRVAAGLGRMFAVLFGVWGLVTLNPFTLVVAFFVLMGAEGESRQVRMKALLERVNVEALMTPRMVGVDLDLSMQDAHWALRHEHVSMLPVTSAGRPVGRVTWAAAQAVPEAQRGGYVVRDAMEDGVVAD... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 383
Sequence Mass (Da): 41004
Location Topology: Multi-pass membrane protein
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A0A2S6Q5N0 | MIRLFVALPLPDDLAVRLVALGCGVDGAHWVSAENLHITLRFIGEVSEPVVDDIAYNLDTVSAGPISVTLAGAGQFASRGRTRGLWIGVNKSPDLEVLRNKVDIVLVRAGLQLDGRKYIPHVTIGRIKNARRNRVIGWLRSNSTFVSTPFSVPNFVLYQSRIGRNGPNYLPIANYRFASAQ | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 181
Sequence Mass (Da): 19863
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A0A8C4T010 | MGLLTLGSPLSWEETKKHADHVRKHGILQFLNIYNKVKDRQKDVTEVGRRGK | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 52
Sequence Mass (Da): 6029
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A0A968KGN5 | MNNPSKTQTPNKAPRPAQPATAAKPRPAGPAGGPSGKTGGGSGKKVDWIKTFKRLSRLAGFFIVPTFTLYSLFTGKKKRGLKHHFGQVPEVRKKTGQKLVWLHALSLGEVNAAVPVLKKIHEVRPNVLLVVSVTTDSGYDAAQRLMPFVHQIMFHPLDSWTFVNRALDRIQPDLFVLVDTGFWPGMLLALKERGIFSMIFNGRISEKSQARYKKFPRLVKPMLESFTLICMQTERGRTTMQQLGAPLPKIRIVGETKFDGVEPVPDSERQRIRDRLKIPPKNLVFVAGSTHEGEEEILMHAFQRIRRKYPLLTMVLAPRK... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A1F6SE13 | MANYYDLLGVSKGASEDEIKRAFRKLAHKHHPDKGGGDEKKFKEINEAYQVLSNKEKRREYDQFGQTFSGNGGGGRQGQRPRGFDFSGFSSQGGQGFDFSGTGFEDIFSDMFGGGGRSRGRARAGADIEVDVEISFEEMVRGVKKDIHLRKLSQCSICHGTGGKPGVPEETCGDCQGRGQIQRAVQTIFGAFAQMTTCERCHGRGKIYREECTECHGAGRLQKEERSSLEIPAGINDGQTLSVRGGGAAGEDGAPTGDLFVNIHIRSHPSFKRRGDDIVSQLQVTFAQAALGDKVAVKTIEGDVMMKIPQGTQPGEVFRV... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A0A914EGZ6 | GDIVITEEFIDKKIAEAEADDGRKKRQINTDPTKVWTLPIPYYFHSSVASAAQTTFRSAVSYIQTYTCVRWQEDPNFTITGRTRIRVVDGSGCSSFVGMQSTWQEQDITLSNSGCNSMGTHIHEMTHAMGSQHEQCRYDRDVSINVDYNNCQTTQQFNYAKETTSTTTNYGMPYDFGSNMHYGPYGFCIDCTKPVMIAKDQFYQSTMGSNEMMTFVDLYRINTLYNCLSTSVCPTPLACKNNGFTNPNGCNQCICPKGFGGTLCDQRAADNNPTCGGATIQANYYWKTLTGTIDKAQNIGTTSSVPFHKCFWHITAPTGK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease.
Subcellular Location: Secreted
Sequence Length: 542
Sequence Mass (Da): 60132
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A0A3D0G469 | MIPDDQGDSAQGLKTVLHWLREGKWIVAVAVAVSVVASVYIVTKVLEPVYYSTSKVKIEASQQPVISFESVAAGLSLSDSLAINSELEVLRSIRLLGKVVDALDLTTDPEFNPHLSNDTPPGVFARFLGPEPEAKTVEPSMVWTDTVSVLRDHIRATNIKETLVFSIRAQSRNPKKAALISNTLAGLYVQDQVEIKLEATQAASAWLSRQVAGMKSELEAADREVSAFRSSIDLVSADGLMALESQLKFMRDRLSRLNSQIAEIEERQNGLTYLTTVDGIADLYDDLDLERSDPDTAAFNARLDLLKRRDQSELERLLQQ... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 683
Sequence Mass (Da): 75410
Location Topology: Multi-pass membrane protein
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A0A0G1VM79 | MIREDIRQVKLEKLEKVREFGMEPYPEKNERSHANAEALEKFDELSGKEITLVGRVRSMRPMGGSAFASIEDETGKIQLFLNKGNMKEELFKLFIKAIELGDFVQVSGELFLTKTEEKSIKVTDWKVLSKNIRPVPTEHFGIKDEEELLRKRYLDLMTNPETRELFRKKNIFWQTVRGFLVKEGFLEVQTPVLEHTPGGADAEPFVTHHNALDQDFYMRISLELPLKRLLVGGYEKVFEIGRVFRNEGIDRQHLQEFDHMEFYWAYADLEKGMGMAEKMYREIASNVLGGYTHEYEGDVIDWEKEFPRVDYFEAFQKETG... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Catalytic Activity: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
EC: 6.1.1.6
Subcellular Location: Cytoplasm
Sequence Length: 484
Sequence Mass (Da): 55987
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A0A2D9YEK7 | MSFFGKLKAKLFRSSSKLDTEIDNLIEQKKEKSEETDPLPAIEKAKTSEINEQNDNAVIIEKGSSGVEDNSKEKKKKSFFRKIIEPVKKLVKKRKIDDELLESLEDLLIAADLGANTAVKVSSKLSEKFSGKEVGTSEIKSLLSXVIEGILEPVAKPLVLSDXSPQVIXIVGVNGSGKTTTIGKLADQYKKLNKNVMVAACDTYRAAAVEQLAIWGQRAGVPVVVGXERADPASLAFEAYERASKEGXDLLLIDTAGRLQNKKDLMAELDKIVRVLXKKNIDAPHNRLIVLDATTGQNAINQVSEFSXICDLTGIIMTKL... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for ... |
A0A914EQ68 | MDEHKKLLQYCAICRGYKAPRSHHCSKCGRCVLKLEHHCPWINNCVGHRNQVFFVRFLASAVIGCTHATIILSICIYRTLDMIWWSGPLRKGSPSFAIDSIYVFFSAIFAFSFSLGVIVSVGALLYVQLKVVFKNKTTIEDYICMKAESRDREIEFVYPYDLGWKENLRQIFSNGSFPLGNGVWWPVREGCDQFTFTIEQLEQKALKRQLAREVIVVRDFPGGICGAWRHGLMVQICQPLSEEPRVKVQKGERWLVTRGNKRWVYGVKHIDDHLMQQNGGELHRLEETANEKLDSKTLDTSAIRPPRGWFPRMCARPKSE | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 320
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 36930
Location Topology: Multi-pass membrane protein
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A0A945HCP2 | MSDFFLATGNKHKIKEVLSLTPEINWKTITDFPKLKKFSPKETGKTFAENAEIKARAFAKKTGKITVAEDSGLSVQALDGSPGVHSARWVKGSDSKRNTALLKKLDGYNNKRAKYVATICLYVPDIDEVSSIKGLKKDSVTFFSGEVHGFIAMEPKGDKGFGYDPIFIPNGYEKTFGELGDKVKQKISHRRDAFEKFVKFLESDK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
H8MMU1 | MASTAKTVEAVISAAWGKPQSWTLDSYRSRGGYDGLKRALSMEPAAIIDEVKKSNLRGRGGAGFPTGMKWSFVPKDSPKPKYLAVNGDESEPGTFKDRYILENDPHMMLEGIAIASYALGVHTCYVYLRGEFKFQAERTQAAIDEAYKAGIFGKSLMGKEGFALDCFLVRGAGAYICGEETALLESLEGKKGWPRLKPPFPAVVGLFGCPTVVNNVETLASVPPILAKGADWYAKLGTDKSGGTHLVCLSGSVNRPGVYEVGMHTTILELIHDDKYGQGMPKGRKVKAVIPGGSSAPVLGADELDVALEFEALKMKQTMA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 447
Sequence Mass (Da): 48467
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A0A914CE27 | MNQLRQEKFDLALGMIGDIPPLSYTGRAKNLVLNILSKYMILKFLQSIEEVVRPIVRPDFNAEEQLGKSAFVLVNVDEHVDFNRPISHKVVYIGGFGQMNPKPLEPKYEQILNSSKNGVVLISFGSVAQSYLMPQEMKKKFLEAFAEFPDVTFLWKYEKDEDNVAAGYKNVITGKWLPQTDLLVHPKLLAFISHGGANSIAEATVTGVPIICIPLFADQPRNSFVVKYRKVGVNLNKKEVMEGKLVDALHQVLDDDRVIERPVDFEITASMADMQGDIWAVKDQDFGDMQKMVKILSTAHSTLCKRMIGDVPPLSYTGRA... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 617
Sequence Mass (Da): 69673
Location Topology: Single-pass membrane protein
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A0A3D5Z304 | MKKEELLVFKSAEELANKFACQLMSWMDNNSGKDYHLAISGGKTPDLLLSVLAAKYSESELWRNVHFWWVDERMVSPNHAESNFGVVQKLLFSRISIPEENIHRIKGENDPKNEALSYSKQIQEKLAFENGWPVFDLILLGMGDDGHTASIFPDQMELLESEQICAVATHPGSGQKRVTLTGKAINNAHKVCFLVTGENKAERISEICSNQEKAILLPASHILPANENLDWYVDEPATKSL | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
A0A5J4PK60 | MQKIKPDSFQAWIWSSRPKTLIAALIPVAIGSAWAYADGKFDGLPAFICAVFAGLMQIAANWMNDFYDYLKGIDKEDRISPERAMAQGWITPKAMKTGIIGILIAACITGSYLLFYGGWKLLFVGMLCLLFANLYTGGPYPLSYCGAGDLLVVVFFGFVPVCGTYYVQALTLTTDVCIASIVSGLTIDTMLIINCECP | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 198
Sequence Mass (Da): 21561
Location Topology: Multi-pass membrane protein
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A0A6G1QY77 | MSKNKDPETVPLMTDARNNYTFAGSMPRQEVVQRDGTGGVKHCHDNSRAQEDREREKKVARKRLCAVSVICLIFMIGEILGGYFAGSLAVMTDAAHLLVDFTSFLISLLSLWLSSRPATHKLNYGWHRAEILGALLSVFTIWLVTGVLVYLAVERLISDDYTIEGTVMLITSGCAVLANIIMALTLHQSGHGHSHGGLSSHGHGDNHKKGKRCSHISNHAHLNNDHVDVEQKAADSGRRAEQANASVRAAFVHVVGDLFQSLSVLVSAIIIFFKPEYKMADPICTFLFSILVLCTTFTIMRDIIIVLMEGTPAGVRYGEV... | Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to... |
A0A2M7RM04 | MADIEKNTKGETATLEKEEASIPLHVGIMMDGNRRWAKKQGLKIILGHKKGVDALEKTLRFLGKKGVKTLTVYAFSTENWKRGKEQVDDLLKVISEYLTKEADNLIKNNVVLRVIGDLAKFPKEIQENLNDVMKKTKDNTGIILNAALNYGGRDEIIRAVKKLVSSGEEIDEANLNSCLDTSGLPDPEIIIRTGGANRISNFLIWQSSYSEFFFTKTLWPDFGENEMEDILEEFSRRKRNFGA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
EC: 2.5.1.-
Sequence Length: 243
Sequence Mass (Da): 27469
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A0A0H2VJJ5 | MNKNKVIVIGSTNVDKFLNVKRFPKPGETLHINQAQKEFGGGKGANQAIAASRLAADTTFISKVGKDGNANFILEDFKKAGIHTQYILTSESEETGQAFITVDEAGQNTILVYGGANMTLSATDVEMSADAFIGADFVVAQLEVPFEAIEQAFKIARKQNITTVLNPAPAIELPKSLLELTDIIIPNETEAELLTGISINNESDMKETATYFLDLGISAVLITLGEQGTYCAYQEQYKMIPACNVKAIDTTAAGDTFIGAFLSELNKDLSNIESAIRLANQASSLTVQRKGAQASIPTRKEVEAEYN | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
C7LU65 | MKKNAEAELQKQGIMQKITDLRIFFDQAKVELKKVVWPDKQETISTSSAVLLLVVVMALFLGVVDLVLTKIIAAVLS | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell inner membrane
Sequence Length: 77
Sequence Mass (Da): 8556
Location Topology: Single-pass membrane protein
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A0A2S0KL96 | MDKKYKPQSEYDRDLSAEKTADDVLSGNEAGLLPDSDNEQNIRPIRPDVNEVEGPRFSDDTDLGSGVRQAKIQMTPRKEYIPSSEGLEEFNLQIEGDTDDLEDSDDNNTNDADFSPKNNNEGSNNKKVLNASDDIFKKRDKRVVVLEILDWIKYILIAIILGLLISKFVIQRSEVVGRSMEDTLHDEDQLVVDKLTLLFSSPERGDIVTVNGAKAHNDNKEVGMLVKRVVALPGDTLDFKDGKVIINGQEIEEDYLSAGTYTMAPFGWQGEIRIPEGHYYVLGDNRGNSADSRVFGPVPENAIEGKVWIRIYPFDKFGKL... | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 321
Sequence Mass (Da): 35999
Location Topology: Single-pass type II membrane protein
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A0A2M7RP34 | MTNKKLTKKQEDVLAFVKGAIEKSGNAPTVREVQAEIGCASPMGAVSHLASLERKGYIRKVEGKKRGIVLVMDGKGKPLEDIVQVPLVGNVACGMPIFAEELIEEWIPLSTKLLRSDPTDIFMLRAKGDSMNLAGIDDGDFVIVRKQNTADEGDKVVALLGTEATVKKFHRTKEGITFIPMSTNPEHKELVPEAGTFMIQGKIVGVIKNYNS | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually ... |
H8MJG3 | MNHPLASLVGPLKYACQRDFAQLGTVRDLRTLMERTLASAGGVDAQALEHLRAALPHVDPPAPPEHRKAALRQVLGALKLSGVVLPEELERVVVTGEINAVAASFPRSPERAHVLEGELNPAPPRRRLTPPPGTVEARGNTVPPWRSQDPVPPVGGGVPAATPAPASRQPQARGPQGGNSGPVKGEPVPYGARMAASRGAANGPAQGEAQPYGARMAAARNAAVPAGAPARAPGAKPAASTDARKGAPPPADRAPTEKARKKKAKAVGAEASRSEAKLLSIAPRTGPLSAPLKTLGKRLGPRLVAVLDKKGLRRTGDILF... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A4Z0KT55 | MWKTLHQLAAPPRLYQICGRLVPWLAAAGIIVLATGWVRGFGFAPADYQQGEGYRIMYLHVPAAIWSMGIYAAMAVAAFTGLVWQMKMASLAVAAMAPVGAVYTFIALVTGAAWGKPMWGTWWVWDARLTSELVLLFLYAGVIALWHAFDDRKMAGRAAGILVLVGVVNLPVIHYSVEWGDALLPGSRLRRLWVG | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 195
Sequence Mass (Da): 21401
Location Topology: Multi-pass membrane protein
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A0A2G6IHL8 | MAEQGRSLVTWFEAGASRLCLRRQMALAAGSGALTALGHAPFNLWPLALVGLAECYALFRIASTLRRTALLGWSAGAGYFAISLFWIVEPFFVDATTHGWMAPFALIFLSGGLALFWAGGFGAARALGGGPLAFIAAMAGVELLRSYILTGFPWALVGYVLAPSPAARFAALIGPHGLSIIALAIGITLWRLAGPAWRKSAPLALGYALTFLLAALSWPAVPADPAAPVVRLIQPNAPQHEKWDPQHIPAFFERQLAFTRAQSDTPPDLIVWPETAIPWLLEDAVTPLAMIAEAAAGTPVVLGLRRTEGLPFYNSLIVLD... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
W6MTW4 | MKHPFQAIASNAEYVFAVSKNSIHAYRIHSDSLELATSWTDETDQRTLLKEQQDQKIKEGNLKKTPKIPVPGPGAPPIYNFIRTVNVFERYVVLTVDMDKSVVVFELTNDESVWRLLKRQRFPKRPDSVTMIDDHTVLMGDKFGDVYAMDVSSPPQTEAFKPVLGHVSMLTSVCSATNNGRQYVISGDRDEHIRVTNYPKTFVIDKWLFGHKEFVSSLTVPKKYGNVLVSGGGDDYFCVWDWTDGTLKQKIEYGKQIENYFKEGILSPEVCPLIFKEGALVELCITLIVSHEDFLVVTIEGCNIALIYKFEQELVFSHYL... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Location: Nucleus
Sequence Length: 389
Sequence... |
A0A2G3E473 | MRKIAIYGGSFDPIHKGHLHMAQAAIRQFELDELIMMPSYYSPNKADVRLCDANDRIQMCRIATESIPQIRVSDFETGQHEVSYTYRTMQAFRNRYPDDKRYFIMGGDSLDYFDKWRHPEIIAECAHILVLEREHFDVAHLNAKIDAIKALFPSTISVIKDSAYTASSSDIKKQLEDNPEQCPKTLPKAVYQYICSNHLYGL | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
N1QXQ3 | MAHKPLNTLLKAYGDPISSQQAVPGTTFIRCHPKSVFSASRVRCFLGDVSCLATIPTDVKAEATFIAKEDGVIAGISLAEMIFNQVDPSLKVEWFEADGNYVHKGLQFGKVYGCAQSIIVAERVVLNFMQRMSGIATMTKAMADAARPACILETRKTAPGLRLVDKWAVLIGGGKNHRLGLFDMVMIKDNHISVAGGITNAMTSVDQFLEKENLAIPVEVETRTLEEVRDLLKYTDENKTSLTRIMLDNMVVPLPNGDLDVSMLKDAVQLINGRFETEASGNVTIDTVKKIGETGVTYISRHEHTFIIPLTDSSLKFSFS... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Catalytic Activity: CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate... |
A0A923ZSE4 | MKILTYPSPILTQIAKSVKLPLSSSDLDLVKNMWQTVQGIGVGLAAPQVGASLQLFIVRLSQDKDLAKKLKESDFIVINPKITFYSQNKVSMIEGCLSFPSEYWDIVRSEIIQLEYDTIKNLKEVITKDAKPVYQKSKKLLAKGWLSRVIQHEYDHLSGKVFIKAGGKKLSKKDLANLEDAIID | Cofactor: Binds 1 Fe(2+) ion.
Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
EC: 3.5.1.88
Catalytic ... |
I3X9F5 | METSVCGDKSKARRYARRPASLPRRSAVPGASGTDCVLSRIERLSSGIPRVCAPAIASVAIGSRSSPSPETDHAITEQNRRGITRPSHNRGSYSIAASCVPDMTLGWRRPAEMQNGRNILILNGGSSSLKFAVCESARRDSWTSRGRFERIGTSDTLFIVTEGRTESRRDAGSINHGTATSFLLDWLEKRLGLASIAAVGHRVVHGGLKYQAPEVIDDSMIAELRRLRPFAPEHLPTELDVISACTKRLEKVLQVACFDTAFHRDMPAVARVLPLPRRFNAEGVLRYGFHGISYTHILESLRTSAPELASKGRLIFAHLG... | Cofactor: Mg(2+). Can also accept Mn(2+).
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
EC: 2.7.2.1
Subcellular Location: Cytoplasm
Catalytic Ac... |
A0A7W5B1G6 | MRKRVRFGIQTKILTGYIVVILCLLMSIVVIGGRLSDQQKEIKFITEHDFILQEVTSSIEKALFDMETAQRGYIITGDSSYLPPYTEGHAKWEEDYATLADLVADNPSQLQRLETIRASILEWIATAGEPTIELKQAGKEEELREFFQSDIGKAHVDEIREQFDEFRAVEKSLAQTRAEELNQQGTYLRWSLGVIVLLIVAVAVFVGIAISRAIVRTIREVEQAIREIAVSDSAGNRRIEVRTDDEIRDLGDATNLLIANRADSEWLESSLAKLVGRHQGITDMEKLGASFIRDIAEHTEAYCAVLYIKGQDQRRKTLVR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 907
Sequence Mass (Da): 101334
Location Topology: Multi-pass membrane protein
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A0A564WE52 | MDHVLETRASARTPIAESSSAPTAQRASRPLTGNEAIARGAWEAGIRVAAAYPGTPSTEIMESLADYPAEDLHAQWSTNEKVALDVAIGASFAGVRALASMKHVGLNVAADALMSLTYIGVNGGLVIVVCDDPGIHSSQNEQDTRLFSRFAMVPCLEPADAQEALVMTREAFDLSERFDTPVIIRSTTRLSHTRSLVTLGERTVPPSGHFREDPRKNVMVPAHARNRHPKLIEREAALRAHFATSGHVRWEAGRRDIGIITAGTPYAYVKEVLPDASILKLPAAYPLPLDLIGRFCASVERVLVVEELEPAMETEIRAAG... | Cofactor: Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Function: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.
EC: 1.2.7.8
Catalytic Activity: CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredo... |
A0A914CCN9 | MVHIFIVLTLLIKGFCSFEDLEMDKQVEQEANRYSDVLLLDYYESYNLVARKVFGFFRYVNQSCPNVKCVLKGDSDTVINLTGMEKLCEIMPDNNLTITGYYGWDKPLRDLQSKWYTPYFVYPIKTWPSLVSGFSYLLSGYGIVPRLMNTLETKTSFFTSENFRRLWEDILFTGIVRDLSEIPLVHNTGFHWGNKPDYWWHEGKRIILALETRTDCTESCSTEYAWNLVQANRRENNFSTFSSYECHLQTLREVPDFRNSIGSSLVRSQARNL | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 273
Sequence Mass (Da): 31979
Location Topology: Single-pass type II membrane protein
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A0A914CDC5 | MNMSTLNGTLPSCHYQCIYTDDRRFEPYASAIVFHIPDLNPLSLPKRRPDVLHVFFIEESAAWRWSWWTFSYKFVPKNYFNLTKTYRKDSDIFASYGAFYPIENTTKKSDIWSQSDINAAMLKKSSPILFLVSDCNTHSKRELYVEELAKYINITQFGKCADKFCDANCEEEQIKKHYFYLAFENSVCKDYVTEKFWRLKKLIVPIVLDRKIVENTIPSDVFIAASDFKDPSKLAEYLQYLMQNPNEYARYLNWTKKFQKSYKEPPRENRLCKLCEMVHKNVHNEIPNIQKWWVHGSDCLKDYAKYLLKES | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 311
Sequence Mass (Da): 36987
Location Topology: Single-pass type II membrane protein
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A0A4Q2J8K1 | LLARAASWPAPGRRLLRAAVTVPLVLPPVVGGIALLLLLGRRGVLGGALGDLFGITVPFTTGAVVLAQVFVALPFLVFAVEGALRSADRRTELAAATLGASRWQVFRHVTLPLVAPGVAAGAVLCFTRALGEFGATITFAGSLPGVTRTLPIASYLAMQTDPDEAIALALLLLAVSVGVLLLLRDRWLPGVRG | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 193
Sequence Mass (Da): 19945
Location Topology: Multi-pass membrane protein
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A0A3C2D8S3 | MARFLNNRKMATGKIPGELIHLGKKRMEAPRLRLMDFTADKLTEKELENLDNCQPYLNKNTVSWVNIDGLHDPEIIQKLGDMFGIHGLLLEDMLNTGQRPKVTETDKLIILILKFLDYDESKHKLHADQVSFILDENYLITLQEKENAHFDPIRDRIRNSAGRVRRKGADYLTYLLLDIIVDNYLINIEILGDLIEKTESRIFIAKPKDQLMQQIYKHKTEINFLRKNIRPVKEIVLHLIENESGFLKEENLKYFHDLSDLVVQATETIEIYQVMLNDQMMIYHATLDSRANEIMKVLTVFSAFFIPLTFVAGVYGTNFD... | Function: Mediates influx of magnesium ions.
Subcellular Location: Membrane
Sequence Length: 355
Sequence Mass (Da): 41697
Location Topology: Multi-pass membrane protein
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A0A9E6K166 | MNTQAIIRENTQRTYLYMFLLILILGTIGHGLSSFFEVGLTGTSTFIITSLLINVVAFFFSDKIILRTVGAKKLDKTVAPDFVELVANLANNQNLPQPKLYYMDTDAMNAFATGRDQKHSAVVITRGLLEKMKQNEVEAVVAHELAHIKYLDVRLMTIVTVLAGLLTLLSDMFWYSNVAQKASERDNSGSVQMIGMALALFAPFTALLIQNAISRKREYIADAAASDMIGSSHPLIEALEKIRRDQIPLPGSQAATAHLFFSQPSKDGFIEKLFSTHPPLEERIEQLKKLA | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 291
Sequence Mass (Da): 32319
Location Topology: Multi-pass membrane protein
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A0A5C5XK59 | MTGKAIRHSLERRGQEIADELLGSQEKSARGSGDTVRLSTKAMACEFSLILNPSENRRQVITATDALDIIHEVETQLTVYRETSDLLAINEAARQGGATVEAEIFKLIELSIQLAQQTHGAFTPTARALNLLWRTNRSLGKVPDAQEIEAAVITSDYRDVLLDSKNHVITFQNELTGLDMSGIGKGYALDRVADFLQQEQVENFLLHGGHSSILARGTHSTPLGWPVGIRHPQAPHKRIATILLQDQAFSASGSGVQFFRHEGKRYGHIFDPRTGWPVEHILNAVVLAPNAAIADALSTAFYVLPLEESIAYCEQHPEIA... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 348
Sequence Mass (Da): 38404
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A0A2M8D927 | MHIVFGVSEYYPLVKVGGMADFAGSFTKKLASCGHRVSVVLPGYSAIERNRLNVKDTGIQFTIPIGKENVAGSVSEIKMSENLTIYLIENEHYFDRDYLFGTGDKGYTDNAERFLFFSRAILELAEKLPDADVFHMNDWHTAIALFYLKEYYQKLGKFTGVKSLLTIHNLGYQGLFWHHDMHLLNMGWEYFTADGIEFYDHINFLKSGIVFADEITTVSPAYAREIQTPETGFGLDGILRSRADHLTGILNGVDYKIWNPWFDKLIESRYSGKQFGRKLANKMELQREMGLEKEPDTPLITIISRLTEQKGIDLILPVFD... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
EC: 2.4.1.21
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Length: 478
Sequence Mass (Da): 54856
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D3LTU8 | MYELTKDSRLRKNKEYRLVYRYGKSYVNRYVVLYVMARSSKQCTRMGFVTGKKIGCAVERNRCRRLMKEVYRLHRQELGSGFDLVLIGRSPLKNINFAQAEYYILKVLRIAGILSKKR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of... |
C6XEP4 | MSKTLIIVESPTKAKKLSEYLGSEYLVKASFGHVRDLPTSNGEIGYHPETFEPIYEVTEKARTTIKVLKAAVKECDRVLLATDPDREGEAISWHLAELLGLRKRERVKFHEITASAILKAINTPSAIDTSLVRAQEARRIIDRQVGWLVSGPLTRKIGQRASAGRVQSPALALVVEREREILAFKKEAFFTVEAEFSEEWGAVWPSDEQQCKDRSVAETIAESKQFSVLEYDLSKLHEDPPPPFRTSKLLQAASVVLGFDPKRTMDLAQSLFQKHGAISYHRTDESNISDDAYGMIVEYGQERNYPMSSEKRTWKGVVAA... | Function: Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is ... |
A0A318A999 | MTTPLNTTDLADHLGESVRSCPVQLRNFGGVQKFAGQIATVRCFEDNTEVRATLSTPGEGRVLVVDGGGSLNRALLGDNIAQLAIDNNWAGVIVHGAIRDSAEIAEMAIGVKALGTNSQKSRKEGLGVTNVNLVIGGIEFIPGEYVYSDADGIVVTNDPVELDDTE | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A914BWZ0 | MKTTLSSQNLFTTTNTTNEYKEVTSTSRSNFKSCIHDKKCDTNNECIKGVCFEGKCRCRCSPFAHCIKNEDCLGRNLCSNKCISENGTSVNCHFKESCALGSQCLQGVCVGIGRYVRDAYEAISCNIENAEIDCQGYGSKSECTIELGVCIRHKNASEIGRNASNECQGGISATYGFPSCISYDDKPIKCGAKGNMQQCSRGSFCGLYKMAQTPSFKVLLLDIEGTTTSISFVKDVLFPYAYDNVEVFLDENFHRDDVKKVIHGLVILSQKEAANDTDIKTPAEDEISQKCREDLVHNVRVWIKKDKKLTALKELQGIMW... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into t... |
A0A1E4SH05 | MPPSKQYLSPLETLSQVYLNKYSLVLALVAIKVYLFKRAVLANIDAVALQNECDKLANEYPGKVSLLINSYILDNLSKARYSYLVLIQALVSTVKHLVLFYVELFLGTYTCLLNAAVSGTANFAVDTSKNVIVMVNSTIVDVTHDIQDGLDGLSAVIQTLVSSLDKIKAFFTGKDPTTTQYEDKIKLSIGALRKLSIPTSVLSSIEEFRNSTVPTFDQLQNTTSVLIASPFDLVSRKLGESSFNSSLDSSRQLLGNESLPVMPNGACSSRIADTVSQLHKDVDLAAKKILFGIVAAAVVVCLPLAYTHVRAWRREARLMD... | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Subcellular Location: Cell membrane
Sequence Length: 667
Sequence Mass (Da): 74341
Location Topology: Multi-pass membrane protein
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A0A090SJB1 | MLPIIIIVGLRGGVFTPTEAGVIAAAYVTIISVAYRELKFKDMYEIFLSSIKTTGIVMFIAASAMVSAYAITVARIPNELASLLNSISSNPTVILLIIMVFLLFIGCVMDLVPAILIFAPVLLPVVTGYGIDPVYFGVLMVINLSIGLITPLLDRTLRWFQYFENWHRSCRSRCLAILNGSRSYIDASCGLPANHSLPNPVTRIMRSSYVRF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 212
Sequence Mass (Da): 23340
Location Topology: Multi-pass membrane protein
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G9LVB7 | IFGAWGGMIGTALSLLIRAELGQPGTLLGDEQMYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAVNFITTAINMKPPALSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A914D6Q0 | MEIEEKEDLVVQETDKNYKERLDAIKKRDLTDAKFGYQRLTDRTPRNGWLVNVQPSESFDELTKTVISVVDFYFLQDDGSRFKISYPFKPYLYVGTTPGYELHVASYLGKKYNYITIDHVEKENLDLKNHLSGLKSKFLKISFPSTMELMRFKKEIMPQIYKNQNDLKARTNYNAFLERHLGSAQYENMREVYQEIIDIREYDLPYHMRVCIDEKFFVGLWYTVIGRDVDTQRPIIKRNEDLIDQPDPV | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 249
Sequence Mass (Da): 29656
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A0A6N0HYN0 | MKIFKSVVLFVSILTLTACSGMGGGEQGDVAVDDHSTTTGGEGADGASTSGAMGGDYFDGRMLNDQSGDPLNRWVIYFDFDSSAVMEENNAMLGAHAAYLLEHPELTLTLEGHADERGTREYNIGLGDRRAQGVREVLTLQGAPGHQINTVSYGEERPEGFGHSEESWRLNRRVVLVYSN | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 180
Sequence Mass (Da): 19459
Location Topology: Lipid-anchor
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H8N1P2 | MNPVELKSPDEIALMRDAGRIVCEILDELEKAVAPGVSTWELDALAEQLIAKKGARSAFKGYHGFPGVLCASVNQEVVHGIPDRKRRLVAGDLMKLDFGVVYRGFFGDSARTVPVGKVTPEAQALVDATRQSLEKAIQVMQPGNRIGDIGHAVQSHVEARGFSVVRDFTGHGIGRKLHEPPQVPNYGQAGSGMKLRPGMVLAVEPMVNQGTPDVEVLEDEWTAVTVDGKLSAHFEHTILISERGPEVLTRRR | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A914BW35 | MCGDGCLFFDDLENFLSTDLSTKLPPYKLKNLENFTFDEKRVKTLVCHDMKGGYLEQDKLEGCILTDSCYPYLILHWWSMDIFCYFSHHFITVPPVVWTEQAHKHGVIVLGTFITEFEGGEKLCEKIFSSQEVIDELIEKMIQLCINLNFEGWLINIENIMKPEHLPNLEYFLQELTQKSRQILGKHSRIIWYDSVTNEGKLDWQNELNLYNRKWFDLTDGIYLNYAWNEEHLQRTLELAAGQRLTEIYLGVDVFGRGCMEQVARIKKFFRHQPLYKQFFSSYINPYTIIRRWTLGISYLSCGQLFPETSKKMILQNRGG... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A7C1F392 | MTGQRAKKKGLPVGSPFRYSITGAKTMATMRLFWAVTLPKDVRDRLAIVQSSFRKLPLDVKWVEVENFHLTLRFLGDTDRAMVDSLLAVAKERLGELLPFTLILRGVGVFPSLRQPRVLWVGVERALPLFNLHHLLEEALRQLGFPPEAKRFSPHITLGRFRTGANTGLLEEAIKELGTAEVAQVNVIGIALIASELTPKGPVYTPVGRVNFNLAAGQNRSPTSV | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 225
Sequence Mass (Da): 24886
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K0JX00 | MTGTTRTYGLIGIGIGVFNLSLAALLEDNGYRDAVFFDRQPEMTWHGGLLLESSELQVHYLKDLVTPVDPTSRFSFLNYLAQRGVLYQFLNRRGGAVGRGQFQRYFRWVADALPSTRFGSTVEAVEFDGEHFRVRVNGEEHRSRHLAVATGPRPTVPDCARPHLGDRVFHASEYRQRREGLHGARITVVGGGQTGAEVVLDAMNTVPHRELAWYGRRLAFSQLEDHSFVNELYVPSFTREFRAAAEDKRLELLDRLAMSSDGITQHVVDAIYRLAYDRMFFSDNEYDYDFRAGQELVGLEPAPGGGYELTMRSWLDDGLR... | Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 1.14.13.59
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6)-hydroxy-L-lysine + NADP(+)
Sequence Length: 449
Sequence Mass (Da): 50060
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Q1D9W4 | MKHAMPSHPLDYPVCLRLEGRSVLLVGGGAIAEGRALAVLDAGARLRVIAPEATATLRRLAADGRLEWQPRSYKAGDVRGHHLVLAATDDVAVGRQVATEARDVGLWVNTADEPALCDFTLPSVGRRGPITVAVSSAGRAPALASHLRKTLTAQVTRHHIWLARLSGWLREHLPRGEGRQRLLKQVAVGDIGALLERGERKAAWARLRTELEHSKIPGETR | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 221
Sequence Mass (Da): 23979
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A0A0Q7EQZ7 | MIEIEVEDEAWTAALPEAAAVAERAAVAALGTVEGDVVILLADDAAVQELNSGYRGKVKPTNVLSFPAAESAAPHLGDLILAYGVCAAEAQAQGKTLADHLSHLTVHGVLHLLGRDHEDEAEAEEMEAEERDILASLGVADPYRPDADA | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 149
Sequence Mass (Da): 15588
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W6MQC6 | MFRVKKRLIPREFTSYLGFRNYKVLSVETSCDDACVALLDRFDPNQPPRVLANMKSTLDSREAGGVIPTDAHVHIQQSLPPLIAQVLKDNGLDKTNSPELVCVTHGPGMAGSLSAGIDVAKGLAIAWGSRFIGVNHLLAHLLTPRLESNGQKPAYPFLTLLASGGHTMLVLSNDLLDHEILLNTRDISAGDALDKCARRIGIRGNMIGKALEELLAESPEDAKIPVDLNIKLPLLNKPGRSNVTAFSFSAFITQVSEQMAANYPQGPADDSIRRALGAKIQDSIFEHIIDKVNLCLSVEKYKVRKVRSLVVSGGVASNMT... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP)... |
A0A1G3L8U6 | MDELVVGLDMGTSQIRCAIGTYDEEGRLEIVSHGVANSEGLRNGVVVSIKAALKSVQEAVEKAEEKGYEVKEVLVGMSGGTVEGLNSRGVVAVAGGEEITQDDMDRVLEAAKAVLLPMDREILHVLPQEYIVDDVGKIKNPLEMMGIRLESEVHIVTAGISAIKNLVNTVNNAGFTVTEVVLESLASSTAVLSKEERDVGVLLIDFGAGTTDAILFLEGAPRYSKIIPLGSERVTKDLAQVLQIPEEEAERIKVQDGCATLSALKEDTSVIVNAVGTRPAEELLRSEICQIIQPRMEEIFSMIHREITKAGFHVEQLGGG... | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 411
Sequence Mass (Da): 44437
Location Topology: Peripheral membrane protein
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A0A9E6FFA0 | MSNEASDTTIILGLGREGLSTARYLLSKHNNLSLLLLDEKPLSELEPEWQKLVEKDTISFAQTVPTETESPLVYCAPGIPPHNPLYKALEAKNAVFTSNLELFCTTISQEYAKVITIGVTGTKGKSTTSALLYHVLQTAGFSVSYAGNVGIPALDILPEISAEETHYVVLELSSHQLGRINTSPNIAVVQNIVPEHLDYYGTFENYLAAKMNIAKHQTDHDRIIYSLDFETSAQVAALSPGKKYGYSLENPNTNEVSQRVLQQIKASNTKLIGQHNRYNIAPSIIIGEVLGIDADLIHTALESFQPLSHRLEMVPSDDGV... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
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