ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9K041 | MISLKNDTFLRALLKQPVEYTPIWMMRQAGRYLPEYKATRAKAGSFLDLCKNTELATEVTIQPLERFDLDAAILFSDILTVPDAMGLGLYFAEGEGPKFKRALQHEADIAKLHVPDMEKLQYVFDAVTSIRKALDGRVPLIGFSGSPFTLACYMVEGGGSKEFRTIKTMMYSRPDLLHKILDTNAQAVTAYLNAQIDAGAQAVQIFDTWGGVLSDAAFKEFSLKYIRQIVAGLKRESEGRRVPVIVFAKGGGLWLESMAQIGADALGLDWTCNIGEARRRVGKQVALQGNFDPFALFGTPESIRTEVARILADYGHGSGH... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39105
Sequence Length: 354
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q2GCG4 | MSLLDKKISTWFMRQAGRYLPEYLKISKEMTFFQMCESPEIASEITLQPIKRFDLDAAIVFSDILVLPRALGCNIDIKKSTGPVIERINNPNWLTYDAFEEKISPTLNTIAITRKSLPQNKSLIGFAGGPWTVALYIIEGGWDKTFLRTKEFINKRYHEFKEIISILTDATIQYLNKQLKHGADFIQIFESFAWAASSNEFKEFIVEPTRRIVSSIDVPVIGFPKGAGVSYLQYVKETSVDVISTDHSLPLDWIADNLQTHAVVQGNLDPYLLAFNKKEALLQTERIVDAFSEKNFIFNLGHGIYKETPLSSVEAVLDFI... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 36899
Sequence Length: 324
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q82X50 | MTKLENDTFIRALLRQPVDYTPVWMMRQAGRYLPEYNQTRARAGSFLSLCKNPDFATEVTLQPLARFSLDAAILFSDILTIPDAMGLGLYFADGEGPRFERPLREEREIRSLIVPDPDTHLRYVTDAVRQIRTALNNRVPLIGFSGSPFTLACYMVEGAGSSEFRQIKTMLYARPDLLHHILGVTAQAVTAYLNAQIEAGAQAVMIFDSWGGALSHAAYQEFSLRYMNQILDGLKREHNGDRIPNILFTKGGGLWLESIMASGCDAIGLDWTIDIGEARRRTQDKVALQGNLDPAVLFSSPEVIAAEAGKILASYGHGHG... | Function: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
Catalytic Activity: 4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen III
Sequence Mass (Da): 39303
Sequence Length: 355
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX b... |
Q6NQ88 | MSSTRSRRKRDPEIVIARDTDSELSSSEEEEEEEDNYPFSESEEEDEAVKNGGKIELEKNKAKGKAPITVKLIKKVCKVCKQPGHEAGFKGATYIDCPMKPCFLCKMPGHTTMSCPHRVVTDHGILPTSHRNTKNPIDFVFKRQLQPRIPPIKPKYVIPDQVHCAVIRYHSRRVTCLEFHPTKNNILLSGDKKGQIGVWDFGKVYEKNVYGNIHSVQVNNMRFSPTNDDMVYSASSDGTIGYTDLETGTSSTLLNLNPDGWQGANSWKMLYGMDINSEKGVVLAADNFGFLHMIDHRTNNSTGEPILIHKQGSKVCGLDC... | Function: May function as the substrate recognition module for a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex including DDB1A and CUL4 (By similarity). Required for DNA repair. Binds to DDB1A to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induce... |
Q0VBY8 | MAPRKRPENQKTPEVVVRPKSKRNRSPRELEPEAKKLCVKGPGSSRRFDSGLWAGLASLRVPPLCSSIVRALHQHKLGTAAWPSLQQGLQQSFLNSLASYRIFQKAAPFDRRATSLAWHPTHPSTLAVGSKGGDILLWNFGIKDKPTFIKGIGAGGSITGMKFNPLNTNQFFTSSMEGTTRLQDFKGNTLRVFASSDTCNVWFCSLDVSVKSRVVVTGDNVGHVILLNMDGRELWNLRMHKKKVTHVALNPCCDWLLATASVDQTVKIWDLRQVRGKSSFLHSLPHRHPVNAAHFSPDGAQLLTTDQKSEIRVYSACQWD... | Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the ... |
Q5ZJL7 | MAPVNQPKDKKHEKAHEHRSEEAKSAGKRKLDYEGLENEPLAKKLFLRKTSKAQEKIGWNRGGTVMRNTRALFHQPKWQCSIVHYVYQNMLGGSIRAQLRQCLQLPFLRSLTSYRLFRTASPFDRRVTCLEWHPTHPSTVAVGSKGGDIILWDYEVLTKTCFIKGKGPGDSLGDIKFSPYEAVKLYVASGDGTLSLQDLEGRAVQVISRAPDCGHENHNVCCWYCSVDVSASCRAVVTGDNLGNVVLLSTSGEEIWKLKLHKKKVTHVEFNSRCEWLLATASVDQTVKIWDLRNIKDKANFLHVLPHDKPVNAAYFSPTD... | Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the ... |
Q2YDS1 | MARGRAQTDSAASKQTKTVNSKKRPNEETPQPSTKKLKAKQQHKSKQKEETYIQASVKWTGGQKKVGQTSILHYIYKSSLGQSIHAQLRQCLQEPFIRSLKSYKLHRTASPFDRRVTSLEWHPTHPTTVAVGSKGGDIILWDYDVLNKTSFIQGMGPGDAITGMKFNQFNTNQLFVSSIWGATTLRDFSGSVIQVFAKTDSWDYWYCCVDVSVSRQMLATGDSTGRLLLLGLDGHEIFKEKLHKAKVTHAEFNPRCDWLMATSSVDATVKLWDLRNIKDKNSYIAEMPHEKPVNAAYFNPTDSTKLLTTDQRNEIRVYSS... | Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the ... |
Q92466 | MAPKKRPETQKTSEIVLRPRNKRSRSPLELEPEAKKLCAKGSGPSRRCDSDCLWVGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDGARLLTTDQKSEIRVYSASQW... | Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively . Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the... |
Q99J79 | MAPKKCPETQKSPDVAVLLRSKSRRGPQELEPEAKKLRVQGPVSSRTCESCCLLAELSSLQIPSRSSSIVRDLYQHKLGKATWSSLQQGLQKSFLHSLASYQVFRKAAPFDRRTTSLAWHPTHPSTLAVGSKGGDIMIWNFGIKDKPIFLKGIGAGGSITGLKFNHLNTNQFFASSMEGTTRLQDFKGNILRVYTSSNSCKVWFCSLDVSAKSRVVVTGDNMGHVILLSTDGKELWNLRMHKKKVAHVALNPCCDWLLATASIDQTVKIWDLRQIKGKDSFLYSLPHRHPVNAACFSPDGARLLTTDQNNEIRVYSASQW... | Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively . Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the... |
Q08949 | MSFKATITESGKQNIWFRAIYVLSTIQDDIKITVTTNELIAWSMNETDTTLCQVRFQKSFFEEYEFKPHEIVFGENGVQVIEDTYGNSHKLYSFRVNGRHLTTISRKPDGDGIKSFTIAVNNTSTCPESLANRLIVVIEMDSLIVKEYCPQFQPIKYDPIIINLKYKRRFLDVFGTAASDRNPQEPLDPKLLDVFTNTERELTSALFNEEVESDIRKRNQLTAADEINYICCNSTLLKNFLDNCNVNVTDEVKLEINVHRLSITAFTKAVYGKNNDLLRNALSMSNTISTLDLEHYCLFTTIEDEKQDKRSHSKRREHMK... | Function: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and t... |
P27718 | MNASEFRRRGKEMVDYVADYLEGIEGRQVFPDVDPGYLRPLIPTTAPQEPETFEAIIEDIEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLQLPEAFLAGEAGEGGGVIQGTASEATLVALLAARTKVTRHLQAASPELMQAAIMEKLVAYASDQAHSSVEKAGLIGGVRLKAIPSDGKFAMRASALQEALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICHEEGLWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRT... | Function: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
Catalytic Activity: H(+) + L-dopa = CO2 + dopamine
Sequence Mass (Da): 54294
Sequence Length: 487
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step ... |
P34751 | MSEKGETLIEDTAEIEFEQTVDKTQQWGRLKNAAAFSLFRDLHMNESLQRKHARSDYKVYDLNNRVIFHVINTTAMPITKDGPFCLKVMNKDKKSVAKFLRNEPKRSYKQTGLASLFGCCSDTEDTMEVLDDNGLIIATSFLHHDQFRGILITMKDPAGKVLIGIQASRDQKDVFAVSGPDNRYLGEIRQKIISSGNSTDNYKGVACWFSTEVSLNVKVFFMAAAFLIEIDYFSETKSRQAPFRTPEADYLNPIIKTPPHNERVPKMKTNISKTRKKKGKVSDASKDSRPSETKKETLMMPEIHHTKHFDSIGGEEQAFA... | Function: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
Catalytic Activity: H(+) + L-dopa = CO2 + dopamine
Sequence Mass (Da): 102004
Sequence Length: 905
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; do... |
B2IGG3 | MAKHVAVLMGGLSAEREVSLCSGAACAEALRGEGFEVTEVDVDRQIGERLAALRPDVAFNALHGRFGEDGIIQGVLEMLAIPYTHSGVLASALAMRKDRARDVLAAAGVPIAKGVTVDRLEAAQRHILPPPYVIKPLGEGSSFGVFIVREDQAYPPQELTRSDWAFGNRVLVESYIGGRELTCAVIGEKAHDVIEIKAVGGGWYDYDAKYRKGGSIHILPAELKRNIYQNVQLLSLKAHKALGCRGVSRTDFRYDDRPEGTGELIVLEVNTQPGMTETSLLPEIAAYAGLSFGELVRWMVDDASCDR | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33305
Sequence Length: 307
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q8G7C4 | MRLLCAAFRARFGPVGGAKHRLENGCSFNKRMVMAKKRVVVLYGGRADEHSISCISTAGVLGAMDTERFEPIPVGITKDGKWIINGEDPRGWNLDGGELPTVKITPESRPVMLDPSRGQDGFFIGEPSHINSADSGFGTSFVSMSDPEMHHVLTSLGHVDAVLPVLHGPYGEDGTVQGLLEMMGVPYVGCGVFASAACMDKHYTKVVLDAAGIPTAPGVTVDARNFTAADVLAEIEDAGLTYPLFVKPSRAGSSFGVTKVEKADDRETQQDRLAAAIATAGEHDWKVLVEQGIDGREIECAVLCPKAGDEPEASWPGEIV... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 46045
Sequence Length: 428
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q492J5 | MSKLCIGIICGGRSLEHEISLKSAMCIAQFIDKFRFEAMILWIDKKGCWHLKDIDFNDLSYHKDEKISILLQNCPYPFKFHTKNINILLKFDVIFPVVHGTLGEDGALQGLLCMMNLPFVGSNVLSSSVGMDKDVSKCLLRDAGLSVVPFRTVLAQDQHNIDFDYFVSIFGLPLFVKPSNQGSSIGVSKVTKCKDFNLALIKAFSFSNKILIEPAIIGRELECAVLGNDNPKISVCGEVILSDNNFYTYHDKYVKRKAQIMIPALINDAISDDIRHIALRAFQVLNCSGMARVDVFLNLDNKIFINEVNTLPGFTFDSMY... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 41585
Sequence Length: 368
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
O51218 | MKKNLMLIFGGVSFEHEISCKSAYSIYLALLDLNKYNIYPVYIDKCTGVWYLLDSVSDPPKPINTDVLPIVSLLPGFGIFSNNKNLEIDVVFPVVHGRTGEDGAIQGVLKVMDIPCVGAGIIGSAISSNKYFCKLLLKSFDIPLVPFIGFRQHDYFLDKEEIKRNVKEVLGYPVIVKPAVLGSSIGINVAYSENQIESFIKEALKYDLTIVIEKFIEAREIECSIIGNEKMKIFSPGEVVVQDFIFYDYDAKYSVIPGNSIIFNIPAHLETNQLLSIKEYAFLTYKNLELRGMARVDFFVEKKSGTIYLNEINTIPGFTD... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 40837
Sequence Length: 361
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q03ZI1 | MTKKRVALIFGGNSSEHDVSKRSAQNFYNAIEATGKYEIIVFAIAQNGFFLDTESSKKILALEDEQPIVDAFMKTVDASDPLARIHALKSAGDFDIFFPVVHGNLGEDGTLQGLFKLLDKPYVGAPLRGHAVSFDKALTKELLTVNGIRNTKYIVVDPESANNWSWDKIVAELGNIVFVKAANQGSSVGISRVTNAEEYTEALSDSFQYDYKVLIEEAVNGARELEVGVIGNDQPLVSEIGAHTVPNQGSGDGWYDYNNKFVDNSAVHFEIPAQLSPEVTKEVKQMALDAYKVLNLRGEARMDFLLDENNVPYLGEPNTL... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 41826
Sequence Length: 377
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q8Y8P1 | MKTKLILLYGGKSAEHEVSLQTAFSVINALDLEKFEAAPIYITNEGEWIQGPLLSGKLDFVEQLRFSATDTIKLATTESEKSEGEAISPAVLEADGQETVVFPLLHGPNGEDGTVQGLFEVLNIPYVGNGVLASSAAMDKIVMKKIFADAGIPQVPAVAVRLIDWKNYQEEMVAEMEEVLTYPVFVKPANLGSSVGISKATNKKELVDAMTEAFLYDRRVVVEQGVVAREIEMGVLGNDTPVCSVPGEILPEGAVATFYDYKAKYQDNNTALIIPTEVDPEILEQMKEYAIQAFLGLDASGLVRADFFLTEDNQLFLNEV... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 40669
Sequence Length: 370
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
A0L5M8 | MDWKQKKIGVLYGGLSEEREVSLRSGQALFVALQSLGYQVVAIDVDRHITKVLEREGIEVAVLALHGPMGEDGTIQGLLEFMGIPYTGPNVAASAICMDKGLSKRLFHSEGLPTPAWIELAGDHEEADELVDHFLGDFHGAAFVKPLDSGSSVGISRAVGKDELIRGVAKALSVSHRCMVERAIEGRELTLSILDGEAFPLIEIVPIDGFYDYDHKYTAGRTNYLVPAPNLDDKSLEAVVKIGLAAYHITGCRGLVRADFILDGEGTPWLLELNTIPGMTELSLAPKAAHAVGIEMPQLAERILQGARLK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 33548
Sequence Length: 310
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
A6VYJ6 | MSKTLKESVIAVIYGGRSAEREVSLQSGPLVAEGLRAKGYQVVELDLYGSNAALDPIVQLQSIEFDLAFIALHGGEGEDGRVQALLEMFGKPYTGSSPLACGLAMDKVLTKRFWNGIGIPTPAYLSFVDHANADLIEEQMSYPVIVKPSREGSTIGINKAMNRAELDDALIKALEYDSDILVEEFIDGPEFTVTVIDDVAYPPIGLKPAPDHKLYDYEAKYIADDTEYLLPCGLDEDDENELQMLALDAYRSLGCFGWGRVDVMRDQAGVFWVLEVNTAPGMTSHSLVPMAAKYVGIDYASLVEKIAQNAWDKVGRN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34724
Sequence Length: 317
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
C6C0B2 | MHVLLIAGGWSEEREVSLSGAKGIEQALLELGHDVEFVDPAKDFKNILLLAEHADFAFINLHGSPGEDGLIQAMLNQVNCPYQGAEPESSFLTLNKAATKTVFDHHGILTPKWELVCAADGCKGLQDLEPPVFIKPNSGGSSLGMTFARTAEELEKGIETVFSLGDSALVEEYTKGIEVTCGILDGEPMPLILINPPDNAEFFDYHSKYALDGAEEICPAPIDPVLTEQIQQITAKAHKLLGLTDYSRADFIISEGVPYLLEVNTLPGMTPTSLVPQAAKEAGYSFNELIAKLIELGQRKRK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32777
Sequence Length: 302
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q3A2G9 | MQRQELQQKKIAVLMGGLSAEREVSLRTGKAISQALTRCGYEVTDIDAGRDLAQQLEKTGVEVAFIALHGRFGEDGTVQGLLELADIPYTGSGVLASSLAMDKVATKKMLCYHGIATPGFAVMRRGQKICGTLPDYPLVVKPAREGSTIGISIVHDEQELAAGLEEAFRHDDLVLVEQFIAGAEVTVGVLDGQPLPIIQVVPKGGFYDYQSKYTPGQTEYLLPAPLPETLYGALQDSAVRVFEAIGCCGAARVDFMVTDTGFYCLEVNTIPGMTETSLLPKAANAVGMSFDELVERILAGASLRK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 32716
Sequence Length: 305
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q0AXT9 | MNKVLVLMGGTSEEREVSLKSGKAVYEGLKDAGYEVEALDFTPETIHRIREYSPDVVFITLHGKNGEDGTVQGYLELLGIPYTGSGVLASAVCMNKVITKKLLSYEGLPTADFQVIKKRGFNRDLFNPDLLMEDFGLPLVVKPATQGSSVGTSIVRKRKNIVPALELALSLDEEILVEKFIAGTELTVTVLGKDNLKTLPVIEIVPKNEYYDYESKYMPGMSDHLIPARISEEERERVEEISCKAYDAVGCRGYGRIDLILDRGGNPYILEINTLPGMTGTSLVPDAARAAGIKFPELLDLFVKMALEK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 34037
Sequence Length: 309
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
P73632 | MRVGLLFGGCSGEHEVSIKSAQAIAKALASDDNQTKYQVSPFYIQKNGVWLGPDVSQQVLDQGVPWGDQPVTAGQRWQFPPEAARMEVWFPILHGPNGEDGTVQGLFSLMQVPYVGSGVLGSCVGMDKLAMKMVFERAGLPQVNYMGVERGEIWSNPCVFPALCEKIEAQVGYPCFVKPANLGSSVGIAKVRNRSELEAALDNAASYDRRIIVEAGLTDIREVECAVLGNENPQASVVGEITYDSDFYDYETKYTDGRSQMHIPANLPKAVVNQIQTMAIQAFKAVDAAGLGRLDFFYQPTTGQIVINEINTLPGFTAFS... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 38774
Sequence Length: 354
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
B7IGP0 | MINVGLLFGSKSVEHEISIITAHQVLSFVDKNKYNIIPIYITKDGKWLTGKILEDLENFKNLERLEKKSKQISSISAKDGKLILHSNIKKITIDVCLLTFHGSNGEDGSIQGMLEFLNVPYTGCGMYSSMYTMDKVITKLILKEKNIPVVDFLYTNKKNYTNDFLNHCKEVLEYPMIVKPARLGSSIGVKKVNDKCELEEAIETAFSFDDKVIVEKWIDSRELNCAVMGYKNIVVSEIEEIKKQKDFFDYNEKYVQKGKKFSNHIIPAPIDENLKNTIKSIARDTFNALECHGNIRIDFLLSKDNKIYVNEVNSIPGALS... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Cell wall formation.
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Mass (Da): 42037
Sequence Length: 367
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cytoplasm
EC: 6.3.... |
Q9VIF6 | MSETSEDEQTQLQTSDEEEDLGSEEEQEDEDNNHKEGDSEAALSGEDDKGSEDDAAEEQKLTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKYKDVYLVHILNELAGNSFMIFCSTCNNTVKTALML... | Function: Part of a translational control module, also containing ath/DHX33 and ais/DDX52, which coordinates germline stem cell differentiation with ribosome biogenesis during oogenesis. This module allows for coregulation of ribosomal proteins and non1/GTPBP4, a p53 repressor, preventing p53 stabilization, cell cycle ... |
Q9H0S4 | MAAPEEHDSPTEASQPIVEEEETKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLAT... | Function: Required for efficient ribosome biogenesis (By similarity). May have a role in mRNA splicing . Involved in apoptosis .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 50647
Sequence Length: 455
Subcellular Location: Nucleus
EC: 3.6.4.13
|
Q55BR9 | MSDKTFEELGLTTWLVANCKQLGFKAPSNIQANTIPEILKGRDIIASAKTGSGKTASFAIPILNQLSEDPYGVFAVILTPTRELAVQIGEQFNAIGAPMNVNCSVVIGGIDNVTQALILDKRPHIIVATPGRLASHLNNGLKIALKFCKFLVLDEADRLLGEDFELEIASILEHLPPPEKRQTLLFSATMTKNLTKLDSIALNKPFIFEDNSKYDTVDTLKQEYIYMPAPTKDCYLVYILKKHEGSSAIVFVNNCYAVEAVKGMLNKLDIPSVSLHSFLDQKSRLAALKTFKSGKVKVLVATDVASRGLDIPDVQIVINY... | Function: Probable ATP-binding RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 57104
Sequence Length: 508
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
EC: 3.6.4.13
|
Q07886 | MQRKEANPFQILGLRPWLVKQLTKLGLKGATPIQQKCIPAILAGQDCIGAAKTGSGKTFAFALPILERLSEEPVSHFALVLTPTHELAYQISEQFLVAGQAMGVRVCVVSGGTDQMVESQKLMQRPHIVVAMPGRLADHLTGCDTFSFDNLKYLVVDEADRMLNGDFDESLSIIERCLPKTRQNLFFSATMKDFIKESSIFPIASDCFEWSQDSDVATVETLDQRYLLCADYDRDMVLIEALRKYREENENANVMIFTNTKKYCQLLSMTLKNMEIDNVCLHGFMRQKERVAALSRFKSNQIRTLIATDVAARGLDIPSV... | Function: Probable ATP-binding RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 59678
Sequence Length: 521
EC: 3.6.4.13
|
Q61496 | MGDEDWEAEILKPHVSSYVPVFEKDKYSSGANGDTFNRTSASSDIGESSKKENTSTTGGFGRGKGFGNRGFLNNKFEEGDSSGFWKESNNDCEDNQTRSRGFSKRGGCQDGNDSEASGPFRRGGRGSFRGCRGGFGLGRPNSESDQDQGTQRGGGLFGSRKPAASDSGNGDTYQSRSGSGRGGYKGLNEEVVTGSGKNSWKSETEGGESSDSQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIVLAGRDLMACAQTGSGKTAAFLLPIL... | Function: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity . Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes compos... |
Q91372 | MEENWDTEIETEKPTYVPNFSTLETENTDNYSAYSNNDINNQNYDSERSFGNRGGYRSERSRPSNFNRGSRTERGRGRGFGTNRNDNYSSERDVFGDDERDQRRGFPGRGGYNGNEDGQKPNAFRGRGGFRNENEQRRGFGERGGFRSENGQRNFDNRGDFGNSGEEEDRPRSYGRGGFNNSDTGGRGRRGGRGGGSQYGGYKGRNEEVGVESGKSQEEGNEKDEKPKKVTYIPPPPPDGEDNIFRQYQSGINFDKYDEILVDVTGKDVPPAILTFEEANLCETLRRNVARAGYVKLTPVQKHSIPIIMAGRDLMACAQT... | Function: Probable ATP-dependent RNA helicase required during spermatogenesis . Required to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by formi... |
Q9BQ39 | MPGKLLWGDIMELEAPLEESESQKKERQKSDRRKSRHHYDSDEKSETRENGVTDDLDAPKAKKSKMKEKLNGDTEEGFNRLSDEFSKSHKSRRKDLPNGDIDEYEKKSKRVSSLDTSTHKSSDNKLEETLTREQKEGAFSNFPISEETIKLLKGRGVTYLFPIQVKTFGPVYEGKDLIAQARTGTGKTFSFAIPLIERLQRNQETIKKSRSPKVLVLAPTRELANQVAKDFKDITRKLSVACFYGGTSYQSQINHIRNGIDILVGTPGRIKDHLQSGRLDLSKLRHVVLDEVDQMLDLGFAEQVEDIIHESYKTDSEDNP... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82565
Sequence Length: 737
Subcellular Location: Nucleus
EC: 3.6.4.13
|
Q6DRI7 | MALFTINRYLGEEEEEDSEKQSRSKALLAKLQKQVKARGQQSVSNTPKEEEEQQDDKEHKKRKHKLQETKGKIKKSESVQNTDPTEEADSSVKKKKKRKKSLSTEDVIVKIEENESENEKSVDITGPTPSSPVQFKAEKAEELTSSSQSNYQVLGGFKEKDVQKVKRVLPQWLSQPDVIQKDIKSNLIPISEVPGICPTLLRKLQTNGIQSFFPVQAEVIPAILESVGSGLLVGPGGYRPRDVCVSAPTGSGKTLAFVIPVVQALSKRVVRQVRALAVLPTKELAQQVSNVFSAYTEGSSLKVVMITGQKSFAAEQTALS... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72460
Sequence Length: 652
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolys... |
Q54BD6 | MTTINYNENINNNNNTLESFGIEEWLINNLKEQSIINLFPVQQEIVPFINRTEGHDICVCAPTGSGKTLAYAIPLVQKIVKRVVRRVRVAVIVPTHDLVIQVEKTFQSIIKGTDLVVLSLGVKPFHIEQKLLIKNHSYGEHALYESLVDIIVSTPGRIVDHINETLGFTLKYLNYLVIDEADRLLRQSFQDWLEIVIDSTNQHSDLNQQQEEQLIKYNSKGDIELFEKSISLKDNNNQMNHLCWSEFKLVKLLLSATMTYNPSKISLLQLNAPLFFTTSKTKEIKYSMPSTLKECYIISNGDQKPLVLLNIIYESLLKNN... | Function: Probable ATP-binding RNA helicase which may be involved in ribosome biogenesis.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 64642
Sequence Length: 563
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydroly... |
Q9NUI1 | MAQPPPDVEGDDCLPAYRHLFCPDLLRDKVAFITGGGSGIGFRIAEIFMRHGCHTVIASRSLPRVLTAARKLAGATGRRCLPLSMDVRAPPAVMAAVDQALKEFGRIDILINCAAGNFLCPAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFFRDHGGVIVNITATLGNRGQALQVHAGSAKAAVDAMTRHLAVEWGPQNIRVNSLAPGPISGTEGLRRLGGPQASLSTKVTASPLQRLGNKTEIAHSVLYLASPLASYVTGAVLVADGGAWLTFPNGVKGLPDFASFSAKL | Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chai... |
Q9WV68 | MAQPPPDVEGDDCLPEYHHLFCPDLLQDKVAFITGGGSGIGFRIAEIFMRHGCHTVIVGRSLQKVTTAAKKLVAATGKRCLPLSMDVRVPPEVMTAVDQALQEFGKINILINCAAGNFLCPASALSFNAFKTVVDIDTIGTFNVSSVLYKKFFRDHGGVIVNITATLSMRGQVLQLHAGAAKAAVDAMTRHLAVEWGPQNIRVNSLAPGAISGTEGLRRLRGSNASSKLKHFSNPIPRLGTKTEIAHSVLYLASPLASYVSGIVLVVDGGSWMTFPNGIKQLLEFESFSAKL | Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chai... |
Q9Z2M4 | MTQQPPDVEEDDCLSEYHHLFCPDLLQDKVAFITGGGSGIGFRIAEIFMRHGCHTVIVSRSLPRVSEAAKKLVAATGKRCLPLSMDVRVPPAVMAAVDQALKEFGKIDILINCAAGNFLCPASALSFNAFKTVVDIDTLGTFNVSRVLYEKFFRDHGGVIVNITATLSMRGQVLQLHAGAAKAAVDAMTRHLAVEWGPQNIRVNSLAPGAISGTEGLRRLGGPKASSKFKYLSSPIPRLGTKTEIAHSVLYLASPLASYVSGIVLVVDGGSWMTLPNDIGRLLEFESSSAKL | Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chai... |
Q22230 | MACKNPKKFFPICNSPILRDGALKGKVALVTGGGTGIGKAIATTFAHLGASVAIAARRMEKLEQTAEEIMKTTGGICEPFRMDIKDPGMVSDTFDKIDKKFGKHPDILVNNAAGNFIMATERLSPNAHGTIIDIVLKGTMNVTTELGKRCIQSKTGASVTSITAAYARSGAPFIVPSAVSKAGVEIMTKSLATEWSKYGLRFNAVSPGPIPTKGAWGRLFSGEMGDVAEKMKELNPEGRSGTPEEVANLVAFISSDHMSFMNGVIIDLDGGQQHFNHGSHMGDFLHTWDQDTWGDVENVIRGRTGKEKP | Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Catalytic Activity: a (2E,4E)-dienoyl-CoA + H(+) + NAD... |
Q16698 | MKLPARVFFTLGSRLPCGLAPRRFFSYGTKILYQNTEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISGEFNDLRKVTKE... | Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Catalytic Activity: a (2E,4E)-dienoyl-... |
Q9CQ62 | MALLGRAFFAGVSRLPCDPGPQRFFSFGTKTLYQSKDAPQSKFFQPVLKPMLPPDAFQGKVAFITGGGTGLGKAMTTFLSTLGAQCVIASRNIDVLKATAEEISSKTGNKVHAIRCDVRDPDMVHNTVLELIKVAGHPDVVINNAAGNFISPSERLTPNGWKTITDIVLNGTAYVTLEIGKQLIKAQKGAAFLAITTIYAESGSGFVMPSSSAKSGVEAMNKSLAAEWGRYGMRFNIIQPGPIKTKGAFSRLDPTGRFEKEMIDRIPCGRLGTMEELANLATFLCSDYASWINGAVIRFDGGEEVFLSGEFNSLKKVTKE... | Function: Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA.
Catalytic Activity: a (2E,4E)-dienoyl-... |
A2QI25 | MADSLKMGNLSLNESQHAPAPAPSTGRAAYIPPHLRGRQMGGNMDGAAAAAPPPGPAAGPGNSWGGPRGGPRGGQWANANAPDFSPRGPNGNTSWSPHEARRPFNPNAYGHPGHGGSYGSGGGSARGSGDGQWRDGKHIPGPANPRLERELFGLPNDPTKQNTGINFANYDDIPVEASGHDVPEPVNAFTNPPLDDHLIENIKLAHYQTPTPVQKYSIPIVMNGRDLMACAQTGSGKTGGFLFPILSQAYQNGPSAAPAQAGGQFGYGRQRKAYPTSLILAPTRELVSQIFDEARKFAYRSWVRPCVVYGGADIGSQLRQ... | Function: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 72132
Sequence Length: 678
Domain: The ... |
Q9K4A0 | MAQQDTDQQHPGVLPVDDEGFVVDSQDCEEREADWRGRGTSRPITVVGNPVLHKECEDVTDFGEEFQQLVADMFASQRTAEGVGLAANQIGVSKKVFVYDCPDDEGVRHVGVVCNPRLVELPADRRRLDDSNEGCLSVPTAYAPLARPDYAEVTGQDEKGNPVKVRGTGYFARCLQHETDHLYGYLYIDRLSKRERKDALRQMAENEPRYPVVAND | 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.
Catalytic Activity: H2O... |
Q01523 | MRTIAILAAILLVALQAQAESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRTGRCATRESLSGVCEISGRLYRLCCR | Function: Host-defense peptide that maintains sterility in the urogenital system . Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes . Confers resistance to intesti... |
B3ETT4 | MIYPIVPYGESILRQTAAPIELGTDLETLIESMFITMNAAKGLGLAAPQIGKSIQLFVVDVSPFVGDGMVQPDKHRKVYINPVLEIYQPNTITHYEEGCLSIPGIYVDVPRNKRVRIKFFDRNWQAQEEDLVDMPARVVQHEYDHLYGKLHIDYLRADRRLRLKSKLENIKQGRVEVAYKMSFTGNKV | 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.
Catalytic Activity: H2O... |
O66847 | MVRDIVIYPNEILKKPTEKVDVIDKEVKNLIRDMFDTMYEAEGVGLAANQIGVPLSVMVIDTSPKEDAPPLKLVLINPEIKEGEGKIKYKEGCLSFPGLSVEVERFQKVKVNALNEHGEPVELTLEGFPAIVFQHELDHLKGITFVDRLKGWRRRMALEKYQKLLKSRK | 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 (By similarity).
Catalyt... |
Q8AAP4 | MILPIYVYGQPVLRKVAEDITPEYPNLKELIANMFETMVHADGVGLAAPQIGLPIRVVTITLDPLSEDYPEFKDFNKAYINPHIIEVGGEEVSMEEGCLSLPGIHESVKRGNKIRVKYMDENFVEHDEVVEGYLARVMQHEFDHLDGKMFIDHLSPLRKQMIRGKLNTMLKGKARSSYKMKQVK | 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.
Catalytic Activity: H2O... |
A1UUB4 | MPIKPLVILPDPILREISKPVEHIDSTIQQLADDMLETMYNAGGIGLAAIQVGIPLRMLVVDVSIFTSIFEPDAPQDPIIVINPEILWLSDERNICMEGCLSIPGYSAEVERPKRLCIRYRNREGEQKEIEADNILATCLQHEIDHLNGCLFIDHLSKVKRNMVIRKFEKRAKENNLEKEIL | 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.
Catalytic Activity: H2O... |
A9ILK4 | MPMRSLVTLPDPILREVSKPVEQVDTALQELADDMLETMYHAKGIGLAAIQIGIPLRMLVIDVSGNAEDTQKKPLVIINPEILWLSDERNVYKEGCLSIPDYFAEVERPKRLRVRYQNREGKQKEIEADDLLATCLQHEIDHLDGRLFIDYISRIKRDMVIRKFKKRAKEKNTQEAVL | 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.
Catalytic Activity: H2O... |
Q8EVJ8 | MFKKLDPSPKWIVYDNNPVMHKPIEDVVFPLTKEDEHVISQMLSYVDASYEGEADKYDIRAGIGIAAIQLGCPKKIIYIHLDDKNGEHKYLMANPKIIKESTSKMYLKNGEGCLSVKKDHKGLSIRKSIVWVKGIDLFTNKEIEVKATDLLAACFQHEVDHNNNKFYYNRINESDPYYVEKNWEEI | 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.
Catalytic Activity: H2O... |
Q0ASK2 | MAIREILTVPDPILKEVSQPVDQVDDDLRELMDDMLQTMYAADGIGLAAIQVGVPKRVIVMDLAGSDEEAKPRYFVNPVLSDPSDTLKPYEEGCLSVPTVYDEIERPDRIHIQYLDYDGNECEEIAEGMFAVCIQHEMDHLEGVLFIDYLSRLKRQRAVQKVKKVEKSKDRDAA | 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.
Catalytic Activity: H2O... |
B3DUG9 | MILKLVLYDNPILRKKGMPIDSFDDRLKRLVQDMLETMAYYKGVGLAAQQVGLNLQLAVIDVSGSKLSSSLLIGGKPAMVEEHMPLFLINPTLSYTQSKEISNEGCLSFPGLRIDVPRSKRVKVKTFDLEGRPWYFEAGGFLSVAIQHEFDHLQGKLFIDYLSAEQKKAIKEELEKIKRGEAILSVKETD | 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.
Catalytic Activity: H2O... |
B8ENG6 | MPLRPIIILPDKRLRLVARPVASVDSEVRALMDDMLETMYEAPGIGLAATQIAVDRRVIVLDVAKRRDDSAKADPICLANPEILWASEELSSYEEGCLSIPEFYEEVFRPEKVRVGYLDRDGRRREIEADGLLATCLQHEIDHLNGVLFIDHISRLKRARIIKKFEKAAKLDAQEPKRAPHSPHTDAQKPGAASDL | 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.
Catalytic Activity: H2O... |
Q2RK25 | MAIHKILTLGDPLLREKSQPVRKITSNVWKLLDNLADTMYDAPGVGLAAPQIGVLKRVIVVDVGEGLTELINPEVIAASGEEVGAEGCLSIPGAQGEVPRAAVVTVRGLDRHGRVREIRAEGLYARALQHEIDHLDGILFIDKVVRWLENQPGER | 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.
Catalytic Activity: H2O... |
Q7NAK8 | MKSKLKPTNDWLVTDDNPKMREVCTEVKFPLSQEVLDIIDKMLAYVDESFDDNAEKYDIRPGIGIAANQLGLNQRFFYVHFTDFCQKEHRYLLINPEWIDKSLNKAYLAVGEGCLSVPKDKDGYVIRSETVKLKGFDYLTQKDVEISAHGLLAMCLQHEMDHLEGKFYYDSINMMKPYFKKDEWVSIDQKVCDQCK | 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.
Catalytic Activity: H2O... |
P47352 | MTFQPTKTWLVFDDNALINKPTEAVNFPIDEQIETCIKKMIAYVDASYDGKAQEYDIIPGIGIAANQIGYWKQLFYIHLNDLNKEKKCLLINPKIIDQSENKAFLESGEGCLSVKKQHKGYVIRSEWITIKGYDWFEKKEITIKATGLFGMCLQHEFDHLQGRFFYQRINPLNPWFKKPEWKVINPTLKTSNG | 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 (By similarity).
Catalyt... |
O83738 | MELKFLGEPCLTTVSEPVSEVDEQLRAFISGMFRVMRGAGGVGLAAPQVGRTVRVFVVDVEHHVRAFINPQITAASEEQSSYEEGCLSIPHIYERVLRPRRVSVQYLDENGKRCAVDADGILARVIQHEYDHLDGILFLDRIDEKRRDDALRRYAALRGTIR | 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 (By similarity).
Catalyt... |
Q83GH8 | MSQDRRYTGCNTHSNTHSAQDREKEGAVPKISGGKILPIYITGHAVLHAPAKPVTDFSGIQEIVRDMFATMFAAPGVGLAGPQIGLGLRIFVYSYTEGDTLHQGVAINPDLLIPKGVPKRQTNKQQANNSTSCDEPDREGCLSFPGYQFPLERAPQVTLSAFDENKKPFTVHATGWLARIFQHEFDHLQGTLYVDRLAQKYSGEVRQAVLNNKWGIPGKYWVPQEPKE | 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.
Catalytic Activity: H2O... |
B1AJA6 | MYNIKFLDLLNSNLKPNPQWIFKDPHPILREVTQDIEGNELSKDDIYYLKKMVRYIDVCYHNQAKKYKIRSGIAIAANQVGWNKRATYIHFNDEAKEHHYLLINPHIIKRSSEIAYLNPGEGCLSVDDDRSGYVIRNKKVHVKAYDLISEQFIDQEFSGIIAICIQHEIGHLDAGLYYDNINQQQPFYADPSWTKIGR | 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.
Catalytic Activity: H2O... |
Q5GTG9 | MPKLSIVVAPDERLTTRASEVTGINDKIKELVNDMFETMYNAEGLGLAAVQIGVLKRIFVMDIQLEDIKGEPVGYESTGKFCMINPEITELSDEQVILKEGCLSIPEQSHEIRRPKYLTVKYKDLNNKEQTLKASGWLARCIQHELDHLNGILYIRHLSKLKYDMAMKKAEKFKRHYER | 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.
Catalytic Activity: H2O... |
A3DD83 | MKRAIIIVLDSVGMGELPDAAKYGDEGSNTLGNIAKNLPDFSLPNLESLGLGNIDGMTGYEPSKNPLGSYGRMAEKSAGKDTTTGHWEIAGLILDKPFPVYPNGFPEDIIKRFEDSIGTKTLGNVPASGTEIIKLLGDEHVKTGYPIVYTSADSVFQIAAHENVIPVERLYDMCRTARNILTGEHAVGRVIARPFIGESGNYKRTDRRKDFSLAPVGKTLLDYAVENGYKVKAVGKIEDIFGGRGITESVHIHDNMDGVDRTLEYMRDDFEGILFTNLVDFDMLYGHRNDIAGYANALKEFDRRIPEILANLREDDLLVI... | Cofactor: Binds 1 or 2 manganese ions.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 42588
Sequence Length: 388
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosyn... |
A9NG16 | MRFKRVFLIVMDSLGVGASEDANQYFNEGVDDTKANTFGHIAESMDLRIPNLEKLGVGNIIPIKGTKSVELSSSYVTKIREKSLGKDTMTGHWEIMGLYVTTPFQTFTDTGFPKELLDELEERTGRKIIGNIAASGTEILKDLGEEHMRTGDLIVYTSADSVLQIAMHEEIIPIEEQYRISAIARDITMRPDWKVGRVITRPFLGTNKDNFKRTSNRKDYALKPSEETTLNFLSDANYDVIALGKINDIFDGYGINKYSKTVSNDDGMKQITEWAKKDFTGLCFLNLVDFDALYGHRRDPHGYGKAIMDMDSQLPELMAN... | Cofactor: Binds 1 or 2 manganese ions.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 44505
Sequence Length: 397
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosyn... |
B8E109 | MKRAILIVLDGVGIGELPDAFKYNDEGSNTLVNTAKVVGGLNLPNMGKMGLSNIEEIPGIPKEEDPIALYGKMAEASPGKDSTTGHWEIAGLILEKPFPVYPNGFPKEIIEAFEKAIGRKVIGNKPASGTEIIKELGEYHMKTGYPIVYTSADSVFQIAAHEDVIPVEELYRMCEIARAMLQGDHAVARVIARPFAGSPGNFYRTPRRRDFSLPPFKPTLLDYLKQNDYDVIGVGKIEDLFAGKGLTSSFHQENNTEGINNIFKAWEKLREGLIFVNLVDFDMLYGHRNDPQGMTRALKEFDDALPDVMGLLSDFDLLII... | Cofactor: Binds 1 or 2 manganese ions.
Function: Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Catalytic Activity: alpha-D-ribose 1-phosphate = D-ribose 5-phosphate
Sequence Mass (Da): 43758
Sequence Length: 394
Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosyn... |
Q65H59 | MTKQIARMIDHTALKPDTVKSEIEALCKEARVYGFASVCVNPCWVKLCAELLKESEVKVCTVIGFPLGAASPETKAFETRQAIADGAGEVDMVINIGALKDRDTGTVEHDIRAVTDAADGKALVKVIIETSLLTDEEKRLACELAVKAGADFVKTSTGFSGGGATVRDIKLMREAVGPDIGVKASGGVRDKESALAMIEAGATRIGASAGVSIVKGLTADEDY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23373
Sequence Length: 223
Pathway: Carbohydrate degradation;... |
Q6A8F1 | MSIAALIDHTLLAPDVTAQHIRTLCREAVDHGFATVCVSPTRVRLAADELAGHAPRVCSVIGFPSGAHLSEIRAAETKAAVNDGADEIDMVINVGAVKDDDWDTVESDISAVVDAAGMAIVKVILEVSELTDEEITRACQAAERCGADFVKTSTGYSRHGATAEAVSLMRRTVGDRLGVKASGGIRTHNDVATMLRAGATRIGASAGVALLVDEEAL | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 22617
Sequence Length: 217
Pathway: Carbohydrate degradation;... |
Q6GKG7 | MKFEKYIDHTLLKPESTRTQIDQIIDEAKAYNFKSVCVNPTHVKYAAERLADSEVLVCTVIGFPLGASTTATKVFETEDAIQNGADEIDMVINIGALKDGRFDDVQQDIEAVVKAAEGHTVKVIIETVLLDHDEIVKASELTKAAGADFVKTSTGFAGGGATAEDVKLMKDTVGADVEVKASGGVRNLEDFNKMVEAGATRIGASAGVQIMQGLEADSDY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23501
Sequence Length: 220
Pathway: Carbohydrate degradation;... |
Q6GCY6 | MKFEKYIDHTLLKPESTRTQIDQIIDEAKAYNFKSVCVNPTHVKYAAERLADSEVLVCTVIGFPLGASTTATKAFETEDAIQNGADEIDMVINIGALKDGRFDDVQQDIEAVVKVAKGHTVKVIIETVLLDHDEIVKASELTKAAGADFVKTSTGFAGGGATAEDVKLMKDTVGADVEVKASGGVRNLEDFNKMVEAGATRIGASAGVQIMQGLEADSDY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 23501
Sequence Length: 220
Pathway: Carbohydrate degradation;... |
Q2SRA7 | MEIKLNKYIDHTLLKPEATKQDIINLCNQAIQYDFATVCVNTCWTSFCKELLKNSNVGITNVVGFPLGACLTEVKVFEVKKAIENGCDEIDMVLNIGALKDKDYDLVLNDMKEVKKAANDHVVKVILENCLLTREEIIKACELAVEAGLEFVKTSTGFNKSGANIEDIKLMSKVVKNKAQVKAAGGVRTYDDAIAMINAGASRLGTSGSVEIMLKQENKSNY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24400
Sequence Length: 222
Pathway: Carbohydrate degradation;... |
Q6MSE7 | MEIKLNKYIDHTLLKPEATKQDIINLCNQAIQYDFATVCVNTCWTSLCKELLKNSNVGITNVVGFPLGACLTEVKVFETKKAIENGCDEIDMVLNIGALKDKDYDLVLNDMKEVKKAANEHVVKVILENCLLTKQEIIKACELAVQAGLEFVKTSTGFNKSGANVKDVKLMSEVVKTKLKLKLLVELELMMMQSQW | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 21958
Sequence Length: 196
Pathway: Carbohydrate degradation;... |
P09924 | MKLEYNRIIDSTLLKADTLPHEIDALCADAHKYQFYAVCVNPSYVRYAKNILKGTGVKLCTVVGFPLGQTTQRQKVYETKIAIKEGADEIDMVMNIAEFKKRCACVISEIRAVKKVCGKRTLKVIIETALLNQDEIRDAVNVCIDGNADFVKTSTGFSMRGASLEDITIMREASGNLIKIKASGGVQTAQQFLDFFNAGVSRIGTSNAVKIMEELHKLESHEHR | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24878
Sequence Length: 224
Pathway: Carbohydrate degradation;... |
Q98QP7 | MELNKYIDHTLLKPEAKSKDIDKLIDEAKKYNFKAICINSSWVKYAKEKLKDSDIKIASVIDFPFGAAITQAKVQEAKLAISHGASEIDMVMNIGKFKDGDYEYVLNDIKSVKKVMGSNILKVIIETALLNEKEIIKACQIVLNSGAEFVKTSTGYSYRGASESDIEIMKKTVGDKVLIKASGGIKNQESLKKMIELGSSRIGTSSSVALMENQEIKKGY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24325
Sequence Length: 220
Pathway: Carbohydrate degradation;... |
Q4A5W6 | MNFNQLIDHTYLKPEATKKNIDNLIMQGFEHNFFSVCVNSIWVKYVKEKIKKLNSNLKITAVVGFPLGASITQAKAHEAKLAVEHGADEIDMVIAVGFLKQKDYEYVLNDIKSVKKAIGNKVLKIIIETALLTKEEIKKATEIVLKSGAEFIKTSTGFSYRGASLDDVVTMKSVIKDQKLEIKAAGGISTLEDMQKMHEAGATRFGLSKSVEILKNQKVETKY | Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Catalytic Activity: 2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde 3-phosphate
Sequence Mass (Da): 24855
Sequence Length: 223
Pathway: Carbohydrate degradation;... |
Q89A58 | MVTPHINAKKGDFSDCVLMPGDPLRARYIAKNYLKNAIEVTNIRSMLGYTGRYKGHRISVMSHGIGIPSSLIYVKELVSEYNVKKIIRIGTCGTVIEHININDIIICLGASTDSKVNRLRFHDNDFSSVADFYLILDLFNSANNAGIKINIGNFFTTDLFYVKNDKLLDTLQRYNILGIDMETAGIYSLASELGIQVASICTVSDHILKKDQMSYIDRESNLNNMIYISLEALILKKV | Function: Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphat... |
K9L8K6 | MALYREGKAAMAADGTVTGTGTKWQSSLSLIRPGATIMFLSSPIQMAVVNKVVSDTEIKAITTNGAVVASSDYAILLSDSLTVDGLAQDVAETLRYYQSQETVIADAVEFFKNFDFDSLQDLANQINADSESAQSSAAAAAASENAAKTSENNAKSSEVAAENARDQVQQIINDAGDASTLVVLANPDGFRHIGRCKDIATLRTIEPVESRQVIEVLSYYNGLAQGGGTFWYDPNDSVTEDNGGSCIVTNGGKRWKRIIDGAVDVLSFGAKPDDISFDSAPHIQAALDNHDAVSLYGRSYYIGSPIYMPSRTVFDGMGGK... | Function: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K63-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membra... |
A0A3T0ZBZ8 | MDQDIKTIIQYPVGATEFDIPFDYLSRKFVRVSLVSDDNRRLLSNITEYRYVSKTRVKLLVATGGFDRVEIRRFTSASERIVDFSDGSVLRAADLNVSQLQSAHIAEEARDVSLMSMLQDDAGNLDAKGRRIVNLSDPVADSDAATKGYVDEGLEHTLRFSESTVQPLPPLSLMDGKILAFSGGKPIGILPESGSAADVLVELSKVSGYNLIGKATSFANMRSASGLKVGDVVLLTSYYEGGTTGGGEFLVKAGSAVDDGGHICVPSGSTNIYLERITSEVHLLDYGILTELNGTGARIDMSGKLQSAINRAKSAVMPLV... | Function: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the KN4-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membra... |
A0A7S6R613 | MDQDTKTIIQYPTSGDEYDIPFDYLSRKFVRVSLVSDTQRILLDNITDYRYVSRTRVKLLVSTDGYSRVEIRRFTSASEMVVDFSDGSVLRATDLNVSALQSAHIAEEARDLFSTSLSIGQLSYFDAKGLQIKNVAAGVDNTDAVTVQQLNKIIADVVTTIPDSVADNIRGLWARVLGDIGITLVDGSFETGATITTRTQALWSISGRKCYTWAGALPKVVPENSTPESTGGISETAWVDSSSKALGVLLAGPSGAERVGLKQGGTVQDAINWLTFDSFDIVKDGSKDVTADIMAACVVANDLGLDIKQNDGTYLVSGNP... | Function: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the KL64-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membr... |
A0A7S6R611 | MDQDIKTVIQYPVGATEFDIPFDYLSRKFVRVSLVADDNRRLLSNITEYRYVSKTRVKLLVETTGFDRVEIRRFTSASERVVDFSDGSVLRAADLNVSQLQSAHIAEEARDSALMAMPQDDAGNLDARNRRIVRLAPGIDGTDAINKNQLDTTLGEAGGILSDMKDLEGEIHDYIEKFADDTSVVRGVAWVYNLGSANGGENVITINKPTRTYAVPYIEVNGSRQEVGYHYQFDLNTQSISLVKPLEKGDFLMAMTTESSVPLESMLASAAGASSVGKLGGGTVQDFITNTESKFGSFSVLEDFGPVGTPEDTAATLLSS... | Function: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the KL47-type polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membr... |
Q8PV96 | MSAGIRTYLELMRYKNCLMAGFAAAIGTLIAFNILISGTSTPNFEDAFPFLDAGLVFLVVFLVSGAGNAINDYFDIKIDSINRPERPIPSGRVKAKEAFYFSYLLFALGTLIAFSINSICGSIALFNSLLLILYAKTLKGTPLLGNLSIGYLTGSVFLFGASIFGFGGIKALSVLFLLAALAITAREIVKDIEDMEGDSLEGADTLPLRIGAKKAGYLAVLTGLLAVILSPLPYFMSVLGLRYIYLVSLADLGFLAAIIQLLVRNNPTKSSKLFKIAMFFALIAFIAGV | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
A5ULR8 | MNPYVEIIRPGNVIMAIIAVILVAILAKSVDIPIILAMLAVFFAMSAGNVINDYFDYKIDLINKPQRPIPSGRISLDNAKNYAYLLFILAAIVGFLISCLVDTWIPCTIVIFSDIILYLYAYKLKSTPLIGNLTVGFMTGLCFIFAGYTFNEGLIIYESYLLAFFALIMTTAREITKDIEDMEGDMAEGAKTFPILYGPKISAIIAISLIIIDCALCPLLYIYHIFNINYLIVVSIAVLIFLYGAVLLRNQDSKTANKVSKYLKTGMLIAFIAFAIGTFTITF | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
O27170 | MNPYIEILRPVNAVMAVITVMLMALITGRFDFSVLLASVVVFTATGAGNVINDYFDHEIDAINRPERPIPSGRISRGVAGVYSIILFALASLMGFYLGLLPGLVVVSSSLLMVYYAWRLKKRCLVGNITISFLTGLSFVFGGIVLGEVRASILLGFYAFLMTMAREIVKDMEDVEGDRAEGATTLPITHGMRISGVLAASFMLIASLTSPSLYLLGIFSALYIPVLLLAVAVFLRAAIMILRGQDRATASRVSRMIKVGMALTFIAFAAGSGTITALTGLS | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
A0B8A0 | MTLLEIMRPANCVMAGAASLTGMLVSGALLQSLHTPVLVFSAVLLITGGGNAINDYFDREIDAVNRPDRPIPSGRISPRAALIWSVALFIAGCLIAGLINQSCLALALLNSFVLIIYAARLKGLPVAGNIAISYLTGTTFLFGGLAASPSSITAFLSILSALATLSREIVKDIEDLPGDLAHGAKTLPAFIGKRKSFVLASLVLIVAMLLSYLVPLGIDYQAAVSIANLAFLLSIKRMLCGDASGSQRWIKMGMGMALVAFLIGYHI | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
Q3INH7 | MERVRGLVELLRPGNAVAAGGLTFIGAFVAGGLSSPQSMAFAVVATVLATGAGNAINDYFDRDIDAINEPDRPIPRGAVSPRGALVYSVALFAVAVVLTLLLPWLAIAIAAINLVALVAYTEVFKGLPGVGNALVAYLTGSTFLYGGAAVGGDLAAVVVLFALAACATMAREIVKDVEDIDGDRAEGLRTLPIVIGERRSLYVAAGFVVVAVLSSPLPYLLGLFGWVYLVVLVPALCGLAAATWRSFSDPTTGQAWLKASMFAAAVAFVIGRLAVVA | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
Q9V2P5 | MEVKAFIEIMRPHNCILAGVVGILGSLVAYEGIPSIEKLGLVFLVVYLGCSAGNTINDYFDVEIDRVNRPNRPIPRGAIPRKVALYYALLQYMLGLALARFLGVEALLFALGAYALTFIYAWKLKPLPFIGNVAVALLTAATPIYGALGVGRVGLAGYLAICAFLVNVSREIMKDIEDIEGDMKMGAKTLPIIIGKRRAAMISSIFGVLTVITSFLPVKVGIGLGYAPIILVDAMILKASIDVVKNPESASKGQKTLKIATFIAVISFLLGALTKGV | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
Q9UWY6 | MSLKSYMQLVRIHNVIGAALGAIMGFLVSSQWYLELKGILLSALVVGLIAAGGYVINDVYDVEIDKINKPYRPIPSGKISVNKAKALSIALFIIGIALSILLNIYALVIALVTAIGLIYYAKDLKKTGFYGNLLVATTTALSIFYGGLAFFSDNWLLRIIIPTLYAFFLTLIREIVKGIEDYNGDSLNNVKTLATTLGINKSWRIAKILLVLLLIISPLPFFIGFNLIYLILLILVFIPFTILSIIQKETIEGASKARTYLKISAISGIIAFLLGSLPFFKG | Cofactor: Magnesium. Can also use Ca(2+), but less efficiently.
Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the bi... |
Q4J8K2 | MSVKAYLELIRVHNVVGSAVSAFMGYVIATTWKFTPLFFLPLLVVSLIAAGGYVINDVYDIEVDKINKPERPLPSGRIAVNIARRFSIVLFAVGLIISIPLGLIPFGFALITIVLLYEYARSLKKLGLVGNFIVALTSALSAYYGGLASGSLLGNFIIPTIYIFFFTLSREFVKGIEDIEGDKRNGVNTLAVKLGEKSTWIIAKIILGILIFTSPLPYFLGFNVIYLIGILALDVLLVYILILHNTIESATKARSLMKIYAIGTLIVFTLGSLRI | Function: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: (2E,... |
B7LK34 | MKITKITTYRLPPRWMFLKIETDEGVVGWGEPVIEGRARTVEAAVHELSDYLIGQDPSRINDLWQVMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLNAPVWQLMGGLVRDKIKAYSWVGGDRPADVIDGIKTLREIGFDTFKLNGCEELGLIDNSRAVDAAVNTVAQIREAFGNQIEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAEYYPKLAAQTHIPLAAGERMFSRFDFKRVLEAGGISILQPDLSHAGGITECYKIAGMAEAYDVTLAPHCPLGPIALAACLHIDFVSYNAVLQEQSMGIHYNKG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate.
Catalytic Activity: D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O
Sequence Mass (Da): 42583
Sequence Length: 382
Pathway: Carbohydrate acid metabolism; D-galactonate degradation; D-gly... |
Q6CYT9 | MKITKITTYRLPPRWMFLKIETDEGIVGWGEPVIEGRARTVEAAVHELSDYLIGQDPARINDIWQVLYRAGFYRGGPILMSAIAGIDQALWDIKGKALGVPVYQLLGGLVRDKIKAYSWVGGDRPSEVIAGIKKLTEIGFDTFKLNGCEEMGIIDNSRKVDAAVAVVAEIREAFGNSIEFGLDFHGRVDAPMAKILIKELEPYRPLFIEEPVLAEQAEYYPRLAAQTHLPIAAGERMFSRFDFKRVLADGGLAIIQPDLSHAGGITECFKIAAMAEAYDVALAPHCPLGPIALASCLHLDFVARNAVLQEQSMGIHYNKG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate.
Catalytic Activity: D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O
Sequence Mass (Da): 42425
Sequence Length: 382
Pathway: Carbohydrate acid metabolism; D-galactonate degradation; D-gly... |
B2UCA8 | MKITRLTTYRLPPRWMFLKVETDEGVTGWGEPVIEGRARTVEAAVHELSDYLIGQDPSRINDLWQTMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLGVPVYELLGGLVRDKMRTYSWVGGDRPADVIAGMKALQAGGFDHFKLNGCEEMGIIDTSRAVDAAVARVAEIRSAFGNTVEFGLDFHGRVSAPMAKVLIKELEPYRPLFIEEPVLAEQAETYARLAAHTHLPIAAGERMFSRFDFKRVLEAGGVSILQPDLSHAGGITECVKIAAMAEAYDVALAPHCPLGPIALAACLHVDFVSWNATLQEQSMGIHYNKG... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate.
Catalytic Activity: D-galactonate = 2-dehydro-3-deoxy-D-galactonate + H2O
Sequence Mass (Da): 42098
Sequence Length: 382
Pathway: Carbohydrate acid metabolism; D-galactonate degradation; D-gly... |
P80705 | MNVQFTVNGRAASIDVPPNTLLVQ | Cofactor: Binds 2 [2Fe-2S] clusters per subunit.
Catalytic Activity: a quinone + an aldehyde + H2O = a carboxylate + a quinol + H(+)
Sequence Mass (Da): 2585
Sequence Length: 24
EC: 1.2.5.2
|
Q927E6 | MKKILNGTDQVVEQMVEGLVKSHADVVHRVEGTRVIARNDKRPGKVGLVSGGGSGHEPAHAGYVGRGMLSAAVCGDVFTSPTPDQIYEGIKAADQGAGVLLIVKNYTGDVMNFEMAADLADADDIKVEQIVVDDDIAVEDSTFTTGRRGVAGTVLVHKIIGAAAEAGASLEELKALGEKVIASVKTLGVALSPCTVPEVGHPGFELGDDEIELGIGIHGEPGFTREKIMPSARLAKQLYERISSESKLLAGDKVVVLVNGMGATPLMEQYVFANDVHELLKNAGVQVEKTLVGDYMTSLEMAGLSLTILKLEDEKWVDML... | Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP.
Catalytic Activity: dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvat... |
Q92EU2 | MRRLVNDGYEAVEEMLAGYVAAQGKYVDFAENDKRVIVSKQMSEEPRVRIIVGGGSGHEPLFLGYVGKDFADAAVVGNINTSPSPEPCYNAVKAVDSGKGCLYMYGNYAGDVMNFDMGAEMAADDGIRVETVLVTDDIYSAENVEDRRGVAGDLIVFKAAASAAAKGLDLDAVKQAAEKANANTFSMGVALSSSTLPVTGKAIFEMKEGEMEVGMGIHGEPGIKRTSIEPADKVVDQIMGYLIEEMKLTAGEEVHVLINGLGGLPVMDQYICYRRVDEILKEKGVHIHSPLVGNYATSMDMIGMSITLVRLDDELKDLLD... | Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP.
Catalytic Activity: dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvat... |
P45510 | MSQFFFNQRTHLVSDVIDGAIIASPWNNLARLESDPAIRIVVRRDLNKNNVAVISGGGSGHEPAHVGFIGKGMLTAAVCGDVFASPSVDAVLTAIQAVTGEAGCLLIVKNYTGDRLNFGLAAEKARRLGYNVEMLIVGDDISLPDNKHPRGIAGTILVHKIAGYFAERGYNLATVLREAQYAASNTFSLGVALSSCHLPQETDAAPRHHPGHAELGMGIHGEPGASVIDTQNSAQVVNLMVDKLLAALPETGRLAVMINNLGGVSVAEMAIITRELASSPLHSRIDWLIGPASLVTALDMKGFSLTAIVLEESIEKALLT... | Cofactor: Divalent metal cations, Mg(2+) or Ca(2+).
Function: Catalyzes the phosphorylation of dihydroxyacetone.
Catalytic Activity: ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+)
Sequence Mass (Da): 57940
Sequence Length: 552
Domain: The C-terminal domain consists of a eight-helix alpha barrel. The e... |
Q55EE0 | MKKIINNPQNVVSEMIDGFTQSSRDLLKLKGNFNVVVRSDYSQIKDRVTLISGGGSGHEPAHIGYIGNAMLTGAVCGDVFASPSAKQIFMAIKSVAGKMGCILIVKNYMGDNGSFSIAREMCKSQLPDIRVEIITVDDDISSILMKLNEFSNDNNDNIQDIRDKYKSITNRRGIAGTVLVHKILGGLAEQGKSIDEILKFYNKYISPSKSLNLVTMGVGLSSCIIPSVGSPSFTLNEKEMEIGLGIHGEFGIEKVELKPSKQIIKSLIDNLLKILPYSNNNNNNNNNNNNNNNNNNNNNNNSCGISCGSDGEDKSLIVLI... | Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
Catalytic Activity: ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+)
Sequence Mass (Da): 71006
Sequence Length: 648
EC: 2.7.1.28
|
P76015 | MKKLINDVQDVLDEQLAGLAKAHPSLTLHQDPVYVTRADAPVAGKVALLSGGGSGHEPMHCGYIGQGMLSGACPGEIFTSPTPDKIFECAMQVDGGEGVLLIIKNYTGDILNFETATELLHDSGVKVTTVVIDDDVAVKDSLYTAGRRGVANTVLIEKLVGAAAERGDSLDACAELGRKLNNQGHSIGIALGACTVPAAGKPSFTLADNEMEFGVGIHGEPGIDRRPFSSLDQTVDEMFDTLLVNGSYHRTLRFWDYQQGSWQEEQQTKQPLQSGDRVIALVNNLGATPLSELYGVYNRLTTRCQQAGLTIERNLIGAYC... | Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP . Binds covalently dihydroxyacetone in hemiaminal linkage . DhaK acts also as corepressor of the t... |
Q9CIV8 | MSDEKIINQPQDVVSEMLDGLTYAYGDLIEKVPDFEIIQRKSPKSGKVALVSGGGSGHKPAHAGFVGEGMLSAAVCGAIFTSPTPDQIYEAIKSADEGAGVLLIIKNYLGDVMNFEMAREMAEMEEIKVEQIIVDDDIAVENSLYTQGRRGVAGTVLVHKILGAAAHQEASLDEIKDLADKVVKNIKTIGLALSAATVPEVGKPGFVLDDNEIEYGVGIHSEPGYRREKMKTSYELATELVGKLKEEFKFEAGQKYGILVNGMGATPLMEQFIFMNDVAKLLTEENIEILFKKVGNYMTSIDMAGLSLTMIKLEDDQWLK... | Function: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP.
Catalytic Activity: dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate
Se... |
Q927E5 | MTYDKDWALRWLNDFGERVQENKQLLSDLDQAIGDGDHGINMARGLSELKKAFTEKEPADLTDVFKTAGMTMVSKVGGASGPLYGTAFLNMSKAVDSETIDAEGLTKVIEAGLEGIEKRGKSHAGEKTMIDVWEPVVNALHQEDLTDDVVEAALQKTKDLKATKGRASYLGERSIGHLDPGAYSSALLFHAMLQTEVS | Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
Catalytic Activity: dihydrox... |
Q92EU3 | MSELVMDSAFFGHVLQDMGALIEKERDYLTGLDSDIGDGDHGINLSIGFREVNKQLDELLTVSPDIATLLKKSGMILLGKVGGASGPLYGSFFMKCGADVPGKTEVNFDELCGMIINGAAAVQHRGKAELGDKTMMDAFLPGVEVLQNRDTNADPIETFSAFVDAMHAGAQSTIPLIAKKGRALRLGERAIGHLDPGSESSWMLMNVILENLKKAV | Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
Catalytic Activity: dihydrox... |
P76014 | MSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKDIGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISRGKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPVALEAASSIAESAAQSTITMQARKGRASYLGERSIGHQDPGATSVMFMMQMLALAAKE | Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone . DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK . DhaL acts also as coactiva... |
Q9CIV7 | MLTIDTTIEWLGKFNEKIQENKAYLSELDGPIGDGDHGANMARGMSETMKALEVSNFGNVSEIFKKVAMTLMSKVGGASGPLYGSAFLAMSKTAIETLDTSELIYAGLEAIQKRGKAQVGEKTMVDIWSAFLNDLQTDSASKDNLEKVVKASAGLLATKGRASYLGERSIGHIDPGTQSSAYLFETLLEVVA | Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
Catalytic Activity: dihydrox... |
Q927E4 | MAKPYGVVIISHSKDVAKGVHDIIKEIAPDVSITHAGGTEDGRIGTSFDTVNEAIESNEADKVYTFYDLGSAKMNIETVEEISEKEIILFNAPILEGAYATAAQIQMDEKPEVIAANLKTIEIK | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
Q92ET9 | MISIVLVSHSQKITEGLQEMIVEMVGDTVHIISSGGTGDGRLGTNALMIADNIATCTNSEHIYIFCDIGSAILSAETALELLDTELLEKTTIIDAPLVEGAFTAAVQSLVNPSKEAILQELTNVH | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.