UniProt: G7M3G4

Database: UniProt
Entry: G7M3G4_9CLOT

LinkDB:  G7M3G4_9CLOT 
Original site:  G7M3G4_9CLOT

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Ontology (6)   
   GO (6)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (36)   
   InterPro (20)   
   Pfam (8)   
   PROSITE (4)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (47)   

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ID   G7M3G4_9CLOT            Unreviewed;      3062 AA.
AC   G7M3G4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Long-chain-fatty-acid--(Acyl-carrier-protein) ligase., 6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:EHJ00281.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:EHJ00281.1};
DE            EC=6.2.1.20 {ECO:0000313|EMBL:EHJ00281.1};
GN   ORFNames=CDLVIII_3725 {ECO:0000313|EMBL:EHJ00281.1};
OS   Clostridium sp. DL-VIII.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ00281.1, ECO:0000313|Proteomes:UP000005106};
RN   [1] {ECO:0000313|EMBL:EHJ00281.1, ECO:0000313|Proteomes:UP000005106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ00281.1,
RC   ECO:0000313|Proteomes:UP000005106};
RX   PubMed=23929491;
RA   Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT   Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL   Genome Announc. 1:e00605-e00613(2013).
CC   -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004789}.
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DR   EMBL; CM001240; EHJ00281.1; -; Genomic_DNA.
DR   RefSeq; WP_009170941.1; NZ_CM001240.1.
DR   STRING; 641107.CDLVIII_3725; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000402_0_0_9; -.
DR   Proteomes; UP000005106; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EHJ00281.1};
KW   Ligase {ECO:0000313|EMBL:EHJ00281.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005106};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHJ00281.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        89..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          600..677
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          697..1153
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2116..2190
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2215..2678
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   3062 AA;  341002 MW;  20A149989C412E59 CRC64;
     MKDNNIKMSI SCGKPITNKY CNKMNIGNLL IEAAENKKDK GILLVQGNDS DIFLSYEEIF
     EKAMLCLGAL QEKGIKQDDF AIISFQNNID FIICFWACVL GGIVVVPIST PSAFKGKNAS
     LEKLINVWNT LEKPVIISDA SIIKGMKNNE LYSECQEMNM LDISILRENT IKGKMNLSEI
     EKTAFVQFSS GSTNTPKGVI LTHKNLLTNI EGIIESGGLT SEDRVLSWMP YYHDMGLIGF
     HISLIALGMF QINMNPMKFV KRPTLWFDLI SKHKITMTSS PNFGYRLLLR KVKDKHLKEW
     DLSSLRLIFN GAEPISMPLV NEFMEKLSEC NLSETSMFMV YGMAEACLAV AFPPVNSKPL
     SHFVSRNSLV NKSKVEEVEE CAKDALQVAD EGYPVAGMQV RVVNDEGEIV SENVLGEIQI
     KGDNVTKGYI NNPEATAKSF QDDWLKTGDT GFIIDGRLCV TGRIKDIIFV NGQNFFAHDI
     EFKLEEIEGV ETGKVVVGGW HDEKEGREKI AIFSSLRVKE DELKSFYGNM LSKISETFGI
     YIDFVVLVKA IPKTTSGKVR RFLLVQSFLD NEFADSTLTS AELLLNIEEK AEEADEDESL
     VLNISRDKIK EIWADVLERP AQSIGYNQSF FSLGGTSIKA VQVLGVLEDE LDITLGHDIL
     INCRTINEME EYLKSFSESN SILTNIDEKI SGEVEEEDGI AVIEMSCRFP EASSPEEFWN
     NIVSGKCSIS EVPEERWDVN QYYSTSGDPT KTYCKTGAFI DKPFDFDAKF FNISDEEAAV
     MDPQQRIILE LVFEILERAG YSKKKVSGES ISLYIGAGTN TYQEYHFNTL NMSSLKNFDS
     FNSLSKEVQE SILEEWKNKL GVTEFHTNLL VDNILNMIAA RTSQEFNFKG PSMVVDTACS
     SSLVTIHLAC EALKKGECEL AIAGGINLLL TPTPYIYLSN AGALSTSGIS RVFDAKADGL
     VPGEGAGLVL LKPLKKALKD KDKVLAVIKA SAINNDGHSI GVMAPNPDGQ REVIESLYVK
     SGINPRDIQY IEAHGTGTKI GDPSEVRALS NAFKRWNPES NSMAIGSVKA NIGHLLNGAG
     IASFIKVILA INNKTMPPNV NLDELNPSIK FDKTPFYTML EARKWEVQEG KMRKAAVNSF
     GFGGTNCHMV LEEAPSEIIP AVEVQDYSRN KYALNLSANS EKSLQLKINN LVKYLKTSKE
     NNLGDICYTE NALRTSFNKY RYSVVSESIE DLINELQNIK VEELNSDAQH KVALMFTGQG
     SQYVGMGREL YNKLPIFKGY VDECSEVFYP YLNEKITDLI YSDKADESIL AQTNITQPVV
     FTMDYAFGRL LIDLGIKPAY MLGHSVGEWA AACLADVITL EDAAKIVSAR GKLMGSIKSS
     GCMCAVFTSS EKLEILFKEF EGAVWIAAYN GTHQVISGDE ADVEKFCNNL LKEGIGFKKL
     KVSQAFHTPL MEPILDAFRE VLKEVKFNSP KIPVISNVTG KIMDEAFDTE YWINHILSSV
     KFEQSIKYLS YKAVDVLIEC GPDRVLSRMA SGVQAQSART ILSLSDRKME SFDVCLAALS
     SLFTLGFNVD FEKFESEIYY NKLQLPSYPF ERKTYKPDFG DESIRVPDEW FYNWNWKPEP
     HKYADSEIKG NIVIFSDNSE IEDEFEEIFK TNKIYVVKVG TEYRFDDYSK FIINPIAEED
     YVKVFNIIQG PVGAVIHLWN LNKESFKLEF AFDDKVMHED IYSVLYIGKA LSKLNIEKTK
     LLLVTNNGVS VNEENKISSP HQASAITLAQ ALDQENAFID SYCIDVDKKE YESNREIAQI
     LSDEIKHDLS KEGIVAIRGG VRFIRELSDA IKFNQTSKIK FNDGETYLIT GGASAVGSEI
     AKVIAKKAKI NLILTGREEL PLIEKWEEEL ANNTRYAKKI SIIMELKELG ANVIYEAVDV
     TKIGDMKALV ERIADEYGAI YGVIHAAGTF DSKTLKLLDK NIKVINKIIE PKLKGGIITD
     LVTRKEPLKF FVMLSSVSCS EKLWSAGVGD YAAANAFLSA YSYYRAADNA PGKTIALNYS
     LWAGTGMGSD FGNGALLALK AQGLNPLPAK KAAEAFIRAL SVESQNVIHI IDKIEISDVE
     KSSTIKMPQV NSRKLKNIKE IVYKVIAKQL KVEEDNFDVG KNFLELGLDS LGAVKVMEML
     GTSIGMELYP TLIFEYQTPQ ALAEYIEMTY LEGFEEAAVS KINDLDTEVI ETERSKDIAI
     ISASLRIPGA NNLNEYWRIL ENGECVIREI PEDRWPANDH YSEDMNSAYT SYSKCGGFID
     NPYEFDPLFF GMSPSEATVT DPQQRIFLEI AWEVMQQAGY GGRYSTNNIG VFVGSEQNGY
     SEHFNNYRIY MELKDKLLKN QTFNNMESNE KSEIMSNILN VLKPAKMVPD AVAGNSLNEV
     AARVSHCLNL SGPSLTVNSA CSSSLSALHL ACESIRTGQC KMAIVGGVNL NTSPTPFIGL
     SRVQALSKTG ACYPFDDRAD GMVLSEGASA ILLKPLEDAI ADNDNIMAVI KGSAMNNDGH
     SQGITAPRPQ GQADAVIKAY LDAKINPETV SYVETHGTGT PLGDPIEIEG MAKAFRAFTS
     EKGFCAIGSV KSSIGHMLSA SGITSLIKVV LALENKKIPH TINYNKTTTN RNIDFANSPF
     FVAAEKTMEW ERSGVTPLRA GVNGFGFGGT NVHVILEEAP EKKNIEKGEE DFPYLLQLTG
     RNQSVIKNIA LNLKEYVKGH EGLNTASICF TINSNQKELS TKNSAVVESK EHLLEILTHL
     INNEDSECIY KGRSNPNRQT EAYLILDGNM KKVEKCKEDL SSRFDAFNIA YKECLKVVEK
     NISNEEILDF ESFAVQYAFG VLLSNFEMKI YGIIAEGTGI LAASVLTGKM SLKQALEEIV
     GTIRAEKDDV LEGDKNAVYL NCSILTSTGV LEDVFNVSQN DDKNIKSLNV FANKNQVIIY
     PGNFNEIKNK EFYDDKNFNW INMDITRNPV KSIMSAFAKI YTLGVRFNPS KLFKGNIKKV
     MLPTYPFENE TYKVSFEEEL TYKEADYISM QRNGLRKMEM KHALSNSEKR SISNQLAIDI
     EK
//

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