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FAC19_MYCTO
ID   FAC19_MYCTO             Reviewed;         548 AA.
AC   P9WQ50; L0TEC7; Q6MWW5; Q7D5D8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase {ECO:0000250|UniProtKB:P9WQ51};
DE            Short=FACL {ECO:0000250|UniProtKB:P9WQ51};
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:P9WQ51};
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:P9WQ51};
DE            EC=6.2.1.42 {ECO:0000250|UniProtKB:P9WQ51};
DE   AltName: Full=Acyl-CoA synthetase {ECO:0000250|UniProtKB:P9WQ51};
DE   AltName: Full=Steroid-CoA ligase {ECO:0000250|UniProtKB:P9WQ51};
DE   AltName: Full=Steroid-coenzyme A ligase {ECO:0000250|UniProtKB:P9WQ51};
GN   Name=fadD19 {ECO:0000250|UniProtKB:P9WQ51}; OrderedLocusNames=MT3616;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as
CC       acyl-coenzyme A (acyl-CoA), which are then transferred to the
CC       multifunctional polyketide synthase (PKS) type III for further chain
CC       extension. Also involved in the degradation of cholesterol via the
CC       degradation of the side chains of C-24 branched-chain sterols.
CC       Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-
CC       oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA.
CC       {ECO:0000250|UniProtKB:P9WQ51}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ51};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ51};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(25S)-3-oxocholest-4-en-26-oate + ATP + CoA = (25S)-3-
CC         oxocholest-4-en-26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:29291,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:71541, ChEBI:CHEBI:83819, ChEBI:CHEBI:456215;
CC         EC=6.2.1.42; Evidence={ECO:0000250|UniProtKB:P9WQ51};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQ51}.
CC   -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC       {ECO:0000250|UniProtKB:P9WQ51}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47976.1; -; Genomic_DNA.
DR   PIR; E70807; E70807.
DR   RefSeq; WP_003901660.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ50; -.
DR   SMR; P9WQ50; -.
DR   EnsemblBacteria; AAK47976; AAK47976; MT3616.
DR   KEGG; mtc:MT3616; -.
DR   PATRIC; fig|83331.31.peg.3895; -.
DR   HOGENOM; CLU_000022_59_0_11; -.
DR   UniPathway; UPA00094; -.
DR   UniPathway; UPA00296; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cholesterol metabolism; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Nucleotide-binding; Steroid metabolism;
KW   Sterol metabolism.
FT   CHAIN           1..548
FT                   /note="Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-
FT                   26-oate--CoA ligase"
FT                   /id="PRO_0000426837"
FT   REGION          520..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         521
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  59741 MW;  E574B4BFA86F324E CRC64;
     MAVALNIADL AEHAIDAVPD RVAVICGDEQ LTYAQLEDKA NRLAHHLIDQ GVQKDDKVGL
     YCRNRIEIVI AMLGIVKAGA ILVNVNFRYV EGELRYLFDN SDMVALVHER RYADRVANVL
     PDTPHVRTIL VVEDGSDQDY RRYGGVEFYS AIAAGSPERD FGERSADAIY LLYTGGTTGF
     PKGVMWRHED IYRVLFGGTD FATGEFVKDE YDLAKAAAAN PPMIRYPIPP MIHGATQSAT
     WMALFSGQTT VLAPEFNADE VWRTIHKHKV NLLFFTGDAM ARPLVDALVK GNDYDLSSLF
     LLASTAALFS PSIKEKLLEL LPNRVITDSI GSSETGFGGT SVVAAGQAHG GGPRVRIDHR
     TVVLDDDGNE VKPGSGMRGV IAKKGNIPVG YYKDEKKTAE TFRTINGVRY AIPGDYAQVE
     EDGTVTMLGR GSVSINSGGE KVYPEEVEAA LKGHPDVFDA LVVGVPDPRY GQQVAAVVQA
     RPGCRPSLAE LDSFVRSEIA GYKVPRSLWF VDEVKRSPAG KPDYRWAKEQ TEARPADDVH
     AGHVTSGG
 
 
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