FAC17_MYCBO
ID FAC17_MYCBO Reviewed; 502 AA.
AC Q7TWC5; A0A1R3Y4B7; X2BPR1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Medium/long-chain-fatty-acid--CoA ligase FadD17;
DE Short=FACL;
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:O53551};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:O53551};
DE AltName: Full=Acyl-CoA synthetase;
GN Name=fadD17; OrderedLocusNames=BQ2027_MB3536;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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. {ECO:0000250|UniProtKB:O53551}.
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:O53551};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:O53551};
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:O53551};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:O53551};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:O53551}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU02163.1; -; Genomic_DNA.
DR RefSeq; NP_857175.1; NC_002945.3.
DR RefSeq; WP_003901655.1; NC_002945.4.
DR AlphaFoldDB; Q7TWC5; -.
DR SMR; Q7TWC5; -.
DR EnsemblBacteria; SIU02163; SIU02163; BQ2027_MB3536.
DR PATRIC; fig|233413.5.peg.3875; -.
DR OMA; NAIMAGW; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001419; 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:0005324; F:long-chain fatty acid transporter activity; IEA:InterPro.
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: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 InterPro; IPR030310; FadD17/FadD6-like.
DR PANTHER; PTHR43107:SF15; PTHR43107:SF15; 1.
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; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding.
FT CHAIN 1..502
FT /note="Medium/long-chain-fatty-acid--CoA ligase FadD17"
FT /id="PRO_0000406788"
SQ SEQUENCE 502 AA; 53739 MW; 0AF9A7B3B9C83A4D CRC64;
MTPTHPTVTE LLLPLSEIDD RGVYFEDSFT SWRDHIRHGA AIAAALRERL DPARPPHVGV
LLQNTPFFSA TLVAGALSGI VPVGLNPVRR GAALAGDIAK ADCQLVLTGS GSAEVPADVE
HINVDSPEWT DEVAAHRDTE VRFRSADLAD LFMLIFTSGT SGDPKAVKCS HRKVAIAGVT
ITQRFSLGRD DVCYVSMPLF HSNAVLVGWA VAAACQGSMA LRRKFSASQF LADVRRYGAT
YANYVGKPLS YVLATPELPD DADNPLRAVY GNEGVPGDID RFGRRFGCVV MDGFGSTEGG
VAITRTLDTP AGALGPLPGG IQIVDPDTGE PCPTGVVGEL VNTAGPGGFE GYYNDEAAEA
ERMAGGVYHS GDLAYRDDAG YAYFAGRLGD WMRVDGENLG TAPIERVLMR YPDATEVAVY
PVPDPVVGDQ VMAALVLAPG TKFDADKFRA FLTEQPDLGH KQWPSYVRVS AGLPRTMTFK
VIKRQLSAEG VACADPVWPI RR
