FAC13_MYCTO
ID FAC13_MYCTO Reviewed; 503 AA.
AC P9WQ36; F2GNX9; L0TEI7; O53306; Q7D654;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase FadD13;
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:P9WQ37};
DE AltName: Full=Fatty acyl-CoA ligase;
DE Short=FACL;
DE Short=FACL13;
DE AltName: Full=Fatty acyl-CoA synthetase;
DE Short=ACS;
DE Short=FACS;
DE AltName: Full=Very-long-chain fatty-acyl-CoA synthetase;
DE Short=ACSVL;
GN Name=fadD13; OrderedLocusNames=MT3174;
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: Required for maintaining the appropriate mycolic acid
CC composition and permeability of the envelope on its exposure to acidic
CC pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme
CC A (acyl-CoA), which are then transferred to the multifunctional
CC polyketide synthase (PKS) type III for further chain extension.
CC {ECO:0000250|UniProtKB:P9WQ37}.
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:P9WQ37};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P9WQ37}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQ37}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WQ37};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P9WQ37}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK47510.1; -; Genomic_DNA.
DR PIR; E70853; E70853.
DR RefSeq; WP_003416081.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ36; -.
DR SMR; P9WQ36; -.
DR EnsemblBacteria; AAK47510; AAK47510; MT3174.
DR KEGG; mtc:MT3174; -.
DR PATRIC; fig|83331.31.peg.3420; -.
DR HOGENOM; CLU_000022_59_0_11; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-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 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; Cell membrane; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Membrane; Nucleotide-binding.
FT CHAIN 1..503
FT /note="Long-chain-fatty-acid--CoA ligase FadD13"
FT /id="PRO_0000426844"
FT SITE 9
FT /note="Membrane interaction"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 17
FT /note="Membrane interaction"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 195
FT /note="Membrane interaction"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 197
FT /note="Membrane interaction"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 214
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 244
FT /note="Membrane interaction"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
FT SITE 302
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000250|UniProtKB:P9WQ37"
SQ SEQUENCE 503 AA; 54459 MW; B4CF011549E7B620 CRC64;
MKNIGWMLRQ RATVSPRLQA YVEPSTDVRM TYAQMNALAN RCADVLTALG IAKGDRVALL
MPNSVEFCCL FYGAAKLGAV AVPINTRLAA PEVSFILSDS GSKVVIYGAP SAPVIDAIRA
QADPPGTVTD WIGADSLAER LRSAAADEPA VECGGDDNLF IMYTSGTTGH PKGVVHTHES
VHSAASSWAS TIDVRYRDRL LLPLPMFHVA ALTTVIFSAM RGVTLISMPQ FDATKVWSLI
VEERVCIGGA VPAILNFMRQ VPEFAELDAP DFRYFITGGA PMPEALIKIY AAKNIEVVQG
YALTESCGGG TLLLSEDALR KAGSAGRATM FTDVAVRGDD GVIREHGEGE VVIKSDILLK
EYWNRPEATR DAFDNGWFRT GDIGEIDDEG YLYIKDRLKD MIISGGENVY PAEIESVIIG
VPGVSEVAVI GLPDEKWGEI AAAIVVADQN EVSEQQIVEY CGTRLARYKL PKKVIFAEAI
PRNPTGKILK TVLREQYSAT VPK
