FAA32_MYCBO
ID FAA32_MYCBO Reviewed; 637 AA.
AC Q7TTR2; A0A1R3Y582; X2BPL9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD32 {ECO:0000250|UniProtKB:O53580};
DE Short=FAAL;
DE EC=6.2.1.20 {ECO:0000250|UniProtKB:O53580};
DE AltName: Full=Acyl-AMP synthetase;
GN Name=fadD32; OrderedLocusNames=BQ2027_MB3831C;
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: Involved in the biosynthesis of mycolic acids (By
CC similarity). Catalyzes the activation of long-chain fatty acids as
CC acyl-adenylates (acyl-AMP), which are then transferred to the
CC phosphopantetheine arm of the polyketide synthase Pks13 for further
CC chain extension (By similarity). {ECO:0000250|UniProtKB:O53580}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC Evidence={ECO:0000250|UniProtKB:O53580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589;
CC Evidence={ECO:0000250|UniProtKB:O53580};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:O53580}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU02460.1; -; Genomic_DNA.
DR RefSeq; NP_857468.1; NC_002945.3.
DR RefSeq; WP_003902741.1; NC_002945.4.
DR AlphaFoldDB; Q7TTR2; -.
DR SMR; Q7TTR2; -.
DR EnsemblBacteria; SIU02460; SIU02460; BQ2027_MB3831C.
DR GeneID; 45427802; -.
DR PATRIC; fig|233413.5.peg.4189; -.
DR OMA; NGRNIWP; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR Pfam; PF00501; AMP-binding; 1.
PE 3: Inferred from homology;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding.
FT CHAIN 1..637
FT /note="Long-chain-fatty-acid--AMP ligase FadD32"
FT /id="PRO_0000406635"
FT BINDING 194..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
SQ SEQUENCE 637 AA; 69260 MW; 4D3A88EA52C3B807 CRC64;
MFVTGESGMA YHNPFIVNGK IRFPANTNLV RHVEKWAKVR GDKLAYRFLD FSTERDGVAR
DILWSDFSAR NRAVGARLQQ VTQPGDRVAI LCPQNLDYLI SFFGALYSGR IAVPLFDPAE
PGHVGRLHAV LDDCAPSTIL TTTDSAEGVR KFIRARSAKE RPRVIAVDAV PTEVAATWQQ
PEANEETVAY LQYTSGSTRI PSGVQITHLN LPTNVVQVLN ALEGQEGDRG VSWLPFFHDM
GLITVLLASV LGHSFTFMTP AAFVRRPGRW IRELARKPGE TGGTFSAAPN FAFEHAAVRG
VPRDDEPPLD LSNVKGILNG SEPVSPASMR KFFEAFAPYG LKQTAVKPSY GLAEATLFVS
TTPMDEVPTV IHVDRDELNN QRFVEVAADA PNAVAQVSAG KVGVSEWAVI VDADTASELP
DGQIGEIWLH GNNLGTGYWG KEEESAQTFK NILKSRISES RAEGAPDDAL WVRTGDYGTY
FKDHLYIAGR IKDLVIIDGR NHYPQDLECT AQESTKALRV GYVAAFSVPA NQLPQTVFDD
SHAGLKFDPE DTSEQLVIVG ERAAGTHKLD HQPIVDDIRA AIAVGHGVTV RDVLLVSAGT
IPRTSSGKIG RRACRAAYLD GSLRSGVGSP TVFATSD
