ID   FAA30_MYCTO             Reviewed;         585 AA.
AC   P9WQ56; L0T3F7; P95213; Q7D9V7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Probable long-chain-fatty-acid--AMP ligase FadD30;
DE            Short=FAAL;
DE            EC=6.2.1.- {ECO:0000250|UniProtKB:P9WQ57};
DE   AltName: Full=Acyl-AMP synthetase;
GN   Name=fadD30; OrderedLocusNames=MT0417;
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 long-chain fatty acids as acyl-
CC       adenylates (acyl-AMP), which are then transferred to a multifunctional
CC       polyketide synthase (PKS) for further chain extension.
CC       {ECO:0000250|UniProtKB:P9WQ57}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQ57}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44641.1; -; Genomic_DNA.
DR   PIR; C70634; C70634.
DR   RefSeq; WP_003900139.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ56; -.
DR   SMR; P9WQ56; -.
DR   EnsemblBacteria; AAK44641; AAK44641; MT0417.
DR   KEGG; mtc:MT0417; -.
DR   PATRIC; fig|83331.31.peg.447; -.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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..585
FT                   /note="Probable long-chain-fatty-acid--AMP ligase FadD30"
FT                   /id="PRO_0000426834"
SQ   SEQUENCE   585 AA;  63843 MW;  B16A77089F760F18 CRC64;
     MSVISTLRDR ATTTPSDEAF VFMDYDTKTG DQIDRMTWSQ LYSRVTAVSA YLISYGRHAD
     RRRTAAISAP QGLDYVAGFL GALCAGWTPV PLPEPLGSLR DKRTGLAVLD CAADVVLTTS
     QAETRVRATI ATHGASVTTP VIALDTLDEP SGDNCDLDSQ LSDWSSYLQY TSGSTANPRG
     VVLSMRNVTE NVDQIIRNYF RHEGGAPRLP SSVVSWLPLY HDMGLMVGLF IPLFVGCPVI
     LTSPEAFIRK PARWMQLLAK HQAPFSAAPN FAFDLAVAKT SEEDMAGLDL GHVNTIINGA
     EQVQPNTITK FLRRFRPYNL MPAAVKPSYG MAEAVVYLAT TKAGSPPTST EFDADSLARG
     HAELSTFETE RATRLIRYHS DDKEPLLRIV DPDSNIELGP GRIGEIWIHG KNVSTGYHNA
     DDALNRDKFQ ASIREASAGT PRSPWLRTGD LGFIVGDEFY IVGRMKDLII QDGVNHYPDD
     IETTVKEFTG GRVAAFSVSD DGVEHLVIAA EVRTEHGPDK VTIMDFSTIK RLVVSALSKL
     HGLHVTDFLL VPPGALPKTT SGKISRAACA KQYGANKLQR VATFP