ID   FAA30_MYCMM             Reviewed;         589 AA.
AC   B2HPY8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=MMAR_0706;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC39165.1; -; Genomic_DNA.
DR   RefSeq; WP_012392657.1; NC_010612.1.
DR   AlphaFoldDB; B2HPY8; -.
DR   SMR; B2HPY8; -.
DR   STRING; 216594.MMAR_0706; -.
DR   EnsemblBacteria; ACC39165; ACC39165; MMAR_0706.
DR   KEGG; mmi:MMAR_0706; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   OMA; HATIRDK; -.
DR   OrthoDB; 572620at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001190; 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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..589
FT                   /note="Probable long-chain-fatty-acid--AMP ligase FadD30"
FT                   /id="PRO_0000406633"
SQ   SEQUENCE   589 AA;  64221 MW;  BA7FDFA33EF2E6F1 CRC64;
     MSLISKLREL AEVKPDHEAF VFTEYDTRSG DRTSTLTWRQ VYVRASNLAR YLNSLNDDLE
     RQKFAAICAP QGIEYIVGFL GALFAGWCPV PLPEPQGGLQ DKRTGLALLD CSAAVVLTTA
     KDEDAVRATL AAYSLAVTTP VIALDTFEVA DVSPSGAGDV SDFRPPEGGM YLQYTSGSTG
     NPRGARISLE NVEINFRQIA KAAFPYKGTE VSLPRSTVSW LPLYHDMGLM VGLFIPVYCA
     CPSYFMSPAA FVRKPIRWMR MLAERDQPFT AAPNFAFDLA TSRISDADMS GIDLAHVSAI
     SNGGERVQPN TVDSFLERFS RYGLRPEVVK PSYGMAEAVV YVAISEVGTP PVSTEFDAQS
     LANGHAELKG PDAEHATRLV RYHKLDADPL VRIVDPESCV ELSPGGIGEI WVHGGNLSSG
     YHNVDNALNK EKFHATIRDK SPGTPRSPWL RTGDLGFEWD GGFYIVGRSK DLIIQDGVNH
     YPDDIENTVK EFTRGRVAAF SIADERSERL VIVAEVKPTG PASGSSGVEL PLVKKRAMAA
     LSRLHGLHVA DFLFVPPQAL PKTTSGKISR SACAKRYLSA GFEQLEVPQ