ID   FAA26_MYCTO             Reviewed;         583 AA.
AC   P9WQ42; L0TDT5; Q10976;
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=Long-chain-fatty-acid--AMP ligase FadD26;
DE            Short=FAAL;
DE            EC=6.2.1.59 {ECO:0000250|UniProtKB:P9WQ43};
DE   AltName: Full=Acyl-AMP synthetase;
GN   Name=fadD26; OrderedLocusNames=MT2999;
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 the
CC       multifunctional polyketide synthase PpsA for further chain extension.
CC       Catalyzes the adenylation of the long-chain fatty acids eicosanoate
CC       (C20) or docosanoate (C22), and potentially the very-long-chain fatty
CC       acid lignocerate (C24). Involved in the biosynthesis of phthiocerol
CC       dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B).
CC       {ECO:0000250|UniProtKB:P9WQ43}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-
CC         [(phenol)carboxyphthiodiolenone synthase] = a long-chain fatty acyl-
CC         [(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate;
CC         Xref=Rhea:RHEA:64660, Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:16648,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215;
CC         EC=6.2.1.59; Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + eicosanoate + holo-[(phenol)carboxyphthiodiolenone
CC         synthase] = AMP + diphosphate + icosanoyl-
CC         [(phenol)carboxyphthiodiolenone synthase]; Xref=Rhea:RHEA:59156,
CC         Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:14985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32360, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:87848, ChEBI:CHEBI:456215; EC=6.2.1.59;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + docosanoate + holo-[(phenol)carboxyphthiodiolenone
CC         synthase] = AMP + diphosphate + docosanoyl-
CC         [(phenol)carboxyphthiodiolenone synthase]; Xref=Rhea:RHEA:59160,
CC         Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:14987, ChEBI:CHEBI:23858,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:142238, ChEBI:CHEBI:456215; EC=6.2.1.59;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQ43}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47327.1; -; Genomic_DNA.
DR   PIR; B70749; B70749.
DR   RefSeq; WP_003900597.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ42; -.
DR   SMR; P9WQ42; -.
DR   EnsemblBacteria; AAK47327; AAK47327; MT2999.
DR   KEGG; mtc:MT2999; -.
DR   PATRIC; fig|83331.31.peg.3240; -.
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..583
FT                   /note="Long-chain-fatty-acid--AMP ligase FadD26"
FT                   /id="PRO_0000426841"
SQ   SEQUENCE   583 AA;  63044 MW;  F97CD6E19E217435 CRC64;
     MPVTDRSVPS LLQERADQQP DSTAYTYIDY GSDPKGFADS LTWSQVYSRA CIIAEELKLC
     GLPGDRVAVL APQGLEYVLA FLGALQAGFI AVPLSTPQYG IHDDRVSAVL QDSKPVAILT
     TSSVVGDVTK YAASHDGQPA PVVVEVDLLD LDSPRQMPAF SRQHTGAAYL QYTSGSTRTP
     AGVIVSHTNV IANVTQSMYG YFGDPAKIPT GTVVSWLPLY HDMGLILGIC APLVARRRAM
     LMSPMSFLRR PARWMQLLAT SGRCFSAAPN FAFELAVRRT SDQDMAGLDL RDVVGIVSGS
     ERIHVATVRR FIERFAPYNL SPTAIRPSYG LAEATLYVAA PEAGAAPKTV RFDYEQLTAG
     QARPCGTDGS VGTELISYGS PDPSSVRIVN PETMVENPPG VVGEIWVHGD HVTMGYWQKP
     KQTAQVFDAK LVDPAPAAPE GPWLRTGDLG VISDGELFIM GRIKDLLIVD GRNHYPDDIE
     ATIQEITGGR AAAIAVPDDI TEQLVAIIEF KRRGSTAEEV MLKLRSVKRE VTSAISKSHS
     LRVADLVLVS PGSIPITTSG KIRRSACVER YRSDGFKRLD VAV