ID   FAA23_MYCTO             Reviewed;         584 AA.
AC   P9WQ46; L0TGV3; O07797; Q7D4S9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Long-chain-fatty-acid--AMP ligase FadD23 {ECO:0000250|UniProtKB:P9WQ47};
DE            EC=6.2.1.57 {ECO:0000250|UniProtKB:P9WQ47};
DE   AltName: Full=Long-chain fatty acid adenylyltransferase FadD23 {ECO:0000250|UniProtKB:P9WQ47};
DE   AltName: Full=Long-chain-fatty-acid adenylase/transferase FadD23 {ECO:0000250|UniProtKB:P9WQ47};
GN   Name=fadD23; OrderedLocusNames=MT3934;
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 (PKS) type III for further chain
CC       extension. Involved in the biosynthesis of sulfolipid 1 (SL-1).
CC       {ECO:0000250|UniProtKB:P9WQ47}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hexadecanoate + holo-[(hydroxy)phthioceranic acid
CC         synthase] = AMP + diphosphate + hexadecanoyl-[(hydroxy)phthioceranic
CC         acid synthase]; Xref=Rhea:RHEA:59164, Rhea:RHEA-COMP:15244,
CC         Rhea:RHEA-COMP:15305, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483,
CC         ChEBI:CHEBI:456215; EC=6.2.1.57;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ47};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + holo-[(hydroxy)phthioceranic acid synthase] +
CC         octadecanoate = AMP + diphosphate + octadecanoyl-
CC         [(hydroxy)phthioceranic acid synthase]; Xref=Rhea:RHEA:59168,
CC         Rhea:RHEA-COMP:15305, Rhea:RHEA-COMP:15306, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78495, ChEBI:CHEBI:456215; EC=6.2.1.57;
CC         Evidence={ECO:0000250|UniProtKB:P9WQ47};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WQ47}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK48301.1; -; Genomic_DNA.
DR   PIR; F70522; F70522.
DR   RefSeq; WP_003899713.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ46; -.
DR   SMR; P9WQ46; -.
DR   EnsemblBacteria; AAK48301; AAK48301; MT3934.
DR   KEGG; mtc:MT3934; -.
DR   PATRIC; fig|83331.31.peg.4232; -.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane;
KW   Nucleotide-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..584
FT                   /note="Long-chain-fatty-acid--AMP ligase FadD23"
FT                   /id="PRO_0000426839"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   584 AA;  62841 MW;  99639AB9BEEA39EF CRC64;
     MVSLSIPSML RQCVNLHPDG TAFTYIDYER DSEGISESLT WSQVYRRTLN VAAEVRRHAA
     IGDRAVILAP QGLDYIVAFL GALQAGLIAV PLSAPLGGAS DERVDAVVRD AKPNVVLTTS
     AIMGDVVPRV TPPPGIASPP TVAVDQLDLD SPIRSNIVDD SLQTTAYLQY TSGSTRTPAG
     VMITYKNILA NFQQMISAYF ADTGAVPPLD LFIMSWLPFY HDMGLVLGVC APIIVGCGAV
     LTSPVAFLQR PARWLQLMAR EGQAFSAAPN FAFELTAAKA IDDDLAGLDL GRIKTILCGS
     ERVHPATLKR FVDRFSRFNL REFAIRPAYG LAEATVYVAT SQAGQPPEIR YFEPHELSAG
     QAKPCATGAG TALVSYPLPQ SPIVRIVDPN TNTECPPGTI GEIWVHGDNV AGGYWEKPDE
     TERTFGGALV APSAGTPVGP WLRTGDSGFV SEDKFFIIGR IKDLLIVYGR NHSPDDIEAT
     IQEITRGRCA AIAVPSNGVE KLVAIVELNN RGNLDTERLS FVTREVTSAI STSHGLSVSD
     LVLVAPGSIP ITTSGKVRRA ECVKLYRHNE FTRLDAKPLQ ASDL