ID   FAD25_MYCTO             Reviewed;         583 AA.
AC   P9WQ44; L0T8I2; Q50586;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Putative fatty-acid--CoA ligase fadD25;
DE            EC=6.2.1.-;
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=fadD25; OrderedLocusNames=MT1572;
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45839.1; -; Genomic_DNA.
DR   PIR; A70723; A70723.
DR   RefSeq; WP_003901187.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ44; -.
DR   SMR; P9WQ44; -.
DR   EnsemblBacteria; AAK45839; AAK45839; MT1572.
DR   GeneID; 45425502; -.
DR   KEGG; mtc:MT1572; -.
DR   PATRIC; fig|83331.31.peg.1693; -.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   Cell membrane; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..583
FT                   /note="Putative fatty-acid--CoA ligase fadD25"
FT                   /id="PRO_0000426840"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          353..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  63142 MW;  1FC1A9B661FDE427 CRC64;
     MSVVESSLPG VLRERASFQP NDKALTFIDY ERSWDGVEET LTWSQLYRRT LNLAAQLREH
     GSTGDRALIL APQSLDYVVS FIASLQAGIV AVPLSIPQGG AHDERTVSVF ADTAPAIVLT
     ASSVVDNVVE YVQPQPGQNA PAVIEVDRLD LDARPSSGSR SAAHGHPDIL YLQYTSGSTR
     TPAGVMVSNK NLFANFEQIM TSYYGVYGKV APPGSTVVSW LPFYHDMGFV LGLILPILAG
     IPAVLTSPIG FLQRPARWIQ MLASNTLAFT AAPNFAFDLA SRKTKDEDME GLDLGGVHGI
     LNGSERVQPV TLKRFIDRFA PFNLDPKAIR PSYGMAEATV YVATRKAGQP PKIVQFDPQK
     LPDGQAERTE SDGGTPLVSY GIVDTQLVRI VDPDTGIERP AGTIGEIWVH GDNVAIGYWQ
     KPEATERTFS ATIVNPSEGT PAGPWLRTGD SGFLSEGELF IMGRIKDLLI VYGRNHSPDD
     IEATIQTISP GRCAAIAVSE HGAEKLVAII ELKKKDESDD EAAERLGFVK REVTSAISKS
     HGLSVADLVL VSPGSIPITT SGKIRRAQCV ELYRQDEFTR LDA