ID   FAD21_MYCLE             Reviewed;         579 AA.
AC   P54200; Q9CC61;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Putative fatty-acid--CoA ligase fadD21;
DE            EC=6.2.1.-;
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=fadD21; Synonyms=masC; OrderedLocusNames=ML1234;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17075.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00010; AAA17075.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583921; CAC31615.1; -; Genomic_DNA.
DR   PIR; D87063; D87063.
DR   PIR; S72711; S72711.
DR   RefSeq; NP_301895.1; NC_002677.1.
DR   RefSeq; WP_010908216.1; NC_002677.1.
DR   AlphaFoldDB; P54200; -.
DR   SMR; P54200; -.
DR   STRING; 272631.ML1234; -.
DR   PRIDE; P54200; -.
DR   EnsemblBacteria; CAC31615; CAC31615; CAC31615.
DR   KEGG; mle:ML1234; -.
DR   PATRIC; fig|272631.5.peg.2266; -.
DR   Leproma; ML1234; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   OMA; QGVIAPI; -.
DR   Proteomes; UP000000806; Chromosome.
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   Fatty acid metabolism; Ligase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..579
FT                   /note="Putative fatty-acid--CoA ligase fadD21"
FT                   /id="PRO_0000193135"
FT   CONFLICT        179
FT                   /note="A -> T (in Ref. 1; AAA17075)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   579 AA;  63102 MW;  16B8AB8384FBBFA1 CRC64;
     MQNSSVLSFL RERAGLQPDD EAFSFTDYEQ DWAGVRKTLT WAQLYQRTLN VAHELRRHGS
     IRDRAVILAP QGLDYIIAFL GAMQAGFIAV PLSVPQAGSH DERVGAVLAD TSPSVVLTTS
     AVADAIAKYV DHSDTDTVPA ILEVDSPNLD VENKSNIRLT DAPSTAYLQY TSGSTRLPAG
     VMVTHRNLMV NFQQLMADYF APTNGVAPLD LTIVSWLPFY HDMGLVLGVV APILGGWRSE
     LTSPISFLQR PARWIQAMAT SSHPFSAGPN FAFELAARRT SDADIAGLDL GACQGIISGS
     ERIHPATLNR FSDRFARINF RDDMMLPSYG LAEGTVYAAS RPKGSSPEVV YFEPAKLSEG
     TVKRCEARTG APLLSYGTPK SPIVRIVDSD TCIECPTGRV GEIWLHGDNV AEGYWHKPEE
     TQRTFGGKLA NPSPGTPEGP WLRTGDLGFI SEDELFIVGR MKDLLIVYGR NHYPEDIEST
     VQEITGGRVA AISVPVDETE KLVTIIEVKK RGDSDAEAMQ KLVAVKNNIT AAISKSHGLN
     VADLVLVPPG SIPTTTSGKV RRTACVEQYR RQQFSRLDG