ID   DESA2_MYCTO             Reviewed;         275 AA.
AC   P9WNZ4; L0T8L4; O53442; Q7D8V3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Putative acyl-[acyl-carrier-protein] desaturase DesA2 {ECO:0000250|UniProtKB:P9WNZ5};
DE            Short=Putative acyl-ACP desaturase DesA2 {ECO:0000250|UniProtKB:P9WNZ5};
DE            EC=1.14.19.- {ECO:0000250|UniProtKB:P9WNZ5};
GN   Name=desA2; OrderedLocusNames=MT1126;
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: May be a desaturase involved in mycobacterial fatty acid
CC       biosynthesis. {ECO:0000250|UniProtKB:P9WNZ5}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P22337};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000250|UniProtKB:P9WNZ5}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WNZ5}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45384.1; -; Genomic_DNA.
DR   PIR; D70896; D70896.
DR   RefSeq; WP_003405801.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNZ4; -.
DR   SMR; P9WNZ4; -.
DR   EnsemblBacteria; AAK45384; AAK45384; MT1126.
DR   KEGG; mtc:MT1126; -.
DR   PATRIC; fig|83331.31.peg.1216; -.
DR   HOGENOM; CLU_034505_3_0_11; -.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR005067; Fatty_acid_desaturase-2.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   PANTHER; PTHR31155; PTHR31155; 1.
DR   Pfam; PF03405; FA_desaturase_2; 1.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Metal-binding; Oxidoreductase.
FT   CHAIN           1..275
FT                   /note="Putative acyl-[acyl-carrier-protein] desaturase
FT                   DesA2"
FT                   /id="PRO_0000427041"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         110
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         159
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
SQ   SEQUENCE   275 AA;  31359 MW;  448D136940150E99 CRC64;
     MAQKPVADAL TLELEPVVEA NMTRHLDTED IWFAHDYVPF DQGENFAFLG GRDWDPSQST
     LPRTITDACE ILLILKDNLA GHHRELVEHF ILEDWWGRWL GRWTAEEHLH AIALREYLVV
     TREVDPVANE DVRVQHVMKG YRAEKYTQVE TLVYMAFYER CGAVFCRNLA AQIEEPILAG
     LIDRIARDEV RHEEFFANLV THCLDYTRDE TIAAIAARAA DLDVLGADIE AYRDKLQNVA
     DAGIFGKPQL RQLISDRITA WGLAGEPSLK QFVTG