DESA1_MYCTO
ID DESA1_MYCTO Reviewed; 338 AA.
AC P9WNZ6; L0T7U2; Q50824; Q79FV9; Q8VKD4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Putative acyl-[acyl-carrier-protein] desaturase DesA1 {ECO:0000250|UniProtKB:P9WNZ7};
DE Short=Putative acyl-ACP desaturase DesA1 {ECO:0000250|UniProtKB:P9WNZ7};
DE EC=1.14.19.- {ECO:0000250|UniProtKB:P9WNZ7};
GN Name=desA1; Synonyms=des; OrderedLocusNames=MT0846;
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:P9WNZ7}.
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:P9WNZ7}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WNZ5}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:P9WNZ7}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45088.1; -; Genomic_DNA.
DR PIR; H70810; H70810.
DR RefSeq; WP_003404321.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNZ6; -.
DR SMR; P9WNZ6; -.
DR EnsemblBacteria; AAK45088; AAK45088; MT0846.
DR GeneID; 45424787; -.
DR KEGG; mtc:MT0846; -.
DR PATRIC; fig|83331.31.peg.905; -.
DR HOGENOM; CLU_034505_3_0_11; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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 CDD; cd01050; Acyl_ACP_Desat; 1.
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..338
FT /note="Putative acyl-[acyl-carrier-protein] desaturase
FT DesA1"
FT /id="PRO_0000427040"
FT REGION 314..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
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="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 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 338 AA; 38770 MW; 9AC9B5A4FFBDAC20 CRC64;
MSAKLTDLQL LHELEPVVEK YLNRHLSMHK PWNPHDYIPW SDGKNYYALG GQDWDPDQSK
LSDVAQVAMV QNLVTEDNLP SYHREIAMNM GMDGAWGQWV NRWTAEENRH GIALRDYLVV
TRSVDPVELE KLRLEVVNRG FSPGQNHQGH YFAESLTDSV LYVSFQELAT RISHRNTGKA
CNDPVADQLM AKISADENLH MIFYRDVSEA AFDLVPNQAM KSLHLILSHF QMPGFQVPEF
RRKAVVIAVG GVYDPRIHLD EVVMPVLKKW RIFEREDFTG EGAKLRDELA LVIKDLELAC
DKFEVSKQRQ LDREARTGKK VSAHELHKTA GKLAMSRR
