DESA3_MYCTO
ID DESA3_MYCTO Reviewed; 427 AA.
AC P9WNZ2; L0TC73; Q6MWZ3; Q7D5W1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=NADPH-dependent stearoyl-CoA 9-desaturase {ECO:0000250|UniProtKB:P9WNZ3};
DE EC=1.14.19.n4 {ECO:0000250|UniProtKB:P9WNZ3};
DE AltName: Full=Delta(9)-stearoyl desaturase {ECO:0000250|UniProtKB:P9WNZ3};
DE AltName: Full=Stearoyl-CoA 9-desaturase (NADPH) {ECO:0000250|UniProtKB:P9WNZ3};
DE AltName: Full=Stearoyl-CoA Delta(9)-desaturase {ECO:0000250|UniProtKB:P9WNZ3};
GN Name=desA3; OrderedLocusNames=MT3326;
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: Is likely involved in the aerobic desaturation system
CC responsible for the synthesis of oleic acid from stearoyl-CoA; oleic
CC acid is a precursor of mycobacterial membrane phospholipids and
CC triglycerides. Catalyzes the conversion of stearoyl-CoA to oleoyl-CoA
CC by introduction of a cis double bond between carbons 9 and 10 of the
CC acyl chain. Requires the electron transfer partner Rv3230c to pass two
CC electrons from NADPH to its active site diiron center. Is also able to
CC catalyze the 9-desaturation of palmitoyl-CoA to palmitoleoyl-CoA.
CC {ECO:0000250|UniProtKB:P9WNZ3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA +
CC 2 H2O + NADP(+); Xref=Rhea:RHEA:37971, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.19.n4; Evidence={ECO:0000250|UniProtKB:P9WNZ3};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:P9WNZ3}.
CC -!- SUBUNIT: Interacts with the electron transfer protein Rv3230c to form a
CC functional acyl-CoA desaturase complex. {ECO:0000250|UniProtKB:P9WNZ3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WNZ3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WNZ3}.
CC -!- PTM: Is rapidly degraded by a mycobacterial protein degradation system
CC that specifically targets the residues LAA at the C-terminus, leading
CC to a post-translational proteolytic regulation of DesA3 essential
CC activity. {ECO:0000250|UniProtKB:P9WNZ3}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK47669.1; -; Genomic_DNA.
DR PIR; G70590; G70590.
DR RefSeq; WP_003416919.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNZ2; -.
DR EnsemblBacteria; AAK47669; AAK47669; MT3326.
DR KEGG; mtc:MT3326; -.
DR PATRIC; fig|83331.31.peg.3582; -.
DR HOGENOM; CLU_045383_0_0_11; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353; PTHR19353; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 3: Inferred from homology;
KW Cell membrane; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; NADP;
KW Oxidoreductase.
FT CHAIN 1..427
FT /note="NADPH-dependent stearoyl-CoA 9-desaturase"
FT /id="PRO_0000427042"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
FT BINDING 309
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WNZ3"
SQ SEQUENCE 427 AA; 48443 MW; 56341F7F1B393A65 CRC64;
MAITDVDVFA HLTDADIENL AAELDAIRRD VEESRGERDA RYIRRTIAAQ RALEVSGRLL
LAGSSRRLAW WTGALTLGVA KIIENMEIGH NVMHGQWDWM NDPEIHSSTW EWDMSGSSKH
WRYTHNFVHH KYTNILGMDD DVGYGMLRVT RDQRWKRYNI FNVVWNTILA IGFEWGVALQ
HLEIGKIFKG RADREAAKTR LREFSAKAGR QVFKDYVAFP ALTSLSPGAT YRSTLTANVV
ANVIRNVWSN AVIFCGHFPD GAEKFTKTDM IGEPKGQWYL RQMLGSANFN AGPALRFMSG
NLCHQIEHHL YPDLPSNRLH EISVRVREVC DRYDLPYTTG SFLVQYGKTW RTLAKLSLPD
KYLRDNADDA PETRSERMFA GLGPGFAGAD PVTGRRRGLK TAIAAVRGRR RSKRMAKSVT
EPDDLAA
