DESET_MYCTO
ID DESET_MYCTO Reviewed; 380 AA.
AC P9WNE8; L0TF04; O05875; Q7D5W0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=NADPH oxidoreductase {ECO:0000250|UniProtKB:P9WNE9};
DE EC=1.-.-.- {ECO:0000250|UniProtKB:P9WNE9};
DE AltName: Full=Stearoyl-CoA 9-desaturase electron transfer partner {ECO:0000250|UniProtKB:P9WNE9};
GN OrderedLocusNames=MT3327;
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. Is the electron transfer partner for the stearoyl-CoA 9-
CC desaturase DesA3. Catalyzes electron transfer reaction between NADPH
CC and the diiron center of DesA3. Cannot use NADH.
CC {ECO:0000250|UniProtKB:P9WNE9}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P33164};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P33164};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WNE9};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:P9WNE9}.
CC -!- SUBUNIT: Interacts with DesA3 to form a functional acyl-CoA desaturase
CC complex. {ECO:0000250|UniProtKB:P9WNE9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WNE9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P9WNE9}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P9WNE9}.
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DR EMBL; AE000516; AAK47670.1; -; Genomic_DNA.
DR PIR; H70590; H70590.
DR RefSeq; WP_003416922.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNE8; -.
DR SMR; P9WNE8; -.
DR EnsemblBacteria; AAK47670; AAK47670; MT3327.
DR KEGG; mtc:MT3327; -.
DR PATRIC; fig|83331.31.peg.3583; -.
DR HOGENOM; CLU_003827_14_2_11; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Cell membrane; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Transport.
FT CHAIN 1..380
FT /note="NADPH oxidoreductase"
FT /id="PRO_0000427139"
FT DOMAIN 58..164
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT DOMAIN 299..380
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 333
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 338
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 341
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 368
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 380 AA; 40795 MW; 1A7D0B80E1C3A045 CRC64;
MSKKHTTLNA SIIDTRRPTV AGADRHPGWH ALRKIAARIT TPLLPDDYLH LANPLWSARE
LRGRILGVRR ETEDSATLFI KPGWGFSFDY QPGQYIGIGL LVDGRWRWRS YSLTSSPAAS
GSARMVTVTV KAMPEGFLST HLVAGVKPGT IVRLAAPQGN FVLPDPAPPL ILFLTAGSGI
TPVMSMLRTL VRRNQITDVV HLHSAPTAAD VMFGAELAAL AADHPGYRLS VRETRAQGRL
DLTRIGQQVP DWRERQTWAC GPEGVLNQAD KVWSSAGASD RLHLERFAVS KTAPAGAGGT
VTFARSGKSV AADAATSLMD AGEGAGVQLP FGCRMGICQS CVVDLVEGHV RDLRTGQRHE
PGTRVQTCVS AASGDCVLDI
