DESET_MYCTU
ID DESET_MYCTU Reviewed; 380 AA.
AC P9WNE9; 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 46.
DE RecName: Full=NADPH oxidoreductase {ECO:0000303|PubMed:17087501};
DE EC=1.-.-.- {ECO:0000305|PubMed:17087501};
DE AltName: Full=Stearoyl-CoA 9-desaturase electron transfer partner {ECO:0000303|PubMed:17087501};
GN OrderedLocusNames=Rv3230c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN ELECTRON TRANSFER PARTNER, INTERACTION WITH DESA3, COFACTOR,
RP SUBCELLULAR LOCATION, SUBUNIT, AND PATHWAY.
RC STRAIN=H37Rv;
RX PubMed=17087501; DOI=10.1021/bi0615285;
RA Chang Y., Fox B.G.;
RT "Identification of Rv3230c as the NADPH oxidoreductase of a two-protein
RT DesA3 acyl-CoA desaturase in Mycobacterium tuberculosis H37Rv.";
RL Biochemistry 45:13476-13486(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000269|PubMed:17087501}.
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:0000269|PubMed:17087501};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:17087501}.
CC -!- SUBUNIT: Interacts with DesA3 to form a functional acyl-CoA desaturase
CC complex. {ECO:0000269|PubMed:17087501}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side {ECO:0000305|PubMed:17087501}.
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DR EMBL; AL123456; CCP46049.1; -; Genomic_DNA.
DR PIR; H70590; H70590.
DR RefSeq; NP_217747.1; NC_000962.3.
DR RefSeq; WP_003416922.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WNE9; -.
DR SMR; P9WNE9; -.
DR STRING; 83332.Rv3230c; -.
DR PaxDb; P9WNE9; -.
DR DNASU; 888748; -.
DR GeneID; 888748; -.
DR KEGG; mtu:Rv3230c; -.
DR TubercuList; Rv3230c; -.
DR eggNOG; COG1018; Bacteria.
DR OMA; MQVHHIH; -.
DR PhylomeDB; P9WNE9; -.
DR BioCyc; MetaCyc:G185E-7504-MON; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001584; 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:0009055; F:electron transfer activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070402; F:NADPH binding; IDA:MTBBASE.
DR GO; GO:0022900; P:electron transport chain; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 2Fe-2S; Cell membrane; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..380
FT /note="NADPH oxidoreductase"
FT /id="PRO_0000392678"
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:0000250|UniProtKB:P33164,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 338
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P33164,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 341
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P33164,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 368
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P33164,
FT 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
