ID M7WM03_RHOT1 Unreviewed; 753 AA.
AC M7WM03;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=NADH dehydrogenase (Ubiquinone) Fe-S protein 1 {ECO:0000313|EMBL:EMS21537.1};
GN ORFNames=RHTO_01597 {ECO:0000313|EMBL:EMS21537.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS21537.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS21537.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS21537.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
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DR EMBL; KB722655; EMS21537.1; -; Genomic_DNA.
DR RefSeq; XP_016272656.1; XM_016415278.1.
DR AlphaFoldDB; M7WM03; -.
DR GeneID; 27365610; -.
DR eggNOG; KOG2282; Eukaryota.
DR HOGENOM; CLU_000422_11_6_1; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR InterPro; IPR015405; NDUFS1-like_C.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR Pfam; PF09326; NADH_dhqG_C; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Ubiquinone {ECO:0000313|EMBL:EMS21537.1}.
FT DOMAIN 33..112
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 112..151
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 251..307
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 753 AA; 81811 MW; 6E421F796EB81135 CRC64;
MLRLSRRIPA SSRNPLALLA SSRAIHATSR ASADVTLEID GVPVTVPQGT ALIQACEKAG
ATIPRFCYHD RLNIAGNCRM CLVEVSPGPP KPQASCALPA MPGQKVKTNS PTVHKAREGV
MEFLLANHPL DCPICDQGGE CDLQDQSMRY GSDRTRFHEI TGKRATEDKN LGPLIKTSMN
RCIHCTRCVR FANEVAGVQD LGTSGRGNDM QIGTYIEKTI NSEMSGNVID LCPVGALTSK
PYAFEARPWE LKKTESVDVL DAVGSNIRVD SRGLVVMRVE PRLNDDINEE WISDKTRFAY
DGLRTQRLNT PLVRVGDRFQ PVTWQNALGA IKDGLASSGA KGNEIQAVAG SLADSESLVA
LKDLVNRLGS DNTALDQPLG QAPPAHGVDH RAAYTFGSSI AGVEYADRVL LIGTNPRHEA
AILNARLRKT WLRNETDCAL IGEQFDSTFG YDHLGADANA VRDVLSGKKG DWAKQLKEAK
RPMIIVGSAV TEHEDGAKVF AEVAKFVEAN KDKFVTPEWT GYNVLQRAAS RTAAYDIGFV
PSASAGKTKP KFVYLLNADD FSPSSIPRDA FVVYQGHHGD VGAQYADVVL PGCAYTEKSV
TWVNTEGRTQ LGRAAVPPPG AAREDWKIIR ALSEVLGETL PYDDTGALRD RMWDVSPTLV
RYGELEKPSS VLEAVQALRK QGEREAGKRN GLGGRKGEFK KLFDSFYRTD PVSRNSVTMG
QCVKTFEQGI DGVEKPVIGD DGMAQAGHHP ARA
//
