ID F2Z6F1_YARLI Unreviewed; 728 AA.
AC F2Z6F1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=YALI0D05467p {ECO:0000313|EMBL:CAG80632.1};
GN ORFNames=YALI0_D05467g {ECO:0000313|EMBL:CAG80632.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG80632.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG80632.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2] {ECO:0007829|PDB:6RFQ, ECO:0007829|PDB:6RFR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=31844670; DOI=10.1126/sciadv.aax9484;
RA Parey K., Haapanen O., Sharma V., Kofeler H., Zullig T., Prinz S.,
RA Siegmund K., Wittig I., Mills D.J., Vonck J., Kuhlbrandt W., Zickermann V.;
RT "High-resolution cryo-EM structures of respiratory complex I: Mechanism,
RT assembly, and disease.";
RL Sci. Adv. 5:eaax9484-eaax9484(2019).
RN [3] {ECO:0007829|PDB:6Y79}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS).
RX PubMed=33243981; DOI=10.1038/s41467-020-19778-7;
RA Galemou Yoga E., Parey K., Djurabekova A., Haapanen O., Siegmund K.,
RA Zwicker K., Sharma V., Zickermann V., Angerer H.;
RT "Essential role of accessory subunit LYRM6 in the mechanism of
RT mitochondrial complex I.";
RL Nat. Commun. 11:6008-6008(2020).
RN [4] {ECO:0007829|PDB:6YJ4}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS).
RX PubMed=32747785; DOI=10.1038/s41594-020-0473-x;
RA Grba D.N., Hirst J.;
RT "Mitochondrial complex I structure reveals ordered water molecules for
RT catalysis and proton translocation.";
RL Nat. Struct. Mol. Biol. 27:892-900(2020).
RN [5] {ECO:0007829|PDB:7O6Y, ECO:0007829|PDB:7O71}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS).
RX PubMed=34767441; DOI=10.1126/sciadv.abj3221;
RA Parey K., Lasham J., Mills D.J., Djurabekova A., Haapanen O., Yoga E.G.,
RA Xie H., Kuhlbrandt W., Sharma V., Vonck J., Zickermann V.;
RT "High-resolution structure and dynamics of mitochondrial complex I-Insights
RT into the proton pumping mechanism.";
RL Sci. Adv. 7:eabj3221-eabj3221(2021).
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; CR382130; CAG80632.1; -; Genomic_DNA.
DR RefSeq; XP_502444.1; XM_502444.1.
DR PDB; 6RFQ; EM; 3.30 A; A=1-728.
DR PDB; 6RFR; EM; 3.20 A; A=1-728.
DR PDB; 6RFS; EM; 4.04 A; A=1-728.
DR PDB; 6Y79; EM; 3.20 A; A=1-728.
DR PDB; 6YJ4; EM; 2.70 A; G=1-728.
DR PDB; 7O6Y; EM; 3.40 A; A=1-728.
DR PDB; 7O71; EM; 2.40 A; A=1-728.
DR PDBsum; 6RFQ; -.
DR PDBsum; 6RFR; -.
DR PDBsum; 6RFS; -.
DR AlphaFoldDB; F2Z6F1; -.
DR SMR; F2Z6F1; -.
DR DIP; DIP-61445N; -.
DR IntAct; F2Z6F1; 2.
DR STRING; 284591.F2Z6F1; -.
DR EnsemblFungi; CAG80632; CAG80632; YALI0_D05467g.
DR GeneID; 2910292; -.
DR KEGG; yli:YALI0D05467g; -.
DR VEuPathDB; FungiDB:YALI0_D05467g; -.
DR HOGENOM; CLU_000422_11_6_1; -.
DR InParanoid; F2Z6F1; -.
DR OMA; QDQAMAY; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000001300; Chromosome D.
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 GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6RFQ, ECO:0007829|PDB:6RFR};
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 Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 35..113
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 113..152
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 252..308
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 728 AA; 78997 MW; 5C471AE77A92D4BF CRC64;
MLSRNLSKFA RAGLIRPATT STHTRLFSVS ARRLAEIELT IDGHKVSIEA GSALIQACEK
AGVTVPRYCY HDKLAIAGNC RMCLVDVERA PKPVASCAYP VAPGMVVRTD TERVKQAREN
VMEMMLQNHP LDCPVCDQGG ECDLQDQSMR YGRDRGRFTE ITGKRSTEDK NIGPLVKTSM
NRCIHCTRCV RFANDIAGAP ELGSSGRGND MQIGTYLEKN LNTELSGNVI DLCPVGALTN
KPYAFRARPW ELKKTESIDV MDAVGSNIRI DSKGVEVMRV IPRVHEDVNE EWINDKSRFA
CDGLKTQRLT TPLIRVGDKF VNATWDDALS TIAKAYQQKA PKGDEFKAVA GALVEVESMV
ALKDMTNALG SENTTTDTPN GNSAPAHGIT FRSNYLFNSS IAGIEDADAI LLVGTNPRRE
AAVMNARIRK AWLRQELEIA SVGPTLDATF DVAELGNTHA DLEKALSGEF GEVLKNAKNP
LIIVGSGITD REDAGAFFNT IGKFVESTPS VLNENWNGYN VLQRSASRAG AYDIGFTPSD
EASKTTPKMV WLLGADEVAA SDIPADAFVV YQGHNGDVGA QFADVVLPGA AYTEKAGTYV
NTEGRSQISR AATGPPGGAR EDWKILRAVS EYLGVALPYE DAYEVRDRLA EISPSLVRYD
LVEPTVFGDV AVQHSLVGPN GSVTPSSAPL TETIENFYMT DSISRSSPTM AKSSIAFNKD
NKKNQAFA
//
