ID F6HSN0_VITVI Unreviewed; 746 AA.
AC F6HSN0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 1, mitochondrial {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_14s0006g02020 {ECO:0000313|EMBL:CCB57671.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB57671.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN596245; CCB57671.1; -; Genomic_DNA.
DR RefSeq; XP_002270157.1; XM_002270121.4.
DR AlphaFoldDB; F6HSN0; -.
DR STRING; 29760.F6HSN0; -.
DR PaxDb; 29760-VIT_14s0006g02020-t01; -.
DR EnsemblPlants; Vitvi14g01032_t001; Vitvi14g01032_P001; Vitvi14g01032.
DR GeneID; 100246750; -.
DR Gramene; Vitvi14g01032_t001; Vitvi14g01032_P001; Vitvi14g01032.
DR KEGG; vvi:100246750; -.
DR eggNOG; KOG2282; Eukaryota.
DR HOGENOM; CLU_000422_11_6_1; -.
DR InParanoid; F6HSN0; -.
DR OrthoDB; 19999at2759; -.
DR Proteomes; UP000009183; Chromosome 14.
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; 3.30.70.20; -; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 73..151
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 151..190
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 288..344
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 80919 MW; 9AE9A3330D43078C CRC64;
MGLGLIASRA LRPAILHRSS RVLASQNPIT RTITSTPELK NPEAATAQPD SPPDLPPRTP
VAGARIHFSK PDDAIEVFVD GYPVKIPKGM TVLQACEVAG VDIPRFCYHS RLSIAGNCRM
CLVEVEKSPK PVASCAMPAL PGMKIKTSTP VAKKAREGVM EFLLMNHPLD CPICDQGGEC
DLQDQSMAFG SDRGRFTDMK RSVVDKNLGP LVKTVMTRCI QCTRCVRFAT EVAGVQDLGM
LGRGSGEEIG TYVEKLMTSE LSGNVIDICP VGALTSKPFA FKARNWELKG TETIDVTDAV
GSNIRIDSRG PEVMRILPRL NEDINEEWIS DKTRFCYDGL KRQRLNDPMI RGADGRFKPV
SWRDALAVVA EVAHQVKPKE IVGIAGQLSD AESMMALKDF LNKMGSNNVL CEGNGSHPCA
DLRSGYLLNS NIAGLEKADV FLLVGTQPRV EAPMVNARIR KTVQATHAKV GYIGPATDFN
YDHQHLGTGP QTLLEIAEGR HPFCSAILNA KNPAIVVGAG LFERGDKDAI FAAVETIAKL
GKVIRPDWNG LNVLLLNAAQ AAALDLGLVP ESSKSIESAK FLYLMGADDV NLEKVPDDAF
VVYQGHHGDQ SVYRANVILP AAAFSEKEGT YENTEGCTQQ TLPAVPTVGD SRDDWKIIRA
LSEVAGVQLP YDTLGAIRSR IKTLAPNLYN MDEREAATFS TSLKPELSEK MSLSAFGSAV
ENFYMTDSIT RASKIMAQCS ATLLKK
//
