ID S6GMY4_9GAMM Unreviewed; 917 AA.
AC S6GMY4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=NADH-quinone oxidoreductase subunit G {ECO:0000256|ARBA:ARBA00019902};
DE AltName: Full=NADH dehydrogenase I subunit G {ECO:0000256|ARBA:ARBA00031577};
DE AltName: Full=NDH-1 subunit G {ECO:0000256|ARBA:ARBA00032783};
GN ORFNames=OFPI_12410 {ECO:0000313|EMBL:EPJ52929.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ52929.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ52929.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000256|ARBA:ARBA00000100};
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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC {ECO:0000256|ARBA:ARBA00026021}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPJ52929.1}.
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DR EMBL; ASZI01000086; EPJ52929.1; -; Genomic_DNA.
DR AlphaFoldDB; S6GMY4; -.
DR PATRIC; fig|1330035.3.peg.1192; -.
DR Proteomes; UP000014830; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 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 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; 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:UP000014830};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 2..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 83..122
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 221..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 917 AA; 101896 MW; DED7D6D4D6009A60 CRC64;
MPEINIDGKT YQVTAGKNLL QACQELKLQL PYFCWHPALD SVGSCRQCAV LMFQNDQDTR
GRITMACMTA VSDGQRFSIQ AGKAQKFRQL CIEATMTSHP HDCPVCEEAG ECHLQDMTLI
SGHIERRFQG PKRTHKNQYL GPFINHEMNR CIACYRCVRY YRDYSGGTDL NVFSSRNNVF
FGRAQAGVLE SEFSGNLAEV CPTGVFTDKT YSAHYSRKWD LQSAPAVCVH CSIGCNTFPA
ERNGILRRIT NRYHPQINGY FLCDRGRFGY DFVNHAQRTE HAWQRNNSSQ TTEQLNSQRA
QDSFSSYLKN TEQLLAIGSS RSSLENNFCL QSLVGAENFY SDNSAQLETQ LQQLLDHYRN
VQPSSDLNSL EASDTVLLIG ADVTQSAPRI ALSIRQMIKN AGIAKAATLG VAYWSAAEVQ
NIRQQLKSPL HIISSHSTRL DDIARSIDNN HPHQQLALIN EICSCFSKDK SNAAQSPADD
DSIAAKAKAI YRDLLQAEKP FIVTGIHPGQ PVELLLASLK LSAMLYQHNK QAGLICAVPW
ANSLGLALLT DRQQNIDTVL QRLEMRTVKT LVILETDLYR YCSTQKMHKL LADVENIIVL
DHLITATGEQ ADLLLPSSSF AEQHGSWVNY EARLQHSLKC FAAASQRRPA YQWLTANTPL
QTIIKDLSGV AECLRELPSL YSIKSDDFHV ARKTVRESGR TALHSFINIK DIQPDADLDS
NYQHSQEGLA SNLHNNQSPA YIWSPHWNSS ESLNQFQDSE SGAIQGAHSG LLLFARRQTA
NSCVTQKQPF DSVKESSADS QNVLRVLPFE HIFADEELSR YVEHIGQLAP ADCIRINTAQ
AQRLGLIANQ LLDYSFVTAD GSALESTEPA STTALPLTID DSIAAGVALL PTLLLQRAPA
SVVCWLSLAS AEESSDA
//
