ID A0A1V8MA22_9GAMM Unreviewed; 924 AA.
AC A0A1V8MA22;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=NADH-quinone oxidoreductase subunit G {ECO:0000256|ARBA:ARBA00019902};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
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=AU255_11720 {ECO:0000313|EMBL:OQK18451.1};
OS Methyloprofundus sedimenti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloprofundus.
OX NCBI_TaxID=1420851 {ECO:0000313|EMBL:OQK18451.1, ECO:0000313|Proteomes:UP000191980};
RN [1] {ECO:0000313|EMBL:OQK18451.1, ECO:0000313|Proteomes:UP000191980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|EMBL:OQK18451.1,
RC ECO:0000313|Proteomes:UP000191980};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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:OQK18451.1}.
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DR EMBL; LPUF01000001; OQK18451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8MA22; -.
DR STRING; 1420851.AU255_11720; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000191980; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000191980}.
FT DOMAIN 11..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 146..176
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..218
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 225..280
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 924 AA; 101616 MW; 5D14EC6C2EDB541F CRC64;
MAANPDTLNQ PMINFTLDGE EVSAFADETI LQTAKRHNKE IPHLCYKEGL RADGNCRACV
VEIEGERTLA PSCCRMPTAG MKVQASSERA IRSQKMVLEL LKSDIPDQGE SPYKIDSELD
QWVKKLQVGA PRFTSRAQPA ADLSHPAIAV NMDACIQCTR CLRACREEQM NDVIGFANRG
AHAEIVFDIA DPMAASSCVA CGECVQVCPT GALMPANNVG LEVVDKTVNS TCPYCGVGCL
IKYHVKDDQI LYTEGRDGDT NKFRLCVKGR YGFNYIHNPL RLTKPLIRRE GVAKTTELLD
PNDLDTIFRE ASWDEALDFA AGGLIKIRDE KGKKALAGLG SAKGSNEEAY LFQKLVRTGF
GSNNVDHCTR LCHASSVVAL LECLGSGAVS NPVEDVKLAD VVIIIGSNPT VNHPVGATFM
KNATKTGTKI ILIDPNRTAI AKYASHVLQF RPDTDVALLN GIMHVILDEG LQNDAYIKKY
TEDFEYMKQH LKDYSPEKVA PICGIDAETL REIARLYATS KNSMILWGMG ISQHIHGTDN
SRCLIAMALM TGQIGRPGTG LHPLRGQNNV QGASDVGLIP MVYPDYEPVE DPVNQAKYEK
LWNVKLDPKR GLTTVEMIHA ILDNEIYGMF VEGENPAMSD PNQNHVREAF SKLEHLVVQD
IFLTETAGFA DVILPASAFY EKTGTFSNTD RRVQMGRQAV NPPGDAKQDL WILQEVANRL
GCGWTYQGPE DVFEEMRLAM GSIAGMTWDR LENEDSLTYP LENVGDPGEP IIFTDGFPTE
SGKGRFVPAS YIHADEMPDD EYPLIFITGR QLEHWHTGSM TRHSPTLDAI EPDPVVMVHP
EDLHKLGIQP GDIITIQSRR GKISAYARAD IGIQKGSLFM AFCYNEASAN LITNEALDPS
AKIPEFKFCA VKASAGGEIS VRIN
//
