ID A0A364Y2H4_9BACT Unreviewed; 912 AA.
AC A0A364Y2H4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=NADH-quinone oxidoreductase subunit G {ECO:0000313|EMBL:RAW00307.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:RAW00307.1};
GN ORFNames=DQQ10_14735 {ECO:0000313|EMBL:RAW00307.1};
OS Pseudochryseolinea flava.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Pseudochryseolinea.
OX NCBI_TaxID=2059302 {ECO:0000313|EMBL:RAW00307.1, ECO:0000313|Proteomes:UP000251889};
RN [1] {ECO:0000313|EMBL:RAW00307.1, ECO:0000313|Proteomes:UP000251889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDU1-6 {ECO:0000313|EMBL:RAW00307.1,
RC ECO:0000313|Proteomes:UP000251889};
RA Li Y., Wang J.;
RT "Chryseolinea flavus sp. nov., a member of the phylum Bacteroidetes
RT isolated from soil.";
RL Submitted (JUN-2018) 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 -!- 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:RAW00307.1}.
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DR EMBL; QMFY01000007; RAW00307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364Y2H4; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000251889; 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:0046872; F:metal ion 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; cd02788; MopB_CT_NDH-1_NuoG2-N7; 1.
DR CDD; cd02771; MopB_NDH-1_NuoG2-N7; 1.
DR Gene3D; 2.40.40.20; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
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; SSF50692; ADC-like; 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:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:RAW00307.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251889};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 1..85
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 912 AA; 101679 MW; 6488E9D1232C4DB4 CRC64;
MATIIIDCKT YEVPLGKNVL ETCLNLGFDV PYFCWHPGLG SVGACRQCAV KVFKDADDKK
GRLVMSCMEP VVHNQHLAVH DADTIDFRKQ VIEWLMTNHP HDCAVCDEGG SCHLQDMTVM
TGHHERRFTF NKRTYKNQDL GPFLNHEMNR CIQCYRCVRF YKDYAGGKDL DAYASKNNVY
FGRAEDGVLE NEFSGNLAEI CPTGVFTDKT LKEHYTRKWD LTMSPSICQH CSVGCNTIAG
ERYGALRMIH NRFHEKINGY FLCDRGRFGY EFVNAENRIK QPSINGDVVE RTELETRLEK
IMKSAKVIGI GSPRASLQSN FALKTLVGED NFYHGVSDHE HDLAELAVRI LKDGPVRTPS
TKEIEKSDAI FVLGEDLTNT APIVALAVRQ AVRQDLSGEP EKIHIQGWQD AARKNLQQQR
KMPLYSATIH ETKLDDICTS ANYATPEDIA RLGFAVAHCV DHNSPAPEHF PEALQVRARS
IANGLLAAKN PTIISGAGCA SSAVMKAAAN VAIALHKNGI VVGLTYTMLE CNSMGLTMIG
GHRLSAAFNA VINGHADTLI LLENDLFRHG SFAEVGDFLA RCKNVIVLDH TKSDSTDRAS
VVIPAGTFAE SDGIIVNNEG RAQRFFQVYE STESIQESWR WIINIGKTLQ HPKLQTWQNF
EDISKAMASE EPMLQNIDEV NPAVDFRIVG QRIPREPHRF SGRTSMHAHI QVSEQKPPTD
DDSPLSYTME GTRIQPPSAM IPFYWSPGWN SVQSVAKYQH EVGGSLKDGD SGIRLLEANA
ASSLVYFQGI PEAFVPLEHH LWIVPTYHIF GSEEMSAKSA SIQKRIPTPY LLISAVDANI
YHLKEQDIIK VSIANISYSF PIKINRNIPV GMAALPYGLC DAPINALPEW GIVETSPLTE
LHDYVRKTKV QH
//
