ID A0A095WXT9_9ACTO Unreviewed; 854 AA.
AC A0A095WXT9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=NADH-quinone oxidoreductase subunit G {ECO:0000313|EMBL:KGF02261.1};
GN ORFNames=HMPREF1628_01745 {ECO:0000313|EMBL:KGF02261.1};
OS Actinomyces sp. S4-C9.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF02261.1, ECO:0000313|Proteomes:UP000035029};
RN [1] {ECO:0000313|EMBL:KGF02261.1, ECO:0000313|Proteomes:UP000035029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4-C9 {ECO:0000313|EMBL:KGF02261.1,
RC ECO:0000313|Proteomes:UP000035029};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KGF02261.1}.
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DR EMBL; JRMU01000004; KGF02261.1; -; Genomic_DNA.
DR RefSeq; WP_034507112.1; NZ_JRMU01000004.1.
DR AlphaFoldDB; A0A095WXT9; -.
DR eggNOG; COG1034; Bacteria.
DR Proteomes; UP000035029; 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: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 CDD; cd00207; fer2; 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; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR43105:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 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; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000035029}.
FT DOMAIN 4..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 93..132
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 287..343
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 854 AA; 91182 MW; 4343EC7BEF5FA5FC CRC64;
MSEELVTLTI DDTEVSVPKG TLIIRAAEQV GIRIPRFCDH PLLAPAGACR QCLVEVAAPD
RTGEVRPFPK PQASCTMTVM PGMVVKTQRT SEVAEKAQKG VMEFLLINHP LDCPICDKGG
ECPLQNQAMS EGREVSRFDD AKRTFVKPIK LSTQIALDRE RCILCQRCTR FSKQIAGDAF
IDLQGRGGGT APTEDHQFMG EQVGRFDTAV LGFHSDASNI NSDEGFAGPF GNPGYESGLN
AGPVGAAEAD TSGRPFASYF SGNTIQICPV GALTSTSYRF RGRPFDLVST PSVSAHDASG
AATRIDIRRG EVVRVLAGED ADVNEEWITD KDRFAFTWST GEDRLTAPLV REDGKLVPTS
WADALDRAAR GLKEAREAGK TVLLPGGRLT VEDGYAWSKF ARVVMNTNQV DGRVRATSLE
ETKFLGTRVA GTGLGVTYKE LEKAGRVLIV GLEAEDEAGN VFLRLRKGAL AGSVKVSVVA
PMTTPSTRKM NADLLRAAPG TEPEVLDAVS GDLATELANG VIVVGERAVE IPGLYTAVAR
LADRTGARIA WIPRRAGERG GLEVGLNPNL LPFGRSAADA DARIDMEAVW GAKLPSDPTK
CTVDILAEAA TDPRSAMILG GVDSRDVTDP ENLKSAIEKS GFVVALEVRR TDLTEMADVV
FPVAPVTEKN GTFINWEGRL RPFGQALATR ALTDREVLHR LAGLMGVNLG VETLKDTHAE
INELMEWDGS RIDSPAISPA PVQAPGAGNA VLATHKLMLD EGRMQDFAPE LAGTARRSVA
RMNVATMQTI GVAEGDLVSV STSRGTITLP VAVTDLPEDV VWLPECSAGS HVHETLGAKN
GSVVSIAANT EVNR
//
