ID A0A0A0JLA4_9MICO Unreviewed; 830 AA.
AC A0A0A0JLA4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=N803_10775 {ECO:0000313|EMBL:KGN38230.1};
OS Knoellia subterranea KCTC 19937.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN38230.1, ECO:0000313|Proteomes:UP000030011};
RN [1] {ECO:0000313|EMBL:KGN38230.1, ECO:0000313|Proteomes:UP000030011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN38230.1,
RC ECO:0000313|Proteomes:UP000030011};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia subterranea.";
RL Submitted (AUG-2013) 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. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|RuleBase:RU003525}.
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 ECO:0000256|RuleBase:RU003525};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|RuleBase:RU003525};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU003525};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU003525};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU003525}.
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:KGN38230.1}.
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DR EMBL; AVPK01000003; KGN38230.1; -; Genomic_DNA.
DR RefSeq; WP_035903803.1; NZ_AVPK01000003.1.
DR AlphaFoldDB; A0A0A0JLA4; -.
DR STRING; 1385521.N803_10775; -.
DR eggNOG; COG1034; Bacteria.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000030011; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
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; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 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; 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: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; 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; 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; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|RuleBase:RU003525};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003525};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003525};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003525};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003525}; NAD {ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:KGN38230.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000030011};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 19..106
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 108..147
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 246..302
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 699..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 87578 MW; 5EC6C3AF89736B63 CRC64;
MTVTSDAKTG ADSDKPAVEM VDLTIDGIDV SVPKNTLVIR AAEEAGIEIP RFCDHPLLEP
VGACRQCLVD VATPGPDGTL RPMPKPQASC TMTVSPGMDV KTQHTSPVAE KAQHGVMELL
LINHPLDCPV CDKGGECPLQ NQAMSTGRPV SRFEDIKRTY PKPINISSQV LLDRERCVLC
ARCTRFSEQI AGDPFIALVE RGALQQVGIY EEKPFESYFS GNTVQICPVG ALTGAAYRFR
ARPFDLVSTP SVTEHDASGA AIRIDHRRGS VLRRMAADEP EVNEEWISDK DRWAFQYVST
PTRLELPMVR EDGELRVASW REALEVAAEG LRAASAAGVL VGGRVSAEDA YAYGKFARTI
LGTNDIDFRA RPHSAEETAF LASHVVATAP QGGAVTYADL ESAKTVVLAG FEPEDESPII
FLRLRKASRK NKTAVYAVSP VATRGLAKVS GRLIPTAPGT EPEVLEALGK GSASGAAGEG
PDTVREAAEA LRGEGAIILV GERLATVPGA LSAAAALAET TGARLAWIPR RAGERGALEA
GAFPTLLPGG RSVSDAAARS DVASVWGVVG LPDTPGRDAA AILEAARTGQ LGALVVGGVD
PLDFGRADAA QAFESTFVVS LELRESAVTQ IADVVLPVAA HAEKAGTFVN WEGRTRPFQQ
ALETGYVSDH RVLDMLADEM GEFLGCRTAA EVRAEMERIG PSTGDRAAAP TTSAGEVPSA
EDGHFVLATW RHLLDKGLLQ DGEPFLAGTA PKPTAKVSPV TADSLGVTDG DTVTVVAGDA
TVTVPVTVTE MADHVVWLPT NSEGCDLRGT LADAPAIRVS VTKVDKVESE
//
