ID A0A366ZFR4_9ACTN Unreviewed; 819 AA.
AC A0A366ZFR4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=DQ238_20715 {ECO:0000313|EMBL:RBY75051.1};
OS Geodermatophilus sp. TF02-6.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY75051.1, ECO:0000313|Proteomes:UP000253027};
RN [1] {ECO:0000313|EMBL:RBY75051.1, ECO:0000313|Proteomes:UP000253027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-6 {ECO:0000313|EMBL:RBY75051.1,
RC ECO:0000313|Proteomes:UP000253027};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL Submitted (JUL-2018) 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:RBY75051.1}.
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DR EMBL; QOHF01000031; RBY75051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366ZFR4; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000253027; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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 CDD; cd02788; MopB_CT_NDH-1_NuoG2-N7; 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; 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; 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; 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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; 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:RBY75051.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000253027};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 22..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..141
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 240..296
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 819 AA; 86221 MW; 889DE71F0F482D51 CRC64;
MTTPQPAPAA VPAVPGPHTP PDAVHCTIDG FDVAVPKGTL IIRAAEMVGI QIPRFCDHPL
LEPVGACRQC LVEVEGQRKP VASCTMPVTD GMAVKTQLTS PVADKAQQGT MELLLINHPL
DCPVCDKGGE CPLQNQAMSN GRTESRFVDV KRTYPKPLPI SAEILLDRER CVLCARCTRF
SQQIAGDPFI ELFERGALEQ VAVYEDEPFS SYFSGNTTQI CPVGALTSAQ YRFRSRPFDL
RSEPSVCEHC ASGCAQRTDY RRGRVLRRLA GEDPAVNEEW NCDKGRFAFR YATANDRLTT
PLVRRDGVLE PASWPEAWAA AAEGLRAARD AGGVGVLPGG RLTVEDAYAY AKFARVALGT
NDVDARARAH SPEELAFLTA HVAGTGPWNG AVTYADLAAA PAVLLAGFEP EEESPIVFLR
LRRAVRKNRL AVFDLAPFTT RAAEKLQATV LTTLPGTEAR SLAALAEGTW GGPAVEALRT
PGAVVLAGER LAEVPGAFSA LSALAAATGA RLAWVPRRAG ERGAVEAGAL PTLLPGGRPV
TDAGARVQVA AAWGVADLPP TPGRDTTGIL TAAAHGELSG LLVGGVDPAD LPDPRLAEAA
LGRAGFVVSL ELLPSAVTAH ADVVLPVAAA AEKAGGYLDW EGRLRSFDAT LHGTGQLPDG
RVLQGLADEL DVDLRLPGPE AARAELAALG VVAERPPVTG LDVAPPAAPR LAEDEAVLAS
WRQLLDVGTL QRDEPELAGT AHPAVARIGK DAARRLGLAD GDRLTVEGEM GHVTLPVLVT
EMPDQVVWLP MRSPGSELRT RLGTPPGGVV TLCTAEGTA
//
