ID H5XEU8_9PSEU Unreviewed; 831 AA.
AC H5XEU8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=SaccyDRAFT_0396 {ECO:0000313|EMBL:EHR59330.1};
OS Saccharomonospora cyanea NA-134.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882082 {ECO:0000313|EMBL:EHR59330.1};
RN [1] {ECO:0000313|EMBL:EHR59330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA-134 {ECO:0000313|EMBL:EHR59330.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "The Noncontiguous Finished sequence of Saccharomonospora cyanea NA-134.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; CM001440; EHR59330.1; -; Genomic_DNA.
DR RefSeq; WP_005453104.1; NZ_CM001440.1.
DR AlphaFoldDB; H5XEU8; -.
DR STRING; 882082.SaccyDRAFT_0396; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_4_0_11; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000002791; Chromosome.
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 CDD; cd02788; MopB_CT_NDH-1_NuoG2-N7; 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 InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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; 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; 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|RuleBase:RU003525};
KW NAD {ECO:0000256|RuleBase:RU003525};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 18..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 253..309
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 831 AA; 88496 MW; C06C16B1BEB8AFE8 CRC64;
MTIAPEAASK DKTPVPEGHV KLTIDGEEVI APKGELLIRT AERLGTVIPR FCDHPLLDPA
GACRQCLVEV EMNGRPMPKP QASCTMTVAD GMVVKTQRTS PVADKAQQGV MELLLINHPL
DCPVCDKGGE CPLQNQAMAH GRPESRFRDR KRTFPKPLPI STQVLLDRER CVLCQRCTRF
SAQIAGDSFI DLLERGAQQQ IGTSETADVL DAASHTSSGT PFQSYFSGNT IQICPVGALT
SAQYRFRSRP FDLVSSPSVC EHCSVGCAMR TDFRRGKVMR RLAGDDPEVN EEWLCDKGRF
AFRYAGAADR IRHPLVRNPE TGELEQASWT QALRVAAEGL AKARDGHGVG VLPGGRLTVE
DAYAYSKFAR AALATNDIDF RARAHSSEEA DFLASHVVGT TPETGVTFDQ LETAPLVLCV
AFEPEEEAPV LFLRLRKGAR KHGTKVVHIG QWTTPAVRKT LGELLACAPG AEAGALDGLA
EHAPDVDEQL RAEGSVVLVG ERAAEVPGLY SALHRLSERT GAPIAWVPRR AGERGALEAG
ALPTLLPGGA AVTDAEARAA LERAWKLEAG SLPARVGRDT DGILTAVRSG DLDGLLVGGV
ELADLPDPEL AREALRRCGF VVSLELRHSE VTEHADVVLP IAPVDEKSGS FLNWEGRRRE
FSVTLDGTGA LPDCRVLDTL AVEMDVDLFT QTPTAAAGDL ARSTEGLADG PRPAAPDVPN
AAVPSLGPGQ ALLATWRQLL DDGALQVDEP HLAGTARRVV ARISRATAAS LDEPSSVTVS
TDRGSVTLPV EIADLPDGVV WLPGNSPGSK LRATLGVGHG AVVSIAAGGE R
//
