GenomeNet

Database: UniProt
Entry: A0A1X6Z981_9RHOB
LinkDB: A0A1X6Z981_9RHOB
Original site: A0A1X6Z981_9RHOB 
ID   A0A1X6Z981_9RHOB        Unreviewed;       662 AA.
AC   A0A1X6Z981;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   Name=nqo3 {ECO:0000313|EMBL:SLN44092.1};
GN   ORFNames=ROH8110_02297 {ECO:0000313|EMBL:SLN44092.1};
OS   Roseovarius halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN44092.1, ECO:0000313|Proteomes:UP000193207};
RN   [1] {ECO:0000313|EMBL:SLN44092.1, ECO:0000313|Proteomes:UP000193207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN44092.1,
RC   ECO:0000313|Proteomes:UP000193207};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FWFU01000003; SLN44092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6Z981; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000193207; 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; 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   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   InterPro; IPR015405; NDUFS1-like_C.
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; PF00384; Molybdopterin; 1.
DR   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   Pfam; PF09326; NADH_dhqG_C; 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   Oxidoreductase {ECO:0000313|EMBL:SLN44092.1};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193207};
KW   Translocase {ECO:0000256|RuleBase:RU003525}.
FT   DOMAIN          5..90
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          90..129
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          227..283
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   662 AA;  71325 MW;  6EBFFC5A994F838F CRC64;
     MSDLRKIIID DQEVEAEGAM TLIQACEQAG IEIPRFCYHE RLSIAGNCRM CLVEVVGGPP
     KPAASCAMQV RDLRPGPEGQ PPVVKTNSPM VKKAREGVME FLLINHPLDC PICDQGGECD
     LQDQAMAYGV DFSRYREPKR AVDDLDLGPL VETHMTRCIS CTRCVRFTTE VAGIAQMGQT
     GRGEDAEITS YLGETLDSNL QGNIIDLCPV GALVSKPYAF TARPWELAKT ETIDVMDALG
     SNIRVDTKGR EVMRILPRNH DGVNEEWISD KTRFVWDGLR RQRLDRPYIR ENGKLRAATW
     GEALELAAQK IKGADKLAGL VGDLVPVEGA FALKQLVEGQ GGNVECRTDG AHLPAGNRSG
     YVGNVAIEEL DTAKEFVLIG TNPAIEAPVL NARIRKAWIN GANVTLVGPA ANLTYEYSHA
     GTGRDALAKV KAGEDAIVIV GQSALNEADG AAVLAAAQAI SGRVLVLHSA AGRVGAMDAD
     CTTEGGMEAA IDGADVIYNL GADEIDIQAG PFVIYQGSHG DRGAHRADVI LPGAAYPEEQ
     GLFVNTEGRP QLALRASFPP GEAKENWAIL RALSGEMGQA LPYDSLIQLR KALVAEVPHL
     SKIDQVVENQ WQPLPEGKLG KADFRLTMRD FYLTNPIARA SELMAELSAN AKTRHQAPVA
     AE
//
DBGET integrated database retrieval system