GenomeNet

Database: UniProt
Entry: G9ZAD7_9ENTR
LinkDB: G9ZAD7_9ENTR
Original site: G9ZAD7_9ENTR 
ID   G9ZAD7_9ENTR            Unreviewed;       184 AA.
AC   G9ZAD7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|ARBA:ARBA00019907, ECO:0000256|RuleBase:RU004429};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN   ORFNames=HMPREF0880_04498 {ECO:0000313|EMBL:EHM44811.1};
OS   Yokenella regensburgei ATCC 43003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Yokenella.
OX   NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM44811.1, ECO:0000313|Proteomes:UP000003044};
RN   [1] {ECO:0000313|EMBL:EHM44811.1, ECO:0000313|Proteomes:UP000003044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM44811.1,
RC   ECO:0000313|Proteomes:UP000003044};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-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:RU004429}.
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|RuleBase:RU004429};
CC   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC       M, N constitute the membrane sector of the complex.
CC       {ECO:0000256|ARBA:ARBA00025811}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU004429};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU004429}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC       {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004429}.
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:EHM44811.1}.
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; AGCL01000047; EHM44811.1; -; Genomic_DNA.
DR   RefSeq; WP_006820944.1; NZ_JH417874.1.
DR   AlphaFoldDB; G9ZAD7; -.
DR   STRING; 1002368.HMPREF0880_04498; -.
DR   GeneID; 66902393; -.
DR   PATRIC; fig|1002368.3.peg.4105; -.
DR   HOGENOM; CLU_085957_0_1_6; -.
DR   Proteomes; UP000003044; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR   InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR   InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR   PANTHER; PTHR33269:SF5; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR33269; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6; 1.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU004429};
KW   Membrane {ECO:0000256|RuleBase:RU004429};
KW   NAD {ECO:0000256|RuleBase:RU004429};
KW   Quinone {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane {ECO:0000256|RuleBase:RU004429};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT   TRANSMEM        6..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        56..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        91..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
FT   TRANSMEM        134..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004429"
SQ   SEQUENCE   184 AA;  19958 MW;  93E814CCCB3699F3 CRC64;
     MEFAFYICGL IAILATLRVI THTNPVHALL YLIISLLAIS GVFFSLGAYF AGALEIIVYA
     GAIMVLFVFV VMMLNLGGAE IQQERQWLKP QIWIGPAILS AVLLVVIVYA IVGLNDQGID
     GAAISAKAVG ITLFGPYVLA VELASMLLLA GLVVAFHIGR EDRMGEVLSN RTEDREKRKT
     EEHA
//
DBGET integrated database retrieval system