ID F9EIS0_9ACTO Unreviewed; 334 AA.
AC F9EIS0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=NADH-quinone oxidoreductase subunit J {ECO:0000256|RuleBase:RU004429};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU004429};
GN Name=nuoJ {ECO:0000313|EMBL:EGQ72837.1};
GN ORFNames=HMPREF9062_2355 {ECO:0000313|EMBL:EGQ72837.1};
OS Actinomyces sp. oral taxon 448 str. F0400.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=888056 {ECO:0000313|EMBL:EGQ72837.1, ECO:0000313|Proteomes:UP000005351};
RN [1] {ECO:0000313|EMBL:EGQ72837.1, ECO:0000313|Proteomes:UP000005351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0400 {ECO:0000313|EMBL:EGQ72837.1,
RC ECO:0000313|Proteomes:UP000005351};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (MAY-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 -!- 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:EGQ72837.1}.
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; AFQC01000056; EGQ72837.1; -; Genomic_DNA.
DR RefSeq; WP_009750253.1; NZ_GL985606.1.
DR AlphaFoldDB; F9EIS0; -.
DR STRING; 888056.HMPREF9062_2355; -.
DR eggNOG; COG0839; Bacteria.
DR HOGENOM; CLU_067307_0_0_11; -.
DR OrthoDB; 13239at2; -.
DR Proteomes; UP000005351; 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 Oxidoreductase {ECO:0000313|EMBL:EGQ72837.1};
KW Quinone {ECO:0000256|RuleBase:RU004429};
KW Reference proteome {ECO:0000313|Proteomes:UP000005351};
KW Transmembrane {ECO:0000256|RuleBase:RU004429};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004429}.
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 50..71
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004429"
FT REGION 256..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 33864 MW; 8A8515716F5397D4 CRC64;
MRILPVLAPA TLTDAGTAST GETILFGVVA LITVVCGLGL LTAKRAVSAA ANMIGIMIGL
AVLYVAGEAP FLGMTQIVVY TGAVMTLVLF VIMMVGIGGD EPVSTAGSSA GRWVIALLGV
GLVAVLAAVV WRSAIPSASG LQGGDAAVPS ALAGVLFGDH VVTMELTGVL LVIAAVGALT
LTHRQRIRPR MTQRDQVDAR MRAYAEEGAH PGQKPMPGVY AATNAATAPA LSADGDALAE
SVPRVLRVRD QGLDLSEASP EAGAAQRAGT IASREDATVG RSGMPAMPGA PAPDVVQPVT
APSPQEDAPG EDRSETDPAP AERGNGHSSK EEQK
//
