ID A0A0G4JXQ8_9GAMM Unreviewed; 599 AA.
AC A0A0G4JXQ8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01359};
DE AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
DE AltName: Full=NDH-1 subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
GN Name=nuoC {ECO:0000256|HAMAP-Rule:MF_01359};
GN Synonyms=nuoCD {ECO:0000256|HAMAP-Rule:MF_01359}, nuoD
GN {ECO:0000256|HAMAP-Rule:MF_01359};
GN ORFNames=AWC36_03210 {ECO:0000313|EMBL:ATA23191.1}, BN1221_03190
GN {ECO:0000313|EMBL:CPR18403.1};
OS Brenneria goodwinii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=1109412 {ECO:0000313|EMBL:CPR18403.1, ECO:0000313|Proteomes:UP000044377};
RN [1] {ECO:0000313|EMBL:CPR18403.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBR1 {ECO:0000313|EMBL:CPR18403.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000044377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBR1 {ECO:0000313|Proteomes:UP000044377};
RA Paterson Steve;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATA23191.1, ECO:0000313|Proteomes:UP000217214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRB141 {ECO:0000313|EMBL:ATA23191.1,
RC ECO:0000313|Proteomes:UP000217214};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. {ECO:0000256|ARBA:ARBA00002378,
CC ECO:0000256|HAMAP-Rule:MF_01359}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01359};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01359}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01359};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01359};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01359}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC subunit family. {ECO:0000256|ARBA:ARBA00010019, ECO:0000256|HAMAP-
CC Rule:MF_01359}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC subunit family. {ECO:0000256|HAMAP-Rule:MF_01359}.
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DR EMBL; CP014137; ATA23191.1; -; Genomic_DNA.
DR EMBL; CGIG01000001; CPR18403.1; -; Genomic_DNA.
DR RefSeq; WP_048638106.1; NZ_MJLY01000060.1.
DR AlphaFoldDB; A0A0G4JXQ8; -.
DR STRING; 1109412.BN1221_03190; -.
DR GeneID; 70905788; -.
DR KEGG; bgj:AWC36_03210; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000044377; Unassembled WGS sequence.
DR Proteomes; UP000217214; Chromosome.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR HAMAP; MF_01359; NDH1_NuoCD_1; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR023062; NADH_DH_suCD.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01961; NuoC_fam; 1.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF45; NADH-QUINONE OXIDOREDUCTASE SUBUNIT C_D; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR SUPFAM; SSF143243; Nqo5-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01359};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01359};
KW Oxidoreductase {ECO:0000313|EMBL:CPR18403.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01359};
KW Reference proteome {ECO:0000313|Proteomes:UP000044377};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01359};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01359, ECO:0000313|EMBL:CPR18403.1}.
FT DOMAIN 49..177
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 328..599
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..189
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
FT REGION 213..599
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
SQ SEQUENCE 599 AA; 68929 MW; 0D417ADF9F36E185 CRC64;
MTDLTTHDIA MPAWQTRDHL DDPVISELCN RFGPEAFTVQ ATRTGLPVVW VKREQLLEVV
SFLKKQPKPY VMLFDLHGVD ERLRTHREGL PAADFSVFYH LISIERNRDI MLKVALVEGD
MHLPTMTGLF PNANWYERET WEMFGMTFDG HPHLTRIMMP HTWEGHPLRK DYPARATEFD
PFVLTKQKED LEMESLTFKP EAWGMKRGTE NEDFMFLNMG PNHPSSHGAF RLILQLDGEE
ILDCVPDVGY HHRGAEKMGE RQSWHSYIPY TDRIEYLGGC VNEMPYVLAV EKLAGIEVPE
RVKTIRVMLS ELFRINSHLL YISTFIQDVG AMTPVFFAFT DRQKIYDLVE AITGFRMHPA
WFRIGGVAHD LPRGWERLLR EFLDWMPSRL DTYVKAALQN TILKGRTQGV AAYNAKEALE
WGVTGAGLRA TGIDFDIRKR RPYSGYENFD FEVPVGDGIS DCYSRVMLKV EELRQSLRIL
EQCLKNMPEG PFKADHPLTT PPPKERTLQH IDTLINHFLQ VSWGPVMPAN ESFQMIEATK
GINSYYLTSD GGTMSYRTRI RTPSYAHLQQ IPSVIRGCLV SDLIVYLGSI DFVMSDVDR
//
