ID A0A250L1Y9_9GAMM Unreviewed; 596 AA.
AC A0A250L1Y9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=sS8_4419 {ECO:0000313|EMBL:BBA36349.1};
OS Methylocaldum marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylocaldum.
OX NCBI_TaxID=1432792 {ECO:0000313|EMBL:BBA36349.1, ECO:0000313|Proteomes:UP000266313};
RN [1] {ECO:0000313|EMBL:BBA36349.1, ECO:0000313|Proteomes:UP000266313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S8 {ECO:0000313|EMBL:BBA36349.1,
RC ECO:0000313|Proteomes:UP000266313};
RA Takeuchi M., Kamagata Y., Hiraoka S., Oshima K., Hattori M., Iwasaki W.;
RT "Genome sequencing of Methylocaldum marinum.";
RL Submitted (DEC-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; AP017928; BBA36349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250L1Y9; -.
DR KEGG; mmai:sS8_4419; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000266313; 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_01357; NDH1_NuoC; 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; IPR020396; NADH_UbQ_OxRdtase_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; PS00542; COMPLEX1_30K; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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 Quinone {ECO:0000256|HAMAP-Rule:MF_01359};
KW Reference proteome {ECO:0000313|Proteomes:UP000266313};
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}.
FT DOMAIN 47..175
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 326..596
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..187
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
FT REGION 211..596
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
SQ SEQUENCE 596 AA; 68116 MW; F4CE9DD07CB46267 CRC64;
MASTASADSA MKAGKPNAGA AVGELRRRFG NDAFTVQAVF DGIPTLWASK ERIVECLSFL
KREIERPYLM LFDLTAVDER LRQNRHGLPA SDFTLIYHLL SFDRNEDIRL KVALPEDGLS
VPSIAGLWPN ANWYEREVFD MFGIRFEGHP NLRRILMPPT WRGYPLRKDH PARATEMGRF
TLSERKQEAE QEALRFVPEE WGMKREKDDV DFLFLNLGPN HPSVHGVFRI ALQLDGEEIV
DAVPDIGYHH RAAEKMGERQ SWHTYIPYTD RVDYLGGSLN NLPYVMALEA MAGIEVPPRA
QMIRVMISEF YRINNHLLFY GTFAQDVGQL SPVFYMFVDR ERVFEIIEAI TGGRMHSSFF
RIGGTAMDLP EGWDKKVREF VDYFPKRLTH YDKMVLGNSI LKRRTQGIGV YSTREAIDWG
ATGPGLRATG FAWDYRKARP YSGYENFEFE IPSGKNGDCY DRCRVRVEEM RQSLRIIEQC
LNNMPSGPYK AFHPLTTPPP KARTMHDIET LIQHFLNVSW GPVIPAGEGS ACVEGTKGLY
RYYLTSDGST MSYRTRVRTA SFPHLQMIPL MSRGLMIADL IAILGSIDFV MSDVDR
//
