ID A0A1G9NM71_9GAMM Unreviewed; 594 AA.
AC A0A1G9NM71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05661010_02779 {ECO:0000313|EMBL:SDL87696.1};
OS Halomonas muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=119000 {ECO:0000313|EMBL:SDL87696.1, ECO:0000313|Proteomes:UP000198654};
RN [1] {ECO:0000313|EMBL:SDL87696.1, ECO:0000313|Proteomes:UP000198654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14789 {ECO:0000313|EMBL:SDL87696.1,
RC ECO:0000313|Proteomes:UP000198654};
RA de Groot N.N.;
RL Submitted (OCT-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; FNGI01000008; SDL87696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9NM71; -.
DR STRING; 119000.SAMN05661010_02779; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000198654; Unassembled WGS sequence.
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; 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 Quinone {ECO:0000256|HAMAP-Rule:MF_01359};
KW Reference proteome {ECO:0000313|Proteomes:UP000198654};
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 45..173
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 324..594
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..185
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
FT REGION 209..594
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
SQ SEQUENCE 594 AA; 67772 MW; B3628C14B8591E0C CRC64;
MSVATPRSDS STTGASADPV VEALKQHFGD QAIREQDTLT GLPVLWVARE ALTDVIGFLR
NMPQPFEMLF DLSALDERLR GQRHGLPDAD FTVFYHLLSV SRNRDVMLKV ALAEGDLALP
SIVSLYPNAN WYEREVWDMF GIDFRGHPHL ARILMPPTWH GHPLRKDYPA RATEFDPYTL
TVEGQDKEQQ ALQFDPEAWG MRRGNDDTEF MFLNLGPNHP SAHGAFRIVL QLDGEEIVDC
VPDIGYHHRG AEKMAERQSW HSFIPYTDRI DYTGGVMNNL PYILAAEKLA GIQVTSRAET
IRVMMAELFR INSHLLFLGT YLQDLGAMTP VFFTFTDRQK AYEVIEAITG FRMHPAWYRI
GGVAHDLPNG WDRLMQGFLD WMPKRLREYE RVMMENAIVI ERTRHIAAFN TKEALAWGVT
GPNLRATGCD FDLRKQRPYS GYENFDFEIP LGANGDAFDR GQLRIDEMRQ SLRIIQQCVD
NMPAGDYKAD HPLTTPPPRD KMLQHIETLI THFLQVSWGP VLKPNESLQM IEATKGINSY
YLTSDGNTMS YRTRIRTPSF PHLQQIPMLM RGGFVPDLIA HLGSIDFVMA DVDR
//
