ID V2TXU9_9GAMM Unreviewed; 596 AA.
AC V2TXU9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=P256_01155 {ECO:0000313|EMBL:ESK40700.1};
OS Acinetobacter nectaris CIP 110549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1392540 {ECO:0000313|EMBL:ESK40700.1, ECO:0000313|Proteomes:UP000023785};
RN [1] {ECO:0000313|EMBL:ESK40700.1, ECO:0000313|Proteomes:UP000023785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110549 {ECO:0000313|EMBL:ESK40700.1,
RC ECO:0000313|Proteomes:UP000023785};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter nectaris CIP 110549.";
RL Submitted (OCT-2013) 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}.
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:ESK40700.1}.
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DR EMBL; AYER01000003; ESK40700.1; -; Genomic_DNA.
DR RefSeq; WP_023272732.1; NZ_KI530712.1.
DR AlphaFoldDB; V2TXU9; -.
DR STRING; 1392540.P256_01155; -.
DR PATRIC; fig|1392540.3.peg.1121; -.
DR eggNOG; COG0649; Bacteria.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_015134_3_2_6; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000023785; 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; 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:UP000023785};
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; 68559 MW; 2B494995CC4B42B0 CRC64;
MAETEIAMPD ESSKVDSRPA FAIIEELKSK FGDNFYVQPT FEDFPTIWVE RAQVQDVLMF
LRTISRPYVM LFDLSAVDER MRQHREGLPA SDFTVFYHLL SLERNADIRI KVALNETDLK
LPTATNIWPN ANWYEREAYD MFGIHFDGHP MLRRILLPTY WEGHPLRKEY SARATEYTPY
MQNQAKQDFE QEHLRFVPED WGLKRGNDDE DFMFLNLGPN HPSAHGAFRI ILQLDGEEVK
DCVPDIGYHH RGVEKMAERQ TWHSFIPYTD RVDYLGGCAQ NMPYVMGVEK LAGITVPDRA
QCIRVMMSEL FRINNHLLFI GTAIQDAGGM TPVFYMFADR QKIYDAIEAI TGFRMHPAWF
RIGGTAHDLP NNWQKLIRDI LDWMPKRLDE YYKAALRNSV FIGRTRNVAQ YNAKSALAWG
VTGTGLRATG IDFDVRKYRP YSGYENYDFD VPVEYEGDAY ARVMVHFHEI RESLKIVQQC
LDNMPSGAYK ADHALAVPPP KDKTLQDIET LITHFLSVSW GPVMPAGESS VMAEVVKGAS
NYYLTSDKAT MSYRTRIRTP TFTHLQQIPS VINGSLVSDL IIYLATIDVV MADVDR
//
