ID A0A401V4T8_9CELL Unreviewed; 447 AA.
AC A0A401V4T8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN Name=nuoD2 {ECO:0000313|EMBL:GCD21917.1};
GN Synonyms=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
GN ORFNames=CTKZ_34790 {ECO:0000313|EMBL:GCD21917.1};
OS Cellulomonas algicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD21917.1, ECO:0000313|Proteomes:UP000288246};
RN [1] {ECO:0000313|EMBL:GCD21917.1, ECO:0000313|Proteomes:UP000288246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD21917.1,
RC ECO:0000313|Proteomes:UP000288246};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (NOV-2018) 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 a
CC menaquinone. 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|HAMAP-Rule:MF_01358}.
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|HAMAP-Rule:MF_01358};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC D, E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC ECO:0000256|RuleBase:RU003685}.
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:GCD21917.1}.
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DR EMBL; BHYL01000375; GCD21917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401V4T8; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000288246; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01962; NuoD; 1.
DR PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01358};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 159..447
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 48817 MW; D1E4F8EE739DD387 CRC64;
MSTPHATAHL VDDETTGVPT FEASGGDWSD IAEEAARLGE ERIVVNMGPQ HPSTHGVLRL
MLEIDGETVT EARAGIGYLH TGIEKNMEFR TWTQGVTFCT RMDYVAPLFQ EAAYCLGVEK
LLGITDDVPE RATVIRVLLM ELNRIASHLV CLATGGNELG ATTIMTVGFT AREEVLRIFE
LITGLRMNHA FIRPGGVAQD IPPGAIDTIR EALTSMRHYF KQLEDLMMAN PILHLRLKEV
GYLGLSGCMA LGITGPVLRS AGLPYDVRKA APYCGYETYD FEVPVATEAD SWARVVLRME
ECYQSMNIVE QTLDRLQKMG PGPVMVGDKK IAWPAQLAIG SDGMGNSLDH IKEIMGTSME
ALIHHFKLVT EGFRVPAGQV FQTVEHPRGE LGVHLVSDGG TRPYRAHFRD PSFNNLQAVS
IMCEGGQVAD VVVAVASLDP VLGGVDR
//
