ID A9A347_NITMS Unreviewed; 378 AA.
AC A9A347;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ABX12175.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ABX12175.1};
GN OrderedLocusNames=Nmar_0279 {ECO:0000313|EMBL:ABX12175.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12175.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX12175.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX12175.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|RuleBase:RU003685}.
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DR EMBL; CP000866; ABX12175.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A347; -.
DR STRING; 436308.Nmar_0279; -.
DR EnsemblBacteria; ABX12175; ABX12175; Nmar_0279.
DR KEGG; nmr:Nmar_0279; -.
DR eggNOG; arCOG01548; Archaea.
DR HOGENOM; CLU_015134_1_2_2; -.
DR InParanoid; A9A347; -.
DR OrthoDB; 43567at2157; -.
DR PhylomeDB; A9A347; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 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 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; 2.
DR SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003685};
KW Oxidoreductase {ECO:0000313|EMBL:ABX12175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000792};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003685};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003685}.
FT DOMAIN 132..297
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT DOMAIN 309..378
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 378 AA; 42863 MW; 1E687ADC90828393 CRC64;
MTDIMPPGLA LKKVDERIMT LNVGPQHPGS GHMRIVVQID GDYIVACDPD PGYVHRGEEK
MAEYRNYITN VPHLERPVIH DSCNVLYPYV LGAEEILGIE VPERAKYVRV ICSELNRCIY
TMYWLAIYGI FLGHSTMFMW PAGDRELLID LMEKVSGARV THAHFIPGGV RNDLPANFED
VCLRQVNYFE KRIKEYAAVF YDNPILISRT QDTGVLSREN AIRYGTTGSV LRASGVDYDL
RVKAPYDVYD ELDVHTNVLK EGDSYARSKV PWLDMMESCN IIRQALQKMP KSGSVRTKLK
PNPKTKGPAT VYKRVESGRG SLGCYIVSDG KTEPYRVKMS VPSFRNLLAM PNLLIGEKLG
NMPSVYWSLN YWPVEADR
//
