ID L8M0B9_9CYAN Unreviewed; 394 AA.
AC L8M0B9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NAD(P)H dehydrogenase, subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit H {ECO:0000256|HAMAP-Rule:MF_01358};
DE Short=NDH-H {ECO:0000256|HAMAP-Rule:MF_01358};
GN Name=ndhH {ECO:0000256|HAMAP-Rule:MF_01358};
GN ORFNames=Xen7305DRAFT_00023260 {ECO:0000313|EMBL:ELS02608.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS02608.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS02608.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS02608.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {ECO:0000256|HAMAP-Rule:MF_01358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01358};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01358};
CC -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC different subcomplexes with different compositions have been identified
CC which probably have different functions. {ECO:0000256|HAMAP-
CC Rule:MF_01358}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01358}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01358}; 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:ELS02608.1}.
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DR EMBL; ALVZ01000189; ELS02608.1; -; Genomic_DNA.
DR RefSeq; WP_006510258.1; NZ_ALVZ01000189.1.
DR AlphaFoldDB; L8M0B9; -.
DR STRING; 102125.Xen7305DRAFT_00023260; -.
DR PATRIC; fig|102125.3.peg.3081; -.
DR eggNOG; COG0649; Bacteria.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
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 Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01358};
KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Thylakoid {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 124..394
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 394 AA; 45461 MW; 3E2F9F3D09C719E4 CRC64;
MAQIETRTEP MVINMGPHHP SMHGVLRLIV TLDGEDVIDC EPVIGYLHRG MEKIAESRTN
VMYVPYVSRW DYAAGMFNEA ITVNAPEKLA GIEVPKRAQY IRVIMLELNR IANHLLWLGP
FLADVGATTP FFYIFREREL IYDLWEAATG QRLINNNYFR IGGVAVDLPY GWIDKCEDFC
DYFDPKIDEY EKLITNNPIF RRRVEGIGTI TRDEAINWGL SGPMLRGSGV KWDLRKVDHY
ECYDDFDWDI QWETVGDCYA RYLVRVKEMR ESVKILRQAL KGIPGGPYEN LEAKRLEEGR
KSQWNDFDYQ YIAKKVAPTF KIPTGEHYVR LESGKGELGI FIVGNDNVFP WRWKIRAPDF
NNLQILPHLL KGVKVADIMA ILGSIDVIMG SVDR
//
