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Database: UniProt
Entry: Q5LPM8_RUEPO
LinkDB: Q5LPM8_RUEPO
Original site: Q5LPM8_RUEPO 
ID   Q5LPM8_RUEPO            Unreviewed;       523 AA.
AC   Q5LPM8;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   23-MAY-2018, entry version 77.
DE   RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203};
DE            EC=1.6.1.2 {ECO:0000256|PIRNR:PIRNR000203};
GN   Name=pntA {ECO:0000313|EMBL:AAV96061.1};
GN   OrderedLocusNames=SPO2820 {ECO:0000313|EMBL:AAV96061.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV96061.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV96061.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV96061.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled
CC       to respiration and ATP hydrolysis and functions as a proton pump
CC       across the membrane. {ECO:0000256|PIRNR:PIRNR000203}.
CC   -!- CATALYTIC ACTIVITY: NADPH + NAD(+) = NADP(+) + NADH.
CC       {ECO:0000256|PIRNR:PIRNR000203}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|PIRNR:PIRNR000203}.
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DR   EMBL; CP000031; AAV96061.1; -; Genomic_DNA.
DR   RefSeq; WP_011048520.1; NC_003911.12.
DR   ProteinModelPortal; Q5LPM8; -.
DR   STRING; 246200.SPO2820; -.
DR   EnsemblBacteria; AAV96061; AAV96061; SPO2820.
DR   KEGG; sil:SPO2820; -.
DR   eggNOG; ENOG4108IIE; Bacteria.
DR   eggNOG; COG3288; LUCA.
DR   HOGENOM; HOG000022121; -.
DR   KO; K00324; -.
DR   OMA; AKVFIMG; -.
DR   OrthoDB; POG091H0397; -.
DR   BioCyc; RPOM246200:G1G48-2870-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR026255; NADP_transhyd_a.
DR   InterPro; IPR024605; NADP_transhyd_a_C.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   Pfam; PF12769; PNTB_4TM; 1.
DR   PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00561; pntA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|PIRNR:PIRNR000203};
KW   NADP {ECO:0000256|PIRNR:PIRNR000203};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000203};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000203,
KW   ECO:0000313|EMBL:AAV96061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    415    434       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    440    458       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    465    484       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    490    512       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        4    139       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      148    316       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
SQ   SEQUENCE   523 AA;  55560 MW;  C2B9136AF47117B7 CRC64;
     MKIGTPKEIF EGENRVAMTP DSAVQLQKLG YDCAIESGAG AAAGFSDALY EAAGVEIIKT
     AAALWKEVDI VAKVRQPDAT ELKRLSKGKT LISFFNPAGN EDGMAAAKSK GANVIAMEMV
     PRISRAQKMD ALSSMANIAG YRAVIEAGNN FGRFFTGQVT AAGKVPPAKV LIVGAGVAGL
     AAIGTSTSLG AITYAFDVRP EVAEQVESMG AEFVYLDFEE EQQDGAATGG YASVSSPEFA
     AAQLAKFREL APEMDIVITT ALIPNREAPE LWTEDMVAAM KPGSVIVDLA AEKGGNCKLT
     VKDEKIVTEN GVTIIGYTDF PSRMAAQAST LYATNIRHMM TDLTPEKDGQ INHNMEDDVI
     RGATVTFEGD ITFPPPPPKV QAIAAKSKEK PKELTPEEKR AQEVAAFKAQ TKNQVTLLTV
     GGLLLLLVGL VAPASFMQHF IVFVLAVFVG FQVIWNVSHS LHTPLMAVTN AISSIIILGA
     LMQIGSGSFL VILLAGLSVF MAGINIFGGF LVTRRMLAMF QKS
//
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