(data stored in SCRATCH zone)

SWISSPROT: A1SDC1_NOCSJ

ID   A1SDC1_NOCSJ            Unreviewed;       471 AA.
AC   A1SDC1;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=NAD(P) transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
DE            EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000204};
DE   AltName: Full=Nicotinamide nucleotide transhydrogenase subunit beta {ECO:0000256|PIRNR:PIRNR000204};
GN   OrderedLocusNames=Noca_0261 {ECO:0000313|EMBL:ABL79806.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79806.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79806.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
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:PIRNR000204}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC         Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349;
CC         EC=7.1.1.1; Evidence={ECO:0000256|PIRNR:PIRNR000204};
CC   -!- SIMILARITY: Belongs to the PNT beta subunit family.
CC       {ECO:0000256|PIRNR:PIRNR000204}.
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DR   EMBL; CP000509; ABL79806.1; -; Genomic_DNA.
DR   RefSeq; WP_011753757.1; NC_008699.1.
DR   STRING; 196162.Noca_0261; -.
DR   EnsemblBacteria; ABL79806; ABL79806; Noca_0261.
DR   KEGG; nca:Noca_0261; -.
DR   eggNOG; ENOG4105C15; Bacteria.
DR   eggNOG; COG1282; LUCA.
DR   HOGENOM; HOG000243958; -.
DR   KO; K00325; -.
DR   OMA; AMTSMPE; -.
DR   OrthoDB; 788546at2; -.
DR   BioCyc; NSP196162:GH4V-263-MONOMER; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008750; F:NAD(P)+ transhydrogenase (AB-specific) activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012136; NADH_DH_b.
DR   InterPro; IPR034300; PNTB-like.
DR   Pfam; PF02233; PNTB; 1.
DR   PIRSF; PIRSF000204; PNTB; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDC1.
DR   SWISS-2DPAGE; A1SDC1.
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR000204};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000204};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000204, ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|PIRNR:PIRNR000204};
KW   NADP {ECO:0000256|PIRNR:PIRNR000204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Translocase {ECO:0000256|PIRNR:PIRNR000204};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     54       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     60     80       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     92    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    185       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    191    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    217    236       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    242    261       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       10    460       PNTB. {ECO:0000259|Pfam:PF02233}.
SQ   SEQUENCE   471 AA;  49211 MW;  46C0E84489CC9497 CRC64;
     MSAVSISVGA YLVASLLFIL SLAGLSRHES ARNGVNYGIA GMALALAATV GLLVHDTDEA
     LPLVLLVVAM TVGAAIGLWR ARVVAMTGMP ELIALLHSFV GLAAVLVGWN GYLHDEGLTG
     SLFRIHSAEV VIGVFIGAVT FTGSIVANLK LSARMKSAPL MLPGKNAINL GALAVFAALT
     VWFTASPNLG VLIAVTAVAL ALGWHLVASI GGGDMPVVVS MLNSYSGWAA AASGFLLDNN
     LLIVTGALVG SSGAYLSYIM CEAMNRSFIS VIAGGFGIEV AASGDTDYGE HHEISAEEVA
     ELLADASSVI ITPGYGMAVA QAQYPVAELT SKLRARGVDV RFGIHPVAGR LPGHMNVLLA
     EAKVPYDVVL EMDEINDDFP STDVVLVIGA NDTVNPAALE EPGSPIAGMP VLHVWEAKDV
     IVFKRSMAVG YAGVQNPLFF RDNTHMLFGD AKDRVEDIVR QLSDIPQQVS R
//

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