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Database: UniProt
Entry: E4U9V3_OCEP5
LinkDB: E4U9V3_OCEP5
Original site: E4U9V3_OCEP5 
ID   E4U9V3_OCEP5            Unreviewed;       380 AA.
AC   E4U9V3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
DE   Flags: Precursor;
GN   OrderedLocusNames=Ocepr_1815 {ECO:0000313|EMBL:ADR37267.1};
OS   Oceanithermus profundus (strain DSM 14977 / NBRC 100410 / VKM B-2274 /
OS   506).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Oceanithermus.
OX   NCBI_TaxID=670487 {ECO:0000313|EMBL:ADR37267.1, ECO:0000313|Proteomes:UP000008722};
RN   [1] {ECO:0000313|Proteomes:UP000008722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC   {ECO:0000313|Proteomes:UP000008722};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Zhang X., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Faehnrich R.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Oceanithermus profundus DSM
RT   14977.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADR37267.1, ECO:0000313|Proteomes:UP000008722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14977 / NBRC 100410 / VKM B-2274 / 506
RC   {ECO:0000313|Proteomes:UP000008722};
RX   PubMed=21677858; DOI=10.4056/sigs.1734292;
RA   Pati A., Zhang X., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Hauser L.,
RA   Jeffries C.D., Brambilla E.M., Rohl A., Mwirichia R., Rohde M.,
RA   Tindall B.J., Sikorski J., Wirth R., Goker M., Woyke T., Detter J.C.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Land M.;
RT   "Complete genome sequence of Oceanithermus profundus type strain (506).";
RL   Stand. Genomic Sci. 4:210-220(2011).
CC   -!- FUNCTION: The transhydrogenation between NADH and NADP is coupled to
CC       respiration and ATP hydrolysis and functions as a proton pump across
CC       the membrane. {ECO:0000256|ARBA:ARBA00003943}.
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; EC=7.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000006};
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005689}.
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DR   EMBL; CP002361; ADR37267.1; -; Genomic_DNA.
DR   RefSeq; WP_013458437.1; NC_014761.1.
DR   AlphaFoldDB; E4U9V3; -.
DR   STRING; 670487.Ocepr_1815; -.
DR   KEGG; opr:Ocepr_1815; -.
DR   eggNOG; COG3288; Bacteria.
DR   HOGENOM; CLU_003376_2_1_0; -.
DR   OrthoDB; 9804592at2; -.
DR   Proteomes; UP000008722; Chromosome.
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   CDD; cd05304; Rubrum_tdh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008143; Ala_DH/PNT_CS2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR   PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000313|EMBL:ADR37267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008722};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          6..141
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          150..312
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   380 AA;  40365 MW;  17FAF01910DDCA93 CRC64;
     MAIKIAVPKE EAPGERRVAL VPEVAGKLVR QGHAVAVESG AGVGAHYLDD AYEKVGAQLV
     ERRTELLGGA QIVLKVQPPT EDEIDALPEG AVLIGFMYPH RYPERVAKMR DKKLTVFAME
     LVPRITRAQA MDALSSQATV AGYKAALIAA DTIDRFLPML TTAAGTIRPA QVLVLGAGVA
     GLQAIATAKR LGAVVSAYDV RRAAGEQVRS LGAKFLELEI DAEAEGGYAR ELTEEEKAKE
     RAMVEEAIVA ADIVITTANI PGRRAPILVT KDMVERMKPG SVIVDLAAES GGNCEVTQPG
     ETVQVGDVRV VGPLNLPSAL AVHASEMYAK NLHNFLELIL TEEGGLELDW DDEILAGSVL
     VHDGEIKHAP TRELVEGGAA
//
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