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Database: UniProt
Entry: Q04GT5_OENOB
LinkDB: Q04GT5_OENOB
Original site: Q04GT5_OENOB 
ID   Q04GT5_OENOB            Unreviewed;       392 AA.
AC   Q04GT5;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   OrderedLocusNames=OEOE_0369 {ECO:0000313|EMBL:ABJ56337.1};
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56337.1, ECO:0000313|Proteomes:UP000000774};
RN   [1] {ECO:0000313|EMBL:ABJ56337.1, ECO:0000313|Proteomes:UP000000774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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};
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DR   EMBL; CP000411; ABJ56337.1; -; Genomic_DNA.
DR   RefSeq; WP_002818168.1; NC_008528.1.
DR   AlphaFoldDB; Q04GT5; -.
DR   STRING; 203123.OEOE_0369; -.
DR   GeneID; 75065166; -.
DR   KEGG; ooe:OEOE_0369; -.
DR   eggNOG; COG3288; Bacteria.
DR   HOGENOM; CLU_003376_2_1_9; -.
DR   Proteomes; UP000000774; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   CDD; cd05304; Rubrum_tdh; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000774};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          6..139
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          148..312
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   392 AA;  41049 MW;  0025E778B0BF29DB CRC64;
     MAIVVSALKE AAGENRVALT PDVVAKLVKS NFDVVIEKGA GEKAFYSDDV YKSAGAKLST
     RTDALKADIV TVVNEPSTAT LNKLTKGQTI IGMLNPLGDK KAVESLAKAG VTSLAFELLP
     RTVSRAQNLD ANSSQKSIAG YKAALLAADT YPQYFPMMMT AAGTARPAKV LVIGAAVAGL
     QAIGTAHRLG AVVSGYDIRE DARGQVESLG ATALISGVQV KDENGYARAL TTDEKKAQQT
     ELEGFIAENN VIITTAQVPG GKPPVVVSKK AVDNAKAGTV FIDLGSSALG GNVEGSKPGE
     TVVTKSGALI VGAGDLASRL PKSSSDMYAK NVQNTINYII KDGKILLDLD DDVLTDLVAT
     YKGEISSNFL RSRFGLEKRV AQKKTEDKKE AE
//
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