ID K4IPI3_BIFAP Unreviewed; 396 AA.
AC K4IPI3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN OrderedLocusNames=BAST_1137 {ECO:0000313|EMBL:AFU71713.1};
OS Bifidobacterium asteroides (strain PRL2011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71713.1, ECO:0000313|Proteomes:UP000007006};
RN [1] {ECO:0000313|EMBL:AFU71713.1, ECO:0000313|Proteomes:UP000007006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71713.1,
RC ECO:0000313|Proteomes:UP000007006};
RX PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA Ventura M.;
RT "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT colonization of the insect gut.";
RL PLoS ONE 7:E44229-E44229(2012).
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; CP003325; AFU71713.1; -; Genomic_DNA.
DR RefSeq; WP_015022151.1; NC_018720.1.
DR AlphaFoldDB; K4IPI3; -.
DR STRING; 1147128.BAST_1137; -.
DR GeneID; 41010365; -.
DR KEGG; bast:BAST_1137; -.
DR PATRIC; fig|1147128.3.peg.1160; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_11; -.
DR Proteomes; UP000007006; 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:AFU71713.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 12..147
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 156..322
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 41109 MW; CD9AC97E0F15FD9C CRC64;
MSGPEQPHVT FGVLKETDKE ESRVALTPDI VTRLTRQDIT CLLESGAGAQ AGFRDEDYQQ
TGAIITDRNT VLSKSQVLGF VNRPDSSLLK RIPAGTWIIG MLGSLSDSDY IKSLEAAGLT
GIAMERLPRQ LSSAQSMDEM TSQNSVMGYK AALVAADAYG SFFPMMTTAA GTIRPAKVLV
LGAGIAGLQA IGTAKRLGAV VTAYDVRPAS RQEVESLGAK FLDLGLDLSK GQGQGGYARQ
LTDQEQAQQQ AAVDAKAAGF DVVITTAKVP GGKPPRLLSA KGVANLHPGA VVVDCAASDL
GGNVEGSHVG TRTTDKGVIM IGAPYLASGV ATTASNLLSR NVADVLVHFL RDGALSIKAD
DEIDQALIVT GAAESGTHGS ADVPDAEETG EKGQEQ
//
