ID A2VSU4_9BURK Unreviewed; 379 AA.
AC A2VSU4;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=BCPG_01037 {ECO:0000313|EMBL:EAY62790.1};
OS Burkholderia cenocepacia PC184.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY62790.1, ECO:0000313|Proteomes:UP000053735};
RN [1] {ECO:0000313|EMBL:EAY62790.1, ECO:0000313|Proteomes:UP000053735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC184 {ECO:0000313|EMBL:EAY62790.1,
RC ECO:0000313|Proteomes:UP000053735};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., White J.,
RA Larson L., Alvarado L., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA LiPuma J., Lory S.;
RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184).";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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; CH482377; EAY62790.1; -; Genomic_DNA.
DR AlphaFoldDB; A2VSU4; -.
DR HOGENOM; CLU_003376_2_1_4; -.
DR Proteomes; UP000053735; Unassembled WGS sequence.
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 Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 145..322
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 379 AA; 39168 MW; 5C0A1AB1E9D07254 CRC64;
MHIGVPAETR ANEARVAATP ETVKKYAAAG HRVSIAKGAG SAASYPDEAY VAAGAELTDQ
SAAFAADLVL KVQAPTDAEL PLLKRGAVLV GMLEPFNGEQ AAQLAAAGVT GFALEAAPRT
TRAQSLDVLS SQANIAGYKA VLVAASLYPR FMPMLMTAAG TVKAARVLIL GAGVAGLQAI
ATAKRLGAVI EASDVRPAVK EQIESLGAKF LDVPFETDEE REAAQGVGGY ARPMPPSWLG
RQAALVHERA KQADIVITTA LIPGRPAPTL ISVDTAQSMK PGSVLVDLAA GRGPEVDGRK
GGNCPLTVAD QVIVHNGVTI AGYTNLASMV ASDASALYAR NLLDFLKLIV TKEGTLNIDL
TDDIVAATLL CRDGEVTRK
//
