ID G9A0L8_RHIFH Unreviewed; 382 AA.
AC G9A0L8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=pntA2 {ECO:0000313|EMBL:CCE97414.1};
GN OrderedLocusNames=SFHH103_02922 {ECO:0000313|EMBL:CCE97414.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE97414.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE97414.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE97414.1,
RC ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(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; HE616890; CCE97414.1; -; Genomic_DNA.
DR RefSeq; WP_014329823.1; NC_016812.1.
DR AlphaFoldDB; G9A0L8; -.
DR STRING; 1117943.SFHH103_02922; -.
DR KEGG; sfh:SFHH103_02922; -.
DR PATRIC; fig|380.5.peg.3104; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_5; -.
DR Proteomes; UP000007735; 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:CCE97414.1};
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..314
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 382 AA; 39415 MW; 81EC4F2523D337CB CRC64;
MSQIVFITKE SDPSEPRVAG SVDSVKKLKS LGFDVVVEAG AGHGSRVPDA EFEKAGARIG
SAADAKSADV ILKVRRPTTE EMAGYRSGAI VIAIMDPYGN DEAIAAMAGA GLTAFAMELM
PRITRAQSMD VLSSQANLAG YQAVIDAAHE YDRALPMMMT AAGTVPAAKI FVMGAGVAGL
QAIATARRLG AMVTATDVRP AAKEQVASLG AKFIAVEDDE FKAAETAGGY AKEMSKDYQA
KQAALVAEHI AKQDIVVTTA LIPGRPAPRL VTRAMLDAMK PGSVVVDLAV ERGGNVEGAE
AGKVVEAGGV KIVGHLNVPG RIAASASLLY AKNLVTFLET MVSKETKALA LNMEDELVKA
TALTHGGAVV HPAFGGANGG DK
//
