ID D7A593_STAND Unreviewed; 387 AA.
AC D7A593;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN OrderedLocusNames=Snov_2692 {ECO:0000313|EMBL:ADH89981.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Ancylobacter.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89981.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH89981.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(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; CP002026; ADH89981.1; -; Genomic_DNA.
DR RefSeq; WP_013167485.1; NC_014217.1.
DR AlphaFoldDB; D7A593; -.
DR STRING; 639283.Snov_2692; -.
DR KEGG; sno:Snov_2692; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_5; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000006633; 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:ADH89981.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..315
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 387 AA; 39415 MW; EC70B6A88B708124 CRC64;
MRIAVVKESS GLEPRVAASP DTVKRYVGLG AEVVVASGAG LASGVGDGDY EGAGAKVVAD
NAAAVANADI VLSVRRPEAS ALKGANRGAL AIAIMDPYGH EKDLEALAKA GVSAFAMELM
PRITRAQVMD VLSSQANLAG YRAVVDAAGE FGRAFPMMMT AAGTVPAARV FVMGAGVAGL
QAVATARRLG AVVSATDVRP AAKEQVESLG GKFIAVEDEE FKQAETAGGY AKQMSAEYQA
KQAALVASHI AKQDVVITTA LIPGRPAPKL VSGEMVASMK PGSVVIDLAV ERGGNVEGAV
PGEVVTTANG VKIVGHLNVP GRLAATASQL YAKNLYAFVE TLIDKGTKSL AVKWEDELVK
ATLLTRDGAV VHPGFKPQGA GDAASAA
//
