ID M2SE51_9SPHN Unreviewed; 376 AA.
AC M2SE51;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=C725_0612 {ECO:0000313|EMBL:EMD83640.1};
OS Pacificimonas flava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingosinicellaceae; Pacificimonas.
OX NCBI_TaxID=1234595 {ECO:0000313|EMBL:EMD83640.1, ECO:0000313|Proteomes:UP000011717};
RN [1] {ECO:0000313|EMBL:EMD83640.1, ECO:0000313|Proteomes:UP000011717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2015 {ECO:0000313|EMBL:EMD83640.1,
RC ECO:0000313|Proteomes:UP000011717};
RX PubMed=23661488;
RA Tang K., Liu K., Li S., Jiao N.;
RT "Draft Genome Sequence of Strain JLT2015T, Belonging to the Family
RT Sphingomonadaceae of the Alphaproteobacteria.";
RL Genome Announc. 1:E00226-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMD83640.1}.
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DR EMBL; AMRV01000002; EMD83640.1; -; Genomic_DNA.
DR RefSeq; WP_008600077.1; NZ_JACHGC010000004.1.
DR AlphaFoldDB; M2SE51; -.
DR PATRIC; fig|1234595.3.peg.611; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000011717; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000011717};
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..314
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 376 AA; 38798 MW; DA3EA6A13C9AF2E7 CRC64;
MKLAVLKETD AGERRVAASP ETVKRFAGWD AEISIEAGAG APSGMPDADF EAAGATIAPS
RAAAVGGADI ILAVRAPDPA SLSGAEAGAI LAAILNPFQA GDTLSGYANA GLTAMAMDFM
PRITRAQSMD VLSSQANLAG YRAVLDAAHE YGRGFPMMMT AAGTVSAAKL FVMGVGVAGL
QAIATGRRLG AQVSATDVRA ATREQIESLG AKAIFVKDVE GIEGEGTGGY ASEMSEEYKA
AQAKLVSDHI ARQDIVITTA LIPGRPAPRL ISDAQLASMK PGSVIVDLAA PQGGNVEGCV
PGETVRKHGV TLMAPTNINA SLAEVSSQLY ARNLWNFLSA FWDGDAKSLV WPDDDDIVRG
VTVVKDGKVS NERLNA
//
