ID G4R9Y6_PELHB Unreviewed; 507 AA.
AC G4R9Y6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=NAD(P) transhydrogenase subunit alpha {ECO:0000256|PIRNR:PIRNR000203};
DE EC=7.1.1.1 {ECO:0000256|PIRNR:PIRNR000203};
GN OrderedLocusNames=KKY_2505 {ECO:0000313|EMBL:AEQ52513.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ52513.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ52513.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(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 ECO:0000256|PIRNR:PIRNR000203}.
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 ECO:0000256|PIRNR:PIRNR000203};
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689, ECO:0000256|PIRNR:PIRNR000203}.
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DR EMBL; CP003075; AEQ52513.1; -; Genomic_DNA.
DR AlphaFoldDB; G4R9Y6; -.
DR STRING; 1082931.KKY_2505; -.
DR KEGG; phl:KKY_2505; -.
DR PATRIC; fig|1082931.4.peg.2474; -.
DR eggNOG; COG3288; Bacteria.
DR HOGENOM; CLU_003376_2_1_5; -.
DR Proteomes; UP000008850; Chromosome.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; 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 InterPro; IPR026255; NADP_transhyd_a.
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 PIRSF; PIRSF000203; NADP_transhydrogenase_alpha; 2.
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, ECO:0000256|PIRNR:PIRNR000203};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000203};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000203};
KW Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|PIRNR:PIRNR000203}.
FT DOMAIN 4..139
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 148..312
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 389..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 50714 MW; 0D8AE8CB58FE662B CRC64;
MKIAVMRERA GGETRVAATP ETIAKLIGFG ATVSVEKGAG EASRILDQFY TDAGAKVEAG
AAATVKGADV ILAVRRPEAS ALTGAAKGAL VLATADPFGN EAALAALAKA GLSVFAMELM
PRITRAQVMD ILSSQANLAG YQAVIEASMV YDRALPMMMT AAGTVRAAKV FVMGAGVAGL
QAIATAKRLG AAVSATDVRA AAGEQVESLG AKFIMTEALK DASGAGGYAR ELTKDEQAAQ
AELVSGHIAK QDIVITTALI PGRPAPKLIT KAMVESMAPG SVLVDLAAER GGNIELTVPG
QTIVHKDVTI IGLLNLQGKI AATASQLYSK NLLAFLETMI DKDAKALKVD WEDELVKATL
LTRDGAVVHP NFAGSAAAAP AKKAPAKATA KAPAKTAATG QAAAGKAAPK AESKPAAKAP
AKTGASGKGR AAKVATAGAV SVPAEEKPAA KPATKSGAAK NAAAPKASAA KKPAAKSAAA
SKPAAKSTAA KKPAAKKPAA KKTDGDV
//
