ID A0A249KN14_9ACTN Unreviewed; 381 AA.
AC A0A249KN14;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=A1sIA105_01010 {ECO:0000313|EMBL:ASY18171.1};
OS Candidatus Planktophila versatilis.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884905 {ECO:0000313|EMBL:ASY18171.1, ECO:0000313|Proteomes:UP000217175};
RN [1] {ECO:0000313|EMBL:ASY18171.1, ECO:0000313|Proteomes:UP000217175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-105 {ECO:0000313|EMBL:ASY18171.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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};
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
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DR EMBL; CP016775; ASY18171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KN14; -.
DR KEGG; pvs:A1sIA79_00985; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000217175; Chromosome.
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 Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 4..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 146..310
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 381 AA; 39307 MW; 584B5C17BBD4F5F2 CRC64;
MRVAVPREIR DGEKRVALVP DIINKLTKLG YEVVIESGAG VHAQATDELF IAAGATIKSG
NVIGDADVVL CVTSLTPAQI SSLKKGAVTI SFLSPVTAID SIDAAVTAGV TAFSLELVPR
ISRAQSMDAL TSQALCAGYR AALVGAELSP RFFPMLMTAA GTVTPAQVLV LGAGVAGLQA
IATARRLGAV VSAYDVRPSS ADEVKSMGAT FIDLELEALE GAGGYAREMT EERAAKQREL
LTPYIAKSHL VITTAAVPGR AAPRLMTAAM IDAMEAGTII VDLAAETGGN AEGSKPGEIV
TTAKGVQIWG GKDVPSQLPF HASSLYSRNV VNLLTLMTTA AKDGEKVALN IDFTDEIIDK
AALTHAGAKH TPGASEKGGS N
//
