ID A0A1I8FED5_9PLAT Unreviewed; 761 AA.
AC A0A1I8FED5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-unitig_31512-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-unitig_31512-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR AlphaFoldDB; A0A1I8FED5; -.
DR WBParaSite; maker-unitig_31512-snap-gene-0.2-mRNA-1; maker-unitig_31512-snap-gene-0.2-mRNA-1; maker-unitig_31512-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
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; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR034300; PNTB-like.
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 Pfam; PF02233; PNTB; 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.
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 59..189
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 192..350
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT REGION 15..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 79164 MW; 40BACB2169A46195 CRC64;
GKGCAFASAA AGRCRDAASA GSRREPSCPP RDIAYQPADH RRAQWESWQN EAAGWRSEGP
PLSRWELPQL LSKKGFRINV EKGAGVGAEF LDGDFQQNGA SIVDQMAAFQ SDIVLKVRAP
STSEGRLAEA GNTLVSFLYP AQNTDLIKAL QTKGGNVIAM DCVPRISRAQ VFERPVLHGQ
HCRYKAVVAS PPTISADFFA GQITAAGKIP PAKVLVIGGG VAGLSSIGAA KNMGAIVRAF
DTRAAVKEQV ESFGAQFLEV SLKESGEGTG GYAKEMSPDR DGAVRQAVPR IDILITTALI
PGKPAPKLIS REMVESMKPG SVVVDLASEA GGNIETTKPG EAYKDVVHIG YTDLPSRLPT
QASTLYANNV SKLLLSMGAK DHFYLDMNDE VVPHLAAAAA AGSARWRCSS SSQGAHTKEL
EAKEPDYFGD TLKSASAYGA GLGTLLGLGY VSPNAAFSGM LTHILAVDPR WLPQLSGDVG
TPGPAQPPDE LGGLLLMGGA PDAIECAAVA RRTQHIGGGF LVTQRMLDMF KRGLTDPPEF
NYLYLVPGAT LVGGYGRSAG GGHNDLHQLA YLGSLLCLRW GADGADLEKS SQKTCRLVAN
ALGMIGVSGG PSVLAQMGAV CLTGASIGGV MAKRMEVTDL PQMVALFHSL PHFAAGDTAA
ANLLKTVAFL VPTLGVTFTG SLVAFGKLQR PAELPGRNAL NAPCSAPAWL SGGALVALPE
MSSGLAALAA TTGLSSVMGV TLTAAIGEES ICSRTTLNFG T
//
