ID A0A164X3C5_9CRUS Unreviewed; 1064 AA.
AC A0A164X3C5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=APZ42_020909 {ECO:0000313|EMBL:KZS13829.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS13829.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS13829.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS13829.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS13829.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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:KZS13829.1}.
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DR EMBL; LRGB01001019; KZS13829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164X3C5; -.
DR STRING; 35525.A0A164X3C5; -.
DR EnsemblMetazoa; XM_032935879.2; XP_032791770.2; LOC116928778.
DR OrthoDB; 313696at2759; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR034300; PNTB-like.
DR NCBIfam; TIGR00561; pntA; 1.
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 Pfam; PF12769; PNTB_4TM; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 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 Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 535..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..774
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..187
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 196..360
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1064 AA; 112297 MW; B5D9A5F0C90BB736 CRC64;
MAGVLRVSLN IQGQVQSPLF CSVRGLRTYA RPLRKDAKQA EPIKGIPYKN LTIGVPKEIW
SNERRVALTP AVTATLVKKG FTVNVESGAG IEARFRNDDY AAAGGKLTDK NTALKSDIVL
KVRQPLETEI GLLKEHGNII SFLYPALNKP LVGKMAERKL TAFAMDAIPR ISRAQVFDAL
SSMANIAGYR AVVEAANHFG RFFTGQITAA GKVPPAKILV IGGGVAGLAA IGQAKNMGAI
VRAFDTRAAV KEQVESMGAE FLEVNIKESG DGAGGYAKVM SKEFIEAEMA LFAKQAKEVD
VIITTALIPG QKAPTLITKA MIESMKPGSV VVDLAAEAGG NIETIKPGEI YTYKDVVHIG
LTDFPSRLPT QASTLYANNI SKFFLSMGEK DHFNINLEDE VVRGAIVLKD GQLLWPAPPV
AVSAQPQAQA AKPAEKVAPP PPDYFNMTLK DSLMYTGGLG SLMALGMNAP NPAFTTMTTT
LGLGCIVGYH TVWGVTPALH SPLMSVTNAI SGITAVGGLL QMGGGYFPSN TAQSLAASAA
FISSINIFGG FLVTKRMLDM FRRPTDPPEF YYLYGIPASV FLGSYGWGVH MGYPEVHQMA
YLASSLCCVG ALAGLSSQKT SRIGNILGQI GVSGGIAATL GLMSPNMDTL TQMAACMGVG
GAIGTVIAKK IEITDLPQLV AAFHSLVGAA AVLTCLSTYI VDFPHFATDP AANVIKTALF
LGTFIGGVTF SGSLIAYGKL QGMLNSSPLL LPGRHAMNSA LMLGNVGAMG YYFYDPSFVA
GMSMLGTTTA LSTIMGVTLT AAIGGADMPV VITVLNSYSG WALCAEGFML NNNLMTIVGA
LIGSSGAILS YIMCKAMNRS LPNVILGGYG TSSTAGGKPM EITGTHTEVN VDNTVEMITN
AKNIIITPGY GLCVAKAQYP VAEMVSLLKS KGKNVRFGIH PVAGRMPGQL NVLLAEAGVP
YDVVLEMDEI NDDFKETDLV LVIGANDTVN SAAEEDPNSI IAGMPVLKVW LSQQVIVMKR
SMGVGYAAVD NPIFYKPNAA MLLGDAKKTC DSLLSKIKEH YESQ
//
