ID A0A087XHI9_POEFO Unreviewed; 1072 AA.
AC A0A087XHI9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000005242.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000005242.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 EMBL; AYCK01009947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XHI9; -.
DR STRING; 48698.ENSPFOP00000005242; -.
DR Ensembl; ENSPFOT00000005251.1; ENSPFOP00000005242.1; ENSPFOG00000005055.1.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR GeneTree; ENSGT00390000004624; -.
DR OMA; KEYFHFE; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
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; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR008142; AlaDH/PNT_CS1.
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:SF30; 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.
DR PROSITE; PS00836; ALADH_PNT_1; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
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 488..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 690..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 731..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..866
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 1072 AA; 112922 MW; 74B6A76DD647E8FC CRC64;
MSTLLRCFSS SCLVLSQRKG HQKIFGRRHF RTFPVLWDQK ASREGVLYKD LVVGVPKETV
LNERRVALSP AGVQALVKQG FKVQVENGAG DEAKFSDQQY KDAGATITDV KGALGSDLVL
KVRAPSLSEA DLLKPKSTLV SFIYPAQNPD LMKKLSERQS TVLAMDQVPR VTIAQGYDAL
SSMANIAGYK AVVLAANHFG RFFTGQITAA GKVPPAKVLV IGGGVAGLAA AGAAKSMGAI
VRGFDTRPAA LEQFKSFGAE PLEVDIKESG EGVGGYAKEM SKEFIEAEMA LFARQCKDVD
IVISTALIPG KKAPVLIKKE FVESMRDGSV VVDLAAETGG NIETTKPGDL YVYKGVTHIG
YTDLPSRMPT QASTLYSNNV LKLLKAISPD KDYFHYEPHE EFDYGTIDHV IRGTLVMKEG
HNMFPSPLPK TTPPAPVKQK TVAELEAEKA ATVSPFNRTL TSAGVYTAGV STCLALGIIS
PNAAFTQMVT TFGLAGIVGY HTVWGVTPAL HSPLMSVTNA ISGLTAVGGL VLMGGGLAPS
SLPETLALAA AFVSSINIAG GFLITQRMLD MFKRPTDPPE YNYLYLLPGA AFVGGYGASL
AAGYSIEQMM YLGSGLCCVG ALAGLSAQHT SRLGNALGMM GVAGGIAATI GALKPSPELL
SQMSLAMATG GTLGLTIAKR IEITDLPQLV AAFHSLVGLA AVLTCVAEYM IEFPHLETHP
AAGVLKTVAY LGTYIGGVTF SGSLVAYGKL QGLLDSAPLL LPGRHMLNAS LMAASMGGMV
PFMLSSSYGT GMGCLMGVSG LSAVMGVTLT AAIGGADMPV VITVLNSYSG WALCAEGFLL
DNNLMTIVGA LIGSSGAILS YIMCVAMNRS LPNVILGGYG TTSTLGGKPM EIVGTHTEVN
VEQTIDIIKE ANTVIITPGW GLCAAKAQYP IADMVKMLRE QGKTVRFGIH PVAGRMPGQL
NVLLAEAGVP YDVVLEMDEI NDDFPETDLT LVIGANDTVN SAAQEDPNSI IAGMPVLEVW
KSKQVIVMKR TLGVGYAAVD NPIFYKPNTS MLLGDAKKTC DALQAKIREV YY
//
