ID Q4SHM6_TETNG Unreviewed; 1041 AA.
AC Q4SHM6;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 13-SEP-2023, entry version 79.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
DE Flags: Fragment;
GN ORFNames=GSTENG00018084001 {ECO:0000313|EMBL:CAF99856.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF99856.1};
RN [1] {ECO:0000313|EMBL:CAF99856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAF99856.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) 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 -!- 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:CAF99856.1}.
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DR EMBL; CAAE01014581; CAF99856.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4SHM6; -.
DR KEGG; tng:GSTEN00018084G001; -.
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 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 458..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 701..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 790..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..836
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..149
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 158..330
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAF99856.1"
FT NON_TER 1041
FT /evidence="ECO:0000313|EMBL:CAF99856.1"
SQ SEQUENCE 1041 AA; 108960 MW; 360BA87BD7274FC6 CRC64;
GVLYKDLVVG VPKETVQNER RVALSPAGVE ALVKQGFRVQ VESGAGEESK FSDQQYKNAG
ATITDVNGAF GSDLVLKVGP HLIRRTPSLS EVDFLKPKST LVSFVYPAQN SELMQKLSER
QSTVLAMDQV PRVTIAQGYD ALSSMANIAG YKAVVLAANN FGRFFTGQIT AAGKVPPAKV
LVIGGGVAGL AAAGAAKSMG AIVRGFDTRP AALEQFKSFG AEPLEVDVKE SGEGVGGYAK
EMSKEFIEAE MELFAKQCKE VDIIISTALI PGKRAPILIK RNFVESMKEG SVVVDLAAEA
GGNIETTRPG ELHVHKVGLL LGQLGVTHIG FTDLPSRMAT QASTLYSNNI LKLLKAISPS
KEYFHYEPKE EFDYGTIDHV IRGTVVMKDG ENMFPSPLPK TAPPAPVKQK TVAELEAEKA
AEISPFNRTM TSASVYTAGV STCLALGIIS PNAAFTQMVT TFGLAGIVGY HTVWGVTPAL
HSPLMSVTNA ISGLTAVGGL ALMGGGLTPS SLPQSLALTA AFVSSINIAG GFLITQRMLD
MFKRPTDPPE YNYLYALPGA AFVGGYGASV AAGYNIEQMM YLGSGLCCVG ALAGLSAQGT
SRLGNALGMM GVAGGIAATL GALKPSPELL SQMSLAMATG GTLGLTIAKR IEISDLPQLV
AAFHSLVGLA AVLTCIAEYM IEFPHLDTHP AAGVLKTVAY LGTYIGGVTF SGSLVAYGKL
QGVLSSAPLL LPGRHVMNAG LMAASMGGLV PFMLSSSYNT GMGCLVGVSG LSTIMGVTLT
AAIGGADMPV VITVLNSYSG WALCAEGFLL ENNLLTIVGA LIGSSGAILS YIMCVAMNRS
LPNVILGGYG TTSTAGGKPM EIVGTHTEVN VDQTIDIIKE ANNIIITPGW GLCAAKAQYP
IADMVKMLRE QGKTVRFGIH PVAGRMPGQL NVLLAEAGVP YDVVLEMDEI NEDFPETDLT
LVIGANDTVN SAAQEDPNSI IAGMPVLEVW KSKQVIVMKR TLGVGYAAVD NPIFYKPNTS
MLLGDAKKTC DSLQAKIREA F
//
