ID F6X3Y2_XENTR Unreviewed; 1077 AA.
AC F6X3Y2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN Name=LOC100490887 {ECO:0000313|Ensembl:ENSXETP00000019304,
GN ECO:0000313|RefSeq:XP_002936617.2, ECO:0000313|RefSeq:XP_004912662.1,
GN ECO:0000313|Xenbase:XB-GENE-29080423};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000019304};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000019304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000019304};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000019304}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002936617.2, ECO:0000313|RefSeq:XP_004912662.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002936617.2,
RC ECO:0000313|RefSeq:XP_004912662.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002936617.2,
RC ECO:0000313|RefSeq:XP_004912662.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_002936617.2; XM_002936571.5.
DR RefSeq; XP_004912662.1; XM_004912605.3.
DR STRING; 8364.ENSXETP00000019304; -.
DR PaxDb; 8364-ENSXETP00000032322; -.
DR Ensembl; ENSXETT00000019304; ENSXETP00000019304; ENSXETG00000008788.
DR GeneID; 100490887; -.
DR KEGG; xtr:100490887; -.
DR Xenbase; XB-GENE-29080423; LOC100490887.
DR eggNOG; ENOG502QQ0A; Eukaryota.
DR HOGENOM; CLU_003376_1_0_1; -.
DR OMA; KEYFHFE; -.
DR TreeFam; TF300636; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Bgee; ENSXETG00000008788; Expressed in skeletal muscle tissue and 3 other cell types or tissues.
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; 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.
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:UP000008143};
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 466..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 738..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..193
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 202..366
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1077 AA; 113668 MW; 865BE2EE8706BA4C CRC64;
MGGLLLYINR SSFPVLRKAR ILQQSTGTRY FKTFQLLWNA QVVKGTLFRD LVVGVPKEIS
KNEKRVAVTP AGVQALIKQG FNIQVETGAG EEAKFSDQQY KKAGASLSDT RSVFGSDIVL
KVRAPCFNEV LGTHESELFK ERATLVSFIY PAQNPDVMDR LAQRKLTVLA MDQVPRVTIA
QGYDALSSMA NIAGYKATVL AANHFGRFFT GQITAAGKVP PAKVLIIGGG VAGLAAAGAA
KAMGAIVRGF DTRPPALEQF KSLGAEPLEV EIAETGEGVG GYAKEMSKEF IEAELALFAK
QCKEIDVIIS TALIPGKKAP VLITKDMVES MKDGSVIVDL AAEAGGNVET TRPGELYLHK
GVVHVGYTDL PSRMASQAST LYSNNIVKLL KAIAPDKEYF YLEPKDEFDY GTIDHVIRGT
MVMREGLHLF PSPLPKTAPP AAPVQHKTVV EIEAERKATE SPFRKTMTSA GVYTAGLTGV
LGLGIVSPNS AFSQMVTTFG LAGIVGYHTV WGVTPALHSP LMSVTNAISG LTAAGGLVLM
GGSYLPSSLP ESLALLAAFV SSINIAGGFL ITQRMLDMFK RPTDPPEYNY LYLLPGGLFV
GGYGTSLALG YNIEQMMYLA SGLCCVGALA GLSSQSTSRL GNALGMIGVA GGLAATLGSL
KPSPELLTQM SAAMTLGGTI GLTIAKKIEI SDLPQLVAAF HSLVGLAAVL TCVAEYMIEY
PHLDVHPSAN VLKTVAYLGT YIGGVTFSGS LVAYGKLQGI LNSAPLLLPG RHYLNAGLLA
ASVGGMVPFM LDPSYSTGMA CLIGVSGLSS VMGVTLTAAI GGADMPVVIT VLNSYSGWAL
CAEGFLLNNN LMTIVGALIG SSGAILSYIM CVAMNRSLPN VILGGYGTSS TGTGKPMEIV
GTHTEVSVDQ SIEMIKEANT IIIVPGWGLC AAKAQYPIAD MVKMLQEQGK TVRFGIHPVA
GRMPGQLNVL LAEAGVPYDI VLEMDEINED FPETDLVLVI GANDTVNSAA QEDPNSIIAG
MPVLEVWKAK QVIIMKRTLG VGYAAVDNPV FYKSNTAMLL GDAKKTCDAL QSKIREI
//
