ID A0A3Q3LJ33_9TELE Unreviewed; 1046 AA.
AC A0A3Q3LJ33;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000014128.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000014128.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q3LJ33; -.
DR Ensembl; ENSMAMT00000014512.2; ENSMAMP00000014128.2; ENSMAMG00000009580.2.
DR GeneTree; ENSGT00390000004624; -.
DR Proteomes; UP000261640; Unplaced.
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:SF22; NAD(P) TRANSHYDROGENASE, MITOCHONDRIAL; 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:UP000261640};
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 519..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..159
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 168..332
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1046 AA; 109261 MW; E3745F648CB65616 CRC64;
SKMLTQHSLS GIPYKQLTVG VPKEIFQNER RVALSPAGVQ ALIKQGFNVV VESGAGEPSK
FPDEQYTQAG ATIKGTKDVL ASDLLVKVRA PVFNPAVGVH EVEMMKDAAT LISFIYPAQN
PELMDMLSQK KTTVLAMDQV PRVTIAQGYD ALSSMANIAG YKAVVLAANS FGRFFTGQIT
AAGKVPPAKV LIIGGGVAGL AAAGTARAMG AIVRGFDTRA AALEQFKSLG AEPLEVDIKE
SGEGQGGYAK EMSKEFIEAE MKLFAKQCQE VDIVISTALI PGRRAPILIT KPMVESMKDG
SVVVDLAAEA GGNIETTVPG ELSLHRGVTH IGYTDLPSRL PTQSSTLYSN NITKLLRAIS
PDKNNFYLDV KDVFDYGTMD HVVRGSIVMQ NGKNLFPAPQ PNNLPTAAPP KPKSVQQLEA
EKAAQITPFR ATLTSASMYT GGLATLLGLG LSAPNAAFTQ IVTTFGLAGI VGYHTVWGVT
PALHSPLMSV TNAISGLTAV GGLSLMGGGY TPTTTAETLA VLAAFISSVN IAGGFLVTQK
MLDMFKRPTD PPEHNYLYLL PGGVFVGGYA AALHSGYNIE QMMYLGSGLC CVGALAGLSN
QTTARLGNAL GMMGVAGGIA ATLGALKPSP ELLTQMSAAM AVGGTAGLAI AKKIQITDLP
QLVAAFHSLV GLAAVLTCVA EYMIEYPHFA TDPAANLTKI VAYLGTYIGG ITFSGSLVAY
GKLQGLLNSA PLMLPARHAL NASLMAASVG GMIPYMMDPS YTTGLTCLGS VSALSAVMGV
TLTAAIGGAD MPVVITVLNS YSGWALCAEG FLLNNNLLTI VGALIGSSGA ILSYIMCVAM
NRSLANVILG GYGTSSTGRG KPMEITGTHT EVNVDQTVDM IKEAQTIIIT PGYGLCAAKA
QYPIAELVKL LTTAGKKVRF GIHPVAGRMP GQLNVLLAEA GVPYDIVLEM DEINEDFAET
DLVMVIGAND TVNSAAQEDP NSIIAGMPVL EVWKSKQVVV MKRSLGVGYA AVDNPIFYKP
NTAMLLGDAK KTCDALQAKV RESLAL
//
