ID A0A3P8RK12_AMPPE Unreviewed; 1071 AA.
AC A0A3P8RK12;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000000392.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000000392.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000000392.1}
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 AlphaFoldDB; A0A3P8RK12; -.
DR STRING; 161767.ENSAPEP00000000392; -.
DR Ensembl; ENSAPET00000000400.1; ENSAPEP00000000392.1; ENSAPEG00000000285.1.
DR GeneTree; ENSGT00390000004624; -.
DR OMA; KEYFHFE; -.
DR Proteomes; UP000265080; Chromosome 1.
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:UP000265080};
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 487..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..186
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 195..359
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1071 AA; 112520 MW; E7A76E6023ADF67B CRC64;
MSTFLRCISS PSVVLFQRGV QRKAPGRRHF RTFPVLWDQK ASRGVLYKDV VVGVPKETVQ
NERRVALSPA GVQALVKQGF RVQVESGAGD ESKFSDQQYR DAGATITDVK GALGSDLVLK
VRAPSLSEAD HLKPKSTLVS FIYPAQNPEL MSKLSERQST VLAMDQVPRV TIAQGYDALS
SMANIAGYKA VVLAANHFGR FFTGQITAAG KVPPAKVLVI GGGVAGLAAA GAAKSMGAIV
RGFDTRPAAL EQFKSFGAEP LEVDIKESGE GVGGYAKEMS KEFIEAEMAL FAKQCKEVDI
VISTALIPGK RAPILIKREF VESMKDGSVV VDLASEAGGN IETTRPGELH VHKGVTHIGY
TDLPSRMATQ ASTLYSNNIL KLLKAISPDK DYFYYEPKEE FDYGTMDHVI RGTLVMQEGK
NMFPSPLPKT APPAPVKQKT VAELEAEKAA AVSPFNRTMT SAGVYTAGLS TCLGLGIISP
NAAFTQMVTT FGLAGIVGYH TVWGVTPALH SPLMSVTNAI SGLTAVGGLV LMGGGLTPST
LPESLALAAA FVSSINIAGG FLITQRMLDM FKRPTDPPEY NYLYALPGTA FVGGYGASVA
AGYSIEQMMY LGSGMCCVGA LAGLSAQGTS RLGNALGMMG VAGGIAATLG ALKPSPELLS
QMSLAMATGG TLGLTIAKRI EISDLPQLVA AFHSLVGLAA VLTCVAEFMI EYPHLETHPA
AGVLKTVAYL GTYIGGVTFS GSLVAYGKLQ GILNSAPLLL PGRHMLNAGL MAASMGGMVP
FMLSSSYGTG MGCLLGVSGL STVMGVTLTA AIGGADMPVV ITVLNSYSGW ALCAEGFLLD
NNLMTIVGAL IGSSGAILSY IMCVAMNRSL PNVILGGYGT TSTAGGKPME IVGTHTEVNV
DQTIDIIKEA NSIIITPGWG LCAAKAQYPI ADMVKMLTEQ GKAVRFGIHP VAGRMPGQLN
VLLAEAGVPY DVVLEMDEIN EDFPETDLTL VIGANDTVNS AAQEDPNSII AGMPVLEVWK
SKQVIVMKRT LGVGYAAVDN PIFYKPNTSM LLGDAKKTCD SLQAKIREAY Y
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