ID A0A3P8SHS8_AMPPE Unreviewed; 1087 AA.
AC A0A3P8SHS8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
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 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:ENSAPEP00000011711.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000011711.1, 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:ENSAPEP00000011711.1}
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; A0A3P8SHS8; -.
DR STRING; 161767.ENSAPEP00000011711; -.
DR Ensembl; ENSAPET00000012022.1; ENSAPEP00000011711.1; ENSAPEG00000008287.1.
DR GeneTree; ENSGT00390000004624; -.
DR OMA; EQCREVD; -.
DR Proteomes; UP000265080; Chromosome 16.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 502..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 623..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..200
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 209..373
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1087 AA; 113357 MW; 35EEE14A1425F309 CRC64;
MASLLRVVAA SCSAPVFSGV SCVKLQSGSA VKWSCQRFFR THQALGRCAS PGIPYKQLTV
GVPKEIFQNE RRVALSPAGV QALIKQGFNV VVESGAGEPS KFPDEQYTQA GATIKDLKDV
LASDVVVKVR APVFNPTVGV HEVEMMKDAA TLISFIYPAQ NPELMDMLSQ KKATVLAMDQ
VPRVTIAQGY DALSSMANIA GYKSVVLAAN SFGRFFTGQI TAAGKVPPAK VLIIGGGVAG
LAAAGTARAM GAIVRGFDTR AAALEQFKSL GAEPLEVDIK ESGEGQGGYA KEMSKEFIEA
EMKLFAKQCQ DVDIVISTAL IPGRRAPILI TKPMVESMKD GSVVVDLAAE AGGNIETTVP
GELSVHKGVT HIGYTDLPSR LPTQSSTLYS NNITKLVRAI SPDKDNFYLD VKDVFDYGTM
DHVVRGSIVM QNGKNLFPAP QPNNVPVAAP PKPKSVQELE AEKTAQISPF RATLTTAGAY
TGGVATLLGL GLSAPNAAFT QMVTTFGLAG IVGYHTVWGV TPALHSPLMS VTNAISGLTA
VGGLSLMGGG YLPGTTAETL AVLAAFISSV NIAGGFLVTQ KMLDMFKRPT DPPEHNYLYL
LPGGVFVGGY AAALQSGYNI EQMMYLGSGL CCVGALAGLS NQTTARLGNA LGMMGVAGGI
AATLGALKPN PELLAQMSAA MAVGGTAGLA IAKKIQITDL PQLVAAFHSL VGLAAVLTCV
AEYMIEYPHF ATDPAANLTK IVAYLGTYIG GITFSGSLVA YGKLQGVLNS APLMLPGRHA
LNASLMAGSV GGMIPYMLDP SYTTGLTCLG SVSALSAVMG VTLTAAIGGA DMPVVITVLN
SYSGWALCAE GFLLNNNLLT IVGALIGSSG AILSYIMCVA MNRSLANVIL GGYGTSSTGT
GKPMEIVGTH TEVNVDQTVE MIKESQNVII VPGYGLCAAK AQYPIAELVK MLKEAGKKVR
FGIHPVAGRM PGQLNVLLAE AGVPYDIVLE MDEINDDFPD TDLVLVIGAN DTVNSAAQED
PNSIIAGMPV LEVWKSKQVV VMKRSLGVGY AAVDNPIFYK PNTAMLLGDA KKTCDALQAK
VREATSQ
//
