ID A0A3M7S295_BRAPC Unreviewed; 1070 AA.
AC A0A3M7S295;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=BpHYR1_047163 {ECO:0000313|EMBL:RNA29750.1};
OS Brachionus plicatilis (Marine rotifer) (Brachionus muelleri).
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Monogononta; Pseudotrocha; Ploima; Brachionidae; Brachionus.
OX NCBI_TaxID=10195 {ECO:0000313|EMBL:RNA29750.1, ECO:0000313|Proteomes:UP000276133};
RN [1] {ECO:0000313|EMBL:RNA29750.1, ECO:0000313|Proteomes:UP000276133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYR1 {ECO:0000313|EMBL:RNA29750.1};
RX PubMed=30375419; DOI=10.1038/s41598-018-34188-y;
RA Franch-Gras L., Hahn C., Garcia-Roger E.M., Carmona M.J., Serra M.,
RA Gomez A.;
RT "Genomic signatures of local adaptation to the degree of environmental
RT predictability in rotifers.";
RL Sci. Rep. 8:16051-16051(2018).
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:RNA29750.1}.
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DR EMBL; REGN01002165; RNA29750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7S295; -.
DR STRING; 10195.A0A3M7S295; -.
DR Proteomes; UP000276133; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; 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:SF19; 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.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000313|EMBL:RNA29750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276133};
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 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 726..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..192
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 201..365
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 1070 AA; 114233 MW; B887D62E6C8C35B7 CRC64;
MSYGFKRASR VLVNNGGHLY EKNYSLVLRI NPKTASFKRF NSTKAEPEGI SYKNLTIGVP
KETFLNERRV AITPAVTETL VKKGFKVIVE ENAGVLAKFP NSHYEASGAT VSQSKNIYSS
SDILLKVRPP TIEEIANLKN DSNLISFFYP AQNKHLIEEL QKKNMTLFAM DCVPRISRAQ
VFDALSSMAN IAGYKAVLEA ANNFGRFLTG QITAAGKVPP CKVMVIGGGV AGLSAIGTAR
NMGAIVRAFD TRSAVKEQVQ SMGAEFLEIN LKEEGEGQGG YAKEMSKEFI EAEMALFAKQ
CKEIDILITT ALIPGKPAPK LISKEMIESM KPGSVVVDLA AEAGGNIVTT RPGELYVYKD
VVHIGYTDLP SRLPTQSSTL YANNISKFLL SIGKQDHFHI DLNDEVVRGS IIINRGELMW
PPPKVEQVVQ ADTPKQIKKE EVKKLLTDAD YFRKYLKDSL VYTTGLSGLI GMSLISPNPA
FANMITTLSL SGIVGYHTVW SVTPALHSPL MSVTNAISGI TAAGGLLLMG GGYFPSTIAQ
WLAMSAAFIS SINITGGFII TQRMLDMFKR PTDPKEFNYL YGIPALSSLA TYGYGITHGF
DDSTNLAYLA ASLCCVGALG GLSSQPSARL GNALGMIGVS TGLAATLGQL NINSELAAQM
GVTLGLGGII GAIIAKKIPI TDLPQLVAAF HSFVGAAAVL TCVSHFMSEA SHLASDPAAS
VIKTSLFLGT FIGAITWTGS LVAYGKLQGV LNSNPLLLPG RHVLNAALLA SNVGALGWYL
NTDDTTMGLA LLGATTLLSS TMGVTLTSAI GGADMPVVIT VLNSYSGWAL CAEGFMLNNN
LMTIVGALIG SSGAILSYIM CKAMNRSLPN VILGGYGTDS TGTGKAMEIT GTHTEIKADQ
AVEYMKEAQN IIITPGYGLC VAKAQYPIAE MVELLKKKGK NVKFAIHPVA GRMPGQLNVL
LAEAGVPYDI VHEMEEVNHE FKETDLTLVI GANDTVNSAA EEDPNSIIAG MPVLKVWNSK
QVIVMKRSLG VGYAAVDNPI FFKPNTAMLL GDAKKTCDAL LTKLKQEYEI
//
