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Database: UniProt
Entry: A0A024VIM3_PLAFA
LinkDB: A0A024VIM3_PLAFA
Original site: A0A024VIM3_PLAFA 
ID   A0A024VIM3_PLAFA        Unreviewed;      1134 AA.
AC   A0A024VIM3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   ORFNames=PFFCH_04489 {ECO:0000313|EMBL:ETW28138.1};
OS   Plasmodium falciparum FCH/4.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=1036724 {ECO:0000313|EMBL:ETW28138.1, ECO:0000313|Proteomes:UP000030656};
RN   [1] {ECO:0000313|EMBL:ETW28138.1, ECO:0000313|Proteomes:UP000030656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28138.1,
RC   ECO:0000313|Proteomes:UP000030656};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Annotation of Plasmodium falciparum FCH/4.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETW28138.1, ECO:0000313|Proteomes:UP000030656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FCH/4 {ECO:0000313|EMBL:ETW28138.1,
RC   ECO:0000313|Proteomes:UP000030656};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Plasmodium falciparum FCH/4.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KI928027; ETW28138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024VIM3; -.
DR   EnsemblProtists; ETW28138; ETW28138; PFFCH_04489.
DR   Proteomes; UP000030656; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; 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; IPR024605; NADP_transhyd_a_C.
DR   InterPro; IPR034300; PNTB-like.
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.
DR   PROSITE; PS00837; ALADH_PNT_2; 1.
PE   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000030656};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1134
FT                   /note="proton-translocating NAD(P)(+) transhydrogenase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001535974"
FT   TRANSMEM        95..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        252..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1065..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1092..1111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          655..781
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          790..961
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   REGION          590..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1134 AA;  126887 MW;  B83C16FA030152FF CRC64;
     MYRNIFASII LCLLLFLSSN CYGKSNLRNY INGFNEFIED DKNSNFEIKL PVINFPVSSN
     DITNDYKNEE KASRDNLLNN EEIEPSTYYS VLPSLLNAVY LFSSICFILC LTGLNAHRTS
     KRGNILGFIG IVAAIMITFS QVGFGFRYKL FLLIVIPAIT IGIYIAHNVS MVQMPQLVAL
     FHSFVGLAAL FVGFSKYHSE SFENYEISTI HLLELYVGTF IASIAFIGSL VAAGKLSGIL
     DSKSLKLQIK KIINILCIVL IIILGYYFVT LKLLYLKSIC LYISLIIDSF LGFHLIASIG
     AADMPVIISV LNSYSGFATA ISGFLLHNNL LIISGALIGS SGAILSYIMC IGMNRDIFNI
     ILGGWDDYEN MGESIYDQNF IEKKNKQTIN STTNKYVAEN LINAKNIIIV PGYGTALSKC
     QRELAEICSI LTSRNINVTF AIHPVAGRMP GHLNVLLAEA NIPYNIVKEM NEINPIISEA
     DIVLVVGAND IVNPSSLDPS SKIYGMPVIE VWKSKQVIVF KRTLNTGYSA IDNPLFYFSN
     TFLLFGDAKH TTNQILTILN DYVNNKYPDI SDQDRHINHD KTQFRYSYSL TDSSHSNDDS
     TSKEQNYPKP RRVIGLIKDD NVQGGNDLLI EHIQSKVENA PNIKDQKRDV NLSIVPISPK
     FIPKLRLMGF RILVERDIGT NILMQNDEYT KYGAEVVSRN VILQQSNIIL KVDPPTVNFI
     EEIQNNTILI SYLWPSINYH LLDKMIQDEE KHNITYLAID EVPRSTRAQK LDVRSSMSNL
     QGYRAVLEAF FILPRFSKSS ITAAGKINPA KVFVIGAGVA GLQAIITAKS LGAIVYSHDS
     RLATEEEVKS CGGIFIRIPT SERGDILNMS TDMNNEEYIK VQSNLFKKII KKCDILICSA
     SIPGKTSPKL VTTEMIKLMK PGSVAVDLST EFGDKKNNWG GNIECSQSNE NILINGVHVL
     GRDKIERNMP MQASDLFSMN MINLLEEMGG GVHFNIDMNN DIIKSLVVIK DGNILYSPDK
     SVEKLIKSES VFINEKNQLI EPISEQKIKY PTGLRLTEKF IESDTFFYIS LLFVIILTFL
     AATYLSQSDL QSLFLFTLST IVGYYCVWSV TPALHTPLMS MTNANRNFFK NIFV
//
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