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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//