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Database: UniProt
Entry: W7K965_PLAFO
LinkDB: W7K965_PLAFO
Original site: W7K965_PLAFO 
ID   W7K965_PLAFO            Unreviewed;      2845 AA.
AC   W7K965;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE            EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN   ORFNames=PFNF54_05062 {ECO:0000313|EMBL:EWC86332.1};
OS   Plasmodium falciparum (isolate NF54).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC86332.1, ECO:0000313|Proteomes:UP000030673};
RN   [1] {ECO:0000313|EMBL:EWC86332.1, ECO:0000313|Proteomes:UP000030673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NF54 {ECO:0000313|EMBL:EWC86332.1,
RC   ECO:0000313|Proteomes:UP000030673};
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 NF54.";
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; KE123877; EWC86332.1; -; Genomic_DNA.
DR   EnsemblProtists; EWC86332; EWC86332; PFNF54_05062.
DR   Proteomes; UP000030673; 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:UP000030673};
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        1764..1783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1795..1813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1819..1839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1846..1864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1884..1909
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1921..1938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2000..2019
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2734..2755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2761..2780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2816..2835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2324..2450
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          2459..2630
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   REGION          2259..2279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2845 AA;  332756 MW;  3F939EFD89C60CAB CRC64;
     MLPRKRVFIH LYNNICGFGI IKEKSFYHKK NEDLYKYNQA YAYKTKKKGN ITKAIEINKE
     ILKESNKNIL DLIKIIEENK EDLNIINYVT FFHRVMQIIN KNKEIYIKYN IYINKTIEQN
     VKIIFDYLKD TNNILNNINN YNKRLFSSFI WSYSKYISFL NKKNKYFSID NKHKLLLNNK
     FTNGSFHNII NYNIHKDTIL PSCDIIKRYE DINISLIQPC NISNSNINHI YQVNKSTNHK
     IYNSHIIYKY SIFNKSNIDL LFSYANQYLP LLNPSRYVIV FWSLSKLNKD NKVLHQKYYK
     KSVSLIPLLK YKELIILLYS YSYVNFRNFY FYLNIKNYIL KHKIYKQIIS ERNYESLVNM
     LLSFINQNIL FLDLYENIVK YIIFKKRYTF INLLNNQELI TLTYCLCKFP IILIDQAQPN
     NINIEKKYII NNNIKNIKNN DALYTHQIIF LYEYLKNVII KRCNMIFKEQ LDINYSIFYK
     SIINNNNNNN IYTLENLILI IWSLSLKHIY SAKLFLYTFI KLNYMMQNEQ LIYNHYNILT
     NFYLSFLSFI LEDHIFINLY FNKENHHSLN ILYQYIDMFL DNFKTCKETI NMNKRKYDVD
     ISNMHKNIYQ IINNIKFPNK INTILEYKNV HNISIDILLY KPNYVLQQKK IFILNIIKDK
     YDTYNHCMYN NNSGTNTSYE NLKINNILIT MWNKNDNMIK SKEKGQINIY KYFSSIKNCS
     KNNIKGTKKQ QKIKMNKNRK IINSNNIFNV KYIKSYFCTN VVKLSNIEKK NNNNNDNLKN
     NKENNLFTFI EKIKNFHLKN NKDQLSDTYK ELHNILDIHI VHMKQSDIIS FFYKFSSILT
     IFYTINFMEH INELIKTFYY FHNFTFLFLK ETNIRINLFI DICWIYFRYM KFLTYIKRER
     NMEKKCIIIN NNNNNNNIYI YNNDQSNIQN VQKIKLYNNS LTYQNCDNNE SNVLFDQLNV
     VDNIFNIVKK KILEEDNMIK GISSKNMSFL ISIFIYLNHS EHIRQYLEKN NFHETVFTIK
     DILFILTALS KCNNNNYNNI CMWDIQHFFV NKFIDNIKNC QVQDLVDFTN LCAELKVNQE
     HISSNIKNKI MSYIYCEANK EKKNIEKKKS ILNHTTIMNI NEGNNKSIMF IELFDEKQLA
     FFVRNCYRMH CFDKSFFDLL CDIILKKYCT FHINNLCIAL LCFSRIYCLH KATKFIHKTR
     DIKRKEFINI NTNKNTNINT NINTNINTNK NTNKKGDDYL EKNISMCRYD IPLSLKKLIK
     YTEKKLLSNT NIDFYNLCYF MESITLLKIQ NKKLYQLALN ETLNNIRQKI YNEQDTKLLG
     KILWCLSYYH KTEFIFSFYL IHFMLQNMIY KHIIPENFIS IYLYFIQSRV YNPILFHNIA
     QVILSKITLN DYFTHNKNKH ANITNIKLNV ISELYATMSW AYAFVYNETL NKEETYILNK
     KEKNEVTNYP LKKREKKISY TENINEDHIL FKTKSYNDDD IMYNDLNFIQ KIYSYIFNEI
     KILEKNNNLS FLLLVRFLWG ISLTNLISEP IINFINLYNW NDVNTKEQND MHLHMLFTFW
     LRIKYDHSNL HLSNSFIQLK DEIFLLLQKR EFKRNMNKND HISDFHVQIC QILDDLNIRY
     HNEYITKDLL SVDIKLERKC CEQKLAIEID GPSHHFLVLN EMQKADPQRI KKNIFASIIL
     CLLLFLSSNC YGKSNLRNYI NGFNEFIEDD KNSNFEIKLP VINFPVSSND ITNDYKNEEK
     ASRDNLLNNE EIEPSTYYSV LPSLLNAVYL FSSICFILCL TGLNAHRTSK RGNILGFIGI
     VAAIMITFSQ VGFGFRYKLF LLIVIPAITI GIYIAHNVSM VQMPQLVALF HSFVGLAALF
     VGFSKYHSES FENYEISTIH LLELYVGTFI ASIAFIGSLV AAGKLSGILD SKSLKLQIKK
     IINILCIVLI IILGYYFVTL KLLYLKSICL YISLIIDSFL GFHLIASIGA ADMPVIISVL
     NSYSGFATAI SGFLLHNNLL IISGALIGSS GAILSYIMCI GMNRDIFNII LGGWDDYENM
     GESIYDQNFI EKKNKQTINS TTNKYVAENL INAKNIIIVP GYGTALSKCQ RELAEICSIL
     TSRNINVTFA IHPVAGRMPG HLNVLLAEAN IPYNIVKEMN EINPIISEAD IVLVVGANDI
     VNPSSLDPSS KIYGMPVIEV WKSKQVIVFK RTLNTGYSAI DNPLFYFSNT FLLFGDAKHT
     TNQILTILND YVNNKYPDIS DQDRHINHDK TQFRYSYSLT DSSHSNDDST SKEQNYPKPR
     RVIGLIKDDN VQGGNDLLIE HIQSKVENAP NIKDQKRDVN LSIVPISPKF IPKLRLMGFR
     ILVERDIGTN ILMQNDEYTK YGAEVVSRNV ILQQSNIILK VDPPTVNFIE EIQNNTILIS
     YLWPSINYHL LDKMIQDEEK HNITYLAIDE VPRSTRAQKL DVRSSMSNLQ GYRAVLEAFF
     ILPRFSKSSI TAAGKINPAK VFVIGAGVAG LQAIITAKSL GAIVYSHDSR LATEEEVKSC
     GGIFIRIPTS ERGDILNMST DMNNEEYIKV QSNLFKKIIK KCDILICSAS IPGKTSPKLV
     TTEMIKLMKP GSVAVDLSTE FGDKKNNWGG NIECSQSNEN ILINGVHVLG RDKIERNMPM
     QASDLFSMNM INLLEEMGGG VHFNIDMNND IIKSLVVIKD GNILYSPDKS VEKLIKSESV
     FINEKNQLIE PISEQKIKYP TGLRLTEKFI ESDTFFYISL LFVIILTFLA ATYLSQSDLQ
     SLFLFTLSTI VGYYCVWSVT PALHTPLMSM TNALSGVIII GSMIEYGNGY KDLSSILSML
     ATFLSSVNLS GGFYVTKRML DMFFI
//
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