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Database: UniProt
Entry: Q968X7
LinkDB: Q968X7
Original site: Q968X7 
ID   PNO_CRYPV               Reviewed;        1934 AA.
AC   Q968X7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-FEB-2019, entry version 107.
DE   RecName: Full=Pyruvate dehydrogenase [NADP(+)];
DE            EC=1.2.1.51;
DE   AltName: Full=CpPNO;
DE   AltName: Full=Pyruvate:NADP(+) oxidoreductase;
GN   Name=PFOR;
OS   Cryptosporidium parvum.
OC   Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=5807 {ECO:0000312|EMBL:AAK48421.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KSU-1;
RX   PubMed=11319255; DOI=10.1093/oxfordjournals.molbev.a003853;
RA   Rotte C., Stejskal F., Zhu G., Keithly J.S., Martin W.;
RT   "Pyruvate: NADP oxidoreductase from the mitochondrion of Euglena
RT   gracilis and from the apicomplexan Cryptosporidium parvum: a
RT   biochemical relic linking pyruvate metabolism in mitochondriate and
RT   amitochondriate protists.";
RL   Mol. Biol. Evol. 18:710-720(2001).
CC   -!- FUNCTION: May have an important role in respiratory metabolism.
CC       Cryptosporidium have a relic mitochondrion with no function in
CC       energy metabolism so it is not known if PFOR has a function.
CC       {ECO:0000303|PubMed:11319255}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + NADP(+) + pyruvate = acetyl-CoA + CO2 + NADPH;
CC         Xref=Rhea:RHEA:17425, ChEBI:CHEBI:15361, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.51;
CC         Evidence={ECO:0000303|PubMed:11319255};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q94IN5}.
CC   -!- DEVELOPMENTAL STAGE: Both sporozoites and intracellular stages of
CC       life cycle. {ECO:0000269|PubMed:11319255}.
CC   -!- MISCELLANEOUS: Arose from gene fusion of pyruvate:ferredoxin
CC       oxidoreductase and cytochrome-P450 reductase. Gene fusion has only
CC       been found in Euglena and Cryptosporidium.
CC       {ECO:0000303|PubMed:11319255}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       pyruvate:ferredoxin/flavodoxin oxidoreductase family.
CC       {ECO:0000305}.
DR   EMBL; AF208233; AAK48421.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q968X7; -.
DR   SMR; Q968X7; -.
DR   ChEMBL; CHEMBL2364026; -.
DR   PRIDE; Q968X7; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   eggNOG; KOG1159; Eukaryota.
DR   eggNOG; COG0369; LUCA.
DR   eggNOG; COG0674; LUCA.
DR   eggNOG; COG1013; LUCA.
DR   eggNOG; COG1014; LUCA.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0050243; F:pyruvate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.920.10; -; 1.
DR   Gene3D; 4.10.780.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR   InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR011895; Pyrv_flavodox_OxRed.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF10371; EKR; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM00890; EKR; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF52518; SSF52518; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   TIGRFAMs; TIGR02176; pyruv_ox_red; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Electron transport; FAD; Flavoprotein; FMN; Iron; Iron-sulfur;
KW   Metal-binding; NADP; Oxidoreductase; Repeat; Thiamine pyrophosphate;
KW   Transport.
FT   CHAIN         1   1934       Pyruvate dehydrogenase [NADP(+)].
FT                                /FTId=PRO_0000215559.
FT   DOMAIN      710    739       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      767    796       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN     1288   1438       Flavodoxin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00088}.
FT   DOMAIN     1501   1759       FAD-binding FR-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00716}.
FT   NP_BIND    1542   1553       FAD. {ECO:0000250}.
FT   NP_BIND    1685   1695       FAD. {ECO:0000250}.
FT   METAL       719    719       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL       722    722       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL       725    725       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL       729    729       Iron-sulfur 1 (4Fe-4S). {ECO:0000255}.
FT   METAL       776    776       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL       779    779       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL       782    782       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL       786    786       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
SQ   SEQUENCE   1934 AA;  217557 MW;  BCDB56F4B2BA3D60 CRC64;
     MGEKEIVDGC VAACHIAYAC SEVAFTYPIT PSSTISEVAD SWMSRGRRNI FDQVVSVVEM
     QSEMGSAGAL HGSLSVGCST TTFTASQGLL LMIPNMYKIA GELWPCVFHV TARAIATSSL
     SIFGDHNDIM AARQTGWAFL GAMTVQEVMD LALVSHVSTF ECSVPFVNFF DGFRTSHELQ
     KIDMISYETI KKIFPYEKLK EFRERALNPT HPTLRGTATS SDVYFQLAEA RNKYYESTPD
     IVQSVMDRLA KLIGRSYHLF DYYGHPDAEF LIVVMGSGGL TIEEMIDYLM EKSNEKVGMI
     KVRLFRPWSI DAFVKKIPKT TKRITVLERC KESGSLGEPL CLDVSTSIMR SELSSNNILV
     LGGRYGLASK EFTPGMALAV WENMISENPI NNFSVGIDDD VTFKSLFVRQ PRLDLLTSET
     KQCLFWGLGS DGTVSANKNA IKIIGESTDL QVQGYFAYDA KKAGGATMSH LRFGPKPIKS
     AYLLQRCDYV AVHHPSYVHK FDVLENIKQG GCFVLNCPWS TLEELNHELP SKIKHQIASR
     DVKFYVIDAQ RIAQESNLGR RINNILMVVF FSLTNIIPLD LAIKLVKEAI KKTYGKKGDA
     VVNSNWKAVD LTLESLIQIS YDKSQWISKD KCGEKSLPAT AVETGNKDQE ITKSTVLKQK
     PEHDVNQFVK DILGPVNALK GDELPVSMFE PTGTVPLGTT AYEKRGIAMS IPIVDMNKCT
     QCNYCSIVCP HAAIRPFLLD EAEFKNAPET MHIPKAKGGQ EFSSYYYRIQ VTPLDCTGCE
     LCVHACPDDA LHMEGLQKME AVEKTHWDYL IGLPNKAEKF DRTTVKGSQF QQPLLEFSAA
     CEGCGETPYV KLLTQLFGER MVIANATGCS SIWGASYPSV PYTKNQKGYG PAWGNSLFED
     NAEYGLGMVV GYRQRRDRFR ELVSNEILKD ITEEEEFLKD DNASVQGRNE IITKYDHLKD
     YLRSWLKNIR NGEACQSLFE EISKLLEDNL INSNNFAQVL KKDRIELLEK LYDSRDLIPK
     ISHWIVGGDG WAYDIGYAGL DHVLSFGEDV NIIILDTEVY SNTGGQASKS TPFGAIAKFA
     QSGNLRQKKD IGSIAMEYGS VYVASVALGA NYSQTIKSLL EAEKYPGTSL IVAYSTCIEH
     GYTKYNLQQE SVKLAVESGY WPLYRYNPEL VRTEVVDNLT TIVSSGFTLD SKKVKVDIEN
     FLKRENRFLQ LIRSNPELAS MAKDKLKAHS DKRFQKMKDM SENVTVTALK DQIKKLKDQL
     ISIQNASKTG ELAASGLINA DLFIEQEMHV LYGTETGNSE EVAQYIQSQL VSRGYSSSSL
     NLDDLDIDEF LNPDKFSTVI IVTSTSGQGE FPGSSGILYE ALLKKHLENQ DDKFCSFMRF
     GIFGLGDSNY VFFNEAAKKW DKLLLDCGAV RIGAVGMGDD QSEEKYETEL IEWLPDYLQL
     INAPEPKHDE KSEIPKATTF KVTILDSCRN DILNESTGTL CEKLDENNNI GNSHYKPIIP
     PNSVLLPVIE NKRITNQDYD KDVRHIVFKL IGDGGDTPSL SYCLGDSLAL YGQNPVNEAI
     KAIEMFGYNP YSLLRLSINE ENEANNTNKV NQRYSSLFGY DITVLQLFVE CLDLWGKPNR
     KFFQEFYRYC SNPEEKIQAK KWAQNEGKKL IEEFSSKTGT YLDVFKMFES ARPTLAQLLD
     IVPFIKSRSY SIASCNKFVN GEKIELCVGI VDWKLESGEI RYGQCTGFLN RLPILDSESK
     IDSIPRLPSN IKASAFNLPF DYRSPVIMAC MGTGIAPFRA FVQNKKYIRD VLKEEIGPVI
     LYFGCRYYDN DYLYREELEN YVKEGVITSL NIAFSRDPKG YKTSNCENIR YAQKMYVQHL
     MLENSQEIYE NMIEKCGYFY LCGTKQVPID IRKAIIQIII KHSSTTEQVT SEEDANSILN
     SIQIMGRYNV EAWS
//
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