PNO_CRYPV
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 03-AUG-2022, entry version 118.
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; Sar; 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 gracilis
RT and from the apicomplexan Cryptosporidium parvum: a biochemical relic
RT linking pyruvate metabolism in mitochondriate and amitochondriate
RT 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 energy
CC 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 life
CC cycle. {ECO:0000269|PubMed:11319255}.
CC -!- MISCELLANEOUS: Arose from gene fusion of pyruvate:ferredoxin
CC oxidoreductase and cytochrome-P450 reductase. Gene fusion has only been
CC found in Euglena and Cryptosporidium. {ECO:0000303|PubMed:11319255}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC pyruvate:ferredoxin/flavodoxin oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF208233; AAK48421.1; -; Genomic_DNA.
DR AlphaFoldDB; Q968X7; -.
DR SMR; Q968X7; -.
DR ChEMBL; CHEMBL2364026; -.
DR DrugCentral; Q968X7; -.
DR PRIDE; Q968X7; -.
DR VEuPathDB; CryptoDB:cgd4_690; -.
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 CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
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
FT /note="Pyruvate dehydrogenase [NADP(+)]"
FT /id="PRO_0000215559"
FT DOMAIN 710..739
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 767..796
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 1288..1438
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 1501..1759
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 719
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 722
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 725
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 729
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 776
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 779
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 782
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 786
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 1542..1553
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1685..1695
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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
