Q968X7 · PNO_CRYPV
- ProteinPyruvate dehydrogenase [NADP(+)]
- GenePFOR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1934 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
May have an important role in respiratory metabolism. Cryptosporidium have a relic mitochondrion with no function in energy metabolism so it is not known if PFOR has a function.
Miscellaneous
Arose from gene fusion of pyruvate:ferredoxin oxidoreductase and cytochrome-P450 reductase. Gene fusion has only been found in Euglena and Cryptosporidium.
Catalytic activity
- CoA + NADP+ + pyruvate = acetyl-CoA + CO2 + NADPH
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 FMN per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 719 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 722 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 725 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 729 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 776 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 779 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 782 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 786 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1542-1553 | FAD (UniProtKB | ChEBI) | ||||
Sequence: YCLGDSLALYGQ | ||||||
Binding site | 1685-1695 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IKSRSYSIASC |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | FMN binding | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | pyruvate dehydrogenase (NADP+) activity | |
Molecular Function | thiamine pyrophosphate binding | |
Biological Process | cellular respiration | |
Biological Process | electron transport chain | |
Biological Process | pyruvate metabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate dehydrogenase [NADP(+)]
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Cryptosporidiidae > Cryptosporidium
Accessions
- Primary accessionQ968X7
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215559 | 1-1934 | Pyruvate dehydrogenase [NADP+] | |||
Sequence: MGEKEIVDGCVAACHIAYACSEVAFTYPITPSSTISEVADSWMSRGRRNIFDQVVSVVEMQSEMGSAGALHGSLSVGCSTTTFTASQGLLLMIPNMYKIAGELWPCVFHVTARAIATSSLSIFGDHNDIMAARQTGWAFLGAMTVQEVMDLALVSHVSTFECSVPFVNFFDGFRTSHELQKIDMISYETIKKIFPYEKLKEFRERALNPTHPTLRGTATSSDVYFQLAEARNKYYESTPDIVQSVMDRLAKLIGRSYHLFDYYGHPDAEFLIVVMGSGGLTIEEMIDYLMEKSNEKVGMIKVRLFRPWSIDAFVKKIPKTTKRITVLERCKESGSLGEPLCLDVSTSIMRSELSSNNILVLGGRYGLASKEFTPGMALAVWENMISENPINNFSVGIDDDVTFKSLFVRQPRLDLLTSETKQCLFWGLGSDGTVSANKNAIKIIGESTDLQVQGYFAYDAKKAGGATMSHLRFGPKPIKSAYLLQRCDYVAVHHPSYVHKFDVLENIKQGGCFVLNCPWSTLEELNHELPSKIKHQIASRDVKFYVIDAQRIAQESNLGRRINNILMVVFFSLTNIIPLDLAIKLVKEAIKKTYGKKGDAVVNSNWKAVDLTLESLIQISYDKSQWISKDKCGEKSLPATAVETGNKDQEITKSTVLKQKPEHDVNQFVKDILGPVNALKGDELPVSMFEPTGTVPLGTTAYEKRGIAMSIPIVDMNKCTQCNYCSIVCPHAAIRPFLLDEAEFKNAPETMHIPKAKGGQEFSSYYYRIQVTPLDCTGCELCVHACPDDALHMEGLQKMEAVEKTHWDYLIGLPNKAEKFDRTTVKGSQFQQPLLEFSAACEGCGETPYVKLLTQLFGERMVIANATGCSSIWGASYPSVPYTKNQKGYGPAWGNSLFEDNAEYGLGMVVGYRQRRDRFRELVSNEILKDITEEEEFLKDDNASVQGRNEIITKYDHLKDYLRSWLKNIRNGEACQSLFEEISKLLEDNLINSNNFAQVLKKDRIELLEKLYDSRDLIPKISHWIVGGDGWAYDIGYAGLDHVLSFGEDVNIIILDTEVYSNTGGQASKSTPFGAIAKFAQSGNLRQKKDIGSIAMEYGSVYVASVALGANYSQTIKSLLEAEKYPGTSLIVAYSTCIEHGYTKYNLQQESVKLAVESGYWPLYRYNPELVRTEVVDNLTTIVSSGFTLDSKKVKVDIENFLKRENRFLQLIRSNPELASMAKDKLKAHSDKRFQKMKDMSENVTVTALKDQIKKLKDQLISIQNASKTGELAASGLINADLFIEQEMHVLYGTETGNSEEVAQYIQSQLVSRGYSSSSLNLDDLDIDEFLNPDKFSTVIIVTSTSGQGEFPGSSGILYEALLKKHLENQDDKFCSFMRFGIFGLGDSNYVFFNEAAKKWDKLLLDCGAVRIGAVGMGDDQSEEKYETELIEWLPDYLQLINAPEPKHDEKSEIPKATTFKVTILDSCRNDILNESTGTLCEKLDENNNIGNSHYKPIIPPNSVLLPVIENKRITNQDYDKDVRHIVFKLIGDGGDTPSLSYCLGDSLALYGQNPVNEAIKAIEMFGYNPYSLLRLSINEENEANNTNKVNQRYSSLFGYDITVLQLFVECLDLWGKPNRKFFQEFYRYCSNPEEKIQAKKWAQNEGKKLIEEFSSKTGTYLDVFKMFESARPTLAQLLDIVPFIKSRSYSIASCNKFVNGEKIELCVGIVDWKLESGEIRYGQCTGFLNRLPILDSESKIDSIPRLPSNIKASAFNLPFDYRSPVIMACMGTGIAPFRAFVQNKKYIRDVLKEEIGPVILYFGCRYYDNDYLYREELENYVKEGVITSLNIAFSRDPKGYKTSNCENIRYAQKMYVQHLMLENSQEIYENMIEKCGYFYLCGTKQVPIDIRKAIIQIIIKHSSTTEQVTSEEDANSILNSIQIMGRYNVEAWS |
Expression
Developmental stage
Both sporozoites and intracellular stages of life cycle.
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 710-739 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: SIPIVDMNKCTQCNYCSIVCPHAAIRPFLL | ||||||
Domain | 767-796 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: YRIQVTPLDCTGCELCVHACPDDALHMEGL | ||||||
Domain | 1288-1438 | Flavodoxin-like | ||||
Sequence: MHVLYGTETGNSEEVAQYIQSQLVSRGYSSSSLNLDDLDIDEFLNPDKFSTVIIVTSTSGQGEFPGSSGILYEALLKKHLENQDDKFCSFMRFGIFGLGDSNYVFFNEAAKKWDKLLLDCGAVRIGAVGMGDDQSEEKYETELIEWLPDYL | ||||||
Domain | 1501-1759 | FAD-binding FR-type | ||||
Sequence: PNSVLLPVIENKRITNQDYDKDVRHIVFKLIGDGGDTPSLSYCLGDSLALYGQNPVNEAIKAIEMFGYNPYSLLRLSINEENEANNTNKVNQRYSSLFGYDITVLQLFVECLDLWGKPNRKFFQEFYRYCSNPEEKIQAKKWAQNEGKKLIEEFSSKTGTYLDVFKMFESARPTLAQLLDIVPFIKSRSYSIASCNKFVNGEKIELCVGIVDWKLESGEIRYGQCTGFLNRLPILDSESKIDSIPRLPSNIKASAFNLP |
Sequence similarities
In the N-terminal section; belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,934
- Mass (Da)217,557
- Last updated2001-12-01 v1
- ChecksumBCDB56F4B2BA3D60