Q4R4U1 · PANK4_MACFA
- Protein4'-phosphopantetheine phosphatase
- GenePANK4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids773 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Phosphatase which shows a preference for 4'-phosphopantetheine and its oxidatively damaged forms (sulfonate or S-sulfonate), providing strong indirect evidence that the phosphatase activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing excess 4'-phosphopantetheine could constitute a directed overflow mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate would forestall their conversion to inactive forms of CoA and acyl carrier protein. May play a role in the physiological regulation of CoA intracellular levels.
Catalytic activity
- (R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphateThis reaction proceeds in the forward direction.
- (R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine sulfonate + phosphateThis reaction proceeds in the forward direction.
- (R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-sulfopantetheine + phosphateThis reaction proceeds in the forward direction.
Cofactor
Ni2+ (UniProtKB | Rhea| CHEBI:49786 )
Activity regulation
Activity is strongly promoted by Co2+, Ni2+, Mg2+ and Mn2+. Activity is inhibited by EDTA.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 196 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 199 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 623 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: D | ||||||
Binding site | 624 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: N | ||||||
Binding site | 659 | Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | pantothenate kinase activity | |
Biological Process | coenzyme A biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4'-phosphopantetheine phosphatase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionQ4R4U1
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000249247 | 2-773 | 4'-phosphopantetheine phosphatase | |||
Sequence: AECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKDTERDHEPPYEISVQEEITARLHFVKFENTYIEACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAGSSGLMSTSPELGPAQRARSGTFDLLEMDRLERPLVNLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDTLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPYFGFEEAKRKLQERPWLVDSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDVTHGESLIVAERIAGMDPVVHSALREERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADLVVIEGMGRAVHTNYHAALCCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE | ||||||
Modified residue | 320 | 3'-nitrotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 393 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 404 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 406 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-402 | Pantothenate kinase | ||||
Sequence: AECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKDTERDHEPPYEISVQEEITARLHFVKFENTYIEACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAGSSGLMSTSPELGPAQRA | ||||||
Region | 403-773 | 4'-phosphopantetheine phosphatase | ||||
Sequence: RSGTFDLLEMDRLERPLVNLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDTLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPYFGFEEAKRKLQERPWLVDSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDVTHGESLIVAERIAGMDPVVHSALREERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADLVVIEGMGRAVHTNYHAALCCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE | ||||||
Motif | 724-728 | Subfamily II EGMGR motif | ||||
Sequence: EGMGR |
Domain
Subfamily II proteins have an EGMGR motif about 50 residues from the C-terminus (By similarity).
This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (By similarity).
Subfamily II proteins occur only in eukaryotes, in two forms: as a stand-alone unit in plants, and as a C-terminal domain of pantothenate kinases in plants, animals, and chytrid fungi (By similarity).
This motif lies near the metal-binding residues in the putative substrate-binding cleft 2 (By similarity).
Subfamily II proteins occur only in eukaryotes, in two forms: as a stand-alone unit in plants, and as a C-terminal domain of pantothenate kinases in plants, animals, and chytrid fungi (By similarity).
Sequence similarities
In the N-terminal section; belongs to the type II pantothenate kinase family.
In the C-terminal section; belongs to the damage-control phosphatase family. Phosphopantetheine phosphatase II subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length773
- Mass (Da)86,011
- Last updated2006-09-05 v2
- Checksum2B8DD62B83A9B502
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 176 | in Ref. 1; BAE01884 | ||||
Sequence: E → G | ||||||
Sequence conflict | 236 | in Ref. 1; BAE01884 | ||||
Sequence: D → G |
Keywords
- Technical term