Q4R4U1 · PANK4_MACFA

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.

Caution

Despite belonging to the type II pantothenate kinase family, the pantothenate kinase domain contains a Val residue at position 147 and a Trp residue at position 211 instead of the two conserved active site residues, Glu and Arg. Lacks pantothenate kinase activity.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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.

TypeIDPosition(s)Description
Binding site196acetyl-CoA (UniProtKB | ChEBI)
Binding site199acetyl-CoA (UniProtKB | ChEBI)
Binding site623Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity
Binding site624Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity
Binding site659Mn2+ (UniProtKB | ChEBI); catalytic; for phosphatase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionhydrolase activity
Molecular Functionmetal ion binding
Molecular Functionpantothenate kinase activity
Biological Processcoenzyme A biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4'-phosphopantetheine phosphatase
  • EC number
  • Alternative names
    • Inactive pantothenic acid kinase 4

Gene names

    • Name
      PANK4
    • ORF names
      QccE-17245

Organism names

Accessions

  • Primary accession
    Q4R4U1
  • Secondary accessions
    • Q2PFY2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00002492472-7734'-phosphopantetheine phosphatase
Modified residue3203'-nitrotyrosine
Modified residue393Phosphoserine
Modified residue404Phosphoserine
Modified residue406Phosphothreonine

Keywords

Interaction

Subunit

Homodimer. Interacts with PKM.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region2-402Pantothenate kinase
Region403-7734'-phosphopantetheine phosphatase
Motif724-728Subfamily II EGMGR motif

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).

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 status
    Complete
  • Length
    773
  • Mass (Da)
    86,011
  • Last updated
    2006-09-05 v2
  • Checksum
    2B8DD62B83A9B502
MAECGASGSGSSGDSLDKSITLPPDEIFRNLENAKRFAIDIGGSLTKLAYYSTVQHKVAKVRSFDHSGKDTERDHEPPYEISVQEEITARLHFVKFENTYIEACLDFIKDHLVNTETKVIQATGGGAYKFKDLIEEKLRLKVDKEDVMTCLIKGCNFVLKNIPHEAFVYQKDSDPEFRFQTNHPHIFPYLLVNIGSGVSIVKVETEDRFEWVGGSSIGGGTFWGLGALLTKTKKFDELLHLASRGQHSNVDMLVRDVYGGAHQTLGLSGNLIASSFGKSATADQEFSKEDMAKSLLHMISNDIGQLACLHARLHSLDRVYFGGFFIRGHPVTMRTITYSINFFSKGEVQALFLRHEGYLGAIGAFLKGAEQDNPNQYSWGENYAGSSGLMSTSPELGPAQRARSGTFDLLEMDRLERPLVNLPLLLDPPSYVPDTVDLTDDALARKYWLTCFEEALDGVVKRAVASQPDSVDAAERAEKFRQKYWNKLQTLRQQPFAYGTLTVRSLLDTREHCLNEFNFPDPYSKVKQRENGVALRCFPGVVRSLDTLGWEERQLALVKGLLAGNVFDWGAKAVSDVLESDPYFGFEEAKRKLQERPWLVDSYSEWLQRLKGPPHKCALIFADNSGIDIILGVFPFVRELLLRGTEVILACNSGPALNDVTHGESLIVAERIAGMDPVVHSALREERLLLVQTGSSSPCLDLSRLDKGLAALVRERGADLVVIEGMGRAVHTNYHAALCCESLKLAVIKNAWLAERLGGRLFSVIFKYEVPAE

Sequence caution

The sequence BAE72988.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict176in Ref. 1; BAE01884
Sequence conflict236in Ref. 1; BAE01884

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB169803
EMBL· GenBank· DDBJ
BAE01884.1
EMBL· GenBank· DDBJ
mRNA
AB220455
EMBL· GenBank· DDBJ
BAE72988.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Similar Proteins

Disclaimer

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