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P34047 · HIS5A_ARATH

Function

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.

Features

Showing features for binding site.

127020406080100120140160180200220240260
TypeIDPosition(s)Description
Binding site84substrate
Binding site110Mn2+ 1 (UniProtKB | ChEBI)
Binding site110-118substrate
Binding site136Mn2+ 2 (UniProtKB | ChEBI)
Binding site136-140substrate
Binding site137Mn2+ 1 (UniProtKB | ChEBI)
Binding site140Mn2+ 2 (UniProtKB | ChEBI)
Binding site162substrate
Binding site184substrate
Binding site208Mn2+ 2 (UniProtKB | ChEBI)
Binding site232Mn2+ 1 (UniProtKB | ChEBI)
Binding site232-240substrate
Binding site233Mn2+ 2 (UniProtKB | ChEBI)
Binding site236Mn2+ 1 (UniProtKB | ChEBI)
Binding site262-264substrate

GO annotations

AspectTerm
Cellular Componentchloroplast
Molecular Functionimidazoleglycerol-phosphate dehydratase activity
Molecular Functionmetal ion binding
Biological ProcessL-histidine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Imidazoleglycerol-phosphate dehydratase 1, chloroplastic
  • EC number
  • Short names
    IGPD 1
  • Alternative names
    • Protein HISTIDINE BIOSYNTHESIS 5A

Gene names

    • Name
      HISN5A
    • ORF names
      MCB17.17
    • Ordered locus names
      At3g22425

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    P34047
  • Secondary accessions
    • Q67YN9
    • Q67YZ9
    • Q8VYM1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, modified residue, chain.

Type
IDPosition(s)Description
Transit peptide1-62Chloroplast
Modified residue63N-acetylserine
ChainPRO_000015825363-270Imidazoleglycerol-phosphate dehydratase 1, chloroplastic

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region250-270Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing. Experimental confirmation may be lacking for some isoforms.

P34047-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    270
  • Mass (Da)
    29,225
  • Last updated
    1994-02-01 v1
  • MD5 Checksum
    138E051B3423C8329BBFF0F95A72DA96
MELSSASAILSHSSSAAQLLRPKLGFIDLLPRRAMIVSSPSSSLPRFLRMESQSQLRQSISCSASSSSSMALGRIGEVKRVTKETNVSVKINLDGTGVADSSSGIPFLDHMLDQLASHGLFDVHVRATGDVHIDDHHTNEDIALAIGTALLKALGERKGINRFGDFTAPLDEALIHVSLDLSGRPYLGYNLEIPTQRVGTYDTQLVEHFFQSLVNTSGMTLHIRQLAGENSHHIIEATFKAFARALRQATETDPRRGGTIPSSKGVLSRS

P34047-2

  • Name
    2
  • Note
    May be due to an intron retention.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 205-270: LVEHFFQSLVNTSGMTLHIRQLAGENSHHIIEATFKAFARALRQATETDPRRGGTIPSSKGVLSRS → VLSLLLELSSFGFICVIRCLVIIESVAKNCLTFRFVVGGALFPVVGEYFWYDSSHPAARW

Features

Showing features for sequence conflict, alternative sequence.

Type
IDPosition(s)Description
Sequence conflict201in Ref. 6; BAD44082
Alternative sequenceVSP_008895205-270in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U02689
EMBL· GenBank· DDBJ
AAA93196.1
EMBL· GenBank· DDBJ
mRNA
AB022215
EMBL· GenBank· DDBJ
BAB01781.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76636.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE76637.1
EMBL· GenBank· DDBJ
Genomic DNA
AK118815
EMBL· GenBank· DDBJ
BAC43405.1
EMBL· GenBank· DDBJ
mRNA
AY070442
EMBL· GenBank· DDBJ
AAL49845.1
EMBL· GenBank· DDBJ
mRNA
AK176319
EMBL· GenBank· DDBJ
BAD44082.1
EMBL· GenBank· DDBJ
mRNA
AK176429
EMBL· GenBank· DDBJ
BAD44192.1
EMBL· GenBank· DDBJ
mRNA
AY087948
EMBL· GenBank· DDBJ
AAM65496.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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