O27199 · PYRC_METTH

Function

function

Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site55Zn2+ 1 (UniProtKB | ChEBI)
Binding site57Zn2+ 1 (UniProtKB | ChEBI)
Binding site57-59substrate
Binding site89substrate
Binding site139Zn2+ 1 (UniProtKB | ChEBI)
Binding site139Zn2+ 2 (UniProtKB | ChEBI)
Binding site169Zn2+ 2 (UniProtKB | ChEBI)
Binding site223Zn2+ 2 (UniProtKB | ChEBI)
Active site290
Binding site290Zn2+ 1 (UniProtKB | ChEBI)
Binding site294substrate
Binding site308-309substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionallantoinase activity
Molecular Functiondihydroorotase activity
Molecular Functionzinc ion binding
Biological Process'de novo' UMP biosynthetic process
Biological Processpurine nucleobase catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydroorotase
  • EC number
  • Short names
    DHOase

Gene names

    • Name
      pyrC
    • Ordered locus names
      MTH_1127

Organism names

Accessions

  • Primary accession
    O27199
  • Secondary accessions
    • Q50488

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001472731-431Dihydroorotase
Modified residue139N6-carboxylysine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    47,946
  • Last updated
    2003-02-01 v2
  • Checksum
    FFE05E8B923ADAF9
MFDLSLENCRVDRDLTVNIGVDDGKIVQISRGRIDASEKIDLKGYFVLPGLIDAHVHFRDPGLEYKEDFRTGSMAAAHGGFSTVLDMPNTVPPADNAAEFERKIRIGERKSVVDFGLHAGFRSVSDVKGILRFMPASFKVFMDLTGISTVDGLFRELKDLSAPVPVTVHCENRDVVMKSMKELKDRSDPSAYALARPPLAEEVSVAEVLALSIHHEHPVHICHLSTVKALQLVEPFREYVTCEVTPHHLLLDSGAFRRFGTMVKTNPPLRPPESRIYPEFLDRINIIGTDHAPHGIEEKRKGIWDAPPGIPNLEVVLKLLLTLVSKGRMSLSTIRRMLAEEPARIFGLRSKGRIAEGMDADFTVIDLKETGRIRSDEFYSKAHYTPFEGFSYTGGPVMTIVRGRAVMRDGEVLEGNGRYIPAEHDGKHGSA

Sequence caution

The sequence AAB85616.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict1-2in Ref. 2; AAA73440
Sequence conflict44in Ref. 2; AAA73440
Sequence conflict133in Ref. 2; AAA73440
Sequence conflict195-201in Ref. 2; AAA73440
Sequence conflict242-243in Ref. 2; AAA73440
Sequence conflict343in Ref. 2; AAA73440
Sequence conflict395-404in Ref. 2; AAA73440

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000666
EMBL· GenBank· DDBJ
AAB85616.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
U09990
EMBL· GenBank· DDBJ
AAA73440.1
EMBL· GenBank· DDBJ
Genomic DNA

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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