SPM_003330
  | Uniprot: A0A037UR84
Description: dihydroorotase EC number: 3.5.2.3 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate. {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00329237}. Cofactor: Enzyme regulation: Function [CC]: Pathway: PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00393543}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 56 56 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 58 58 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 137 137 Zinc 1; via carbamate group. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 137 137 Zinc 2; via carbamate group. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 173 173 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 227 227 Zinc 2. {ECO:0000256|HAMAP-Rule:MF_00220}.; METAL 300 300 Zinc 1. {ECO:0000256|HAMAP-Rule:MF_00220}. Nucleotide binding: Site: Gene names (primary): pyrC Gene names (synonym): Mass: 46,481 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00220, ECO:0000256|SAAS:SAAS00329235}. Gene ontology (GO): dihydroorotase activity [GO:0004151]; zinc ion binding [GO:0008270]; 'de novo' UMP biosynthetic process [GO:0044205] Gene ontology IDs: GO:0004151; GO:0008270; GO:0044205 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. {ECO:0000256|SAAS:SAAS00571224}. Protein families: DHOase family, Type 2 subfamily Coiled coil: Domain [FT]: DOMAIN 48 409 Amidohydro-rel. {ECO:0000259|Pfam:PF01979}. Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI93011 UniPathway: CDD: Gene3D: HAMAP: 2.30.40.10 InterPro: MF_00220_B PANTHER: IPR006680;IPR004722;IPR002195;IPR011059;IPR032466 PIRSF: PRINTS: PROSITE: Pfam: PS00482;PS00483 ProDom: PF01979 SMART: SUPFAM: TIGRFAMs: SSF51338;SSF51556 |
627013-628276(+) >nucleotide sequence ATTACGATTAAAGGAAATAAAATTATGCGCATTGGTCCAACTATTTTGGGAACAGAAATT AAGTTGTCAGCAAATTGTCTCATTGTTCCTAGTTTTATTGATTTACATGCTCATTTTCGT GAACCTGGTCAAACAACAAAAGAAGATTTAATAACAGGAGCAAATAGTGGTTTATATGGT GGTTATCAGACAGTATGTGTGATGGCGAATACAAAGCCAGCAATTGATAATATTGCTGTT TTAGCACCATTATTAGTTAAAGCAGCGAAATTACCAATTAATGTTCAATTTTTTGGGGCA ATTACAAAACAATTAGCTGGTCAAGAATTGGTTGATTTTGCAAAAATCAAGGATGATGTT ATTGGTTTTAGCGATGATGGGGTTTATTTAGCAAATCAATCTTTATTAATTAAGGCTTTA GAATATGGTCAAGCAAACCAAAAACTTATTTCATTGCACGTTGATAATCGTCAAAATATA AATGAACAAACAGTTGTTTTGCAGCACCAAATTGCCCAAAAGTTTGGATTAATTGGTGTT GATGATAATTATGAAGCCGAACCATTACACAATGATCTAAAACTTGTTAATAAACAGCAA TTACCTTATCATGTATGTCATGTTTCAACAGCTAAAAGTATTGCTTTAATTCGCAAAGGT AAAAAAATTAATCCATTTTTAACTTGTGAAGTCACTCCGCATCATTTAACATTATCAGTT GATGATATTACAACAAATGATGGGAATTATTTAATGAATCCACCCTTAAATAGGATAAAT GATCAATTAAGTTTAATAAAAGCTTTAAATGAGGGCATAATTGATGTTATTGCAACTGAT CATGCTCCACACCAAACAAGGGAGAAAGGTGAGTTTGCAAATAGTGCTATGGGAATTATA GGTTTACAATTAACATTTCCATTATTATATACAAAGTTAGTGCTTCCACAACAAGTGTCA TTATCAACTATTATTAATGCTTTAACAGTTAATCCACAGCAATTAATTAAACATCATAAT GTTCAATTAGAGGTTAATAATTATGCTAATTTTACAGTGATTGATTTATCGTTAAGCAAA GTTGTGACCCCAGAGTTATTACAATCAAAATCAATAAATACTCCATTTTTAGGAGAAAAA TTAACGGGATGACCCATTATTAATGTTTATCAAGGTCAAATATATCATTTAAAGGAGGAA TAA >protein sequence EPGQTTKEDLITGANSGLYGGYQTVCVMANTKPAIDNIAVLAPLLVKAAKLPINVQFFGA ITKQLAGQELVDFAKIKDDVIGFSDDGVYLANQSLLIKALEYGQANQKLISLHVDNRQNI NEQTVVLQHQIAQKFGLIGVDDNYEAEPLHNDLKLVNKQQLPYHVCHVSTAKSIALIRKG KKINPFLTCEVTPHHLTLSVDDITTNDGNYLMNPPLNRINDQLSLIKALNEGIIDVIATD HAPHQTREKGEFANSAMGIIGLQLTFPLLYTKLVLPQQVSLSTIINALTVNPQQLIKHHN VQLEVNNYANFTVIDLSLSKVVTPELLQSKSINTPFLGEKLTGWPIINVYQGQIYHLKEE |
© Fisunov Lab of Proteomics, 2016.