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
ATGATTTATACTTTTACTAACGCCAACGTTTATTTACCAACTGGTTTCAAACAAACAAAT
ATTACGATTAAAGGAAATAAAATTATGCGCATTGGTCCAACTATTTTGGGAACAGAAATT
AAGTTGTCAGCAAATTGTCTCATTGTTCCTAGTTTTATTGATTTACATGCTCATTTTCGT
GAACCTGGTCAAACAACAAAAGAAGATTTAATAACAGGAGCAAATAGTGGTTTATATGGT
GGTTATCAGACAGTATGTGTGATGGCGAATACAAAGCCAGCAATTGATAATATTGCTGTT
TTAGCACCATTATTAGTTAAAGCAGCGAAATTACCAATTAATGTTCAATTTTTTGGGGCA
ATTACAAAACAATTAGCTGGTCAAGAATTGGTTGATTTTGCAAAAATCAAGGATGATGTT
ATTGGTTTTAGCGATGATGGGGTTTATTTAGCAAATCAATCTTTATTAATTAAGGCTTTA
GAATATGGTCAAGCAAACCAAAAACTTATTTCATTGCACGTTGATAATCGTCAAAATATA
AATGAACAAACAGTTGTTTTGCAGCACCAAATTGCCCAAAAGTTTGGATTAATTGGTGTT
GATGATAATTATGAAGCCGAACCATTACACAATGATCTAAAACTTGTTAATAAACAGCAA
TTACCTTATCATGTATGTCATGTTTCAACAGCTAAAAGTATTGCTTTAATTCGCAAAGGT
AAAAAAATTAATCCATTTTTAACTTGTGAAGTCACTCCGCATCATTTAACATTATCAGTT
GATGATATTACAACAAATGATGGGAATTATTTAATGAATCCACCCTTAAATAGGATAAAT
GATCAATTAAGTTTAATAAAAGCTTTAAATGAGGGCATAATTGATGTTATTGCAACTGAT
CATGCTCCACACCAAACAAGGGAGAAAGGTGAGTTTGCAAATAGTGCTATGGGAATTATA
GGTTTACAATTAACATTTCCATTATTATATACAAAGTTAGTGCTTCCACAACAAGTGTCA
TTATCAACTATTATTAATGCTTTAACAGTTAATCCACAGCAATTAATTAAACATCATAAT
GTTCAATTAGAGGTTAATAATTATGCTAATTTTACAGTGATTGATTTATCGTTAAGCAAA
GTTGTGACCCCAGAGTTATTACAATCAAAATCAATAAATACTCCATTTTTAGGAGAAAAA
TTAACGGGATGACCCATTATTAATGTTTATCAAGGTCAAATATATCATTTAAAGGAGGAA
TAA


>protein sequence
MIYTFTNANVYLPTGFKQTNITIKGNKIMRIGPTILGTEIKLSANCLIVPSFIDLHAHFR
EPGQTTKEDLITGANSGLYGGYQTVCVMANTKPAIDNIAVLAPLLVKAAKLPINVQFFGA
ITKQLAGQELVDFAKIKDDVIGFSDDGVYLANQSLLIKALEYGQANQKLISLHVDNRQNI
NEQTVVLQHQIAQKFGLIGVDDNYEAEPLHNDLKLVNKQQLPYHVCHVSTAKSIALIRKG
KKINPFLTCEVTPHHLTLSVDDITTNDGNYLMNPPLNRINDQLSLIKALNEGIIDVIATD
HAPHQTREKGEFANSAMGIIGLQLTFPLLYTKLVLPQQVSLSTIINALTVNPQQLIKHHN
VQLEVNNYANFTVIDLSLSKVVTPELLQSKSINTPFLGEKLTGWPIINVYQGQIYHLKEE






















© Fisunov Lab of Proteomics, 2016.