SPM_004795
  | Uniprot: A0A037UN41
Description: ornithine carbamoyltransferase EC number: 2.1.3.3 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|SAAS:SAAS00392956}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00341537}. Pathway: Active site: Binding site: BINDING 108 108 Carbamoyl phosphate. {ECO:0000256|HAMAP-Rule:MF_01109}.; BINDING 135 135 Carbamoyl phosphate. {ECO:0000256|HAMAP-Rule:MF_01109}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: SITE 32 32 Important for structural integrity. {ECO:0000256|HAMAP-Rule:MF_01109}.; SITE 148 148 Important for structural integrity. {ECO:0000256|HAMAP-Rule:MF_01109}. Gene names (primary): Gene names (synonym): Mass: 37,267 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; amino acid binding [GO:0016597]; ornithine carbamoyltransferase activity [GO:0004585] Gene ontology IDs: GO:0004585; GO:0005737; GO:0016597 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00578869}. Protein families: ATCase/OTCase family Coiled coil: Domain [FT]: DOMAIN 8 148 OTCace_N. {ECO:0000259|Pfam:PF02729}.; DOMAIN 156 330 OTCace. {ECO:0000259|Pfam:PF00185}. Motif: Region: REGION 57 61 Carbamoyl phosphate binding. {ECO:0000256|HAMAP-Rule:MF_01109}.; REGION 273 276 Ornithine binding. {ECO:0000256|HAMAP-Rule:MF_01109}. EMBL: AGBZ02000004 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92058 UniPathway: CDD: Gene3D: HAMAP: 3.40.50.1370 InterPro: MF_01109 PANTHER: IPR006132;IPR006130;IPR006131;IPR002292;IPR024904 PIRSF: PRINTS: PROSITE: PR00100;PR00102 Pfam: PS00097 ProDom: PF00185;PF02729 SMART: SUPFAM: TIGRFAMs: SSF53671 |
28607-29612(+) >nucleotide sequence ATTTACTATTTATTAGATTTAGCAAGACAATTAAAAGAAGCAAAATATGCTGGAACTGAA CAAAAACCATTAGCTGGAAAATCTGTTGCTTTATTATTTGCAAAAGATTCAACACGAACA AGATGTGCTTTTGAAGTAGGAGCATTTGATTTAGGTATGCACCCTGTTTATTTAGGACCA AGTGGTAGTCAAATGGGGAAAAAAGAATCAATTGAAGATACTGCAAAAGTGTTAGGGAGA ATGTTTGATGGAATTCAATTTCGTGGATTTAAACAAACTGATGTTGAAGCATTAGCAAAA TATTCAGGTGTTCCAGTATGAAATGGATTAACTGATGAATTTCACCCAACCCAAATGTTA GCTGATATTTTAACATTGCAAGAAGAAAAAGGACAACGCAATATGAAAGGGCTAAAATTT GTTTATTTTGGTGATTCTCGTTTTAATATGGCAAATAGTTATATGGTTGTTAGTGCTAAA TTAGGAATGCATTTTGTTGCTTGTGCGCCAAAAGACTTATGACCAAATGCAGAATTATTG AAAAAAGTACAAGCAATTGCGAAAGAACATGGTGGTTCAATTACGTTAACTGAAGACCAC AAAACAGCAGCAAAAGATGCTGATGCAATTGCCACTGATGTTTGAGTGTCAATGGGAGAA GATCCTGCCGTTTGAGGAAAAAGAATTAAGGATTTAACACCATATCAAGTAACAATGGAA AAAATGAAACAAGCAAAAGAAGATGCTATCTTTTTACATTGTTTACCAAGTTTCCATGAT GGGAATACAGATACTGCACAACAAGTGATTAAACAATTTGGTGGAACTGGAGAATTAGAA GTTACTGATGAAGTTTTCCAATCAAAATATTCACGTGTTTTTGAAGAAGCAGAAAATCGT TTACATACTATTAAAGCAGTAATGCTAGCAACAATTCGTGGCTAG >protein sequence RCAFEVGAFDLGMHPVYLGPSGSQMGKKESIEDTAKVLGRMFDGIQFRGFKQTDVEALAK YSGVPVWNGLTDEFHPTQMLADILTLQEEKGQRNMKGLKFVYFGDSRFNMANSYMVVSAK LGMHFVACAPKDLWPNAELLKKVQAIAKEHGGSITLTEDHKTAAKDADAIATDVWVSMGE DPAVWGKRIKDLTPYQVTMEKMKQAKEDAIFLHCLPSFHDGNTDTAQQVIKQFGGTGELE VTDEVFQSKYSRVFEEAENRLHTIKAVMLATIRG |
© Fisunov Lab of Proteomics, 2016.