ID PYRB1_SHEHH Reviewed; 310 AA. AC B0TSQ4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 16-JUN-2009, entry version 11. DE RecName: Full=Aspartate carbamoyltransferase 1; DE EC=2.1.3.2; DE AltName: Full=Aspartate transcarbamylase 1; DE Short=ATCase 1; GN Name=pyrB1; OrderedLocusNames=Shal_0654; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from HCO(3)(-): step 2/6. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000931; ABZ75229.1; -; Genomic_DNA. DR RefSeq; YP_001672888.1; -. DR GeneID; 5906714; -. DR GenomeReviews; CP000931_GR; Shal_0654. DR KEGG; shl:Shal_0654; -. DR OMA; B0TSQ4; RFDESEY. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00001; -; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P_bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn_bd. DR InterPro; IPR002082; Aspartate_carbamoyltransf_euk. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00101; ATCASE. DR TIGRFAMs; TIGR00670; asp_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Complete proteome; Pyrimidine biosynthesis; Transferase. FT CHAIN 1 310 Aspartate carbamoyltransferase 1. FT /FTId=PRO_0000334593. SQ SEQUENCE 310 AA; 34626 MW; 8E7CDFB017B9FB28 CRC64; MSNPLYNKNI ISITDLSRAE LELIVSTANE LKQHPRPDLL KNKVIASCFF EASTRTRLSF ETAVQRLGGS VIGFPDSGNT SLGKKGETLA DSVQVISSYS DAFFMRHNQE GAARLASEFS SVPVINGGDG SNQHPTQTLL DLFSIYETQG TLDKLQVAFV GDLKYGRTVH SLTQALSLFD CEFHFVAPPA LSMPEYIIDE LKEKGCTFTQ YDSLDGVLSK LDILYMTRVQ KERFDETEYQ HMKSSFILTA QMFEGVKDNL KVLHPLPRVD EITTDVDSTP YAYYFQQAKN GVYARQALLA LVLTNEFGDK //