ID PYRB2_SHEHH Reviewed; 310 AA. AC B0TST3; 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 2; DE EC=2.1.3.2; DE AltName: Full=Aspartate transcarbamylase 2; DE Short=ATCase 2; GN Name=pyrB2; OrderedLocusNames=Shal_0683; 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; ABZ75258.1; -; Genomic_DNA. DR RefSeq; YP_001672917.1; -. DR GeneID; 5906168; -. DR GenomeReviews; CP000931_GR; Shal_0683. DR KEGG; shl:Shal_0683; -. DR OMA; B0TST3; LYTIREN. 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 2. FT /FTId=PRO_0000334594. SQ SEQUENCE 310 AA; 34729 MW; 91D62C9AF791552C CRC64; MTNTIYNKNI ISISDLSRSE LELIVATANE LKQNPRPELL KNKVVASCFF EASTRTRLSF ETAVQRLGGS IIGFPDGGNT SLGKKGETLA DSVQVISSYC DAFFIRHNQE GAARLASEFS SVPVINGGDG SNQHPTQTLL DLFSIYETQG TLEKLQVAFV GDLKYGRTVH SLTQALSLFD CEFHFVAPKA LLMPDYIIDE LKEKGCKYTL HETLDEIMDS LDILYMTRVQ KERFDETEYQ HLKSSFILTA NMLKGVKDNL KILHPLPRVD EITTDVDSTP YAYYFQQAKN GVYARQALLT LVLTNEFGDL //