ID PYRB_BIFLO Reviewed; 320 AA. AC Q8G655; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 03-MAR-2009, entry version 42. DE RecName: Full=Aspartate carbamoyltransferase; DE EC=2.1.3.2; DE AltName: Full=Aspartate transcarbamylase; DE Short=ATCase; GN Name=pyrB; OrderedLocusNames=BL0794; OS Bifidobacterium longum. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=216816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705; RX MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599; RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., RA Pridmore R.D., Arigoni F.; RT "The genome sequence of Bifidobacterium longum reflects its adaptation RT to the human gastrointestinal tract."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002). 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; AE014295; AAN24609.1; ALT_INIT; Genomic_DNA. DR RefSeq; NP_695973.1; -. DR HSSP; P77918; 1ML4. DR GeneID; 1022093; -. DR GenomeReviews; AE014295_GR; BL0794. DR KEGG; blo:BL0794; -. DR HOGENOM; Q8G655; -. DR BioCyc; BLON206672:BL0794-MON; -. DR BRENDA; 2.1.3.2; 39917. 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 1 320 Aspartate carbamoyltransferase. FT /FTId=PRO_0000113103. SQ SEQUENCE 320 AA; 35264 MW; AEC328C7F9EFA0DC CRC64; MVGKSVVTLD GLSTNQILDL LHKAEYIDSH RKEIAHTCDG RVLATLFYEP STRTRLSFET AMLRLGGKVI GFAGAQLASV TKGESIADTL KTVSNYVDVV AIRHPKEGAA LVASRAASVP VINAGDGGHM HPTQTLADLA TLQSRFGRIT DLTVGLCGDL TFGRTVHSLI ETLCRFGNVR FVLISPDELK TPQYVIDRIN ATDSCSYVEV RDLASVIGDL DVLYMTRVQK ERFFNEDDYL RLRDTYILDE EKLQLAKPSM AVLHPLPRVN EIAVDVDDDP RAAYFEQVKN GMLVRMALES TVVGDELPGY EPLNPKEVQA //