ID   PYRB_BARHE              Reviewed;         321 AA.
AC   Q6G3F3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=BH08200;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27619.1; -; Genomic_DNA.
DR   RefSeq; YP_033626.1; -.
DR   GeneID; 2864779; -.
DR   GenomeReviews; BX897699_GR; BH08200.
DR   KEGG; bhe:BH08200; -.
DR   NMPDR; fig|283166.1.peg.754; -.
DR   HOGENOM; Q6G3F3; -.
DR   OMA; Q6G3F3; RTVVNLF.
DR   BioCyc; BHEN283166:BH08200-MON; -.
DR   BRENDA; 2.1.3.2; 277357.
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    321       Aspartate carbamoyltransferase.
FT                                /FTId=PRO_0000113101.
SQ   SEQUENCE   321 AA;  34848 MW;  7338C1CBBC35FDAB CRC64;
     MTQNTFFSLF PHQHLLGIKD LSVQDLTILL DRANANVPFL KKSDKKQSIL HGRTQINLFF
     EASTRTQSSF ELAGKRLGAD VMSMAIGNSS VKKGETLVDT ATTLNAMKPD ILVIRHSCAG
     AAALLAQKVD CCVINAGDGA HEHPTQALLD ALTIQRTKGR IEGLTVAICG DILHSRVARS
     NILSLNALGA CVRVIAPSTL LPASIADMSV EVYNTMKEGL KGADVIMMLR LQQERMTGSF
     IPSIREYFHY FGLHKENLAY AKSDCIILHP GPINRGVEIA SDIADGPQSM IHTQVEMGIA
     VRMAVMEALL DSRLKASGEK K
//