PYRB_LACLA
ID PYRB_LACLA Reviewed; 310 AA.
AC Q9CF79;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=LL1602; ORFNames=L45002;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005176; AAK05700.1; -; Genomic_DNA.
DR PIR; B86825; B86825.
DR RefSeq; NP_267758.1; NC_002662.1.
DR RefSeq; WP_003129382.1; NC_002662.1.
DR AlphaFoldDB; Q9CF79; -.
DR SMR; Q9CF79; -.
DR STRING; 272623.L45002; -.
DR PaxDb; Q9CF79; -.
DR EnsemblBacteria; AAK05700; AAK05700; L45002.
DR KEGG; lla:L45002; -.
DR PATRIC; fig|272623.7.peg.1723; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_1_9; -.
DR OMA; FPTEREY; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113145"
SQ SEQUENCE 310 AA; 34558 MW; EEDE6B8EC6F00B94 CRC64;
MSVKNGLVQL ENLTSMEKLS VDEVMGLIKR ASAFKAGTAE FDLEKQTFAS NLFFENSTRT
HHSFHIAERK LGLDVLEFDA QASSISKGET LYDTVLTLDA LGVDICVIRS GVEHYYEELV
NSDNIHCAIV NGGDGSGQHP SQCLLDLMTI YEEFGKFEGL KIAISGDLTH SRVAKSNMMM
LQKLGARLYF TGPAAWYSEE FDDYGHYANL DRILPELDVH MLLRVQHERH DSGESFSKEG
YHNHFGLTEE RAKMLKPTAI IMHPAPVNRG VEIADSLVES PQSRIVQQMS NGVYTRMAIL
EAILAGKKAK