PYRB_STRP2
ID PYRB_STRP2 Reviewed; 307 AA.
AC Q04K46;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Aspartate carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=SPD_1133;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00001};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00001}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR EMBL; CP000410; ABJ55115.1; -; Genomic_DNA.
DR RefSeq; WP_001293822.1; NC_008533.2.
DR AlphaFoldDB; Q04K46; -.
DR SMR; Q04K46; -.
DR STRING; 373153.SPD_1133; -.
DR EnsemblBacteria; ABJ55115; ABJ55115; SPD_1133.
DR GeneID; 60233690; -.
DR KEGG; spd:SPD_1133; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_1_9; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR BioCyc; SPNE373153:G1G6V-1224-MON; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000001452; 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; Transferase.
FT CHAIN 1..307
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000321162"
SQ SEQUENCE 307 AA; 34706 MW; 34208B4A16839663 CRC64;
MSENQQALNH VVSMEDLTVD QVMKLIKRGI EFKNGAQIPY EDHPIVSNLF FEDSTRTHKS
FEVAEIKLGL ERLDFDVKTS SVNKGETLYD TILTLSALGV DVCVIRHPEV DYYRELIASP
TITTSIINGG DGSGQHPSQS LLDLMTIYEE FGHFEGLKVA IAGDLDHSRV AKSNMQILKR
LGSELFFAGP EEWRSQEFAD YGKFVTIDEI IDQVDVMMFL RVQHERHDSG AVFSKEDYHA
QHGLTQERYD RLKETAILMH PAPINRDVEI ADHLVEAPKS RIVQQMTNGV FVRMAILESV
LASRNAN
