PYRB_BUCAI
ID PYRB_BUCAI Reviewed; 310 AA.
AC P57450;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=BU369;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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 -!- SUBUNIT: Contains six catalytic and six regulatory chains.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; BA000003; BAB13073.1; -; Genomic_DNA.
DR RefSeq; NP_240187.1; NC_002528.1.
DR RefSeq; WP_010896091.1; NC_002528.1.
DR AlphaFoldDB; P57450; -.
DR SMR; P57450; -.
DR STRING; 107806.10039039; -.
DR EnsemblBacteria; BAB13073; BAB13073; BAB13073.
DR KEGG; buc:BU369; -.
DR PATRIC; fig|107806.10.peg.383; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_1_2_6; -.
DR OMA; GDGPNEH; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000001806; 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 catalytic subunit"
FT /id="PRO_0000113110"
SQ SEQUENCE 310 AA; 35553 MW; B02131513FA8D388 CRC64;
MRNSLYKKNI ISINDLQRNE LELVLNKSAM LKKTPQPNLL KNKVIASCFF EASTRTRLSF
ETAIYRLGAS IVGFSDGNNI SLEKKGETLT DTISVISSYV DAIIIRHPQE GSARLAAEFS
NKKPIFNAGD GANQHPTQTL LDLFTIQETQ NRLTQLNIAI VGDLKYGRTV HSLTQALAKF
KHNKFYFISP DALKMPNYIN NMLDKKEIYW KRHNNIEEII SEIDILYMTR IQKERLDSTE
YANAKSKFVL RAAILKNARN NMKILHPLPR IDEIDRDVDY TPYAWYFKQA ANGIYARQAI
LSLVLIEKHL