ID PYRB_PSEFA Reviewed; 334 AA.
AC P56585; Q9F4I6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit {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};
OS Pseudomonas fluorescens biotype A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=32035;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WCS365;
RA Camacho-Carvajal M.M., Scheublin T., Lugtenberg B.J.J., Bloemberg G.V.;
RT "The regulatory protein PyrR of Pseudomona fluorescens is required for
RT competitive root colonization.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-19.
RC STRAIN=ATCC 13525 / DSM 50090 / JCM 5963 / NBRC 14160 / NCIMB 9046 / NCTC
RC 10038 / VKM B-894;
RX PubMed=8234318; DOI=10.1073/pnas.90.21.9818;
RA Bergh S.T., Evans D.R.;
RT "Subunit structure of a class A aspartate transcarbamoylase from
RT Pseudomonas fluorescens.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9818-9822(1993).
CC -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC committed step in the de novo pyrimidine nucleotide biosynthesis
CC pathway. {ECO:0000255|HAMAP-Rule:MF_00001}.
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 -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC organized as two trimers (C3), and six regulatory PyrI chains organized
CC as three dimers (R2). {ECO:0000255|HAMAP-Rule:MF_00001}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001,
CC ECO:0000305}.
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DR EMBL; AY007523; AAG15558.1; -; Genomic_DNA.
DR AlphaFoldDB; P56585; -.
DR SMR; P56585; -.
DR UniPathway; UPA00070; UER00116.
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:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00670; asp_carb_tr; 1.
DR PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..334
FT /note="Aspartate carbamoyltransferase catalytic subunit"
FT /id="PRO_0000113177"
FT BINDING 71
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 72
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 99
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 121
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 151
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 154
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 184
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 239
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 280
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 281
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT CONFLICT 6
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="D -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36463 MW; 18500AC9EBD1C659 CRC64;
MTPLETKRPL QLNDQGQLQH FLSLDGLRRE LLTEILDTAD SFLEVGARAV KKVPLLRGKT
VCNVFFENST RTRTTFELAA QRLSADVITL NVSTSSASKG ETLLDTLRNL EAMAADMFVV
RHGDSGAAHF IAEHVCPQVA IINGGDGRHA HPTQGMLDML TIRRHKGSFE NLSVAIVGDI
LHSRVARSNM LALKTLGCPD IRVIAPKTLL PIGVEQYGVK VYTDMTEGLK DVDVVIMLRL
QRERMTGGLL PSEGEFYRLF GLTTARLAGA KPDAIVMHPG PINRGVEIES AVADGPHSVI
LNQVTYGIAI RMAVLSMAMS GQTAQRQFDQ ENAQ
//
