ID PYRB_CLAMS Reviewed; 318 AA.
AC B0REW3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
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}; OrderedLocusNames=CMS2033;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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}.
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DR EMBL; AM849034; CAQ02129.1; -; Genomic_DNA.
DR RefSeq; WP_012299355.1; NZ_MZMN01000003.1.
DR AlphaFoldDB; B0REW3; -.
DR SMR; B0REW3; -.
DR STRING; 31964.CMS2033; -.
DR KEGG; cms:CMS2033; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_11; -.
DR OrthoDB; 9774690at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000001318; 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: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 3: Inferred from homology;
KW Pyrimidine biosynthesis; Transferase.
FT CHAIN 1..318
FT /note="Aspartate carbamoyltransferase catalytic subunit"
FT /id="PRO_1000073723"
FT BINDING 54
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 55
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 82
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 104
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 134
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 137
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 174
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 230
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 271
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 272
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
SQ SEQUENCE 318 AA; 34070 MW; 8EDFF3BF2BE7A665 CRC64;
MRHLLSTRDL SRDEAVRILD VAEDMADVGT REIKKTPALR GRTVVNLFFE DSTRTRISFE
AAAKRLSADV INFSAKGSSV SKGESLKDTA QTLQAMGADG VVVRHPSSGA PHTLAGSGWI
DAGIVNAGDG THEHPTQALL DAFTIRRRLH GSAARGKGLD GTRVVIVGDV LHSRVARSNA
WLLTTLGAEV TLVAPPTLVP VGVGSWPVTV RYDLDAALRD GAPDAVMMLR IQAERMRAAF
FPNPREYARI WGLDDARLAL LGPDTIVMHP GPMNRGLEIS AAAADSERST VREQVANGVS
VRMAVLYLLL SGDGKADR
//
