PYRB_LACLE
ID PYRB_LACLE Reviewed; 336 AA.
AC Q60252;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB;
OS Lactobacillus leichmannii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=28039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB
RC 7854 / 326 / F59;
RX PubMed=8725005; DOI=10.1016/0300-9084(96)81323-x;
RA Becker J., Brendel M.;
RT "Molecular cloning and characterization of the pyrB gene of Lactobacillus
RT leichmannii encoding aspartate transcarbamylase.";
RL Biochimie 78:3-13(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-336.
RC STRAIN=ATCC 4797 / DSM 20076 / BCRC 10699 / JCM 1148 / NBRC 3073 / NCIMB
RC 7854 / 326 / F59;
RX PubMed=8589056; DOI=10.1016/0300-9084(96)88135-1;
RA Schenk-Groeninger R., Becker J., Brendel M.;
RT "Cloning, sequencing, and characterizing the Lactobacillus leichmannii pyrC
RT gene encoding dihydroorotase.";
RL Biochimie 77:265-272(1995).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA59021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X84262; CAA59021.1; ALT_INIT; Genomic_DNA.
DR EMBL; X78999; CAA55634.1; -; Genomic_DNA.
DR PIR; T46956; T46956.
DR AlphaFoldDB; Q60252; -.
DR SMR; Q60252; -.
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: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..336
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113147"
SQ SEQUENCE 336 AA; 38135 MW; 24CFC94AE1F94FB9 CRC64;
MTTVSQNQVV VETEDKQDNL LRLPYFVSVE QLSADDVLHL LQRAQYFKNG GEVPALSRPI
FCTNMFFENS TRTHTSFEVA ERRLGLTVIP FDPSHSSVNK GENLYDTELT MASLGIELSV
IRHPENAYYN EIIRPKEGQH LQMGLVNAGD GSGQHPSQSM LDMMTIYNEF GHFDGLKIMI
VGDLTNSRVA RSNMEILNTL GAEVYFSGPE YWYNAEEFSK YGTYVKNIDD EIPELDVLML
LRVQHERHNG AEAKTEQLFD AKDYNAAYGL NQRRYDMLKD DAIIMHPGPI NRGVEWDGDL
VEAPKSRYAV QMHNGVFVRM AMIEAVLRGR KLGGLE
