ID F0G152_9BURK Unreviewed; 431 AA.
AC F0G152;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=aspartate carbamoyltransferase {ECO:0000256|ARBA:ARBA00013008};
DE EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
GN ORFNames=B1M_09737 {ECO:0000313|EMBL:EGD04772.1};
OS Burkholderia sp. TJI49.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD04772.1, ECO:0000313|Proteomes:UP000003049};
RN [1] {ECO:0000313|EMBL:EGD04772.1, ECO:0000313|Proteomes:UP000003049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD04772.1,
RC ECO:0000313|Proteomes:UP000003049};
RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT isolated from dieback affected mango orchards.";
RL World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00001363};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004852}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000256|ARBA:ARBA00008896}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD04772.1}.
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DR EMBL; AEXE01000505; EGD04772.1; -; Genomic_DNA.
DR AlphaFoldDB; F0G152; -.
DR PATRIC; fig|987057.7.peg.1585; -.
DR BioCyc; BSP987057:G10O5-1193-MONOMER; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000003049; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
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 CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
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 InterPro; IPR001387; Cro/C1-type_HTH.
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 {ECO:0000256|ARBA:ARBA00022975};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT DOMAIN 92..231
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 243..397
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
SQ SEQUENCE 431 AA; 47771 MW; 5C35F7E8394F22E1 CRC64;
MTVPQQAFLR DAMRRLNMTR EAFASRIGVS RRALDTWLLP DDSQESRGMP EIVERFVSEI
VERSAPEGGD YTQRVDNQGL AKQFLFEGKP QLISVDQFSR ESVEALFRVA DVMQPIARRH
KISRVLEGAV LGNLFFEAST RTRVSFGAAF CRLGGSVCDT TGFTFSSMAK GESIYDTSRV
MAGYVDALVI RHPEKGSVAE FARATNLPVI NGGDGPGEHP SQALLDLYTI QREFSRLGKI
VDGAHIALVG DLKYGRTVHS LVKLLALYRG LKFTLVSPPT LEMPAYIIDQ IATNGHVIEQ
TNDLAAGLRG ADVVYATRIQ KERFTDESFE GYTPDFQINQ ALVDTVCKPD TLIMHPLPRD
SRPGANDLST DLNRDPRLAI FRQTDNGIPV RMAIFAVLLG VENLVQHSMR DATWRPPAYL
GPEDAVFHGI D
//
