PYRB_BIFLO
ID PYRB_BIFLO Reviewed; 320 AA.
AC Q8G655;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Aspartate carbamoyltransferase {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=BL0794;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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 -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN24609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014295; AAN24609.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_695973.1; NC_004307.2.
DR RefSeq; WP_007054218.1; NC_004307.2.
DR AlphaFoldDB; Q8G655; -.
DR SMR; Q8G655; -.
DR STRING; 206672.BL0794; -.
DR EnsemblBacteria; AAN24609; AAN24609; BL0794.
DR GeneID; 66505152; -.
DR KEGG; blo:BL0794; -.
DR PATRIC; fig|206672.9.peg.495; -.
DR HOGENOM; CLU_043846_1_2_11; -.
DR OMA; FPTEREY; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000000439; 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..320
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113103"
SQ SEQUENCE 320 AA; 35264 MW; AEC328C7F9EFA0DC CRC64;
MVGKSVVTLD GLSTNQILDL LHKAEYIDSH RKEIAHTCDG RVLATLFYEP STRTRLSFET
AMLRLGGKVI GFAGAQLASV TKGESIADTL KTVSNYVDVV AIRHPKEGAA LVASRAASVP
VINAGDGGHM HPTQTLADLA TLQSRFGRIT DLTVGLCGDL TFGRTVHSLI ETLCRFGNVR
FVLISPDELK TPQYVIDRIN ATDSCSYVEV RDLASVIGDL DVLYMTRVQK ERFFNEDDYL
RLRDTYILDE EKLQLAKPSM AVLHPLPRVN EIAVDVDDDP RAAYFEQVKN GMLVRMALES
TVVGDELPGY EPLNPKEVQA