PYRB_PROM9
ID PYRB_PROM9 Reviewed; 339 AA.
AC Q31CU8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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};
GN OrderedLocusNames=PMT9312_0235;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000111; ABB49297.1; -; Genomic_DNA.
DR RefSeq; WP_011375801.1; NC_007577.1.
DR AlphaFoldDB; Q31CU8; -.
DR SMR; Q31CU8; -.
DR STRING; 74546.PMT9312_0235; -.
DR EnsemblBacteria; ABB49297; ABB49297; PMT9312_0235.
DR KEGG; pmi:PMT9312_0235; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_3; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 1844275at2; -.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000002715; 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; Transferase.
FT CHAIN 1..339
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000321136"
SQ SEQUENCE 339 AA; 37524 MW; D8EED0A8FFA28ABE CRC64;
MQTIWPHKHI HTLANFSIQD YKSVFELAHR FDVLKNAGTK KIPALQGTLV TSLFFEASTR
TKNSFELAAK RLSADVQTFA PSSSSLTKGE TIIDTALTYS AMGADTLVIR HSSSYITFEI
AKKLDAINAK TSVLNAGDGL HSHPSQGLLD IYTLIKFFSK KSLSPDVLNS KKILIIGDVN
HSRVARSNLW ALSAFGADII LCGPKTLIPD EFINFLKTPA PKQKEDPVKS RGSITISRSL
EESIKIADAI IVLRLQKERM MENLLSSIDS YSLDYGLTPE KLSLNSKEIP ILHPGPINRG
IEITSKVVDE YPNCLINNQV ANGIPIRMAL LYLLQKYNK