ID   PYRB2_PEA               Reviewed;         385 AA.
AC   Q43087;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Aspartate carbamoyltransferase 2, chloroplastic;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase 2;
DE            Short=ATCase 2;
DE   Flags: Precursor;
GN   Name=PYRB2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wando; TISSUE=Leaf;
RX   PubMed=8029359; DOI=10.1104/pp.105.1.377;
RA   Williamson C.L., Slocum R.D.;
RT   "Molecular cloning and characterization of the pyrB1 and pyrB2 genes
RT   encoding aspartate transcarbamoylase in pea (Pisum sativum L.).";
RL   Plant Physiol. 105:377-384(1994).
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   -!- ACTIVITY REGULATION: Allosterically regulated by UMP.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; L15798; AAA62444.1; -; mRNA.
DR   PIR; T10181; T10181.
DR   AlphaFoldDB; Q43087; -.
DR   SMR; Q43087; -.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate 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   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   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   2: Evidence at transcript level;
KW   Allosteric enzyme; Chloroplast; Plastid; Pyrimidine biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..63
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           64..385
FT                   /note="Aspartate carbamoyltransferase 2, chloroplastic"
FT                   /id="PRO_0000020350"
SQ   SEQUENCE   385 AA;  43745 MW;  1EC989FF0845EEB9 CRC64;
     MTASSSLFSC SMHMEVLTPK ISKWPKNFVS CHSKISYVET NYLKSTCYPI SRFFCINNLK
     KTRQRDGIHC FSEGQKFQLD DVVEAQQFDR DILNAIFEVA RDMEKIERNS PESQILKGYL
     MATLFYEPST RTRLSFESAM RRLGGEVLTT ENAREFSSAA KGETLEDTIR TVEGYSDLIV
     LRHFESGAAR RAATIAGIPI VNAGDGPGQH PSQALLDVYT IEREIGKLDG IKVGLVGDLA
     NGRTVRSLTY LLAKYKDVKI YFVSPEVVKM KDDIKDYLTS KGVDWEESSD LVEVASECDV
     VYQTRIQKER FGERLDLYEK ARGKFIVNQN ILNAMQRHAV IMHPLPRLDE ITVDVDADPR
     AAYFRQAKYG LYIRMALLKL LLVGW