ID   OTC_PEA                 Reviewed;         375 AA.
AC   Q43814;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Ornithine carbamoyltransferase, chloroplastic;
DE            EC=2.1.3.3;
DE   AltName: Full=Ornithine transcarbamylase;
DE            Short=OTCase;
DE   Flags: Precursor;
GN   Name=ARGF;
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=8914525; DOI=10.1007/bf00040826;
RA   Williamson C.L., Lake M.R., Slocum R.D.;
RT   "Isolation and characterization of a cDNA encoding a pea ornithine
RT   transcarbamoylase (argF) and comparison with other transcarbamoylases.";
RL   Plant Mol. Biol. 31:1087-1092(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3;
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; U13684; AAA74997.1; -; mRNA.
DR   PIR; T06436; T06436.
DR   AlphaFoldDB; Q43814; -.
DR   SMR; Q43814; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_01109; OTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; OTCase_ArgI.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Chloroplast; Plastid;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT   CHAIN           ?..375
FT                   /note="Ornithine carbamoyltransferase, chloroplastic"
FT                   /id="PRO_0000020341"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         123..126
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         174
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         201
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         204
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         232
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         293
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         297
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         298
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         333..334
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
FT   BINDING         361
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P00480"
SQ   SEQUENCE   375 AA;  41356 MW;  F39167839DDD49DE CRC64;
     MGVITAHCYC FTTVGSHKPY LSPSSHNFRH SPSVSLSSSS SSSPSPLRRI SCQASSAPAA
     ESTLTAKVGN GLKDFIHIDD FDKETILKIL DRAIEVKTLL KSGDRTFRPF EGKTMSMIFA
     KPSMRTRVSF ETGFSLLGGH AIYLGPNDIQ MGKREETRDV ARVLSRYNDI IMARVFSHQD
     ILDLAKYASV PVINGLTDYN HPVQIMADAL TMIEHIGRFE GTKVVYVGDG NNIVHSWLLL
     AAVVPFHFVC ACPKGFEPDA KTVEKARKAG ISKIEISHDP KEAVRGADVV YSDVWASMGQ
     KEEAAYRREA FKGFQVDQNL MDAAGSKAFF MHCLPAERGV EVTDEVVEAP YSIVFPQAEN
     RMHAQNAIML HVLGK