OTC1A_PSESH
ID OTC1A_PSESH Reviewed; 306 AA.
AC Q02047;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Ornithine carbamoyltransferase 1, anabolic {ECO:0000303|PubMed:3592910};
DE Short=OTCase 1 {ECO:0000303|PubMed:3592910};
DE EC=2.1.3.3 {ECO:0000305|PubMed:3592910};
DE AltName: Full=Ornithine carbamoyltransferase 1, phaseolotoxin-sensitive {ECO:0000305|PubMed:3592910};
DE AltName: Full=SOCT {ECO:0000303|PubMed:3592910};
GN Name=argF {ECO:0000303|PubMed:3592910};
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=4419;
RX PubMed=1522066; DOI=10.1128/jb.174.18.5895-5909.1992;
RA Hatziloukas E., Panopoulos N.J.;
RT "Origin, structure, and regulation of argK, encoding the phaseolotoxin-
RT resistant ornithine carbamoyltransferase in Pseudomonas syringae pv.
RT phaseolicola, and functional expression of argK in transgenic tobacco.";
RL J. Bacteriol. 174:5895-5909(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Texcoco;
RA Mosqueda-Cano G.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION AS AN OTCASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX PubMed=3592910; DOI=10.1007/bf00415280;
RA Jahn O., Sauerstein J., Reuter G.;
RT "Characterization of two ornithine carbamoyltransferases from Pseudomonas
RT syringae pv. phaseolicola, the producer of phaseolotoxin.";
RL Arch. Microbiol. 147:174-178(1987).
RN [4]
RP INDUCTION.
RX PubMed=15150254; DOI=10.1128/jb.186.11.3653-3655.2004;
RA Hernandez-Flores J.L., Lopez-Lopez K., Garciduenas-Pina R.,
RA Jofre-Garfias A.E., Alvarez-Morales A.;
RT "The global arginine regulator ArgR controls expression of argF in
RT Pseudomonas syringae pv. phaseolicola but is not required for the synthesis
RT of phaseolotoxin or for the regulated expression of argK.";
RL J. Bacteriol. 186:3653-3655(2004).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline, which is a substrate for argininosuccinate
CC synthetase, the enzyme involved in the final step in arginine
CC biosynthesis. {ECO:0000269|PubMed:3592910}.
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; Evidence={ECO:0000305|PubMed:3592910};
CC -!- ACTIVITY REGULATION: Reversibly inhibited by inhibited by phaseolotoxin
CC and octicidine. {ECO:0000269|PubMed:3592910}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for L-ornithine {ECO:0000269|PubMed:3592910};
CC KM=0.7 mM for carbamoyl phosphate {ECO:0000269|PubMed:3592910};
CC pH dependence:
CC Optimum pH is between 8.5 and 9.5. {ECO:0000269|PubMed:3592910};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC {ECO:0000305|PubMed:3592910}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Negatively regulated by ArgR. {ECO:0000269|PubMed:15150254}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; M99382; AAA25909.1; -; Genomic_DNA.
DR EMBL; X76945; CAA54264.1; -; Genomic_DNA.
DR PIR; S41291; S41291.
DR RefSeq; WP_011169325.1; NZ_RBTC01000080.1.
DR AlphaFoldDB; Q02047; -.
DR SMR; Q02047; -.
DR OMA; DGNNVCN; -.
DR SABIO-RK; Q02047; -.
DR UniPathway; UPA00068; UER00112.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..306
FT /note="Ornithine carbamoyltransferase 1, anabolic"
FT /id="PRO_0000112991"
FT BINDING 53..56
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 80
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 104
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 131..134
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 162
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 219
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 223..224
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 259..260
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 287
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ SEQUENCE 306 AA; 34151 MW; D37B503563D53F50 CRC64;
MNARHFLSMM DYTPDELLGL IRRGVELKDL RIRGELFEPL KNRVLGMIFE KSSTRTRLSF
EAGMIQLGGQ AIFLSHRDTQ LGRGEPIADS AKVMSRMLDA VMIRTYAHSN LTEFAANSRV
PVINGLSDDL HPCQLLADMQ TFLEHRGSIK GKTVAWIGDG NNMCNSYIEA AIQFDFQLRV
ACPAGYEPNP EFLALAGERV TIVRDPKAAV AGAHLVSTDV WTSMGQEEET ARRMALFAPF
QVTRASLDLA EKDVLFMHCL PAHRGEEISV DLLDDSRSVA WDQAENRLHA QKALLEFLVA
PSHQRA
