OTC2A_PSESH
ID OTC2A_PSESH Reviewed; 327 AA.
AC P68747; P23752;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ornithine carbamoyltransferase 2, anabolic {ECO:0000303|PubMed:3592910};
DE Short=OTCase 2 {ECO:0000303|PubMed:3592910};
DE EC=2.1.3.3 {ECO:0000305|PubMed:3592910};
DE AltName: Full=Ornithine carbamoyltransferase 2, phaseolotoxin-insensitive {ECO:0000303|PubMed:2274044};
DE AltName: Full=Phaseolotoxin-resistant ornithine carbamoyltransferase {ECO:0000303|PubMed:1522066};
DE AltName: Full=Toxin-resistant enzyme {ECO:0000303|PubMed:2274044};
DE Short=ROCT {ECO:0000303|PubMed:1522066};
GN Name=argK {ECO:0000303|PubMed:1522066};
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], AND NOMENCLATURE.
RC STRAIN=Isolate Texcoco;
RX PubMed=2274044; DOI=10.1007/bf00633857;
RA Mosqueda G., van den Broeck G., Saucedo O., Bailey A.M.,
RA Alvarez-Morales A., Herrera-Estrella L.;
RT "Isolation and characterization of the gene from Pseudomonas syringae pv.
RT phaseolicola encoding the phaseolotoxin-insensitive ornithine
RT carbamoyltransferase.";
RL Mol. Gen. Genet. 222:461-466(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE
RP PHASEOLOTOXIN-RESISTANCE.
RC STRAIN=NPS 3121;
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 [3]
RP FUNCTION AS AN OTCASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND PATHWAY.
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 FUNCTION IN THE PHASEOLOTOXIN-RESISTANCE.
RC STRAIN=NPS 3121;
RX PubMed=16453811; DOI=10.1002/j.1460-2075.1987.tb02689.x;
RA Peet R.C., Panopoulos N.J.;
RT "Ornithine carbamoyltransferase genes and phaseolotoxin immunity in
RT Pseudomonas syringae pv. phaseolicola.";
RL EMBO J. 6:3585-3591(1987).
RN [5]
RP INDUCTION.
RC STRAIN=NPS 3121;
RX PubMed=14679234; DOI=10.1128/jb.186.1.146-153.2004;
RA Lopez-Lopez K., Hernandez-Flores J.L., Cruz-Aguilar M., Alvarez-Morales A.;
RT "In Pseudomonas syringae pv. phaseolicola, expression of the argK gene,
RT encoding the phaseolotoxin-resistant ornithine carbamoyltransferase, is
RT regulated indirectly by temperature and directly by a precursor resembling
RT carbamoylphosphate.";
RL J. Bacteriol. 186:146-153(2004).
RN [6]
RP INDUCTION.
RC STRAIN=NPS 3121;
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: Plays an important role in the survival and pathogenicity of
CC P.syringae (PubMed:1522066). Phaseolotoxin is a virulence factor that
CC inhibits the catalysis of the host OTCase (PubMed:1522066,
CC PubMed:16453811). Phaseolotoxin-producing bacteria do not suffer
CC autointoxication because they possess the anabolic OTCase ArgK which
CC can function even in the presence of phaseolotoxin (PubMed:1522066,
CC PubMed:3592910, PubMed:16453811). Reversibly catalyzes the transfer of
CC the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon)
CC atom of ornithine (ORN) to produce L-citrulline, which is a substrate
CC for argininosuccinate synthetase, the enzyme involved in the final step
CC in arginine biosynthesis (PubMed:3592910). {ECO:0000269|PubMed:1522066,
CC ECO:0000269|PubMed:16453811, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for L-ornithine {ECO:0000269|PubMed:3592910};
CC KM=2.8 mM for carbamoyl phosphate {ECO:0000269|PubMed:3592910};
CC pH dependence:
CC Optimum pH is 8.4. {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: By N-sulfodiaminophosphinyl, the inorganic moiety of
CC phaseolotoxin, at 18 degrees Celsius. {ECO:0000269|PubMed:14679234,
CC ECO:0000269|PubMed:15150254}.
CC -!- MISCELLANEOUS: This enzyme is insensitive to phaseolotoxin, a potent
CC inhibitor of OTCase. {ECO:0000269|PubMed:3592910}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved threonine residue in position 60, which is
CC part of the carbamoylphosphate binding site; it is replaced by a
CC glycine residue. {ECO:0000305}.
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DR EMBL; M94049; AAA25722.1; -; Genomic_DNA.
DR EMBL; X55520; CAA39136.1; -; Genomic_DNA.
DR PIR; S11943; OWPSY.
DR RefSeq; WP_011169509.1; NZ_RBUR01000291.1.
DR AlphaFoldDB; P68747; -.
DR SMR; P68747; -.
DR OMA; VYVKNWS; -.
DR BRENDA; 2.1.3.3; 5194.
DR SABIO-RK; P68747; -.
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;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..327
FT /note="Ornithine carbamoyltransferase 2, anabolic"
FT /id="PRO_0000112992"
FT BINDING 109
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 136..139
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 168
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 232
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 236..237
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 273..274
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 313
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT CONFLICT 153
FT /note="R -> P (in Ref. 1; CAA39136)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="E -> Q (in Ref. 1; CAA39136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36562 MW; 7D31F3A728A7352F CRC64;
MKITSLKNRN LLTMNEFNQS ELSHLIDRAI ECKRLKKDRI FNLGLNHLNI CGIFLKPSGR
TSTSFVVASY DEGAHFQFFP ADNIRFGHKE SIKDFARVVG RLFDGIAFRG FEHEVAEELA
KHSGIPVWNA LTDTHHPTQV LADVMTVKEE FGRIEGVTIA YVGDGRNNMV TSLAIGALKF
GYNLRIIAPN ALHPTDAVLA GIYEQTPERN GSIEIFTEVA AGVHQADVIY TDVWISMGES
VSVEERIALL KPYKVTEKMM ALTGKADTIF MHCLPAFHDL DTEVARETPD LVEVEDSVFE
GPQSRVFDQG ENRMHTIKAL MLETVVP
