ID   OTC2_PSESF              Reviewed;         327 AA.
AC   P68746; P23752;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ornithine carbamoyltransferase 2, phaseolotoxin-insensitive;
DE            Short=OTCase 2;
DE            EC=2.1.3.3;
DE   AltName: Full=ROCT;
GN   Name=argK;
OS   Pseudomonas syringae pv. actinidiae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=103796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KW-11;
RX   PubMed=8979356; DOI=10.1128/aem.63.1.282-288.1997;
RA   Sawada H., Takeuchi T., Matsuda I.;
RT   "Comparative analysis of Pseudomonas syringae pv. actinidiae and pv.
RT   phaseolicola based on phaseolotoxin-resistant ornithine
RT   carbamoyltransferase gene (argK) and 16S-23S rRNA intergenic spacer
RT   sequences.";
RL   Appl. Environ. Microbiol. 63:282-288(1997).
CC   -!- FUNCTION: Plays an important role in the survival and pathogenicity of
CC       P.syringae. Phaseolotoxin is a virulence factor that inhibits the
CC       catalysis of the host OTCase. Phaseolotoxin-producing bacteria do not
CC       suffer autointoxication because they possess the anabolic OTCase ArgK
CC       which can function even in the presence of phaseolotoxin (By
CC       similarity). {ECO:0000250}.
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. {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- MISCELLANEOUS: This enzyme is insensitive to phaseolotoxin, a potent
CC       inhibitor of OTCase.
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; D86356; BAA19878.1; -; Genomic_DNA.
DR   RefSeq; WP_011169509.1; NZ_RBSR01000014.1.
DR   AlphaFoldDB; P68746; -.
DR   SMR; P68746; -.
DR   UniPathway; UPA00068; UER00112.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..327
FT                   /note="Ornithine carbamoyltransferase 2, phaseolotoxin-
FT                   insensitive"
FT                   /id="PRO_0000112993"
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"
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