OTCA_PSEAE
ID OTCA_PSEAE Reviewed; 305 AA.
AC P11724;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ornithine carbamoyltransferase, anabolic {ECO:0000303|PubMed:4962140};
DE Short=OTCase {ECO:0000303|PubMed:3131308};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000303|PubMed:3131308}; OrderedLocusNames=PA3537;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-38.
RC STRAIN=PAO;
RX PubMed=3131308; DOI=10.1128/jb.170.6.2725-2734.1988;
RA Itoh Y., Soldati L., Stalon V., Falmagne P., Terawaki Y., Leisinger T.,
RA Haas D.;
RT "Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa:
RT nucleotide sequence and transcriptional control of the argF structural
RT gene.";
RL J. Bacteriol. 170:2725-2734(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION AS AN ANABOLIC OTCASE, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=4962140; DOI=10.1016/0005-2744(67)90115-5;
RA Stalon V., Ramos F., Pierard A., Wiame J.M.;
RT "The occurrence of a catabolic and an anabolic ornithine
RT carbamoyltransferase in Pseudomonas.";
RL Biochim. Biophys. Acta 139:91-97(1967).
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 (ArgG) involved in the final step in arginine biosynthesis.
CC {ECO:0000269|PubMed:4962140}.
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:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 8.5 and 9. {ECO:0000269|PubMed:4962140};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC {ECO:0000305|PubMed:4962140}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:4962140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; M19939; AAA25720.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06925.1; -; Genomic_DNA.
DR PIR; A32013; OWPSAA.
DR PIR; E83203; E83203.
DR RefSeq; NP_252227.1; NC_002516.2.
DR RefSeq; WP_003092090.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; P11724; -.
DR SMR; P11724; -.
DR STRING; 287.DR97_4405; -.
DR PaxDb; P11724; -.
DR PRIDE; P11724; -.
DR DNASU; 878793; -.
DR EnsemblBacteria; AAG06925; AAG06925; PA3537.
DR GeneID; 878793; -.
DR KEGG; pae:PA3537; -.
DR PATRIC; fig|208964.12.peg.3701; -.
DR PseudoCAP; PA3537; -.
DR HOGENOM; CLU_043846_3_2_6; -.
DR InParanoid; P11724; -.
DR OMA; DGNNVCN; -.
DR PhylomeDB; P11724; -.
DR BioCyc; PAER208964:G1FZ6-3605-MON; -.
DR SABIO-RK; P11724; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000002438; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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;
KW Direct protein sequencing; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3131308"
FT CHAIN 2..305
FT /note="Ornithine carbamoyltransferase, anabolic"
FT /id="PRO_0000112985"
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"
FT CONFLICT 170..172
FT /note="AAL -> EEM (in Ref. 1; AAA25720)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> M (in Ref. 1; AAA25720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33925 MW; 6C196BC06BD27F0B CRC64;
MSVRHFLSFM DYSPEELIGL IRRGSELKDL RNRGVLYEPL KSRVLGMVFE KASTRTRLSF
EAGMIQLGGQ AIFLSPRDTQ LGRGEPIGDS ARVMSRMLDG VMIRTFAHAT LTEFAAHSKV
PVINGLSDDL HPCQLLADMQ TFHEHRGSIQ GKTVAWIGDG NNMCNSYIEA ALKFDFQLRV
ACPEGYEPKA EFVALAGDRL RVVRDPREAV AGAHLVSTDV WASMGQEDEA AARIALFRPY
QVNAALLDGA ADDVLFMHCL PAHRGEEISE ELLDDPRSVA WDQAENRLHA QKALLELLIE
HAHYA
