ID OTCC_PSEAE Reviewed; 336 AA.
AC P08308;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic {ECO:0000303|PubMed:4962140};
DE Short=OTCase {ECO:0000303|PubMed:4962140};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=arcB {ECO:0000303|PubMed:3109911}; OrderedLocusNames=PA5172;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-35, FUNCTION,
RP INDUCTION, AND SUBUNIT.
RC STRAIN=PAO;
RX PubMed=3109911; DOI=10.1111/j.1432-1033.1987.tb13489.x;
RA Baur H., Stalon V., Falmagne P., Luethi E., Haas D.;
RT "Primary and quaternary structure of the catabolic ornithine
RT carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence
RT homology with the anabolic ornithine carbamoyltransferases of Escherichia
RT coli.";
RL Eur. J. Biochem. 166:111-117(1987).
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 A CATABOLIC OTCASE, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=113384; DOI=10.1128/jb.139.3.713-720.1979;
RA Hass D., Evans R., Mercenier A., Simon J.P., Stalon V.;
RT "Genetic and physiological characterization of Pseudomonas aeruginosa
RT mutants affected in the catabolic ornithine carbamoyltransferase.";
RL J. Bacteriol. 139:713-720(1979).
RN [5]
RP INDUCTION.
RX PubMed=6252188; DOI=10.1128/jb.144.1.159-163.1980;
RA Mercenier A., Simon J.P., Vander Wauven C., Haas D., Stalon V.;
RT "Regulation of enzyme synthesis in the arginine deiminase pathway of
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 144:159-163(1980).
RN [6]
RP PATHWAY.
RX PubMed=6438064; DOI=10.1128/jb.160.3.928-934.1984;
RA Vander Wauven C., Pierard A., Kley-Raymann M., Haas D.;
RT "Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine:
RT evidence for a four-gene cluster encoding the arginine deiminase pathway.";
RL J. Bacteriol. 160:928-934(1984).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLU-106.
RX PubMed=2118516; DOI=10.1016/s0021-9258(18)77171-8;
RA Baur H., Tricot C., Stalon V., Haas D.;
RT "Converting catabolic ornithine carbamoyltransferase to an anabolic
RT enzyme.";
RL J. Biol. Chem. 265:14728-14731(1990).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLU-106, ACTIVITY REGULATION, AND REACTION
RP MECHANISM.
RX PubMed=8102605; DOI=10.1111/j.1432-1033.1993.tb18099.x;
RA Tricot C., Nguyen V.T., Stalon V.;
RT "Steady-state kinetics and analysis of pH dependence on wild-type and a
RT modified allosteric Pseudomonas aeruginosa ornithine carbamoyltransferase
RT containing the replacement of glutamate 105 by alanine.";
RL Eur. J. Biochem. 215:833-839(1993).
RN [9]
RP SUBUNIT.
RX PubMed=10489456; DOI=10.1107/s0907444999007970;
RA Sainz G., Vicat J., Kahn R., Tricot C., Stalon V., Dideberg O.;
RT "Purification, crystallization and preliminary X-ray analysis of catabolic
RT ornithine carbamoyltransferase from Pseudomonas aeruginosa.";
RL Acta Crystallogr. D 55:1591-1593(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT GLY-106, MUTAGENESIS OF
RP GLU-106, AND SUBUNIT.
RX PubMed=7479879; DOI=10.1073/pnas.92.23.10762;
RA Villeret V., Tricot C., Stalon V., Dideberg O.;
RT "Crystal structure of Pseudomonas aeruginosa catabolic ornithine
RT transcarbamoylase at 3.0-A resolution: a different oligomeric organization
RT in the transcarbamoylase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10762-10766(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF MUTANT GLY-106, AND SUBUNIT.
RA Sainz G., Vicat J., Kahn R., Duee E., Tricot C., Stalon V., Dideberg O.;
RT "Catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa.";
RL Submitted (JAN-2000) to the PDB data bank.
CC -!- FUNCTION: Involved in the catabolism of arginine. Catalyzes the
CC phosphorolysis of citrulline, the reverse reaction of the biosynthetic
CC one, yielding ornithine and carbamoyl phosphate which serve to generate
CC ATP from ADP (PubMed:4962140, PubMed:2118516). This catabolic OTCase
CC does not carry out the biosynthetic reaction because of a poor affinity
CC and a marked cooperativity for carbamoyl phosphate (PubMed:2118516).
CC {ECO:0000269|PubMed:2118516, ECO:0000269|PubMed:4962140,
CC ECO:0000305|PubMed:113384, ECO:0000305|PubMed:3109911,
CC ECO:0000305|PubMed:8102605}.
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 -!- ACTIVITY REGULATION: Inhibited by 2-aminopentanoic acid (norvaline).
CC Activated by phosphate and nucleoside monophosphates such as AMP, GMP,
CC CMP, UMP. Allosterically inhibited by the polyamines such as spermidine
CC and putrescine. {ECO:0000269|PubMed:8102605}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.3. {ECO:0000269|PubMed:4962140};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC {ECO:0000305|PubMed:113384, ECO:0000305|PubMed:4962140,
CC ECO:0000305|PubMed:6438064}.
CC -!- SUBUNIT: Nonameric or dodecamer (tetramer of trimers).
CC {ECO:0000269|PubMed:10489456, ECO:0000269|PubMed:3109911,
CC ECO:0000269|PubMed:7479879, ECO:0000269|Ref.11}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: During limiting aeration and in the presence of arginine.
CC {ECO:0000269|PubMed:6252188, ECO:0000305|PubMed:3109911}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are blocked in the
CC arginine deiminase pathway. {ECO:0000269|PubMed:113384}.
CC -!- MISCELLANEOUS: Proceeds by an ordered sequential mechanism with CP
CC identified as the initial reactant. {ECO:0000305|PubMed:8102605}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; X05637; CAA29124.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08557.1; -; Genomic_DNA.
DR PIR; S00032; OWPSCA.
DR RefSeq; NP_253859.1; NC_002516.2.
DR RefSeq; WP_003100031.1; NZ_QZGE01000002.1.
DR PDB; 1DXH; X-ray; 2.50 A; A=2-336.
DR PDB; 1ORT; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-336.
DR PDBsum; 1DXH; -.
DR PDBsum; 1ORT; -.
DR AlphaFoldDB; P08308; -.
DR SMR; P08308; -.
DR STRING; 208964.PA5172; -.
DR PaxDb; 208964-PA5172; -.
DR GeneID; 881792; -.
DR KEGG; pae:PA5172; -.
DR PATRIC; fig|208964.12.peg.5420; -.
DR PseudoCAP; PA5172; -.
DR HOGENOM; CLU_043846_3_1_6; -.
DR InParanoid; P08308; -.
DR OrthoDB; 9802587at2; -.
DR PhylomeDB; P08308; -.
DR BioCyc; PAER208964:G1FZ6-5289-MONOMER; -.
DR SABIO-RK; P08308; -.
DR UniPathway; UPA00254; UER00365.
DR EvolutionaryTrace; P08308; -.
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; IMP:PseudoCAP.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; IMP:PseudoCAP.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1.
DR PANTHER; PTHR45753:SF2; ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3109911"
FT CHAIN 2..336
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000112986"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 135..138
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 274..275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 321
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT MUTAGEN 106
FT /note="E->A,G: Loss of homotropic cooperativity; gain of
FT anabolic activity. Conformational change which modifies the
FT catalytic site. This mutant is blocked in the active R
FT (relaxed) state."
FT /evidence="ECO:0000269|PubMed:2118516,
FT ECO:0000269|PubMed:7479879, ECO:0000269|PubMed:8102605"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1DXH"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1DXH"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1DXH"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:1DXH"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1DXH"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:1ORT"
FT HELIX 314..333
FT /evidence="ECO:0007829|PDB:1DXH"
SQ SEQUENCE 336 AA; 38109 MW; 4E780414EADA4724 CRC64;
MAFNMHNRNL LSLMHHSTRE LRYLLDLSRD LKRAKYTGTE QQHLKRKNIA LIFEKTSTRT
RCAFEVAAYD QGANVTYIDP NSSQIGHKES MKDTARVLGR MYDAIEYRGF KQEIVEELAK
FAGVPVFNGL TDEYHPTQML ADVLTMREHS DKPLHDISYA YLGDARNNMG NSLLLIGAKL
GMDVRIAAPK ALWPHDEFVA QCKKFAEESG AKLTLTEDPK EAVKGVDFVH TDVWVSMGEP
VEAWGERIKE LLPYQVNMEI MKATGNPRAK FMHCLPAFHN SETKVGKQIA EQYPNLANGI
EVTEDVFESP YNIAFEQAEN RMHTIKAILV STLADI
//
