OCD_AGRT4
ID OCD_AGRT4 Reviewed; 356 AA.
AC Q59701;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ornithine cyclodeaminase {ECO:0000303|PubMed:2644238};
DE Short=OCD {ECO:0000303|PubMed:2644238};
DE EC=4.3.1.12 {ECO:0000269|PubMed:2644238};
GN Name=ocd {ECO:0000303|PubMed:2644238};
OS Agrobacterium tumefaciens (strain Ach5).
OG Plasmid pTiAch5.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176298;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, ACTIVITY REGULATION, AND PATHWAY.
RX PubMed=2644238; DOI=10.1128/jb.171.2.847-854.1989;
RA Schindler U., Sans N., Schroeder J.;
RT "Ornithine cyclodeaminase from octopine Ti plasmid Ach5: identification,
RT DNA sequence, enzyme properties, and comparison with gene and enzyme from
RT nopaline Ti plasmid C58.";
RL J. Bacteriol. 171:847-854(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schroeder J., von Lintig J., Zanker H.;
RT "Catabolism of the guanidino compounds nopaline, octopine, and L-arginine
RT in Agrobacterium tumefaciens: enzymes, genes, and regulation.";
RL (In) De Deyn P.P., Marescau B., Stalon V., Qureshi I.A. (eds.);
RL Guanidino compounds in biology and medicine, pp.19-28, J. Libbey, London
RL (1992).
CC -!- FUNCTION: Catalyzes the conversion of L-ornithine into L-proline with
CC release of ammonia. Is involved in the utilization of octopine, a
CC catabolic pathway that proceeds through L-arginine and L-ornithine to
CC L-proline. Octopine is a predominant opine in plant cells transformed
CC with Ti plasmid pTiAch5. {ECO:0000269|PubMed:2644238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine = L-proline + NH4(+); Xref=Rhea:RHEA:24368,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:46911, ChEBI:CHEBI:60039; EC=4.3.1.12;
CC Evidence={ECO:0000269|PubMed:2644238};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:2644238};
CC -!- ACTIVITY REGULATION: Is inhibited by L-proline and L-lysine. Is not
CC activated by small concentrations of L-arginine, and is even inhibited
CC by about 50% at 0.5 mM L-arginine. {ECO:0000269|PubMed:2644238}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for L-ornithine {ECO:0000269|PubMed:2644238};
CC KM=7.5 uM for NAD(+) {ECO:0000269|PubMed:2644238};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:2644238};
CC Temperature dependence:
CC Optimum temperature is 30-35 degrees Celsius.
CC {ECO:0000269|PubMed:2644238};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-ornithine: step 1/1. {ECO:0000269|PubMed:2644238}.
CC -!- INDUCTION: Is induced by octopine. Is part of the occ operon.
CC {ECO:0000269|PubMed:2644238}.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000305}.
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DR EMBL; M24146; AAA50518.1; -; Genomic_DNA.
DR EMBL; Z30328; CAA82989.1; -; Genomic_DNA.
DR PIR; A32049; A32049.
DR RefSeq; NP_059708.1; NC_002377.1.
DR AlphaFoldDB; Q59701; -.
DR SMR; Q59701; -.
DR UniPathway; UPA00098; UER00357.
DR GO; GO:0008473; F:ornithine cyclodeaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1780.10; -; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; PTHR13812; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Lyase; NAD; Plasmid.
FT CHAIN 1..356
FT /note="Ornithine cyclodeaminase"
FT /id="PRO_0000200668"
FT ACT_SITE 235
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 53
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 77
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 120
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 147..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 232..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
FT BINDING 301
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:Q88H32"
SQ SEQUENCE 356 AA; 39166 MW; 5B3D3765E4800395 CRC64;
MPIDPKLNVV PFISVDHMMK LVLKVGIDTF LTELAAEIEK DFRRWPIFDK KPRVGSHSQD
GVIELMPTSD GSLYGFKYVN GHPKNTHQGR QTVTAFGVLS DVGNGYPLLL SEMTILTALR
TAATSALAAK YLARPNSKTM AIIGNGAQSE FQARAFRAIL GIQKLRLFDI DTSATRKCAR
NLTGPGFDIV ECGSVAEAVE GADVITTVTA DKQFATILSD NHVGPGVHIN AVGGDCPGKT
EISMEVLLRS DIFVEYPPQT WIEGDIQQLP RTHPVTELWQ VMTGEKTGRV GDRQITMFDS
VGFAIEDFSA LRYVRAKITD FEMFTELDLL ADPDEPRDLY GMLLRCEKKL EPTAVG
