ID OCD_BRUSU Reviewed; 358 AA. AC Q8FVE4; G0KDQ9; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Ornithine cyclodeaminase {ECO:0000250|UniProtKB:Q59175}; DE Short=OCD {ECO:0000250|UniProtKB:Q59175}; DE EC=4.3.1.12 {ECO:0000250|UniProtKB:Q59701}; GN Name=ocd {ECO:0000250|UniProtKB:Q59175}; GN Synonyms=arcB {ECO:0000312|EMBL:AAN34071.1, GN ECO:0000312|EMBL:AEM20347.1}; GN OrderedLocusNames=BRA0899, BS1330_II0891; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). CC -!- FUNCTION: Catalyzes the conversion of L-ornithine into L-proline with CC release of ammonia. {ECO:0000250|UniProtKB:Q59701}. 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:0000250|UniProtKB:Q59701}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000250|UniProtKB:Q59701}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline CC from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:Q59701}. CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014292; AAN34071.1; -; Genomic_DNA. DR EMBL; CP002998; AEM20347.1; -; Genomic_DNA. DR RefSeq; WP_006192192.1; NZ_KN046805.1. DR AlphaFoldDB; Q8FVE4; -. DR SMR; Q8FVE4; -. DR GeneID; 45053897; -. DR KEGG; bms:BRA0899; -. DR KEGG; bsi:BS1330_II0891; -. DR PATRIC; fig|204722.21.peg.404; -. DR HOGENOM; CLU_042088_3_2_5; -. DR PhylomeDB; Q8FVE4; -. DR UniPathway; UPA00098; UER00357. DR Proteomes; UP000007104; Chromosome II. DR GO; GO:0008473; F:ornithine cyclodeaminase activity; IEA:UniProtKB-EC. DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR003462; ODC_Mu_crystall. DR InterPro; IPR023401; ODC_N. DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1. DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1. DR Pfam; PF02423; OCD_Mu_crystall; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Arginine metabolism; Lyase; NAD. FT CHAIN 1..358 FT /note="Ornithine cyclodeaminase" FT /id="PRO_0000200672" FT ACT_SITE 234 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 52 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 76 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 91 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 119 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 146..147 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 168 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 208 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 231..234 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 234 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 238 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 299 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q88H32" FT BINDING 300 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000250|UniProtKB:Q88H32" SQ SEQUENCE 358 AA; 39299 MW; DA2F02B1171B4C81 CRC64; MTQPNLNIVP FVSVDHMMKL VLRVGVETFL KELAGYVEED FRRWQNFDKT PRVASHSKEG VIELMPTSDG TLYGFKYVNG HPKNTRDGLQ TVTAFGVLAN VGSGYPMLLT EMTILTALRT AATSAVAAKH LAPKNARTMA IIGNGAQSEF QALAFKAILG VDKLRLYDLD PQATAKCIRN LQGAGFDIVA CKSVEEAVEG ADIITTVTAD KANATILTDN MVGAGVHINA VGGDCPGKTE LHGDILRRSD IFVEYPPQTR IEGEIQQLPE DYPVNELWEV ITGRIAGRKD ARQITLFDSV GFATEDFSAL RYVRDKLKDT GLYEQLDLLA DPDEPRDLYG MLLRHEKLLQ SESTKPAA //