OCD_BRUSU
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 03-AUG-2022, entry version 101.
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, ECO:0000312|EMBL:AEM20347.1};
GN OrderedLocusNames=BRA0899, BS1330_II0891;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; 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}.
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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 EnsemblBacteria; AEM20347; AEM20347; BS1330_II0891.
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 OMA; DMIEPGM; -.
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; 3.30.1780.10; -; 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 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
