OCD_BRUAB
ID OCD_BRUAB Reviewed; 359 AA.
AC Q59175; Q579B9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ornithine cyclodeaminase {ECO:0000303|PubMed:9375792};
DE Short=OCD {ECO:0000303|PubMed:9375792};
DE EC=4.3.1.12 {ECO:0000250|UniProtKB:Q59701};
GN Name=ocd {ECO:0000303|PubMed:9375792};
GN Synonyms=arcB {ECO:0000312|EMBL:AAX75765.1}; OrderedLocusNames=BruAb2_0334;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=19;
RX PubMed=9375792; DOI=10.1016/s0167-4781(97)00125-5;
RA Kim J., Mayfield J.E.;
RT "Brucella abortus arginase and ornithine cyclodeaminase genes are similar
RT to Ti plasmid arginase and ornithine cyclodeaminase.";
RL Biochim. Biophys. Acta 1354:55-57(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAX75765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U57319; AAC05589.1; -; Genomic_DNA.
DR EMBL; AE017224; AAX75765.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q59175; -.
DR SMR; Q59175; -.
DR EnsemblBacteria; AAX75765; AAX75765; BruAb2_0334.
DR KEGG; bmb:BruAb2_0334; -.
DR HOGENOM; CLU_042088_3_2_5; -.
DR UniPathway; UPA00098; UER00357.
DR Proteomes; UP000000540; 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..359
FT /note="Ornithine cyclodeaminase"
FT /id="PRO_0000200670"
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 359 AA; 39420 MW; 94CFD9C69CB785F4 CRC64;
MMTQPNLNIV PFVSVDHMMK LVLRVGVETF LKELAGYVEE DFRRWQNFDK TPRVASHSKE
GVIELMPTSD GTLYGFKYVN GHPKNTRDGL QTVTAFGVLA DVGSGYPMLL TEMTILTALR
TAATSAVAAK HLAPKNARTM AIIGNGAQSE FQALAFKAIL GVDKLRLYDL DPQATAKCIR
NLQGAGFNIV ACKSVEEAVE GADIITTVTA DKANATILTD NMVGAGVHIN AVGGDCSGKT
ELHGDILRRS DIFVEYPPQT RIEGEIQQLP EDYPVNELWE VITGRIAGRK DARQITLFDS
VGFATEDFSA LRYVRDKLKD TGLYEQLDLL ADPDEPRDLY GMLLRHEKLL QSESTKPAA
