OCD_BRUME
ID OCD_BRUME Reviewed; 359 AA.
AC Q8YCY1;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=BMEII0397;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53639.1; -; Genomic_DNA.
DR PIR; AD3559; AD3559.
DR AlphaFoldDB; Q8YCY1; -.
DR SMR; Q8YCY1; -.
DR STRING; 224914.BMEII0397; -.
DR EnsemblBacteria; AAL53639; AAL53639; BMEII0397.
DR KEGG; bme:BMEII0397; -.
DR eggNOG; COG2423; Bacteria.
DR OMA; DMIEPGM; -.
DR UniPathway; UPA00098; UER00357.
DR Proteomes; UP000000419; 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_0000200671"
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; 39460 MW; F29E90021EF950B5 CRC64;
MMTQPNLNIV PFVSVDHMMK LVLRVGVETF LKELAGYVEE DFRRWQNFDK TPRVASHSKE
GVIELMPTSD GTLYGFKYVN GHPKNTRDGL QTVTAFGVLA DVGSGYPMLL TEMTILTALR
TAATSAVAAK HLAPKNARTM AIIGNSAQSE FQALAFKAIL GVDKLRLYDL DPQATAKCIR
NLQGAGFNIV ACKSVEEAVE GADIITTVTA DKANATILTD NMVGAGVHIN AVGGDCPGKT
ELHGDILRRS DIFVEYPPQT RIEGEIQQLP EDYPVNELWE VITGRIAGRK DARQITLFDS
VGFATEDFSA LRYVRDKLKD TGLYEQLDLL ADPDEPRDLY GMLLRHEKLL QSESTKPAA
