ID   ORR_ACESD               Reviewed;         353 AA.
AC   C1FW08; E3PY93;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   27-NOV-2024, entry version 79.
DE   RecName: Full=Ornithine racemase {ECO:0000303|PubMed:10715017};
DE            Short=OR {ECO:0000303|PubMed:10715017};
DE            EC=5.1.1.12 {ECO:0000269|PubMed:10715017, ECO:0000269|PubMed:19251850};
GN   Name=orr {ECO:0000303|PubMed:10715017};
GN   OrderedLocusNames=CLOST_1288 {ECO:0000312|EMBL:CAQ42981.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Bacillota; Clostridia; Peptostreptococcales; Filifactoraceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RG   Genoscope - CEA;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=19251850; DOI=10.1128/jb.01777-08;
RA   Fonknechten N., Perret A., Perchat N., Tricot S., Lechaplais C.,
RA   Vallenet D., Vergne C., Zaparucha A., Le Paslier D., Weissenbach J.,
RA   Salanoubat M.;
RT   "A conserved gene cluster rules anaerobic oxidative degradation of L-
RT   ornithine.";
RL   J. Bacteriol. 191:3162-3167(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=10715017; DOI=10.1128/jb.182.7.2052-2054.2000;
RA   Chen H.P., Lin C.F., Lee Y.J., Tsay S.S., Wu S.H.;
RT   "Purification and properties of ornithine racemase from Clostridium
RT   sticklandii.";
RL   J. Bacteriol. 182:2052-2054(2000).
CC   -!- FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the
CC       conversion of L-ornithine to D-ornithine (PubMed:10715017,
CC       PubMed:19251850). OR could also racemize basic amino acids such as
CC       lysine and arginine (PubMed:19251850). Serine, asparagine and alanine
CC       could be also converted by OR, but at a lower rate (PubMed:19251850).
CC       {ECO:0000269|PubMed:10715017, ECO:0000269|PubMed:19251850}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57668; EC=5.1.1.12;
CC         Evidence={ECO:0000269|PubMed:10715017, ECO:0000269|PubMed:19251850};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:10715017, ECO:0000269|PubMed:19251850};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=520 uM for L-ornithine {ECO:0000269|PubMed:19251850};
CC         KM=770 uM for L-ornithine {ECO:0000269|PubMed:10715017};
CC         Note=kcat is 1660 sec(-1) for L-ornithine as substrate
CC         (PubMed:19251850). kcat is 980 sec(-1) for L-ornithine as substrate
CC         (PubMed:10715017). {ECO:0000269|PubMed:10715017,
CC         ECO:0000269|PubMed:19251850};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:10715017};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10715017,
CC       ECO:0000269|PubMed:19251850}.
CC   -!- SIMILARITY: Belongs to the alanine racemase 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; CU695250; CAQ42981.1; -; Genomic_DNA.
DR   EMBL; FP565809; CBH21408.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1FW08; -.
DR   SMR; C1FW08; -.
DR   STRING; 1511.CLOST_1288; -.
DR   KEGG; cst:CLOST_1288; -.
DR   eggNOG; COG3457; Bacteria.
DR   HOGENOM; CLU_067103_0_0_9; -.
DR   BioCyc; MetaCyc:MONOMER-12478; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:TreeGrafter.
DR   GO; GO:0050157; F:ornithine racemase activity; IDA:UniProtKB.
DR   GO; GO:0070280; F:pyridoxal binding; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR   GO; GO:0006591; P:ornithine metabolic process; IDA:UniProtKB.
DR   CDD; cd06815; PLPDE_III_AR_like_1; 1.
DR   FunFam; 3.20.20.10:FF:000013; Alanine/ornithine racemase family PLP-dependent enzyme; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; NF040742; racem_Orr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF3; LYSINE RACEMASE; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..353
FT                   /note="Ornithine racemase"
FT                   /id="PRO_0000438122"
FT   ACT_SITE        35
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P10724"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P10724"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P10724"
SQ   SEQUENCE   353 AA;  39341 MW;  D81B9585C9675B68 CRC64;
     MYPKITIDIN KLRDNATFIK NLCEKGGCKT ALVVKSMCAN HDIVKELDSV EVDYFADSRI
     QNLKKLKDLK TKKMLLRIPM LCEVEDVVKY ADISMNSELD TLKALNKAAK TLNKVHSVII
     MVDLGDLREG YFEAEDLKEN IKEIIKLENI EIKGIGVNLT CYGAVIPKND NLSRLCDIAD
     ELRTEFNLEL PIVSGGNSSS IYLIDKGELP EGITNLRVGE SMLLGRETAY GEDIIGMNND
     VFELKCQIVE LKEKPSLPIG EIGVDAFGNK PYYEDKGIRK RAILAIGQQD TDISSLMPID
     DKLEILGASS DHLIVDVSDS NTSYKVGDII TFRMGYGALL KGFTSEYIEK ELL
//