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   25-OCT-2017, entry version 52.
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 /
OS   NCIMB 10654) (Clostridium sticklandii).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Acetoanaerobium.
OX   NCBI_TaxID=499177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654;
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 / NCIMB 10654;
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 / NCIMB 10654;
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
RT   degradation:revisiting its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   AND SUBUNIT.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654;
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.
CC       Catalyzes the conversion of L-ornithine to D-ornithine
CC       (PubMed:19251850, PubMed:10715017). OR could also racemize basic
CC       amino acids such as lysine and arginine (PubMed:19251850). Serine,
CC       asparagine and alanine could be also converted by OR, but at a
CC       lower rate (PubMed:19251850). {ECO:0000269|PubMed:10715017,
CC       ECO:0000269|PubMed:19251850}.
CC   -!- CATALYTIC ACTIVITY: L-ornithine = D-ornithine.
CC       {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,
CC         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
CC         substrate (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}.
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DR   EMBL; CU695250; CAQ42981.1; -; Genomic_DNA.
DR   EMBL; FP565809; CBH21408.1; -; Genomic_DNA.
DR   ProteinModelPortal; C1FW08; -.
DR   STRING; 499177.CLOST_1288; -.
DR   EnsemblBacteria; CBH21408; CBH21408; CLOST_1288.
DR   KEGG; cst:CLOST_1288; -.
DR   eggNOG; ENOG4106M28; Bacteria.
DR   eggNOG; COG3457; LUCA.
DR   HOGENOM; HOG000057993; -.
DR   KO; K21898; -.
DR   OMA; GTNLNCL; -.
DR   OrthoDB; POG091H0HFT; -.
DR   BioCyc; CSTI499177:GJE9-1336-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-12478; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0050157; F:ornithine racemase activity; IDA:UniProtKB.
DR   GO; GO:0070280; F:pyridoxal binding; IDA:UniProtKB.
DR   GO; GO:0006591; P:ornithine metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    353       Ornithine racemase.
FT                                /FTId=PRO_0000438122.
FT   ACT_SITE     35     35       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P10724}.
FT   BINDING     128    128       Substrate.
FT                                {ECO:0000250|UniProtKB:P10724}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {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
//