ORR_ACESD
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 03-AUG-2022, entry version 70.
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; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
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:19251850,
CC PubMed:10715017). 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}.
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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 PRIDE; C1FW08; -.
DR EnsemblBacteria; CBH21408; CBH21408; CLOST_1288.
DR KEGG; cst:CLOST_1288; -.
DR eggNOG; COG3457; Bacteria.
DR HOGENOM; CLU_067103_0_0_9; -.
DR OMA; VGCFGGV; -.
DR BioCyc; MetaCyc:MON-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 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
