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 07-JUN-2017, entry version 51. 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}. 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 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 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 //