ID F5Y3D8_RAMTT Unreviewed; 376 AA. AC F5Y3D8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN Name=alr2 {ECO:0000313|EMBL:AEG91225.1}; GN OrderedLocusNames=Rta_01610 {ECO:0000313|EMBL:AEG91225.1}; OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 / OS TTB310). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Ramlibacter. OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG91225.1, ECO:0000313|Proteomes:UP000008385}; RN [1] {ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B., RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E., RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M., RA Barras F., Heulin T.; RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEG91225.1, ECO:0000313|Proteomes:UP000008385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310 RC {ECO:0000313|Proteomes:UP000008385}; RX PubMed=21912644; DOI=10.1371/journal.pone.0023784; RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C., RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O., RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I., RA Vermeglio A., Achouak W., Heulin T.; RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment."; RL PLoS ONE 6:E23784-E23784(2011). CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249, CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01201}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP- CC Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50}; CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}. CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP- CC Rule:MF_01201}. 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; CP000245; AEG91225.1; -; Genomic_DNA. DR AlphaFoldDB; F5Y3D8; -. DR STRING; 365046.Rta_01610; -. DR KEGG; rta:Rta_01610; -. DR PATRIC; fig|365046.3.peg.167; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_1_0_4; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000008385; Chromosome. DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd06827; PLPDE_III_AR_proteobact; 1. DR Gene3D; 3.20.20.10; Alanine racemase; 1. DR HAMAP; MF_01201; Ala_racemase; 1. DR InterPro; IPR000821; Ala_racemase. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS. DR InterPro; IPR029066; PLP-binding_barrel. DR NCBIfam; TIGR00492; alr; 1. DR PANTHER; PTHR30511; ALANINE RACEMASE; 1. DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PRINTS; PR00992; ALARACEMASE. DR SMART; SM01005; Ala_racemase_C; 1. DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000008385}. FT DOMAIN 247..376 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 47 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 268 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 316 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 47 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 376 AA; 41032 MW; 9BFD8F3AA623FA86 CRC64; MPKSPRHPRD YPMPRPIQAT IHTESLRHNL ARMRRAAPDA RAWGVVKANA YGHGIERAFE GLRGADGFAL LDLQEAERVR ALGWRGPILL LEGVFEPRDL ELCSRLSLWH TVHCDEQIDM LAAHKTQLPH RVFLKMNSGM NRLGFAPHRY RAAWARLDAL PQVDEITLMT HFSDADTARG IGHQARVFAE TTRDLPGERT LGNSAAALRF GQEAAVRADW VRPGIAVYGS APDFPEHDIA HWGLQPTMTL ASRLIAVQQL RPGDTVGYGS SFTAEAPLRI GVVACGYADG YPRHGPTGTP VLVDGVRTRL VGRVSMDMVT VDLTPVPQAG FGSEATLWGR AANGAVLPID EVARAAGTVG YELMCAVAPR VPFAVD //