ID E1VY23_GLUAR Unreviewed; 399 AA. AC E1VY23; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 27-MAR-2024, entry version 80. 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=alr {ECO:0000313|EMBL:CBT76526.1}; GN OrderedLocusNames=AARI_23060 {ECO:0000313|EMBL:CBT76526.1}; OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 / OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Glutamicibacter. OX NCBI_TaxID=861360 {ECO:0000313|EMBL:CBT76526.1, ECO:0000313|Proteomes:UP000006878}; RN [1] {ECO:0000313|EMBL:CBT76526.1, ECO:0000313|Proteomes:UP000006878} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117 RC {ECO:0000313|Proteomes:UP000006878}; RX PubMed=21124797; DOI=10.1371/journal.pone.0015489; RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B., RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F., RA Vallaeys T.; RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic RT adaptation to the surface of cheese."; RL PLoS ONE 5:E15489-E15489(2010). RN [2] {ECO:0000313|Proteomes:UP000006878} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117 RC {ECO:0000313|Proteomes:UP000006878}; RA Genoscope.; RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 / RT CIP 108037 / JCM 13566 / Re117)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. 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; FQ311875; CBT76526.1; -; Genomic_DNA. DR RefSeq; WP_013349643.1; NC_014550.1. DR AlphaFoldDB; E1VY23; -. DR STRING; 861360.AARI_23060; -. DR KEGG; aai:AARI_23060; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_11; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000006878; 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; cd00430; PLPDE_III_AR; 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:UP000006878}. FT DOMAIN 264..390 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 55 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 285 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 332 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 55 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 399 AA; 42689 MW; 4E26069039B3EB1E CRC64; MNSEALEESN LTNSTSSAQA TGFERRAVID LSAIRNNVKQ ISDVVAPAAV MAVVKADAYG HGAIQVAKAA LEGGARWIGC AHVTEALALR EAGIDAPMLA WLHTEDTPFE AAIDAGLDLG VSGWELERVA AAARAVQTPA RIHIKVDTGL GRNGSTMEAL PDLLNRASDF QEEGLLRAVG IFSHLAVADE PERPETDEQL AVFNTAIELI EAAGFDLEVR HIANTPGILS RPDSHYEMVR LGLGLYGLSP FEEDTPQSFG LRPAMTVKTR VANVKKVRPG QGVSYGLNYK TEGETYLGLI PMGYADGLPR IATGAPVTVN GRTYPVRGRI AMDQCVIDLG ADINPEDFLG AEAIIFGDGG QSVNTWAYAA NTINYEVVTR ISPRVPRYYI EGSWGEAGE //