ID Q11LC5_CHESB Unreviewed; 385 AA. AC Q11LC5; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 122. DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201}; GN OrderedLocusNames=Meso_0396 {ECO:0000313|EMBL:ABG61800.1}; OS Chelativorans sp. (strain BNC1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Chelativorans. OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG61800.1}; RN [1] {ECO:0000313|EMBL:ABG61800.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG61800.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Chelativorans sp. BNC1."; RL Submitted (JUN-2006) 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|ARBA:ARBA00000316, ECO:0000256|HAMAP- CC 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. CC {ECO:0000256|ARBA:ARBA00007880, ECO:0000256|HAMAP-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; CP000390; ABG61800.1; -; Genomic_DNA. DR AlphaFoldDB; Q11LC5; -. DR STRING; 266779.Meso_0396; -. DR KEGG; mes:Meso_0396; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_1_1_5; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. 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}. FT DOMAIN 239..362 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT REGION 366..385 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 39 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 260 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 306 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 39 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 385 AA; 40978 MW; 8B1E02B2655AC69A CRC64; MTAAKRAGAF LTVDLEAVTA NWLLLAGRAA GAECAAVVKA DAYGLGAAEV ATALQDAGCR TFFVAHLEEG LSLRRTLGSG SRIFVLNGTP PDTQEEFGQA ALTPVVGTIN ELQAWRKHAA TKRGPIPVAL QLDTGMSRLG LSPSDVSGIA ADTTLLRGIH IELVMSHLAC ADEPGHSANE SQRSRFQRLR RMLPQAPASI ANSSGTFLGK GFHFSMIRPG AALYGINPTP YQPNPMCQVV KVAARVLQVR QARAGTGIGY GHAARARRLS MLATIALGYA DGWPCQASGA AYYRGQRLPF IGRVSMDSII LDVTGCSNPP REGDLVEFIC PSQTVDEIGR LAGSIGYEVL TRLGRRFHRR YIRPNISPAQ STRSGSPLLA DDTAE //