ID A3DIW7_ACET2 Unreviewed; 391 AA. AC A3DIW7; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN OrderedLocusNames=Cthe_2697 {ECO:0000313|EMBL:ABN53896.1}; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN53896.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; 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., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABN53896.1, ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RX PubMed=24295562; DOI=10.1186/1754-6834-6-179; RA Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M., RA Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H., RA Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.; RT "Global transcriptome analysis of Clostridium thermocellum ATCC 27405 RT during growth on dilute acid pretreated Populus and switchgrass."; RL Biotechnol. Biofuels 6:179-179(2013). 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; CP000568; ABN53896.1; -; Genomic_DNA. DR AlphaFoldDB; A3DIW7; -. DR STRING; 203119.Cthe_2697; -. DR KEGG; cth:Cthe_2697; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_9; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000002145; 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:UP000002145}. FT DOMAIN 249..378 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 41 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 270 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 41 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 391 AA; 43669 MW; E8D3E5C6DD62681E CRC64; MGMDYKFNRA WAEVNLDNIA HNVKEIRRIV DKKVEIMGVV KADAYGHGVM EIARTLLENG VTRLAVSMLD EAIQLRQNGI KVPILILSYT DPVRAEEIVL NDVTQTVFSH DLAEALSEAA VKHHRNVKIH IKIDTGMTRV GFMPGYSAVK NVVQISKLPG IIIEGLFTHF ASADEADKSY TYMQFERFMS IVGELNRIGV YIPVKHVCNS AALIEFPEMH LNMVRPGIAL YGLYPSDEVD KTKIDLRPAM SLKANVILVK DVEKDTFISY GRIFKTSRNS RIATIPIGYA DGYTRLLTGK GKVLLNGQLA PIVGRICMDQ CMVDITDIEG DVKVGDEAVL IGKQKDNEIK VEDLAKSVGT INYELVSIIG KRIPRVYLKE GKIYNVLNYL I //