ID F8DL25_LIMRS Unreviewed; 375 AA. AC F8DL25; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 74. 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:AEI57644.1}; GN OrderedLocusNames=HMPREF0538_21434 {ECO:0000313|EMBL:AEI57644.1}; OS Limosilactobacillus reuteri (strain ATCC 55730 / SD2112) (Lactobacillus OS reuteri). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Limosilactobacillus. OX NCBI_TaxID=491077 {ECO:0000313|EMBL:AEI57644.1, ECO:0000313|Proteomes:UP000001924}; RN [1] {ECO:0000313|Proteomes:UP000001924} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55730 / SD2112 {ECO:0000313|Proteomes:UP000001924}; RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A., RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X., RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J., RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A., RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B., RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J., RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M., RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G., RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M., RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L., RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.; RT "The complete genome of Lactobacillus reuteri ATCC 55730 / SD2112."; RL Submitted (JUN-2011) 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; CP002844; AEI57644.1; -; Genomic_DNA. DR RefSeq; WP_003671252.1; NC_015697.1. DR AlphaFoldDB; F8DL25; -. DR KEGG; lru:HMPREF0538_21434; -. DR HOGENOM; CLU_028393_2_1_9; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000001924; 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}. FT DOMAIN 247..372 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 40 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 140 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 315 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 40 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 375 AA; 41270 MW; 8C070DDEBC68098C CRC64; MVNGRLRDTS LIVDLDALRH NIQEQRKVLP ENSRILAVVK ANAYGNGLIP VAQTAMTSGA SGLCVAILDE ALELWDNGIE AMTLVLGITP VEDALIAAQA GVSLTVGSLD WLEQYHQLAQ VAKPKKPLKV HLGIDSGMGR IGFTEVATFK QAVKLLDSPE FEFEGMFTHF ATADSPDENY FNQQVQRWHQ FVASLDELPP YVHMANSATG LWHREKITAN TVRMGISMYG QNPSGRDLKL TLDLQPVSSL VSSISFVKQL KAGRSVSYGA TYTAEQDEWL ATLPIGYADG YPRCMTGYKV LVDGQFCDIA GRVCMDQMMI QLPKYYPVGT PVVLMGKSGD QEITATDLAE QAGTINYEIL TNISNRVHRI YHQSK //