ID G8NU73_GRAMM Unreviewed; 385 AA. AC G8NU73; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAR-2024, entry version 67. 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=AciX8_4435 {ECO:0000313|EMBL:AEU38708.1}; OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Granulicella. OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU38708.1, ECO:0000313|Proteomes:UP000007113}; RN [1] {ECO:0000313|EMBL:AEU38708.1, ECO:0000313|Proteomes:UP000007113} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8 RC {ECO:0000313|Proteomes:UP000007113}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M., RA Haggblom M., Woyke T.; RT "Complete sequence of Granulicella mallensis MP5ACTX8."; RL Submitted (NOV-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; CP003130; AEU38708.1; -; Genomic_DNA. DR RefSeq; WP_014267579.1; NC_016631.1. DR AlphaFoldDB; G8NU73; -. DR STRING; 682795.AciX8_4435; -. DR KEGG; gma:AciX8_4435; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_0; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000007113; 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:UP000007113}. FT DOMAIN 260..385 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 34 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 281 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 134 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 34 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 385 AA; 40559 MW; 0B30B0D43E0CF219 CRC64; MKSWIEISSA RLAENFRAIQ AVAGQGVEAL AVIKANAYGH GTTICAPVLA EAGAQWLGVS DVAEGEAVRT ALPHSGIRVL VMCGMELADA PALVAHGLTP VVWTPEHIAA LERAARSAGH RIQVHLEVDT GMGRQGAAPG EDLARTLEAL ADSRWVSCEG IMTHLCCSES AEAKITEEQR ERFASALDQA LAAGMRPEFV HLANTSAVDE GSTMQWIRDT AKSLGARAMV RIGFAIYGHC LEIEGEHAHA GALAPKVSPV LVWKTRIIGL RGVAAGATVG YGATFVATQP MRLALLPVGY ADGYRRAASS GVGNGWVMIA GRRAPVVGRV SMNLTVVDVS GHADVQEGME AVLLGEGVTA EDQARWSGTI AYDILCGIRA NFELR //