ID G2NF88_STREK Unreviewed; 384 AA. AC G2NF88; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201}; DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201}; GN ORFNames=SACTE_4016 {ECO:0000313|EMBL:AEN11859.1}; OS Streptomyces sp. (strain SirexAA-E / ActE). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11859.1, ECO:0000313|Proteomes:UP000001397}; RN [1] {ECO:0000313|EMBL:AEN11859.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K., RA Adams S., Book A., Currie C., Woyke T.; RT "Complete sequence of Streptomyces sp. SirexAA-E."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEN11859.1, ECO:0000313|Proteomes:UP000001397} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397}; RX PubMed=24710170; DOI=10.1371/journal.pone.0094166; RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F., RA Book A.J., Currie C.R., Fox B.G.; RT "Biochemical properties and atomic resolution structure of a RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp. RT SirexAA-E."; RL PLoS ONE 9:e94166-E94166(2014). 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; CP002993; AEN11859.1; -; Genomic_DNA. DR RefSeq; WP_014047820.1; NC_015953.1. DR AlphaFoldDB; G2NF88; -. DR STRING; 862751.SACTE_4016; -. DR KEGG; ssx:SACTE_4016; -. DR PATRIC; fig|862751.12.peg.4167; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_0_0_11; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000001397; 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:UP000001397}. FT DOMAIN 250..377 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 39 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 271 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 319 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 384 AA; 40150 MW; 9D4E024DBF3DEE94 CRC64; MNETASLRAR AEIDLAALRA NVRVLRARAS GAQLMAVVKS DAYGHGALPC ARAALEAGAT WLGTATPQEA LALREAGVGG RVMCWLWTPG GPWREAIEAD IDVSVSGMWA LREVVEAATA AGRPARVQLK ADTGLGRNGC QPADWPELVS AARGAEEAGT LRVTGLWSHF ACADEPGHPS IAAQLTAFRD MVAYAEKEGV RPEVRHIANS PATLTLPESH FDLVRTGIAM YGLSPSPALG TPADFGLRPV MTLSASVALV KEVPPGHGIS YGHHYTTSAE TTLALVPLGY ADGIPRHASG RGPVLIDGAV RTVAGRVAMD QFVVDLGGDT PRPGARAVLF GPGDQGEPGA EDWAVAADTI GYEIVTRISG RVPRVHLHAS PERG //