ID A1SMF0_NOCSJ Unreviewed; 380 AA. AC A1SMF0; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 111. 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=Noca_3485 {ECO:0000313|EMBL:ABL82985.1}; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL82985.1, ECO:0000313|Proteomes:UP000000640}; RN [1] {ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; 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 Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABL82985.1, ECO:0000313|Proteomes:UP000000640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640}; RX PubMed=21551312; DOI=10.1128/JB.05109-11; RA Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A., RA Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S., RA Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A., RA Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R., RA Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.; RT "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete RT Nocardioides sp. strain JS614."; RL J. Bacteriol. 193:3399-3400(2011). 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; CP000509; ABL82985.1; -; Genomic_DNA. DR RefSeq; WP_011756918.1; NC_008699.1. DR AlphaFoldDB; A1SMF0; -. DR STRING; 196162.Noca_3485; -. DR KEGG; nca:Noca_3485; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_0_0_11; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000640; 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; 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. 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:UP000000640}. FT DOMAIN 244..371 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 44 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 265 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 313 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 44 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 380 AA; 39731 MW; C7B2AB9641F4F2A7 CRC64; MTILLADRQR TGAGPRPDID LAAVAHNTRL LAGRATGELM AVVKADDFGH GAVELARTAL ANGATWLGVT TIDEALALRA AGLTAPLLSW LNPVDADLAA AVRAGVDLGV PGLPHLDATT AARGARVHLH VDAGMARDGA APATWGQLCR AARRAEQRGE IQVVGVMGHL GCAEDPTDEC NALGRTRFAW ALETARAAGL RPAHRHLAAT AATLTDPRSH HTMSRVGAGL VGIDPSHTTR LRPALTLIAP VVQVRRVRGG TPVGYGHAYR TSAATHLGLV PLGYADGLPR LASGRAEVLV RGRRRPVVGR ISMDQLVVDL GERPVDVGEG VTVFGPGDAG EPTVAEWAAW SETIEHEIVT GIGARVPRRI GRSAHLRSLS //