ID F8AUZ4_9ACTN Unreviewed; 442 AA. AC F8AUZ4; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 24-JAN-2024, entry version 70. 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=FsymDg_3922 {ECO:0000313|EMBL:AEH11197.1}; OS Candidatus Protofrankia datiscae. OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; OC Protofrankia. OX NCBI_TaxID=2716812 {ECO:0000313|EMBL:AEH11197.1, ECO:0000313|Proteomes:UP000001549}; RN [1] {ECO:0000313|EMBL:AEH11197.1, ECO:0000313|Proteomes:UP000001549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4085684 {ECO:0000313|Proteomes:UP000001549}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A., RA Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.; RT "Complete sequence of chromosome of Frankia symbiont of Datisca RT glomerata."; RL Submitted (MAY-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; CP002801; AEH11197.1; -; Genomic_DNA. DR AlphaFoldDB; F8AUZ4; -. DR STRING; 656024.FsymDg_3922; -. DR KEGG; fsy:FsymDg_3922; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_0_0_11; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000001549; 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:UP000001549}. FT DOMAIN 251..378 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT REGION 377..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 40 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 272 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 320 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 442 AA; 44366 MW; 2919D5013DA8C90F CRC64; MTTQSEGLRA CAIVDLDAVR ASVATLVARA GNAATMAVVK SDGYGHGMSA CARAAVEAGA SWLGVAVIEE GLALRAAGFT VPVFAWLTAP GEPLADALAA DIDLSASAPW MLAEIAAAAR HTGRRARVHL KADTGLGRGG ATEADWPSLC DAAAALAAED LIEVTGVWSH LAFADSPGHP TVRGQIGRFA DAVTIAEKTG LRPQVRHLAN SAATLVSPDA RFDMVRPGIS VYGLSPGPQV GSPAALGLRP AMTLTARLAL AKRVPAGSGV SYAHRYTTAV ASTLGLVPLG YADGVPRAAG NTAEVLLAGR RRRIAGTVCM DQFVVDVGDD PVQAGDQVIL FGSGEHGEPT AQDWADALGT INYEIVTRVG VRVPRVHLNA SDGPRGTGRQ APGGPGAARP APGMAGSAPA AVGPSDAGLS GAGSSGPGLP GAGPSAPGWL PS //