ID A0A6L7HC45_BACAN Unreviewed; 389 AA. AC A0A6L7HC45; A0A0F7R3Y0; E9R9C7; E9R9C8; Q6I4F7; Q6KY59; Q81VF6; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 27-MAR-2024, entry version 16. 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=dal1 {ECO:0000313|EMBL:AAT29333.1}; GN OrderedLocusNames=GBAA_0252 {ECO:0000313|EMBL:AAT29333.1}; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAT29333.1, ECO:0000313|Proteomes:UP000000594}; RN [1] {ECO:0007829|PDB:2VD8, ECO:0007829|PDB:2VD9} RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-41. RX PubMed=18453697; DOI=10.1107/s1744309108007252; RA Au K., Ren J., Walter T.S., Harlos K., Nettleship J.E., Owens R.J., RA Stuart D.I., Esnouf R.M.; RT "Structures of an alanine racemase from Bacillus anthracis (BA0252) in the RT presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P)."; RL Acta Crystallogr. F Struct. Biol. Commun. 64:327-333(2008). RN [2] {ECO:0007829|PDB:3HA1} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). RX PubMed=19695097; DOI=10.1186/1472-6807-9-53; RA Counago R.M., Davlieva M., Strych U., Hill R.E., Krause K.L.; RT "Biochemical and structural characterization of alanine racemase from RT Bacillus anthracis (Ames)."; RL BMC Struct. Biol. 9:53-53(2009). RN [3] {ECO:0000313|EMBL:AAT29333.1, ECO:0000313|Proteomes:UP000000594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor {ECO:0000313|Proteomes:UP000000594}; RX PubMed=18952800; DOI=10.1128/JB.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). 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; AE017334; AAT29333.1; -; Genomic_DNA. DR RefSeq; WP_000390596.1; NZ_WXXJ01000025.1. DR PDB; 2VD8; X-ray; 1.47 A; A/B=1-389. DR PDB; 2VD9; X-ray; 2.10 A; A/B=1-389. DR PDB; 3HA1; X-ray; 1.95 A; A/B=1-389. DR AlphaFoldDB; A0A6L7HC45; -. DR SMR; A0A6L7HC45; -. DR IntAct; A0A6L7HC45; 3. DR GeneID; 45020290; -. DR KEGG; bar:GBAA_0252; -. DR PATRIC; fig|1392.230.peg.248; -. DR OMA; WEILCGF; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000000594; Chromosome. DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2VD8, ECO:0007829|PDB:2VD9}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201}; KW Metal-binding {ECO:0007829|PDB:2VD8, ECO:0007829|PDB:2VD9}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP- KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000000594}. FT DOMAIN 249..374 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 41 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 270 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 17 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 41 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 45 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 138 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 209 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 224 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 226 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 227 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 359 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0007829|PDB:2VD8" FT MOD_RES 41 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 389 AA; 43662 MW; 5B55B2C4920D6BA5 CRC64; MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KGNAYGHDYV PVAKIALEAG ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF DKQYNTFLEQ LSWLKEFGVD PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP FLPFKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF EVLVNGKRVP IVGRVTMDQF MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE IITTISFRVP RIFIRNGKVV EVINYLNDI //