ID H2IYL6_RAHAC Unreviewed; 357 AA. AC H2IYL6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, 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 OrderedLocusNames=Rahaq2_2166 {ECO:0000313|EMBL:AEX52027.1}; OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / OS NCIMB 13365 / CIP 78.65). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Rahnella. OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX52027.1, ECO:0000313|Proteomes:UP000009010}; RN [1] {ECO:0000313|EMBL:AEX52027.1, ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RX PubMed=22582378; DOI=10.1128/JB.00380-12; RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S., RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S., RA Tapia R., Woyke T., Sobecky P.A.; RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65."; RL J. Bacteriol. 194:3020-3021(2012). RN [2] {ECO:0000313|Proteomes:UP000009010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 / RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P., RA Martinez R., Woyke T.; RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65."; RL Submitted (JAN-2012) 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; CP003244; AEX52027.1; -; Genomic_DNA. DR RefSeq; WP_015697199.1; NZ_JMPO01000047.1. DR AlphaFoldDB; H2IYL6; -. DR STRING; 745277.Rahaq2_2166; -. DR GeneID; 61512230; -. DR KEGG; raq:Rahaq2_2166; -. DR PATRIC; fig|745277.3.peg.2086; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_1_0_6; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000009010; 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; cd06827; PLPDE_III_AR_proteobact; 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:UP000009010}. FT DOMAIN 232..356 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 35 FT /note="Proton acceptor; specific for D-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT ACT_SITE 253 FT /note="Proton acceptor; specific for L-alanine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 301 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 35 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 357 AA; 38340 MW; AC74F197C90E2193 CRC64; MPRPISATLS LSALTQNLNI IRGFAPNSKV WTVVKANGYG HGISRIWRSL SATDGFALLD FNEAILLRES GWQGPILLLE GFFTAEDLAM VDHYRLTTSI HSEWQIKALA QASVSQPVSI YLKVNSGMNR LGFAPERAGA VWQQLRELKQ VGEITLMSHF ATADSVEGVD AQMTVINLAG QNIRGPRCLA NSAATLWHPH THHDWIRPGI IIYGASPSGE WNDIAHTGLQ PVMTLKSELI AIQELNAGAR VGYGGRYSVT SPQRIGVVAC GYADGYPRHA PSGTPVWVDG VRTTTTGTVS MDMLAVDLTP CPQAQIGAPV ELWGNNLPVD DVATAAGTLG YELLSALAPR VPVSTIG //