ID E4RPE3_HALHG Unreviewed; 377 AA. AC E4RPE3; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 76. 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=Halsa_0353 {ECO:0000313|EMBL:ADQ13828.1}; OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)). OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ13828.1, ECO:0000313|Proteomes:UP000007434}; RN [1] {ECO:0000313|EMBL:ADQ13828.1, ECO:0000313|Proteomes:UP000007434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.; RT "Complete sequence of Halanaerobium sp. sapolanicus."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ13828.1, ECO:0000313|Proteomes:UP000007434} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434}; RX PubMed=21602336; DOI=10.1128/JB.05209-11; RA Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A., RA Pitluck S., Land M.L., Hauser L.J., Elias D.A.; RT "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing RT Halanaerobium hydrogenoformans."; RL J. Bacteriol. 193:3682-3683(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; CP002304; ADQ13828.1; -; Genomic_DNA. DR RefSeq; WP_013404934.1; NC_014654.1. DR AlphaFoldDB; E4RPE3; -. DR STRING; 656519.Halsa_0353; -. DR KEGG; has:Halsa_0353; -. DR eggNOG; COG0787; Bacteria. DR HOGENOM; CLU_028393_2_2_9; -. DR OrthoDB; 9813814at2; -. DR UniPathway; UPA00042; UER00497. DR Proteomes; UP000007434; 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:UP000007434}. FT DOMAIN 249..377 FT /note="Alanine racemase C-terminal" FT /evidence="ECO:0000259|SMART:SM01005" FT ACT_SITE 43 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 141 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-52" FT MOD_RES 43 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201, FT ECO:0000256|PIRSR:PIRSR600821-50" SQ SEQUENCE 377 AA; 41849 MW; FD06B63011385E11 CRC64; MLKKLEKSKR PVWVEIDLNN LKFNIKEIKK TLNSDTIFTA VVKADGYGHG AVPTAEAAIE AGADRLAVAI PEEGIELREA GIAAPIEILG ELLPEQLPEL IRYDLIPTIS KFKTAERLNN LCAGYNLKKK IHLNIDTGMN RVGVNYKKAL PLLKKITELP NLEIEGIMTH FARADELEKE YTLIQWERFN QLIEKLEAEN IEIPIKHCAN SAAVIDFPEF ALDMVRAGIM IYGLKPSPDL KNNFNLKAVL SWKSRIVRLK DVPAGEGISY GSEYITPKRE KIATIPLGYA DGYARILGNK ASVLVKGKRA PIRGRICMDQ FMVDVSGIEG VKVGDEVVLI GSQNGLSLSA DKLAEQAGTI NYEIVSRISK RVARIYK //