ID   ALR_HALOH               Reviewed;         379 AA.
AC   B8D0W1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Hore_01680;
OS   Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halothermothrix.
OX   NCBI_TaxID=373903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H 168 / OCM 544 / DSM 9562;
RX   PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA   Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA   Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT   "Genome analysis of the anaerobic thermohalophilic bacterium
RT   Halothermothrix orenii.";
RL   PLoS ONE 4:E4192-E4192(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|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; CP001098; ACL68930.1; -; Genomic_DNA.
DR   RefSeq; WP_012635128.1; NC_011899.1.
DR   AlphaFoldDB; B8D0W1; -.
DR   SMR; B8D0W1; -.
DR   STRING; 373903.Hore_01680; -.
DR   EnsemblBacteria; ACL68930; ACL68930; Hore_01680.
DR   KEGG; hor:Hore_01680; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OMA; HMTHFSD; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000719; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Alanine racemase"
FT                   /id="PRO_1000164600"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        267
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   379 AA;  42138 MW;  4B8C82F948689246 CRC64;
     MNKRITRPTW AEIDLSCLQF NFNQVKEILG SNVKIMSVVK ADAYGHGVIP VAKTLVEAGT
     QRLAVAIPEE GVELREAGLS VPIQVLGEVL PSQYELLFKY DLIPTVGREE TALSLNRLAA
     KYNVVKKVHI KVDTGMGRIG VRPREAVGFV KKVNSLSNIK IEGLMTHFAS ADERDKSYTY
     EQWDKFKQVL DGLNKLRIDI PIKHSSNSAA IIDFKKFGLD MVRPGIMLYG LKPSRDLINN
     IDLKPVLTWK TRIVYLKEVP PGTGISYGTT YVTNRKSKIA TLPVGYADGY PRILSNQGQV
     LVRGRKAPIR GRVCMDQIMI DVTEIPDVRV GDEVVLIGEQ GTQKISATDI AEKADTINYE
     IVCGISQRVP REYKNKIGG