ID   ALR_SULNB               Reviewed;         336 AA.
AC   A6QC54;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SUN_2123;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
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DR   EMBL; AP009179; BAF73063.1; -; Genomic_DNA.
DR   RefSeq; WP_012083893.1; NC_009663.1.
DR   AlphaFoldDB; A6QC54; -.
DR   SMR; A6QC54; -.
DR   STRING; 387093.SUN_2123; -.
DR   EnsemblBacteria; BAF73063; BAF73063; SUN_2123.
DR   KEGG; sun:SUN_2123; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_7; -.
DR   OMA; HMTHFSD; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006378; 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; 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.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..336
FT                   /note="Alanine racemase"
FT                   /id="PRO_1000138629"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        243
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   336 AA;  37520 MW;  DB0D9848889E8AD3 CRC64;
     MATIIINKEN FYHNLNQIAL KTGSVEKIAI VLKDNAYGHG LQLMASLSAE FGIRHAVVRS
     MEEAKNIKEL FRTVLVLGDH AVKDDICSFA LNCLNDIENA ELGARVELKV DTGMHRNGIA
     PEELERALQM IQKKDLELVG VMTHFRSADE MGSELFWQQK QFASVKERVK EAGFMNVRFH
     SHNSAATLRS KTFDEDLVRV GIGAYGYNEL PDVFDDIPLK PVLSLSAKKI ATRRLKKGER
     VGYGGDFTAP EEMTVSTYDL GYGDGWCRGD SAHPYITAEG LPILGRVSMD FIILESAKEE
     LVIMNDAQKA ARQFGTISYE MTTALSINIE RKIVDR