ID   ALR_SHELP               Reviewed;         358 AA.
AC   A3QI45;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Shew_3277;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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: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; CP000606; ABO25143.1; -; Genomic_DNA.
DR   RefSeq; WP_011867073.1; NC_009092.1.
DR   AlphaFoldDB; A3QI45; -.
DR   SMR; A3QI45; -.
DR   STRING; 323850.Shew_3277; -.
DR   EnsemblBacteria; ABO25143; ABO25143; Shew_3277.
DR   KEGG; slo:Shew_3277; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_6; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001558; 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..358
FT                   /note="Alanine racemase"
FT                   /id="PRO_1000164615"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        255
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   358 AA;  38734 MW;  7F18670DFAD1099D CRC64;
     MKPFPRAEIS GDALKANLKR LRQLAPQSKV MAVVKANGYG HGLLNVAHCL ASADGFGLAR
     LEEALELRAG GVSAKLLLLE GFFRPSDVAT LVEHDIDTVV HHESQLEMLE AASLAKPVTV
     WMKIDTGMHR LGFNLDQFEA IYQRLQACAN VAKPINLMTH FACADEPDNP ATAEQARRFE
     QMTANLPGDR TLANSAATLY WQATQADWIR PGIALYGVSP VVGDLGRNHG LEPAMELVSQ
     LIAVRDHKAG DPVGYGSYWR AKQDTKLGVV AIGYGDGYPR NAPEGTPVWV NGRLVPVVGR
     VSMDMLTVDL GLDATDKVGD TAVLWGKALP VEEVAEHIGT IAYELVTKLT PRVAVCLE