ALR_AQUPY
ID ALR_AQUPY Reviewed; 341 AA.
AC Q9RER4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
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;
OS Aquifex pyrophilus.
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=2714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND PATHWAY.
RA Kim S.S., Yu Y.G.;
RT "Molecular cloning of an extremely thermostable alanine racemase from
RT Aquifex pyrophilus and enzymatic characterization of the expressed
RT protein.";
RL J. Biochem. Mol. Biol. 33:82-88(2000).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC {ECO:0000269|Ref.1}.
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, ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01201, ECO:0000269|Ref.1};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201,
CC ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: Strong thermostability.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
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DR EMBL; AF212103; AAF23014.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RER4; -.
DR SMR; Q9RER4; -.
DR UniPathway; UPA00042; UER00497.
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 1: Evidence at protein level;
KW Isomerase; Pyridoxal phosphate.
FT CHAIN 1..341
FT /note="Alanine racemase"
FT /id="PRO_0000114496"
FT ACT_SITE 33
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 236
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 284
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 341 AA; 39014 MW; B90B63A00C0EE1EF CRC64;
MRRAVLEILE ERIIHNVKEI HRFSGKRIIA VVKANAYGIG VREVSRILEG LEEVDAFAVA
CTQEGVELRE CGIKKKILIL GGILEEDVKL LEEYDLTPVI SDPEHLKVLK DRNIKFHVKY
DTGMGRLGFT NEIIKDPRVE GVMSHFSSPA DRNFSKLQIK RFEEILKNYE KVKYIHLESS
AGLIYRVPFT THVRVGLAIY GEKPLKDYPL EVKPALRLRA RLISVKELPE NYPVSYGRTY
ITKRKTKLGV VAFGYADGLM KTLSNRSFLI FEGRKVPIIG NITMDMTMVD LSGTEARTGD
WVYIVNEERS FTPLARDAGT IPYEIMCNLS RRVERLVIKK R
