ALR_FRATM
ID ALR_FRATM Reviewed; 365 AA.
AC B2SHB9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=FTM_1271;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(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}.
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DR EMBL; CP000915; ACD31127.1; -; Genomic_DNA.
DR RefSeq; WP_012429679.1; NC_010677.1.
DR AlphaFoldDB; B2SHB9; -.
DR SMR; B2SHB9; -.
DR KEGG; ftm:FTM_1271; -.
DR HOGENOM; CLU_028393_2_2_6; -.
DR OMA; WEILCGF; -.
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; 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.
FT CHAIN 1..365
FT /note="Alanine racemase"
FT /id="PRO_1000138599"
FT ACT_SITE 32
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 257
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 32
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 365 AA; 41432 MW; 90F5F4FE7B8BA060 CRC64;
MNILKISKQT LRNNIKIIRE YIGNAKMCFP VKANAYGHGI EDIVENTHDL VDFFAVANSL
EAFRVTAVAK NPVLVFGVIY YEYIEKMISE NIRVSIQDYE DIEKLEQIAK ELDKKVYAHI
NINTGMNRMG VNYNDACRTI QRAYESDWLI LEGVYSHLAC ADNRDHPTNI KQKNRFDSIV
KFTKGLSQDI ICHLSNSYGF LGQKGICYDM VRPGILSYGF LPEFYVDRVI REIKPIARLL
SKVVKIITLQ EGEGVGYSLI YRGFEGEQLA VIPIGYGDGF PRELGDRGFV NINDVMYPMA
GRMSMDGLTV SLGINEYDVK VGDTVELISA IPRNRNSAFS IAKQTNTIEY DIMSTLNDRI
IRKII