ALR_RICBR
ID ALR_RICBR Reviewed; 410 AA.
AC Q1RGU4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, 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=RBE_1339;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05420.1; -; Genomic_DNA.
DR RefSeq; WP_011477989.1; NC_007940.1.
DR AlphaFoldDB; Q1RGU4; -.
DR SMR; Q1RGU4; -.
DR STRING; 336407.RBE_1339; -.
DR EnsemblBacteria; ABE05420; ABE05420; RBE_1339.
DR KEGG; rbe:RBE_1339; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_1_5; -.
DR OMA; HMTHFSD; -.
DR OrthoDB; 859043at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000001951; 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 InterPro; IPR005728; Rickett_RPE.
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 TIGRFAMs; TIGR01045; RPE1; 1.
PE 3: Inferred from homology;
KW Isomerase; Pyridoxal phosphate.
FT CHAIN 1..410
FT /note="Alanine racemase"
FT /id="PRO_0000272404"
FT DOMAIN 28..76
FT /note="RPE1 insert"
FT ACT_SITE 83
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 305
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 83
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ SEQUENCE 410 AA; 45476 MW; 91E898D4A3B5E1B6 CRC64;
MSLCTLEINL SAIKANYRLL KNICENSVDF LHNVANKEEF AGNTSPRTAA YTLVREDASL
GSTPKLPLGA SYAKNLLVGA AVKANSYGLG AIEISKTLLE ENCRYFFVAS SNEGISLRKA
IGDEVNILIL NGVFEHDALE LIEYNLIPVL NNLNQIKIWQ KFSNLKNQLL PCYLHFNTGI
NRLGLNHNEI EQLINNRDLL KGLNVEYIIS HLSASEDSDN PYNLEQLNKF KAYLEYFPNA
KASLANSGGI FLGKDYHFNL VRPGAALYGL NPLGSNKPNP MQNPVTLKAP IIHLQNLTYG
SRIGYNMTFT TKRDSLIATL PFGYADGFSR NFSNQGTVFI NSRNVPIIGR ISMDLVNIDV
TDLPPSDIFL GQEVEIIGNN CTPDKIADII GTIGYEILTS LGNRYKRIYT