ID E2XIE2_SHIDY Unreviewed; 165 AA.
AC E2XIE2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Alanine racemase, catabolic {ECO:0000256|ARBA:ARBA00040146};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=Asd1617_01605 {ECO:0000313|EMBL:AHA64432.1};
OS Shigella dysenteriae 1617.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA64432.1, ECO:0000313|Proteomes:UP000031647};
RN [1] {ECO:0000313|EMBL:AHA64432.1, ECO:0000313|Proteomes:UP000031647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1617 {ECO:0000313|EMBL:AHA64432.1,
RC ECO:0000313|Proteomes:UP000031647};
RA Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA Hale T.L., Mason C.J.;
RT "Comparative genomics of Sd1617 to representative strains in evaluating its
RT pathogenesis.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to
CC pyruvate by DadA. {ECO:0000256|ARBA:ARBA00037715}.
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:0000256|ARBA:ARBA00000316};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006736; AHA64432.1; -; Genomic_DNA.
DR AlphaFoldDB; E2XIE2; -.
DR KEGG; sdz:Asd1617_01605; -.
DR PATRIC; fig|754093.4.peg.1566; -.
DR HOGENOM; CLU_132462_0_0_6; -.
DR Proteomes; UP000031647; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AHA64432.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 10..149
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 165 AA; 18709 MW; 435EF9ACA9232F19 CRC64;
MTRPIQASLD LQALKQNLSI VRQAAPHARV WSVVKANAYG HGIERIWSAL GATDGFALLN
LEEAITLRER GWKGPILMLE GFFHAQDLEI YDQHRLTTCV HSNWQLKALQ NARLKAPLDI
YLKVNSGMNR LGFQPDRVLT VWQQLRASEC WRNDLDVAFC RGGTS
//
