ID ALR1_SHIDY Reviewed; 359 AA.
AC Q932V0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=Alanine racemase, biosynthetic;
DE EC=5.1.1.1;
GN Name=alr;
OS Shigella dysenteriae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21.
RX PubMed=11676496; DOI=10.1006/bbrc.2001.5817;
RA Yokoigawa K., Hirasawa R., Ueno H., Okubo Y., Umesako S., Soda K.;
RT "Gene cloning and characterization of alanine racemases from Shigella
RT dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei.";
RL Biochem. Biophys. Res. Commun. 288:676-684(2001).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-10.;
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.;
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBUNIT: Monomer but homodimer in the presence of the substrate.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
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DR EMBL; AB069859; BAB71770.1; -; Genomic_DNA.
DR RefSeq; WP_001147344.1; NZ_UYIT01000003.1.
DR AlphaFoldDB; Q932V0; -.
DR SMR; Q932V0; -.
DR BRENDA; 5.1.1.1; 5711.
DR UniPathway; UPA00042; UER00497.
DR UniPathway; UPA00219; -.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd06827; PLPDE_III_AR_proteobact; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF4; ALANINE RACEMASE, BIOSYNTHETIC; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate.
FT CHAIN 1..359
FT /note="Alanine racemase, biosynthetic"
FT /id="PRO_0000114564"
FT ACT_SITE 34
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 255
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 39081 MW; D49583FB6D640394 CRC64;
MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL
EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW
MKLDTGMHRL GVRPEQAGAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT
FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS
LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD
//
