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Database: UniProt
Entry: Q93HP9
LinkDB: Q93HP9
Original site: Q93HP9 
ID   ALR1_SHISO              Reviewed;         359 AA.
AC   Q93HP9;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JAN-2019, entry version 96.
DE   RecName: Full=Alanine racemase, biosynthetic;
DE            EC=5.1.1.1;
GN   Name=alr;
OS   Shigella sonnei.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=624;
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
RT   sonnei.";
RL   Biochem. Biophys. Res. Commun. 288:676-684(2001).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       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-
CC       alanine 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}.
DR   EMBL; AB070928; BAB71773.1; -; Genomic_DNA.
DR   RefSeq; WP_001147324.1; NZ_UIQX01000055.1.
DR   ProteinModelPortal; Q93HP9; -.
DR   SMR; Q93HP9; -.
DR   BRENDA; 5.1.1.1; 5713.
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   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   Cell shape; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Isomerase; Peptidoglycan synthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    359       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114566.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     129    129       Substrate. {ECO:0000250}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   359 AA;  39165 MW;  E7C0B4380B7A491B CRC64;
     MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL
     EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW
     MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT
     FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSIGADFG CQPVMSLTSS
     LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
     VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD
//
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