ID   ALR1_SHIBO              Reviewed;         359 AA.
AC   P0A6B6; P29743; P78136;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   26-MAY-2009, entry version 23.
DE   RecName: Full=Alanine racemase, biosynthetic;
DE            EC=5.1.1.1;
GN   Name=alr;
OS   Shigella boydii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21, AND
RP   CHARACTERIZATION.
RX   MEDLINE=21534269; 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: Provides the D-alanine required for cell wall
CC       biosynthesis.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR: Pyridoxal phosphate.
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.
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DR   EMBL; AB070926; BAB71771.1; -; Genomic_DNA.
DR   HSSP; P10724; 1BD0.
DR   BRENDA; 5.1.1.1; 96885.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:HAMAP.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_01201; -; 1.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR000821; Ala_racemase_reg.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
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_0000114563.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   359 AA;  39153 MW;  FDE9B438115342C2 CRC64;
     MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL
     EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW
     MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT
     FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS
     LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
     VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD
//