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Database: UniProt
Entry: A0AH04
LinkDB: A0AH04
Original site: A0AH04 
ID   ALR_LISW6               Reviewed;         368 AA.
AC   A0AH04;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   16-JAN-2019, entry version 81.
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=lwe0868;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 /
OS   SLCC5334).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / SLCC5334;
RX   PubMed=16936040; DOI=10.1128/JB.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R.,
RA   Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T.,
RA   Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J.,
RA   Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W.,
RA   Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AM263198; CAK20286.1; -; Genomic_DNA.
DR   RefSeq; WP_011701704.1; NC_008555.1.
DR   ProteinModelPortal; A0AH04; -.
DR   SMR; A0AH04; -.
DR   STRING; 386043.lwe0868; -.
DR   EnsemblBacteria; CAK20286; CAK20286; lwe0868.
DR   KEGG; lwe:lwe0868; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; LWEL386043:G1GJF-895-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000779; 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; 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   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    368       Alanine racemase.
FT                                /FTId=PRO_1000066006.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   368 AA;  40948 MW;  2FF668FF305295DC CRC64;
     MVTGWHRPTW IEIDREAIRA NIKNEQHRLP ENVALWAVVK ANAYGHGIIE TAKTAKEAGA
     KGFCVAILDE ALALREAGFR NDFILVLGAT RQEDANLAAK NNISLTVFRE DWLHNLTLEA
     PLRIHLKVDS GMGRLGIRST EEAKQIEARI ALDHQLILEG IYTHFATADQ LETSYFEQQL
     DKFTTILTSF ESRPTFVHTA NSAASLLQPQ MDFDAVRFGI SMYGLTPSLE IKNSLPFELK
     PALALYTEMV HVKELAPGDS VSYGATYTAT EKEWVATLPI GYADGLIRHY SGYHVLVDGE
     LAPIIGRVCM DQTIIKLPRE FQTGSKVTII GTDHGNTITA DDAADYLGTI NYEVTCLLSD
     RIPRKYIN
//
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