ID ALR_LISMO Reviewed; 368 AA.
AC P0DJL8; O85045;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 01-MAY-2013, entry version 9.
DE RecName: Full=Alanine racemase;
DE EC=5.1.1.1;
GN Name=alr; Synonyms=dal; OrderedLocusNames=lmo0886;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC alanine. May also act on other amino acids (By similarity).
CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC alanine from L-alanine: step 1/1.
CC -!- SIMILARITY: Belongs to the alanine racemase family.
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DR EMBL; AL591977; CAC98964.1; -; Genomic_DNA.
DR PIR; AF1185; AF1185.
DR RefSeq; NP_464412.1; NC_003210.1.
DR ProteinModelPortal; P0DJL8; -.
DR SMR; P0DJL8; 4-367.
DR EnsemblBacteria; CAC98964; CAC98964; CAC98964.
DR GeneID; 986294; -.
DR KEGG; lmo:lmo0886; -.
DR GenoList; LMO0886; -.
DR eggNOG; COG0787; -.
DR HOGENOM; HOG000031444; -.
DR KO; K01775; -.
DR OMA; IRLPKAY; -.
DR UniPathway; UPA00042; UER00497.
DR GO; GO:0008784; F:alanine racemase activity; IEA:EC.
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 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 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; Racem_decarbox_C; 1.
DR TIGRFAMs; TIGR00492; alr; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1 368 Alanine racemase.
FT /FTId=PRO_0000114534.
FT ACT_SITE 40 40 Proton acceptor; specific for D-alanine
FT (By similarity).
FT ACT_SITE 263 263 Proton acceptor; specific for L-alanine
FT (By similarity).
FT BINDING 134 134 Substrate (By similarity).
FT BINDING 310 310 Substrate; via amide nitrogen (By
FT similarity).
FT MOD_RES 40 40 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 368 AA; 40987 MW; 589812C3014193F7 CRC64;
MVTGWHRPTW IEIDRAAIRE NIKNEQNKLP ESVDLWAVVK ANAYGHGIIE VARTAKEAGA
KGFCVAILDE ALALREAGFQ DDFILVLGAT RKEDANLAAK NHISLTVFRE DWLENLTLEA
TLRIHLKVDS GMGRLGIRTT EEARRIEATS TNDHQLQLEG IYTHFATADQ LETSYFEQQL
AKFQTILTSL KNRPTYVHTA NSAASLLQPQ IGFDAIRFGI SMYGLTPSTE IKTSLPFELK
PALALYTEMV HVKELAPGDS VSYGATYTAT EREWVATLPI GYADGLIRHY SGFHVLVGGE
LAPIIGRVCM DQTIIKLPRE FQTGSKVTII GKDHGNTITA DDAAQYLDTI NYEVTCLLNE
RIPRKYIH
//
