ID ALR_HAEIN Reviewed; 360 AA.
AC P45257;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 01-MAY-2013, entry version 99.
DE RecName: Full=Alanine racemase;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=HI_1575;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC23218.1; -; Genomic_DNA.
DR PIR; E64130; E64130.
DR RefSeq; NP_439721.1; NC_000907.1.
DR ProteinModelPortal; P45257; -.
DR SMR; P45257; 4-360.
DR STRING; 71421.HI1575; -.
DR EnsemblBacteria; AAC23218; AAC23218; HI_1575.
DR GeneID; 950435; -.
DR KEGG; hin:HI1575; -.
DR PATRIC; 20191881; VBIHaeInf48452_1648.
DR eggNOG; COG0787; -.
DR KO; K01775; -.
DR OMA; NFKSIEI; -.
DR ProtClustDB; PRK00053; -.
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 1 360 Alanine racemase.
FT /FTId=PRO_0000114522.
FT ACT_SITE 36 36 Proton acceptor; specific for D-alanine
FT (By similarity).
FT ACT_SITE 256 256 Proton acceptor; specific for L-alanine
FT (By similarity).
FT BINDING 132 132 Substrate (By similarity).
FT BINDING 304 304 Substrate; via amide nitrogen (By
FT similarity).
FT MOD_RES 36 36 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 360 AA; 39705 MW; A9FF1283C56AD71B CRC64;
MNVKPATAKI SSHALKQNLE IIKQKAPNSK IIAVVKANAY GHGVVFVAST LEQNVDCFGV
ARLEEALALR SNGITKPILL LEGFFNEQDL PILAVNNIET VVHNHEQLDA LKRANLPSPI
KVWLKIDTGM HRLGVALDEV DYFYQELKKL PQIQPHLGFV SHFSRADELE SDYTQLQINR
FLSVTKDKQG ERTIAASGGI LFWPKSHLEC IRPGIIMYGI SPTDTIGKEF GLTPVMNLTS
SLIAVRHHKQ GDPVGYGGIW TSPRDTKIGV VAMGYGDGYP RDVPEGTPVY LNGRLVPIVG
RVSMDMLTVD LGADSQDLVG DEVILWGKEL PIETVAKFTG ILSYELITKL TPRVITEYVD
//
