GenomeNet

Database: UniProt
Entry: Q75FF2
LinkDB: Q75FF2
Original site: Q75FF2 
ID   ALR_LEPIC               Reviewed;         389 AA.
AC   Q75FF2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 94.
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=LIC_20241;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar
OS   copenhageni (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A.,
RA   Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H.,
RA   Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H.,
RA   Ferro E.S., Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A.,
RA   Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R.,
RA   Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T.,
RA   Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R.,
RA   de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals
RT   novel insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016824; AAS72263.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q75FF2; -.
DR   SMR; Q75FF2; -.
DR   STRING; 267671.LIC20241; -.
DR   PaxDb; Q75FF2; -.
DR   PRIDE; Q75FF2; -.
DR   EnsemblBacteria; AAS72263; AAS72263; LIC_20241.
DR   KEGG; lic:LIC_20241; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007037; Chromosome II.
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    389       Alanine racemase.
FT                                /FTId=PRO_0000114530.
FT   ACT_SITE     48     48       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    281    281       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     144    144       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     329    329       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      48     48       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   389 AA;  43277 MW;  B2632B05490DBB3D CRC64;
     MQDINSGSSS MKDTYSSWIE ISKRSLSNNL DNFRSILRPN STLTAILKSN AYGHGIEPMT
     RLCIEAGISR IGVNSIEEAL LIRNIDSKIP ILIMGEIQNP EKRKNVLSDP NFWIVFSRPE
     TARILSSFLP APKLHLKIDT GMGRLGSHGE TLKQTLSELK NVGITLGGIC THFASTEDVL
     EHKYSLMQTQ KFEEAIFLAK SFGYNHLIRH ACASASTMLF PNAHFDMVRI GISLYGLWPS
     IQTRLSLNLT GNKNFQLNPI LSWKSRIVHI QYHPADSYIG YGSTFQTSYP TKVAIVPVGY
     YEGLDRKLSS NGDMLVLGKK ARIIGRICMN MTMLDVTHIP GAEVGSIVTI IGQDGEESIT
     ADDLADRTHT INYEVMTRIS ESIPRIVVD
//
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