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Database: UniProt/TrEMBL
Entry: E4UD03_LIBSC
LinkDB: E4UD03_LIBSC
Original site: E4UD03_LIBSC 
ID   E4UD03_LIBSC            Unreviewed;       348 AA.
AC   E4UD03;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=CKC_02470 {ECO:0000313|EMBL:ADR52243.1};
OS   Liberibacter solanacearum (strain CLso-ZC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52243.1, ECO:0000313|Proteomes:UP000007038};
RN   [1] {ECO:0000313|Proteomes:UP000007038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA   Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y.,
RA   Zhou L., Glynn J.;
RT   "Complete genome sequence of Candidatus Liberibacter solanacearum
RT   CLso-ZC1.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CLso-ZC1;
RA   Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y.,
RA   Zhou L., Glynn J.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP002371; ADR52243.1; -; Genomic_DNA.
DR   ProteinModelPortal; E4UD03; -.
DR   STRING; 658172.CKC_02470; -.
DR   EnsemblBacteria; ADR52243; ADR52243; CKC_02470.
DR   KEGG; lso:CKC_02470; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007038; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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 {ECO:0000313|Proteomes:UP000007038};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      213    348       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     15     15       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    234    234       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     112    112       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     293    293       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      15     15       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   348 AA;  37924 MW;  CEC2DD0BE1C71DF4 CRC64;
     MNVLSGCART AAVVKDNAYG LGFEKIAQTL YNSGVQDFFV AHVGEGVKLR AYVPKAKIFV
     LYGIHPGEEK ILFDANLIPV ISSSQQLTFY LKLMSNGFSH PYALQVDTGF NRLGLSLQEA
     LNFAKNFSNK KSDKLSLIMS HLACSEDPVS LMNSSQLEQF LTLMKSYKGI EASLASSAGI
     LLGENYHFQL TRPGISLYGG TPAINKLNPM QTVVTAEARI ILIREAAAGE VISYGGQKKL
     KRNSLIAVAA IGYADGYPLT LSGIDLEHNQ AQFPGGKGFI KGYMVPILGK ITMDITMFDI
     TDSIGIEAGD YIEVFGPNIK LDDVALASRT TNYDLLVRIG TRYARFYT
//
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