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Database: UniProt/TrEMBL
Entry: A0A0E3KT95_CORUL
LinkDB: A0A0E3KT95_CORUL
Original site: A0A0E3KT95_CORUL 
ID   A0A0E3KT95_CORUL        Unreviewed;       370 AA.
AC   A0A0E3KT95;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 19.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AKA96011.1};
GN   ORFNames=CUL131002_0463 {ECO:0000313|EMBL:AKA96011.1};
OS   Corynebacterium ulcerans.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=65058 {ECO:0000313|EMBL:AKA96011.1, ECO:0000313|Proteomes:UP000033037};
RN   [1] {ECO:0000313|EMBL:AKA96011.1, ECO:0000313|Proteomes:UP000033037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=131002 {ECO:0000313|EMBL:AKA96011.1,
RC   ECO:0000313|Proteomes:UP000033037};
RA   Benevides L.J., Viana M.V.C., Mariano D.C., Rocha F.S., Bagano P.,
RA   Folador E.L., Pereira F.L., Dorella F.A., Leal C.A., Carvalho A.F.,
RA   Soares S.C., Carneiro A.R., Ramos R.T.J., Silva A., Figueiredo H.C.,
RA   Azevedo V., Guimaraes L.;
RL   Submitted (MAR-2015) 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}.
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}.
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DR   EMBL; CP011095; AKA96011.1; -; Genomic_DNA.
DR   RefSeq; WP_046095545.1; NZ_CP011095.1.
DR   STRING; 945712.CULC22_00462; -.
DR   EnsemblBacteria; AKA96011; AKA96011; CUL131002_0463.
DR   KEGG; cuj:CUL131002_0463; -.
DR   PATRIC; fig|65058.63.peg.457; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000033037; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000033037};
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      241    367       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     36     36       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   370 AA;  39700 MW;  C77E4D8C7346A06C CRC64;
     MNLLEARIDL DAIAHNTRLI KDKAAAQGAQ LMCVVKADGY NHGAVEVATV MEDNGADQFG
     VATIREALAL REGGIESSIL SWIWSPEQDL GAAIAAGIDL AAISLAHVKA LVRASESYGE
     NPVRVTVKVD TGLHRSGVDK QDWEEAFCAL RDAENIQVTG VFSHFSSADE SDSPETEQQV
     EAFLAAIELG RSLGLELPVN HIANSPATLN RPDLYFDMVR PGLALYGHEP IPGENHGLRE
     AMSWVGRVTV VKPIAKGEGT SYNLTWRAEQ GGYLCVVPVG YADGLPRSAQ GHLEVTIGGR
     RYPQVGRVCM DQIVVSLGEN PHGVAQGDEA VILGPTGMTA TELATAIGTI NYELVCRPCG
     RTVRVFEHRD
//
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