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Database: UniProt/TrEMBL
Entry: A0A0N1R196_SALSV
LinkDB: A0A0N1R196_SALSV
Original site: A0A0N1R196_SALSV 
ID   A0A0N1R196_SALSV        Unreviewed;       346 AA.
AC   A0A0N1R196;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
DE   AltName: Full=Galactose mutarotase {ECO:0000256|PIRNR:PIRNR005096};
GN   Name=galM {ECO:0000313|EMBL:ACF92860.1};
GN   OrderedLocusNames=SeSA_A0923 {ECO:0000313|EMBL:ACF92860.1};
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843 {ECO:0000313|EMBL:ACF92860.1, ECO:0000313|Proteomes:UP000001865};
RN   [1] {ECO:0000313|EMBL:ACF92860.1, ECO:0000313|Proteomes:UP000001865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633 {ECO:0000313|EMBL:ACF92860.1,
RC   ECO:0000313|Proteomes:UP000001865};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- FUNCTION: Converts alpha-aldose to the beta-anomer.
CC       {ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucose = beta-D-glucose.
CC       {ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|PIRNR:PIRNR005096}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family.
CC       {ECO:0000256|PIRNR:PIRNR005096}.
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DR   EMBL; CP001127; ACF92860.1; -; Genomic_DNA.
DR   RefSeq; WP_000931425.1; NC_011094.1.
DR   ProteinModelPortal; A0A0N1R196; -.
DR   EnsemblBacteria; ACF92860; ACF92860; SeSA_A0923.
DR   KEGG; sew:SeSA_A0923; -.
DR   KO; K01785; -.
DR   OMA; ATWLSCK; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001865; Chromosome.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR013458; Ald_epimerase_bac.
DR   InterPro; IPR015443; Aldose_1-epimerase.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   TIGRFAMs; TIGR02636; galM_Leloir; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001865};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR005096,
KW   ECO:0000313|EMBL:ACF92860.1}.
FT   ACT_SITE    175    175       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR005096-1}.
FT   ACT_SITE    309    309       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR005096-1}.
FT   BINDING     245    245       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005096-2}.
SQ   SEQUENCE   346 AA;  38561 MW;  891E37870BD7F602 CRC64;
     MLNETPALAP DGQPYRLLTL RNSAGMVVTL MDWGATLLSA RIPLSDGSVR EALLGCASPE
     HYPEQTSFLG ASIGRYANRI ANSRYTFAGE TVQLSPSQGE NQLHGGPEGF DKRRWQIVNQ
     NDRQVLFALT SDDGDQGFPG HLCATAQYRL TDDNRISITY RATVDKPCPV NLTNHVYFNL
     DGDRTDVRQH KLQILADEYL PVDESGIPRQ GLKSVANTSF DFRMPKIIAS EFLADDDQRK
     VKGYDHAFLL QTQGDGKKPA ARLWSQDGKL QMMVYTTAPA LQFYSGNYLA GTPSRGPEPY
     ADWQGLALES ELLPDSPNHP EWPQPDCILR PGEEYASLTE YQFIPF
//
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