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Database: UniProt
Entry: A0A2C1Z628_9BACI
LinkDB: A0A2C1Z628_9BACI
Original site: A0A2C1Z628_9BACI 
ID   A0A2C1Z628_9BACI        Unreviewed;       776 AA.
AC   A0A2C1Z628;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-DEC-2018, entry version 5.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=COD92_09275 {ECO:0000313|EMBL:PGV52860.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV52860.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV52860.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV52860.1,
RC   ECO:0000313|Proteomes:UP000225442};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers
RT   conserved roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PGV52860.1}.
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DR   EMBL; NUNF01000016; PGV52860.1; -; Genomic_DNA.
DR   Proteomes; UP000225442; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 2.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000225442};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000313|EMBL:PGV52860.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225442}.
FT   DOMAIN       41    190       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      273    390       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      429    580       BetaGal_dom2. {ECO:0000259|Pfam:PF10435}.
SQ   SEQUENCE   776 AA;  89008 MW;  BA55E7013FE1E1D6 CRC64;
     MRAYRIDVKN TQKEIYPLET KLGGSNIAGE NYSFTNYYME KNGRPFFGIS GEFHFSRYNF
     EKWEDEIIKM KMGGINIIPT YIFWNHHEEE QGIFDWEANK NLRRFVGLCR KHGMGVILRI
     GPFAHGEARN GGIPDWLFGR PFDLRSNDKE YLTYVKRFYQ EIGKQVQGFL FKEGGPIIGT
     QIENEYEHAG APWEITNGTG NEWVPAGRDG DVHIITLKEL AIQAGIQTPI YTSTGWGGAA
     APVEEVLPLW GGYAFWPWIF YGDVKEHPAT PEFIFRDYHN DQQKNYGFTP AYRPESLSFA
     CCEMGGGMTV FYKYRFKLPY ESVDAMAEMK VAGGCNFVGY YVFHGGSNPK GKKTPFLNEN
     ATPKISYDYQ APIGEFGQIR ESYKRLKRQH YFYKTVEESF CKTKTVLPYD TKDMDPYDIE
     TLRFAVRANR DSGFVFINNY QDHVETKDQQ DFAITVNLEN EEIRLPKSDS MSLAKDECCI
     LPFNLDLQGL NLKYSTTQLL TSIEHDGEIY FFFFIPKGMN GEYYFESDDI QEVSVDNGNI
     ISDENTLIQV SNQEISLIDI MLQTGRRLHV CTLTNEQSLN FWKYPYGGKE QVFITNATLL
     VAGEKIRLES AGLESVEIKS FPGFNGMLKI TGEELSCHNH GLFKEYKKII NVSHTGLEVK
     MVNHNKAVIH FQPEAFDDVK ELLLQIEYVG DIGYAFIDGK LIHDNFCNND IWEIGLQQHK
     QDLLAKGMYI YISPLKEESF VKSDSPMAAR AEVITKQIAE IKSIKATAIR ELEIDI
//
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