(data stored in ACNUC7421 zone)

SWISSPROT: B2TD44_PARPJ

ID   B2TD44_PARPJ            Unreviewed;       660 AA.
AC   B2TD44;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|PIRNR:PIRNR001084};
GN   OrderedLocusNames=Bphyt_4585 {ECO:0000313|EMBL:ACD18958.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18958.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18958.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP001053; ACD18958.1; -; Genomic_DNA.
DR   RefSeq; WP_012426472.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4585; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   EnsemblBacteria; ACD18958; ACD18958; Bphyt_4585.
DR   KEGG; bpy:Bphyt_4585; -.
DR   eggNOG; ENOG4105C4C; Bacteria.
DR   eggNOG; COG1874; LUCA.
DR   HOGENOM; HOG000117811; -.
DR   KO; K12308; -.
DR   OMA; SRRHYCF; -.
DR   OrthoDB; 831762at2; -.
DR   BioCyc; BPHY398527:GJEX-4572-MONOMER; -.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; PTHR36447; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2TD44.
DR   SWISS-2DPAGE; B2TD44.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084,
KW   ECO:0000313|EMBL:ACD18958.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084,
KW   ECO:0000313|EMBL:ACD18958.1}.
FT   DOMAIN        6    389       Glyco_hydro_42. {ECO:0000259|Pfam:
FT                                PF02449}.
FT   DOMAIN      405    606       Glyco_hydro_42M. {ECO:0000259|Pfam:
FT                                PF08532}.
FT   ACT_SITE    142    142       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001084-1}.
FT   ACT_SITE    313    313       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001084-1}.
FT   BINDING     103    103       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001084-2}.
FT   BINDING     141    141       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001084-2}.
FT   BINDING     321    321       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001084-2}.
SQ   SEQUENCE   660 AA;  73998 MW;  C35E1BB0582B3EA0 CRC64;
     MRLGVCYYPE HWPESMWQDD ARRMKALGIE QVRIAEFAWS RIEPTPGEYD WGWLDRSIDV
     LGAAGLQVVM CTPTATPPKW LIDRHPDILP VGADGRPRAF GSRRHYDFSS PSYFAASQKI
     CTAVAERYGK HPAVAYWQTD NEFGCHHTVV SYSPAAVGRF REWLKARYQT IDALNRAWGT
     VFWSMEYRSF DEIDAPVATV TEAHPSHRLD YRRFASDEVA RYNRMQVEII RAHSPGRPVA
     HNFMQLFTEF DHYKVAADLD VATWDSYPLG ALEEQWFAPE VKARWLRSGH PDFASFNHDV
     YRGMSKLPFW VMEQQPGPVN WALWNPAPLP GMVRLWSWEA FAHGAGCVSY FRWRQAPFAQ
     EQMHAGLNTP DNRLDVGGNE ASQVAGEIRT VLAANADADA AVRSKVALVY DYEAKWLFEI
     HPQGADFHYP RFAFEYYSAL RALGLDVDVV PVDAPLDGYS LIVVPPLPVV PEAFAQRLAS
     SGAQVVLGPR TGSKTKDLQI PANLPPGALT SVLPLRVWRV ESMRPNVTEA VRLADGESAG
     EADGFARHWR DFIDTDAAQS LDVRARFADG HPAYVQGGAF HYLASLFDDA LTVRLFARIA
     QEAGLETMPL GDSVRVSRRG ALTYVFNYGD ETHTLSGVAD DALVFGSRAI EPQGVAVYRS
//

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