ID B3PBE0_CELJU Unreviewed; 575 AA.
AC B3PBE0;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 02-SEP-2026, entry version 81.
DE SubName: Full=Beta-galactosidase, putative, bgl35A {ECO:0000313|EMBL:ACE85180.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:ACE85180.1};
GN Name=bgl35A {ECO:0000313|EMBL:ACE85180.1};
GN OrderedLocusNames=CJA_2707 {ECO:0000313|EMBL:ACE85180.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Cellvibrionales; Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85180.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85180.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85180.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
RN [2] {ECO:0007829|PDB:4D1I, ECO:0007829|PDB:4D1J}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 36-575.
RX PubMed=25171165; DOI=10.1111/mmi.12776;
RA Larsbrink J., Thompson A.J., Lundqvist M., Gardner J.G., Davies G.J.,
RA Brumer H.;
RT "A complex gene locus enables xyloglucan utilization in the model
RT saprophyte Cellvibrio japonicus.";
RL Mol. Microbiol. 94:418-433(2014).
RN [3] {ECO:0007829|PDB:5JAW}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-575.
RX PubMed=29116266; DOI=10.1039/c7cc07730k;
RA Schroder S.P., van de Sande J.W., Kallemeijn W.W., Kuo C.L., Artola M.,
RA van Rooden E.J., Jiang J., Beenakker T.J.M., Florea B.I., Offen W.A.,
RA Davies G.J., Minnaard A.J., Aerts J.M.F.G., Codee J.D.C.,
RA van der Marel G.A., Overkleeft H.S.;
RT "Towards broad spectrum activity-based glycosidase probes: synthesis and
RT evaluation of deoxygenated cyclophellitol aziridines.";
RL Chem. Commun. (Camb.) 53:12528-12531(2017).
RN [4] {ECO:0007829|PDB:6TBF, ECO:0007829|PDB:6TBG}
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 36-575.
RX PubMed=32899288; DOI=10.3390/molecules25174025;
RA Weber P., Thonhofer M., Averill S., Davies G.J., Santana A.G., Muller P.,
RA Nasseri S.A., Offen W.A., Pabst B.M., Paschke E., Schalli M., Torvisco A.,
RA Tschernutter M., Tysoe C., Windischhofer W., Withers S.G., Wolfsgruber A.,
RA Wrodnigg T.M., Stutz A.E.;
RT "Mechanistic Insights into the Chaperoning of Human Lysosomal-Galactosidase
RT Activity: Highly Functionalized Aminocyclopentanes and C-5a-
RT Substituted Derivatives of 4-epi-Isofagomine.";
RL Molecules 25:E4025-E4025(2020).
RN [5] {ECO:0007829|PDB:8PEJ}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 36-575.
RX PubMed=37724332; DOI=10.1039/d3ob01261a;
RA Kuo C.L., Su Q., van den Nieuwendijk A.M.C.H., Beenakker T.J.M.,
RA Offen W.A., Willems L.I., Boot R.G., Sarris A.J., Marques A.R.A.,
RA Codee J.D.C., van der Marel G.A., Florea B.I., Davies G.J.,
RA Overkleeft H.S., Aerts J.M.F.G.;
RT "The development of a broad-spectrum retaining beta-exo-galactosidase
RT activity-based probe.";
RL Org. Biomol. Chem. 21:7813-7820(2023).
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DR EMBL; CP000934; ACE85180.1; -; Genomic_DNA.
DR RefSeq; WP_012488301.1; NC_010995.1.
DR PDB; 4D1I; X-ray; 1.80 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 4D1J; X-ray; 1.80 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 5JAW; X-ray; 1.60 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBF; X-ray; 1.50 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBG; X-ray; 1.50 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBH; X-ray; 1.50 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBI; X-ray; 1.46 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBJ; X-ray; 1.50 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 6TBK; X-ray; 1.60 A; A/B/C/D/E/F/G/H=36-575.
DR PDB; 8PEJ; X-ray; 1.50 A; A/B/C/D/E/F/G/H=36-575.
DR AlphaFoldDB; B3PBE0; -.
DR MDposit; B3PBE0; -.
DR MDRepo; B3PBE0; -.
DR SMR; B3PBE0; -.
DR STRING; 498211.CJA_2707; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR KEGG; cja:CJA_2707; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_027430_0_0_6; -.
DR OrthoDB; 9800974at2; -.
DR EvolutionaryTrace; B3PBE0; -.
DR Proteomes; UP000001036; Chromosome.
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 FunFam; 3.20.20.80:FF:000135; Beta-galactosidase, putative, bgl35A; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.220.20; putative beta-Galactosidase from caulobacter crescentus; 1.
DR InterPro; IPR040719; DUF5597.
DR InterPro; IPR017853; GH_hydrolase_sf.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR Pfam; PF18120; DUF5597; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PDBsum; 4D1I; -.
DR PDBsum; 4D1J; -.
DR PDBsum; 5JAW; -.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4D1I, ECO:0007829|PDB:4D1J};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ACE85180.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACE85180.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..575
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002796469"
FT DOMAIN 77..227
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 399..558
FT /note="DUF5597"
FT /evidence="ECO:0000259|Pfam:PF18120"
SQ SEQUENCE 575 AA; 64765 MW; F5B373BC49757B02 CRC64;
MWKTNNDKCF PTVIVNLWRR LSVALGCGLL SATCVAAPLP ELLSNNGKHA LMVDGAPYII
LGSQTNNSSN YPDALKDVWP SMEKMGANTL SIPVAWEQIE PVEGQFDFSF VDVLLKEARQ
RKVRLVLLWF ATWKNNAPHY APAWVKLDNA RFPRVVKEDG DTLNSLSPLG QNTLAADKKA
FVELMKYLAK RDKDHTVIMV QVQNEVGTYG AVRDYSPMAQ AVFNAAVPDD LIQKLQLKPG
TWSQVFGRDA DEFFHAYQIA RYCDEVTVAG KAIKNLPMYV NVALRNPFNP GLPGQYSSGG
GTDNVLHIWK AAAPNIDLIA PDIYFRDYKT VSKVLELYTR PDNALFVAEI GNDQPFARYL
FPTLGKGGIG FSPFGMDDTD YTNYPLGAKV YNDETIEQFA QVYRLVNPMM REWARLSYQG
QVWGVAEPLD STTETQKIWN AEATPEEKEQ HKKDRASALT QQLDLGLWDA EVTYGRPMFW
VTPPEGNTPA AGGALIAQLD DNEYLVTAYK ARVEFKPSQE LAGKKFMIER VEEGRFEKGK
WVMERVWNGD QTDWGLNFTD RPHLLRVKMA SYSVQ
//