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Database: UniProt
Entry: A0A0Q4J1E7_9SPHN
LinkDB: A0A0Q4J1E7_9SPHN
Original site: A0A0Q4J1E7_9SPHN 
ID   A0A0Q4J1E7_9SPHN        Unreviewed;       883 AA.
AC   A0A0Q4J1E7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KQN04215.1};
GN   ORFNames=ASE85_21000 {ECO:0000313|EMBL:KQN04215.1};
OS   Sphingobium sp. Leaf26.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQN04215.1, ECO:0000313|Proteomes:UP000051336};
RN   [1] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQN04215.1}.
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DR   EMBL; LMKV01000014; KQN04215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4J1E7; -.
DR   STRING; 1735693.ASE85_21000; -.
DR   Proteomes; UP000051336; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR048229; GalB-like.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   NCBIfam; NF041463; GalB; 1.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..883
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006222379"
FT   DOMAIN          122..242
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          257..367
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          374..580
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          705..764
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          777..877
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   883 AA;  96471 MW;  27D25A582D904BE4 CRC64;
     MVSLSAMALA SLPAQLLAAD SVSISKNWRF TKGDPAGLTT DLRYDVRPPI EDAGDGKLAD
     ARPDAAVKVD DNGAKVLKPW ILPSANPFIK DPAKHHVRPA GNPGGDVPYV QAGFDDSGWT
     PVDLPHDWAI AGPFIKDGPY GGMGRLPSWG IGWYRKTLDI PASAKGQSIF LDVEGAMSYA
     TVWLNGKLVG GWPYGYNSFR LDLTPYAVAG GRNQLAIRLD NPAASARWYP GGGLYRDIYL
     TTANKVHVGQ WGSTIRTPKV SREQATVDLS LTLDNDGDKP AQVEVATALY VLDAHGQRTG
     RPVASIARQS ASIAPGEKAV LNGSAILTNP RLWGPPPTQA PNRYVAVSTV TQGGKTIDTH
     ETRFGVRDVQ FDPDKGVIVN GEHIPLRGVN NHHDLGALGA AFNARAAERQ LEILRDMGTN
     AVRMSHNPPA PELLELTDRM GFLVMDEVFD SWEKKKTPHD FHLIFPDWHE ADARAMLRRD
     RNHPSIILWS VGNEVGEQYD GEAGAKIGRE LVAIAHEEDP TRPATGAMNF AKADMLLPTT
     VDVISLNYQG AGIRGIIGQY PAFRAKFPDK MILSTESASA LSSRGEYMFP VAGAISGPVR
     PWSGGNPDTH QVSAYELHAS DFGSSPDRVW AADDQNPYVA GEFVWTGFDY LGEPTPYYTS
     RSSYSGIVDL AGFRKDRFWL YQARWRPDLK FAHILPHWNW PDRVGQITPV HVFSSADEGE
     LFVNGKSQGK IRKRDYEYRF RWDYVVYEPG EVKVVTWKKG QPWATETIHT VGEAAKLSLT
     ADRAAIASDG RDLSFVTLKV LDKDGNVVPA AKQKVDFSIE GPGTIVATDN GDPTDMTAFP
     SKSRDAFNGR ALAIVKAQRP GKIILRARAE GLGETQVEIG AKR
//
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