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Database: UniProt
Entry: A0A0Q4LIN3_9SPHN
LinkDB: A0A0Q4LIN3_9SPHN
Original site: A0A0Q4LIN3_9SPHN 
ID   A0A0Q4LIN3_9SPHN        Unreviewed;       828 AA.
AC   A0A0Q4LIN3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KQN39332.1};
GN   ORFNames=ASE97_04330 {ECO:0000313|EMBL:KQN39332.1};
OS   Sphingomonas sp. Leaf42.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736219 {ECO:0000313|EMBL:KQN39332.1, ECO:0000313|Proteomes:UP000051880};
RN   [1] {ECO:0000313|EMBL:KQN39332.1, ECO:0000313|Proteomes:UP000051880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf42 {ECO:0000313|EMBL:KQN39332.1,
RC   ECO:0000313|Proteomes:UP000051880};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN39332.1, ECO:0000313|Proteomes:UP000051880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf42 {ECO:0000313|EMBL:KQN39332.1,
RC   ECO:0000313|Proteomes:UP000051880};
RA   Schulze-Lefert P.;
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:KQN39332.1}.
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DR   EMBL; LMLF01000004; KQN39332.1; -; Genomic_DNA.
DR   RefSeq; WP_055757611.1; NZ_LMLF01000004.1.
DR   AlphaFoldDB; A0A0Q4LIN3; -.
DR   PATRIC; fig|1736219.3.peg.977; -.
DR   OrthoDB; 9758603at2; -.
DR   Proteomes; UP000051880; 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; IPR048230; GalA-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
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; IPR006311; TAT_signal.
DR   NCBIfam; NF041462; GalA; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051880};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..828
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006225822"
FT   DOMAIN          72..231
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          247..347
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          357..516
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          650..706
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          721..820
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   828 AA;  89694 MW;  2C320620E1C20F4A CRC64;
     MLISRREAIA AGALAGAVAL PGLGSAHAGV SGEAPAPVYI GPRRVERLAD WRFHLGHAAD
     VEQDFGFGRY QRTYAKAGVT ADASSPAFDD KGWQAVMVPH DWAVALPFAR PAAAATKETE
     DAAAAHGFKA IGRDFPGNSV GWYRTPIAID AADRDRALWI EFDGVFRDCI VFVNGYVAGR
     NESGYAPFAV PIGDFLDYDG GPNVIALRVD ASLGEGWFYE GAGIYRHVDL VRANRVHVPQ
     WGSVVRSTVG SDGASVAVVL EVRNDGPAPV AAVVRQRIVG ANGQAVATLP ETSLTVAPHT
     TATATGSARI AAPQLWSVET PYRYRLHSEV AVDGITVDTY VTPFGIRTVR FDGARGFLLN
     ERPVKLLGSC NHQDHAGVGT GIPDALHAWR IAQLQEMGSN AWRSAHNPPA AAMLDLCDAM
     GMLMIVEARR NSSDPAAMDE LSRIVRRDRN HPSVISWSLG NEEPQQGSPR GARVTQAMQD
     LVRELDPTRP TTFAFDNSWD KGAARIVDTV GFNYRTDRMP AFKAAHPGVP VYGSETGSTV
     ATRGAYANDA ARQIVRAYDT EHPWWASTAE EWWTIVTDRS DIAGGFIWTG FDYRGEPTPY
     PAFPSISSYF GVLDTCGFPK DNFYYYRAWW RPDQPLVHLL PHWNWPGKEG QPIEVWVHGN
     CAEVELLLNG RSLGRKPMPR NRHLRWDVPY APGRIEARGF DKGRRTARDV RETAGTAAAV
     VLTADRRRPL ASGQDVVMVR AEVVDAKGRI VPDAADLLRF AVAGNATIIG VGNGNPTSLE
     ADQADRRRAF AGLAQAIVRV GRGTGPVRIT ATGDGLTSGQ LILLPQPG
//
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