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
//