ID A0A0N1GFL5_9ACTN Unreviewed; 1031 AA.
AC A0A0N1GFL5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KPI22206.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:KPI22206.1};
DE Flags: Precursor;
GN ORFNames=OK074_1044 {ECO:0000313|EMBL:KPI22206.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI22206.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI22206.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI22206.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI22206.1}.
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DR EMBL; LJCV01000022; KPI22206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1GFL5; -.
DR PATRIC; fig|1592327.3.peg.563; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF00754; F5_F8_type_C; 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; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KPI22206.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KPI22206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1031
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005872389"
FT DOMAIN 48..204
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 215..316
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 325..477
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 648..744
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 758..857
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT DOMAIN 890..1015
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
FT REGION 530..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 110180 MW; 656B36B784EE1CE6 CRC64;
MTVTRRSVLL AGTAAPAAGA LLGAPAARAA TATAPAPGRH TVALRDGWRF ALVDPGGITD
PTGAYDGAAD PSYDDSAWRE VAVPHDWSIE QTPTTEYGTT SGTGFLPGGL GWYRLAFTLP
PGYAGKRIAV EFDGVYMNAV VHCNGTEAGH HPYGYTGFAF DLTDLLHTDG STENVLAVRV
QNRLPSSRWY SGSGIYREAR LVVTEPVHVG RWGTYVTTPE ITAERAAVRV RTTVVNESGA
AADVRVLSRI VDPDGRTVAR ADSTVSVTGT ADESHELAVA RPKLWDFATP DTYTLHTELR
VGGATTDTFS TTFGIRSYVF DPQEGFSLNG AYAKIKGVDL HHDQGALGAA ISLDAVRRQM
TVMKSMGVNA FRTSHNPPSP QMIQVCEELG IVMMVEAFDC WRTGKTSYDY HLYFDEWCEK
DATEMVLAAR NSPAVVLWSI GNEIPDSTST AGLAMADRII GAIRAADDTR PLVIGSDKYR
GVPAKGSASD LMLAKLDGLG LNYNTAKSVD ALHAAYPDLF LFESESSSET STRSAYQEPE
HLNTGENHTP GRRATSSYDN NLSSWTMSGE YGHKKDRDRK WFAGQFLWSG IDYIGEPTPY
DVFPVKASFF GAVDTAGFPK DMYHLFRSQW AAEPLVHLLP MSWNHDSGDT VEVWAYANVD
TVELFLNGKS LGTRVFDTKK TTDGRTYLET TEASGDDKTV TTGPYPGSYT SPNGSAGKLH
LSWQVPYEPG ELKAVARQDG KAVATDVLRT AGPAHAVRLT TDRDSLAADG RSLVFVTAEV
VDAHGVVLPD AEDLISFAVR GGSLAGLDNG REESAERYQA STRTVFHGKA LAIVRAGTEP
GALKVTAHAD GLRTGTATVR TTPVRSAAST PPAAFAPDLP APPDHPLADA SYSGRPDTLP
AAMLDGDAAT GWSNAFAKSA TALLPAFSGA RARDWVSVDF GRGRSFDRVE VSFTVDATHS
LPASVAVSAW DGGRWTPVTG AVVDWADGSD APTVITFDPV RGSRLRLDLT SAHPGAANGA
QRIVRLDAPA A
//
