ID A0A0A1UXP1_9HYPO Unreviewed; 1019 AA.
AC A0A0A1UXP1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=X797_004937 {ECO:0000313|EMBL:EXV02098.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV02098.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV02098.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV02098.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:EXV02098.1}.
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DR EMBL; JELW01000006; EXV02098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1UXP1; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000030151; 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; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1019
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001992184"
FT DOMAIN 390..569
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 110606 MW; FF4A99EF7F5F1C33 CRC64;
MKPSTALGAI ALPFCHALSL GGRPYQVIHE VDRRSGALQD FVTWDEHSLF VHGERAMMFS
GEVHPFRLPV PSLYLDVFEK VKALGFNMVS FYVDWALLEG KPGEFRADGI FALEPFFEAA
SEAGVYLLAR PGPYINAEVS GGGFPGYLQQ LEGILRSQAP DFLNSTDNYM AHVCDIIAKH
QITKGGPVVL FQPENEYSSG HNIPFPNGQY MQYVINQARS AGISVPMINN DVGPAGNYAP
GKGVGSMDIY GHDSYPLGFD CGNPTVWPPN GLPTSFHQLH ERQSPKSPYS IIEFQGGAFD
PWGGWGFEKC AALVNHEFAR VFYKNNLAAG VSIFNIYMIY GGTNWGNLGH PGGYTSYDYG
ACIRENRVID REKYSEVKLE AQFIKVSPGY ITASVGLAST TAYSNNPGIT ITPLTSNKTG
NFFVARQTDY TATGSVSYTV TLPTSNGILT IPQRGGSLSL HGRDSKIHLT DYPVGDYVLL
YTTAEVFTWK KYADKTVLVL YGGPDELHEF AVNSPSATRI LHVEGSSISS HEQASSTIVV
QWTTSPERQY IQVGNLAIYL VDRNSAYNYW VPVLPGSKSS PYGTSLMNPD AAIINGGYLI
RSASINGNTL SLRADFNGST TLEVVGIPDG VTKLSVNGRP LKHTTSPTGT WLAQPDITIP
TVQLPSLADL TWHTIDSLPE IHPQYDDSLW RTASQSPGNN RPQAHHKTSN ETLFAAPPRA
SLYGSDYGFN TGTLLFRGHF TASGRESLFR AWTSGGTAYA SSAWLNDRFL GSFKGNSAAE
NQNSTYALPS LTAGEQYVVT VVVDTMGFNE NFNPGYEDMK APRGILDYAL SSPDGAPTAV
AWKITGNLGG HDYADSFRGP LNEGGLFFER QGYHYPRPPV DDAPFAPGSP FDGADGAGVA
YYAARMPLDL PADAYDIPLS FVFANASRGG GDYRALLYIN GFQFGKYLSN IGPQTEFPVP
EGVLDYGGDN WVGLAVWSLD STGARVPGLA LRAGTPVQSS RNKVRLVTGP AYSKRPEAY
//