ID H1UYZ3_COLHI Unreviewed; 818 AA.
AC H1UYZ3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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};
DE Flags: Fragment;
GN ORFNames=CH063_05430 {ECO:0000313|EMBL:CCF33194.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF33194.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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}.
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DR EMBL; CACQ02000669; CCF33194.1; -; Genomic_DNA.
DR AlphaFoldDB; H1UYZ3; -.
DR STRING; 759273.H1UYZ3; -.
DR EnsemblFungi; CCF33194; CCF33194; CH063_05430.
DR VEuPathDB; FungiDB:CH63R_10548; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR Proteomes; UP000007174; 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; 1.
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; 1.
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; 1.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..818
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003554690"
FT DOMAIN 387..568
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
FT NON_TER 818
FT /evidence="ECO:0000313|EMBL:CCF33194.1"
SQ SEQUENCE 818 AA; 90461 MW; C7D6D57272CA1C7D CRC64;
MLLSRVKALS LLALAWLDGV SARAIGRDLK LLNGRQQDIV TWDDKSLFIN GERLMIFSAE
FHAFRMPVTS LWLDILQKIK AAGYNSVSFY VNWGLIEAKP GEVRAEGIFA LEPLFEAAEK
AGIYLFARPG PYINAEVTGG GLPGWLQRVQ GALRSGDEAY LKASDNYTAA LGGIIAKAQI
TNGGPVILFQ MENEYNAAVP PYPFPDYDYW RYVDNQFRSQ GVVVPYVNNE AWQLGAITAL
TPAKVDIYGH DSYPLGFDCW NPTVWPPNGL PTDWLATNDR IAPTSPYTIV EFQGGGFQPW
GGAGFESCAA LLNHEFERVL FKNNYAVGTT IFNVYMTWGG TNWGNLGHSD GYTSYDYGAQ
ITEERLVHRE KYSETKLQSN FLHVSPAYLE ADRYNSSLEW TNNAAITVTP ATTNSTKFYI
ARHTQYDSLE TVAYKLKVKT VSHGDLEVPQ LSDSLYLTRR DSKIHVSDYA VGDKNLVYST
AEIFTWKKYA DKTVLVVYGG ADEHHELAVE GEQADVTDEN VIEGSDVTIE QRDGYTVLGW
AVSDERKVVR VHEDLYVYLL TRNEAYNFWV PPAVGDFATS DVIVKAGYLV RNVAVTTDSL
SFSGDVNSTT TIEVIGGAPN PLKALNFNGK SLDFKQNEHG VVTATVAFAV PEIKLPCLGQ
AGWKYIDSLP EIKPDYSDDL WTDADLEKTF NTANPLKTPT SLYGGDYGYH TGSLLFRGRF
TANGDESTLD ITTQGGNAYG ASVWLGDEFV GSWVGNAVSP ARNSTFTLPK LTKDKEYVFT
VVVDNMGLNG NWVVGEEQQK NPRGILNYAL AGHEQADV
//
