ID E3QKY6_COLGM Unreviewed; 993 AA.
AC E3QKY6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=GLRG_06813 {ECO:0000313|EMBL:EFQ31524.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
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; GG697356; EFQ31524.1; -; Genomic_DNA.
DR RefSeq; XP_008095544.1; XM_008097353.1.
DR AlphaFoldDB; E3QKY6; -.
DR STRING; 645133.E3QKY6; -.
DR EnsemblFungi; EFQ31524; EFQ31524; GLRG_06813.
DR GeneID; 24412178; -.
DR VEuPathDB; FungiDB:GLRG_06813; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000008782; 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:SF165; BETA-GALACTOSIDASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..993
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003180666"
FT DOMAIN 388..568
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 993 AA; 110020 MW; 591255103F64DD4C CRC64;
MLLSRLKALA LLSLAWFDGV GARSIDAGIK LLNGRQQDIV TWDDKSLFIN GKRLMIFSAE
FHAFRMPVPS LWLDILQKIK AAGYNSVSFY VNWGLLEAKP GEVRAEGIFA LEPLFEAAQK
AGLYLFARPG PYINAEVSGG GFPGWLQRVQ GVLRSNDEAY LEASENYTAT LGSIIAKAQI
TNGGPVVLFQ MENEYNAAID PYPFPDYDYW KFVDNQFRSQ GVVVPYVNNE AWQLGAITAL
TPAKVDIYGH DAYPLGFDCW NPTVWPANGL PTDWLATNNK LAPTTPYTIV EFQGGGFQPW
GGAGFEYCAA LLNHEFERVL YKNNYAAGVT IFNIYMTWGG TNWGNLGHSD GYTSYDYGAQ
ISEERLVNRE KYSETKLQSN FLHVSPAYLV ADRHNSSLEW TNNDAITVTP ATTNSTKFYI
ARHTQYESLE TVSYKLKVKT VGYGELEVPQ LSDSLYLTRR DSKIHVSDYP VGDKNLVYST
AEIFTWKKYE NKTVLVVYGG PGEHHELAVE GEEADVTDEN VIEGSDVSIE QKDGYTVLGW
AVSDERKVVR VQSNLYVYLL TRNEAYNFWV PPAVGDFATC DVIVKAGYLI RNVAVGGDSL
GFSGDVNSTT TIEVIGGVPT PLKSLTFNGK SLDFEQNEHG VVTATVDFAV PEIKLPCLSR
MSWRYIDSLP EIKPGYSDEL WADADLEETY NTAHPLKTPV SLYGGDYGYH TGSLLYRGRF
KANGEESIFN VTTQGGNAYG ASVWLDGEFI GSWVGDAVTP GRNSTFALPK LTKDREYVFT
VAVDHMGLNG NWVVGEEQQK NPRGILDYGL SGHEMSDIRW KITGNLGGED YTDKERGPLN
EGGLFAERQG YHWPEPPSQS WEASKGPTVG IETAGIAYYS TTFDLDLPAG FDIPLSLTFA
NTTESAYRAQ IFVNGYQFGK FVHHIGPQTR FPVPEGILNY QGPNHLGITL WAMEEGGAKI
EGLKWEVGMV SATGFGKVEP APQPKWAKRE GAY
//
