ID A0A484FB46_COLOR Unreviewed; 985 AA.
AC A0A484FB46;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 Name=lacA-0 {ECO:0000313|EMBL:TDZ15148.1};
GN ORFNames=Cob_v011953 {ECO:0000313|EMBL:TDZ15148.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ15148.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ15148.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCV02000043; TDZ15148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484FB46; -.
DR STRING; 1213857.A0A484FB46; -.
DR Proteomes; UP000014480; 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:UP000014480};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..985
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019786790"
FT DOMAIN 387..560
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 985 AA; 108765 MW; 9EF976BE7D38023F CRC64;
MLLSRAKLLS VLALGWLNGV SGRAVGRDMH LLNGRQQDIV TWDDKSLFIN GERTMIFSAE
FHAFRMPVTH LWLDILQKIK AAGYNSISFY VNWGLLEAKP GEVRAEGIFS LQPLFEAAEK
AGLYLFARPG PYINAEVTGG GFPGWLQRVQ GVLRSNDEAY LKATDNYTAA IGKIIADAQI
TNGGPVILFQ QENEYNAAIE PYPFPDYDYW NYVDNQFRSV GVIVPYVNNE AWQLGAITTS
TPAKVDIYGH DAYPLGFDCW NPTVWPENGL PTDWLATNDA IAPDSPYTIV EFQGGGFQPW
GGAGFESCAG LLNHEFERVL YKNNYAVGVT IFNVYMTWGG TNWGNLGHSD GYTSYDYGAQ
VTEERLVNRE KYSESKLQAN FLHVTPAYLE ADRFNSSLEF TNNEAITVTP ATTNTTKLYI
TRQVSPELLK VDTVNHGKLE IPLLSDSLYL TRRDSKIHVS DYPVGDKNLV YSSAEIFTWK
KYADKTVLVV YGGADEQHEL AVEGDNGEVT EDDVIEGSDV TIEAKDGFTV FGWAVSDERK
VVRVGDLYIY LLTRNEAYDF WVPPTEGNYG TSDVIVKAGY LVRTVEVSGD TLSFSGDVNA
TTPIEVIGGA PASLKTLNFN GQSLDFKQND RGVVTATVDF AVPEIRLPCI SQLNWKYIDS
LPEIRSNYSD ELWTDADLAE TYNTANPLKT PTSLYGGDYG YHTGSLLFRG HFTANGDETV
FNVTTQGGNA YGASVWLDDE FVGSWAGNAV TPGHNSTFTL PKLTRDKGYV LTVVVDHMGL
NGNWVINEEQ QKNPRGILDY NLAGHEQSDV RWKITGNLGG EDYADGERGP LNEGGLFAER
QGYHWPGPPS GSWRDSKGPA EGLARAGVAF YSATFDLDLP AGYDIPVSLT FANTTTTAYR
AQIFVNGYQF GKFVHHVGPQ TRFPVPEGVL NYRGSNHLGI TLWAQEKGGA RVEGLKWEVG
MVTATGFGKI QPAPQPKWVQ RAGAY
//
