ID A0A2V5IGS8_9EURO Unreviewed; 993 AA.
AC A0A2V5IGS8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Probable beta-galactosidase C {ECO:0000256|ARBA:ARBA00040694};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase C {ECO:0000256|ARBA:ARBA00042635};
GN ORFNames=BP00DRAFT_390028 {ECO:0000313|EMBL:PYI34462.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI34462.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI34462.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI34462.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; KZ825475; PYI34462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IGS8; -.
DR Proteomes; UP000248817; 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; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF125; BETA-GALACTOSIDASE C-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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..993
FT /note="Probable beta-galactosidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015993125"
FT DOMAIN 379..557
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 993 AA; 107456 MW; 5CC785F78B16ACDB CRC64;
MKLWSSLLLG ASLLTGSRAT TDGLTDLVSW DPYSLSVNGN RLFVFSGEFA YPRLPVPELW
LDIFQKMRAN GFNAASVYLF WNFHSPVNGT FDFETGAHNI QRLFDYAQEA GIYLIARPGP
YDNAEINGGG LALHLSDGSG GSLRTSDATY TAAWQPWVEE IGKIIAANSI TNGGPVILNQ
IENELQETTH SASNTLVQYM IKLEDAFRAA GVDVPFTHNE KGMRSESWST DYEDVGGAVN
VYGLDSYPGG LSCTNEATGF NVVRTYYQWF QNYSYTQPSY IPEFEGGWFS AWGASSFYDT
CTSELSPQFA DVYYKNNIGQ KITLQSIYMT YGGTNWGHLA APVVYTSYDY SAPLSESRVV
RDKMSQTKLI GLYTRVSTGL LTADMEGNGT GYTSSTSAYT WVLRDSQSDA GFYVVQQATT
SSRSSLAFDL DVTTSAGNVT LTDITLDGRQ SKIISTDYPL GHSTLLYVST DIATYGTFGD
TDVVVLYSRV GQTASFAFKS PGRLNFTEYG PSVNLTQSSG NSTTPSYTYT QASGTSVVQF
SNKTIFYLLD TDTAFRFWAP PTTNDPYVTA DQHIFVIGPY LVRNASVDGS VVNLVGDNDN
TTTIEVFAGS SVNTVKWNGK RISVTKTAYG SLVGSIDGAS STISLPALSG WKVKNSLPEL
ESDYDDSNWT VCNKTTTLSP VQPSTLPVLY ASDYGYYTGI KIYRGRFDGA NVTGASLTAQ
GGVGFGWNVW LNGDLVATLP GDASATSSIA TLDFSNQTLK DTDNLLTVVI DYTGHDETST
AKGVENPRGL LAATLTGGNF TSWKIQGNAG GAAGAYELDP VRAPMNEGGL LAERQGWHLP
GYKAQSSDGW TSGSPLDGLN KSGVAFYLTT FTLDLPKSYD VPLGIRFTSP STVSPVRIQL
FINGYQYGKY VPYLGPQTTF PVPPGIINNR DKNTIGLSVW AQTDAGAALE NIELVTYGAY
ASGFDAGSGT SFDMNGAKLG YQPEWTEARL KYT
//
