ID A0A401KVC4_ASPAW Unreviewed; 994 AA.
AC A0A401KVC4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=AAWM_06100 {ECO:0000313|EMBL:GCB23215.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB23215.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB23215.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB23215.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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}.
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:GCB23215.1}.
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DR EMBL; BDHI01000014; GCB23215.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KVC4; -.
DR STRING; 105351.A0A401KVC4; -.
DR Proteomes; UP000286921; 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 Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..994
FT /note="Probable beta-galactosidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019566772"
FT DOMAIN 379..557
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 994 AA; 108655 MW; 3FF96BC4B657BAF1 CRC64;
MKLQSILSCW AILVAQIWAT TDGLTDLVAW DPYSLTVNGN RLFVYSGEFH YPRLPVPEMW
LDVFQKMRAH GFNAVSLYFF WDYHSPINGT YDFETGAHNI QRLFDYAQEA GIYIIARAGP
YCNAEFNGGG LALYLSDGSG GELRTSDATY HQAWTPWIER IGKIIADNSI TNGGPVILNQ
IENELQETTH SASNTLVEYM EQIEEAFRAA GVDVPFTSNE KGQRSRSWST DYEDVGGAVN
VYGLDSYPGG LSCTNPSTGF SVLRNYYQWF QNTSYTQPEY LPEFEGGWFS AWGADSFYDQ
CTSELSPQFA DVYYKNNIGQ RVTLQNLYML YGGTNWGHLA APVVYTSYDY SAPLRETRQI
RDKLSQTKLV GLFTRVSSGL LGVEMEGNGT SYTSTTSAYT WVLRNPNTTA GFYVVQQDTT
SSQTDITFSL NVNTSAGAFT LPNINLQGRQ SKVISTDYPL GHSTLLYVST DIATYGTFGD
TDVVVLYARS GQEVSFAFKN TTKLTFEEYG DSVNLTSSSG NRTITSYTYT QGSGTSVVKF
SNGAIFYLVE TETAFRFWAP PTTTDPYVTA EQQIFVLGPY LVRNVSISGS VVDLVGDNDN
ATTVEVFAGS SAKAVKWNGK EITVTKTDYG SLVGSIGGAD SSSITIPSLT GWKVRDSLPE
TQSSYDDSKW TVCNKTTTLS PVDPLSLPVL FASDYGYYTG IKIYRGRFDG TNVTGANLTA
QGGLAFGWNV WLNGDLVASL PGDADETSSN AAIDFSNHTM KQTDNLLTVV IDYTGHDETS
TGDGVENPRG LLGATLNGGS FTSWKIQGNA GGAAGAYELD PVRAPMNEGG LLAERQGWHL
PGYKAKSSDG WTDGSPLDGL NKSGVAFYLT TFTLDLPKNY DVPLGIQFTS PSTVDPVRIQ
LFINGYQYGK YVPYLGPQTT FPIPPGIINN RDKNTIGLSL WAQTDAGAKL ENIELISYGA
YESGFDAGNG TGFDLNGAKL GYQPEWTEAR AQYT
//
