ID A0A3N4JC62_9PEZI Unreviewed; 1007 AA.
AC A0A3N4JC62;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=L873DRAFT_1791948 {ECO:0000313|EMBL:RPA95845.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA95845.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA95845.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA95845.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML120420; RPA95845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4JC62; -.
DR STRING; 1336337.A0A3N4JC62; -.
DR Proteomes; UP000276215; 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:UP000276215};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1007
FT /note="Probable beta-galactosidase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018013779"
FT DOMAIN 385..565
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1007 AA; 111150 MW; 19668B69BD4BD95D CRC64;
MGLLGSLLLC CVLLLPGSAL GQNTTLKDNG LTKLVQWDET SLFINGEPIF IFSGEFHYWR
IPNPSLYLDI FQKIRATGYN AISVYFHWGF HSPNPETFDF ETPAHDLQPV FDAAKQAGLW
VIARPGPYLH AETTAGGFPA WLISIDIEVR TNETLYTEAW KEYIAKIGPI IARNQITVNN
GPVILAQIEN EYRSGERHTF IGADEYMEDL SISFKKAGIV VPIFHNDFNK NIRGGSWNPR
DYQGVLDLYG LDSYPRGFDC GNPQRNFNID TGYHRHFAAV GYGGPGFMPE FQGGAFDPWA
GPGYEKCADM VGPEFVDVYY KNNLAQGATM HSYYMIFGGT NWGHVATPVV YTSYDYGSGI
TEGRLLRDRA NESKLLGLFT RVTRSVLHAP QVANSTVKTY TPNSAAFVTE LRNKQDNSGY
YLVRSSNTNS TDTKQFTLNV DTSAGALTLP SSNGSIVLEG RQTKIITTDY SAGSTKLLYS
TAEIATWTVV DGKDVILFYL NKGQAGGIAV MGAQNDIQVN GAGAVSGKQG NGALILSFVQ
AEGLTVVELP KATLLLADRP TAYKFWAPGV KLAYYEPPQE QVLVSGPYLV RNATISGRTL
NLIGDINADT KLEVFANSTY SEITWNGKRV HTQKSSYGSR VADLSGPRLK SLNIPSLNST
HTRWKVMDSL PEIDPKFDDS TWVVADKNSS TNEYYPPKTL PVLYAGEYGY HTGFTIYRGR
FNAGNGTGPQ AVALEVWGGA AFGFTAWLNG KYLGHHAGTP DPKGFIATNY TFANHTLQSE
NILVILADRM GYERDDGVFG DPYSTKKPRG IRAASLLPSG TFTKWTLQGN VGQETFDDPV
RAPYNEDGLY AERIGAHFPG YDDSKWKSGS PMEGFQGADV KFYRTVIDLD LPKDWDVPLG
FNFKIKNGTS ARAELFVNGW QFGKYVGDIG PQTMFPVFPG IIHLRGKNTI AIALWGQHEV
ECKFEELYIA PLDVFESGYG PVETEGLTPG YIEGRKKYEI KHPPTKN
//
