BGALC_TALMQ
ID BGALC_TALMQ Reviewed; 999 AA.
AC B6QHA9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Probable beta-galactosidase C;
DE EC=3.2.1.23;
DE AltName: Full=Lactase C;
DE Flags: Precursor;
GN Name=lacC; ORFNames=PMAA_093700;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; DS995902; EEA22754.1; -; Genomic_DNA.
DR RefSeq; XP_002148921.1; XM_002148885.1.
DR AlphaFoldDB; B6QHA9; -.
DR SMR; B6QHA9; -.
DR STRING; 441960.B6QHA9; -.
DR EnsemblFungi; EEA22754; EEA22754; PMAA_093700.
DR GeneID; 7026488; -.
DR KEGG; tmf:PMAA_093700; -.
DR VEuPathDB; FungiDB:PMAA_093700; -.
DR HOGENOM; CLU_005732_2_1_1; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; B6QHA9; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.20.10; -; 1.
DR Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 2.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF117100; SSF117100; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..999
FT /note="Probable beta-galactosidase C"
FT /id="PRO_0000395240"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 285
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 255..302
FT /evidence="ECO:0000250"
SQ SEQUENCE 999 AA; 110430 MW; CD1A02A994EB2050 CRC64;
MFFFRFLTTV LLLFNAKLLV AQSSNTSSPV HWDKYSLSIN GERLFVFAGE FHYIRLPVPE
LWLDVFQKLK ANGFNAISVY FYWNHHSASE GVYDFETGGH NVQRLFDYAK QAGVYIIARP
GPYANGELSA GGYALWAANG RLGGERTRDS QYYDLWSPWM TKIGKIIAAN QITEGGPVIL
VQHENELQET THRANNTLVL YMEQITQILD AAGIVVPSTH NEKGMRSMSW SMDYEDVGGA
VNIYGLDSYP GGLSCTNPNA GFNLIRTYYQ WFQNYSYTQP EYLAEFQGGY FTPWGGVFYD
DCASMLQPEY ADVFYKNNIG NRVTLQSLYM AYGGTNWGHI AAPVVYTSYD YSAPLRETRE
IRDKLKQTKL LGLFTRVSPD LLQTEMEGNG TSYTTGANIF TWALRNPETN AGFYVVAQDD
SSSTTDVVFD LEVETSAGSV NITNIGLDGR QSKIITTDYK VGDTTLLYCS ADILTYATLD
VDVLALYLNK GQTGTFVLAN AASHLKYTVY GNSTVTSSNS SQGTIYTYTQ GQGISAIKFS
NRFLVYLLDK YTAWDFFAPP LQLSDPNVKP NEHIFVIGPY LVREATIKGR TLELTGDNQN
TTSIEIYHGN PFITSITWNG KHLSTKRTAY GSLTATIPGA EAITITLPKL TSWKSHDMIP
EIDPEYDDSN WVVCNKTTSF NAIAPLSLPV LYSGDYGYHA GPKIYRGRFG STNATGVTVT
AQNGNAAGWS AWLNGIYIGG VTGDPSIEAT SAVLKFNSST TLKQEGSENV LTVLVDYTGH
DEDNVKPARA QNPRGLLGVI FEGSTSTNFT SWKLQGNAGG EKNIDALRGP MNEGGFYGER
LGWHLPGFEP STKSGWDTRA PSDGVDGGSH RFYITEFTLD LGPNSHALDV PIGIHLNASS
TSGPAVAYVW LNGYKFAHYL PHIGPQTVFP FQPGVLNIQG SEGHKRKNTL AVSLWALTDQ
PAALDVVELV AYGKYTSSFD FARDWSYLQP RWVDRSKYA
