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Database: UniProt
Entry: BGALC_TALMQ
LinkDB: BGALC_TALMQ
Original site: 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   16-JAN-2019, entry version 54.
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.
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.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000305}.
DR   EMBL; DS995902; EEA22754.1; -; Genomic_DNA.
DR   RefSeq; XP_002148921.1; XM_002148885.1.
DR   ProteinModelPortal; B6QHA9; -.
DR   SMR; B6QHA9; -.
DR   STRING; 441960.XP_002148921.1; -.
DR   PRIDE; B6QHA9; -.
DR   EnsemblFungi; EEA22754; EEA22754; PMAA_093700.
DR   GeneID; 7026488; -.
DR   EuPathDB; FungiDB:PMAA_093700; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   OrthoDB; 179316at2759; -.
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; 2.60.120.260; -; 2.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    999       Probable beta-galactosidase C.
FT                                /FTId=PRO_0000395240.
FT   ACT_SITE    186    186       Proton donor. {ECO:0000255}.
FT   ACT_SITE    285    285       Nucleophile. {ECO:0000255}.
FT   BINDING      80     80       Substrate. {ECO:0000250}.
FT   BINDING     125    125       Substrate. {ECO:0000250}.
FT   BINDING     127    127       Substrate. {ECO:0000250}.
FT   BINDING     185    185       Substrate. {ECO:0000250}.
FT   BINDING     249    249       Substrate. {ECO:0000250}.
FT   BINDING     351    351       Substrate. {ECO:0000250}.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    195    195       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    274    274       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    389    389       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    441    441       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    512    512       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    519    519       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    600    600       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    675    675       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    713    713       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    757    757       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    808    808       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    897    897       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    255    302       {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
//
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