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Database: UniProt
Entry: BGALB_TALMQ
LinkDB: BGALB_TALMQ
Original site: BGALB_TALMQ 
ID   BGALB_TALMQ             Reviewed;        1009 AA.
AC   B6QLF0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   16-JAN-2019, entry version 53.
DE   RecName: Full=Probable beta-galactosidase B;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase B;
DE   Flags: Precursor;
GN   Name=lacB; ORFNames=PMAA_057160;
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; DS995903; EEA21927.1; -; Genomic_DNA.
DR   RefSeq; XP_002150536.1; XM_002150500.1.
DR   ProteinModelPortal; B6QLF0; -.
DR   SMR; B6QLF0; -.
DR   STRING; 441960.XP_002150536.1; -.
DR   EnsemblFungi; EEA21927; EEA21927; PMAA_057160.
DR   GeneID; 7028036; -.
DR   EuPathDB; FungiDB:PMAA_057160; -.
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   1009       Probable beta-galactosidase B.
FT                                /FTId=PRO_0000395231.
FT   ACT_SITE    191    191       Proton donor. {ECO:0000255}.
FT   ACT_SITE    303    303       Nucleophile. {ECO:0000255}.
FT   BINDING      85     85       Substrate. {ECO:0000250}.
FT   BINDING     130    130       Substrate. {ECO:0000250}.
FT   BINDING     131    131       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     132    132       Substrate. {ECO:0000250}.
FT   BINDING     190    190       Substrate. {ECO:0000250}.
FT   BINDING     260    260       Substrate. {ECO:0000250}.
FT   BINDING     368    368       Substrate. {ECO:0000250}.
FT   CARBOHYD     28     28       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    247    247       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    375    375       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    427    427       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    451    451       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    682    682       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    740    740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    771    771       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    784    784       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    826    826       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    883    883       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    266    319       {ECO:0000250}.
SQ   SEQUENCE   1009 AA;  111835 MW;  CCE39753CD678910 CRC64;
     MAQLFTKIIV YFLLFASPLL ANQWPLHNNS LNDVVQWDHY SFEINGQRLF VFAGEWHYWR
     IPVPELWIDI LEKIKAAGFT AFGIYVNWAY HAPNNYTVDF ATGAHDITPI LKMAKDVGLY
     VLLRPGPYIN AEVNAGGFPL WVTTGEYGSL RNDDSRYTAA WEPYFTKISE IASEYQITKG
     GNVVTYQIEN EFGDQWTGSP SRRVQYEPAA KYMELLEANA RRNGIDIPLV ANEPNMRAIS
     WGKDWSNSSA NVDVVGLDSY PSCWTCDLSV CTGTTGEYIA YQVIDYYGYF QETQPTMPSF
     FAEFQGGSYN PWGGPVGGCP EDIGPDFANL FYRWNIGQRV TAINLYMLYG GTNWGAIAAP
     VVASSYDYSS PISENRTIGA KYYETKLLTM FTRAARDLIV TDLIGNGTQY STNPAIQTHV
     IRNPITNGTF YVTLHTISSS STDETFQLHV NTSAGAFSIP RYGNSIRLNG HQSKIIVTDF
     QFGTHKLLYS TAEVLTYTVL DGIPTLALWV PTGESGEFSV LGGKWASVLR CEWCSDIQFH
     PEQDQTSNPT VSRLTVSFTQ GQGMSVIKLD TGLRVVLLDR ESAYYFWAPA LNSDPSVPED
     QSVLVQGPHL VRSAKIVGST IRLTGDSAQT SPIEVFAPKQ VRIIFWNDKE LKTSKTSYDS
     LQASLPQPAY VKLPLLGPWK YNGSLPEKAQ DYKDTSAAWI SADHMKTSNP SPPATFPVLY
     ADEYGFHNSI RIWRGYFTGN ATGVVLKVQG GYAFGFSGWL NGKLLGSYLG NASVEHSHLT
     LPFNVSHVST SSDNVLVIVH DDTGHDETTG ALNPRGILEA TLLSDNSSSK FSHWRVAGTA
     GGETNIDPMR GPYNEGGLYA ERMGWHLPGF NDNAWSDAGS KLNFTGADIK FYRTTVPLNI
     PKGVDVSISF ELSACGTTNA FRSQLFVNGY QMGRFNPWVG NQIEFPVPPG ILDYTGDNTI
     GLSLWAQTED GACAIVDWKI NYVLGSSLDV TFNGEYLRPG WTSERLQYS
//
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