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 03-AUG-2022, entry version 66.
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;
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; DS995903; EEA21927.1; -; Genomic_DNA.
DR RefSeq; XP_002150536.1; XM_002150500.1.
DR AlphaFoldDB; B6QLF0; -.
DR SMR; B6QLF0; -.
DR STRING; 441960.B6QLF0; -.
DR EnsemblFungi; EEA21927; EEA21927; PMAA_057160.
DR GeneID; 7028036; -.
DR KEGG; tmf:PMAA_057160; -.
DR VEuPathDB; FungiDB:PMAA_057160; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; B6QLF0; -.
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..1009
FT /note="Probable beta-galactosidase B"
FT /id="PRO_0000395231"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 266..319
FT /evidence="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
