ID A0A094EMZ5_9PEZI Unreviewed; 1454 AA.
AC A0A094EMZ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Probable beta-galactosidase B {ECO:0000256|ARBA:ARBA00040693};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase B {ECO:0000256|ARBA:ARBA00042633};
GN ORFNames=V499_01005 {ECO:0000313|EMBL:KFY80116.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY80116.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY80116.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY80116.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY80116.1}.
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DR EMBL; JPKB01000103; KFY80116.1; -; Genomic_DNA.
DR HOGENOM; CLU_251116_0_0_1; -.
DR Proteomes; UP000029295; 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:SF64; BETA-GALACTOSIDASE (EUROFUNG)-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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1454
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001896106"
FT DOMAIN 395..576
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
FT REGION 1338..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 154434 MW; B27A88D47BFAFF25 CRC64;
MRLTSFLSCL LVQSLAVNVV SSKQWPLHDD GLNKVVEWDH YSFKINGERL FIWSGEMHYW
RAPVPEMWID ILQKVKAAGF NTISFYGNWG YHNAKNGSLD FENGAHNFER LFEIAKEVGL
YVLFRPGPYV NAEATAGGFP GWVTTGAYGE LRNNDTRYTD AWTPYMDRMS QIIAKHQVTN
GGNVFIYQIE NEFGNQWLDR VKKIPDLVAI DYMELMESSA RRNGIDVPLI HNNPNMNTKS
WSKDYSNEGG NVDIYSADHY PSCWSCDLTE CTGTNGNVPD FTTFEYYTSF QDVAPTQPSF
LAEFQGGSYL PWGGPEGGCV NNTGPDWVNV FYRHNVAQKI TAVNVYMAFG GTTGIPFPGV
GTSYDYSAPI SETRFVGDKY SETKLFAQFL RVARDLTKVD RVNNGTTYAS NSAIMTTELR
NPDTNAAFYV TAHAFSPSTD RSPFKLDVST SAGRLTIPQN GGNIVLNGRE SKIIVTDFSV
GREKLIYSTA EVLTVSIQDG KPVVFLWLPA GESGEFLLDC IRIPLVLKKD GCSNIKFKQG
RKGFVTSYTQ SKGSCVLQFE TGIRFVLLDR SAAYDTWVPS LSNNPFTYEN TTVVVQGPYL
VRNVAIEKKT IDISGDWSEK TDLEVFAPKA VNSITFNGKK VQTRKTLYGS LIGTLKASTH
SVDSVKSSLP ALTSWKVNDG LPERKAAYDD SKWTDADHTT TQNPTAPATY PVLYSDEYGF
HHGNLLWRGR FSGAATGVYL DVIGGAFSGW SAYLNDKYIG SWVGNKDSNG ALELSFANAT
LNTDSENVLF VIQDHMGKDL RGGATIARGI YNATLVGGGK FSSWKLTGTA GGEDNIDPVR
GVYAEGGLHA ERLGWHLPGF NDAAWKKGTP DTGLSTDGAN FYRTVVPLDI PKGIDVSLGL
KLSSPTGLHL RAQVYVNVFP GILDYHGDNT IAVSLWAQDA AGASLTVDWT VLGVVESAFD
PGFEADYLRP GWTDNRTRAV AGASAELRLA QRGGVAASGL AAGIDGGGAV RGAHGVASTV
FGEGGFEGGG GEGEGEGEGE EGFGVHDGWW IDLLGLDKWA GPFLVATAFS CLNINNSPSF
AFAVLDAFIS SLTVISSPTL AIMLATMNTA APFWVSIALL VPRALAAPAD SSATAAAPSC
TASLITSLCD YPSAGPEFSV AISSRASCWE YCNDHPPCNF AIFSAGNPYT GSGACLLYPG
ENFDASKGST DCGNPSLSVY DKPVCAGGSA TTTAGACAAT ASPSAVASVC GYPTPPDNCQ
SSCYASSGSA HCLSICAKAD SCNYAIFKAM SESKSPYSAG NCWIYTEGKF NPGLATACTG
SPDQFVYNNL DNVCPKPSPT SSSLASSATA HSSGTETASA TTGSHGSGGS GGTTGDTTGS
ADGAATSSTG TETTGNTGSS TNSSGTNSNG TGTKSNGTET AAAPATTTTN SAAAGLSLTN
PLAIGAAVLM WMAL
//
