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Database: UniProt
Entry: A0A1F5LHV8_9EURO
LinkDB: A0A1F5LHV8_9EURO
Original site: A0A1F5LHV8_9EURO 
ID   A0A1F5LHV8_9EURO        Unreviewed;      1008 AA.
AC   A0A1F5LHV8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PENARI_c009G11111 {ECO:0000313|EMBL:OGE52798.1};
OS   Penicillium arizonense.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE52798.1, ECO:0000313|Proteomes:UP000177622};
RN   [1] {ECO:0000313|EMBL:OGE52798.1, ECO:0000313|Proteomes:UP000177622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE52798.1,
RC   ECO:0000313|Proteomes:UP000177622};
RX   PubMed=27739446; DOI=10.1038/srep35112;
RA   Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA   Workman M., Frisvad J.C.;
RT   "Penicillium arizonense, a new, genome sequenced fungal species,
RT   reveals a high chemical diversity in secreted metabolites.";
RL   Sci. Rep. 6:35112-35112(2016).
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         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OGE52798.1}.
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DR   EMBL; LXJU01000009; OGE52798.1; -; Genomic_DNA.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000177622; 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; -; 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; IPR019801; Glyco_hydro_35_CS.
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.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000177622};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1008       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5009519604.
FT   DOMAIN      390    569       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1008 AA;  111270 MW;  7F4F1BEB798D31F6 CRC64;
     MLLSKVTLLT LWSVAASLVP GSISSKIPTE SNGLQDLVTW DQHSIIVRGE RLMIFSGEFH
     PFRLPVPGLW LDVFQKIKSM GFTGVSFYTD WSLLEGNPGH VITDGIWNLD EFFNAAAQAG
     IYLIARPGPY INAETTGGGI PGWVLRKQAI IRSDDPEYLN ATEQYVSTLG QIIERAQITH
     GGPVIMVQPE NEYSTWPDVT DFPSEMNSNY MAYVEKQLLD IGISVPLIVN DNLNLGYFAP
     GSGVGEVDIY GIDSYPMRYD CAHPTVWPTY RFPYNWQVLH DQESPTTPFA IAEFQGGSGE
     GWGGVDQDMC GQLVNEEAVR VVYKNNYSFG VKIFNIYMTF GGTNWGNLGY MGGDTSYDYG
     AAIAEDRTIW REKYSEQKLE ANFLKVSPAY LTATSHLGVN GSYGAPATIA VTPLIGNGTQ
     TNFYVIRHAD FTSIDKTQYT LTLATSVGNI TVPQLGGHLT LNGRDSKFHV TDYDVGGINL
     IYSSAEIFTW ARGAESARVL ILYGGVGESH EFALPSHLGK PTVSEGTDIT VQRRGATWVI
     HWHVTPDRRI VRAADLEIYL LWRNEAYNYW VMELPASGAI GNYSSPSKNV VILKAGYLIR
     TANLIETRLH LTGDVNATTE IEIISSPVKH LQDITFNGEA LKTSKSTNRK IFGTVRYDPP
     KFDIPDLSNL DWKFLDSLPE IMTSYDDSAW TRCTLKSTHN PRPLDTPTSL YSMDYGYHTG
     SLFYRGHFNA NGQESNVWLN VSGGIGFGHS FWLNNTFLGS WVGSSANSTI VHNVSLPSAL
     TQGSAYVLSV LIDHMGQDEE APGTDAIKFP RGILNYGISG HDQSDVSWKL TGNLGGEQYQ
     DLVRGPLNEG SMYAERQGYH YPSPPDSKWK KSNPVKDGLS HAGVGFYTAS FQLRIPSGWD
     VPMSVVFGNS SQINSGNGRD NYRCQLFING YQFGKYINKL GPQNIFPVPE GILNHEGENF
     IALTVWAQDK LGAALGGLEL VPTSAIKSGY SRPQPAPQPT WVRRSGAY
//
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