ID B8PAX4_POSPM Unreviewed; 1025 AA.
AC B8PAX4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=POSPLDRAFT_127993 {ECO:0000313|EMBL:EED81936.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED81936.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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}.
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DR EMBL; EQ966297; EED81936.1; -; Genomic_DNA.
DR RefSeq; XP_002472828.1; XM_002472783.1.
DR AlphaFoldDB; B8PAX4; -.
DR STRING; 561896.B8PAX4; -.
DR KEGG; ppl:POSPLDRAFT_127993; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR InParanoid; B8PAX4; -.
DR OMA; FYIARQT; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000001743; 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:SF165; BETA-GALACTOSIDASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000001743};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1025
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002877108"
FT DOMAIN 416..598
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1025 AA; 111293 MW; 162999E52DB8A232 CRC64;
MLWYRGRLWA FPALLAVCLV LLTWPLSRTA DAAKLSTEHT PAASVAAASD PPRQSDNYTT
VVQWDNYTIF LNDQRMFLHS GEFHPFRLPV PDLWLDIFQK MVAAGLNAAS HASAERRNIH
GWAGTLTNPA PGVLDFNDWR ALQPVFDAAK LAGIFIVLRP GPYINAETTA GGIALWATSL
VAGELRTNAT DYRDAWTPYI DEIAASVVPN QVSDGGPILV VQIDNEYYQD AYTGEYFVEL
EEAYRQAGVV IPLTYNDPGE GKNFVNGTGA VNIYGLDSYP QGFDCSTPEV WSPVVTNYHQ
YHEETDPAEP WYMPEFQGGS FDPWGGSGYD ACEILTGADF QDVFNKQNWA SNVKLISYYM
VYGGTNWGGL AEPGVYTSYD YGSSIRESRL LSDKFDELKR QGIFLRSSPE FYKTDWVGDT
DTTMPGVTVN GSEAYVTWLR NPDTGAGFYI VRQANSSSLA DITFRISVPT SAGTLSLPRT
TDSIALDGRQ SKVLVTDYTF GTSSSVLYST ASVFYAGTIG GRDILFLYGD FNQSHEIALE
FTGTGTQFAK STVSFSTGAD IDGYTTVTLL PGIEGFVPLY ESDTQLILYS DSVTAATFWA
PVIPASEGTA FQSYYQFGSN TTILVGGPYL VRNASISDGT LALRGDLNQS ALLTIIAPDD
VTSVTWNGAP VSAYSLTDGI LAGYLSTNLT TSSITVPALT GWKYADSLPE VQSNFSDADW
VIANHTTTNI TPGMLYGDGQ VLFGCDYGFC ENTVLWRGHF TGTGSETSVN LTINGGTAFA
GSVWINDYFI SSTWSVSEEQ TTVVYAFPEG SVLVGQDNVV TVVQDGMGND ESPNEKSPRG
IPGFLLNGGS FTEWKVQGKL GGYTAYPDKV RGILNEGGLY GERDGWHLPG YDTSSWTARE
LSEGLPSSGA GIGFFVTTFD LSIPQETDAL MSFQFDTLNQ AYRALLFVNG WSYGKRVANI
GPQTIFPVPQ GILDYDGTNT VAVALWALEN SSVSPTLELV VDNVYEGGVG SIATNNPSWS
PRSLL
//
