ID I1RHT0_GIBZE Unreviewed; 1016 AA.
AC I1RHT0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 Name=FG03343.1 {ECO:0000313|EnsemblFungi:CEF78130};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EnsemblFungi:CEF78130};
RN [1] {ECO:0000313|EnsemblFungi:CEF78130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF78130};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF78130}
RP GENOME REANNOTATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF78130};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EnsemblFungi:CEF78130}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF78130};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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}.
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DR EMBL; HG970333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011322389.1; XM_011324087.1.
DR AlphaFoldDB; I1RHT0; -.
DR EnsemblFungi; CEF78130; CEF78130; FGRRES_03343.
DR GeneID; 23550658; -.
DR KEGG; fgr:FGSG_03343; -.
DR HOGENOM; CLU_005732_2_1_1; -.
DR OrthoDB; 1032627at2759; -.
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1016
FT /note="Probable beta-galactosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010161300"
FT DOMAIN 395..573
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1016 AA; 112831 MW; 719CCC79D6E20FB1 CRC64;
MKLLSLSTVG LLALTGFSIA QENANVPIQD NGLTNIVQCY LINGERIFVF SGEFHYWRLP
VPELWRDLLE KIKAAGFNAF SIYNSWGYHE ASPGALDFKN GAHDFESIMT LAKELGLYLL
IRPGPYVNAE ANAGGFPLWV TTGEYGKLRN DDPRFTKAWS KYWTEISKVI EPHLITNGGN
VAMFQIENEL GGQWKNDDKR ILNEPVANYM QLLKDAARDA GIDVPVFHNA PNTRTFSWSN
DFEANATGNV DVTGVDSYPS CWSCNLDECT GTNGEYVPYN IQDYVTYFSK QSPAQPHFLP
EFQGGSYNPW GGPEGGCPGD IGPDFANIFY RDLVAQQATA ISLYMMYGGT NWGWFACPVV
ATSYDYSSPI SENREIWDKY YETKSLTLFT RVAHDLTKTN RVTNSTSLST NDDVLVTELR
HEDNGAAFYV SRHDHSPSGT KETFKIRVNT SEGKLTIPQN DHITINGHQS KIIPTDFHFG
EKTLLYTTAE VLTYSVIDKK EVIVLWLPEG EHGEFTLKGH TELKHDKSLK GINVKAGKKS
ITVNYTQKKG LFTLNMKDGS TIVLADRQTA YKFWAPTLDN DPFAPVNKTV LVHGPYLVRH
ATVKNGQLNI EGDLDKSTDI TVFASESLKS ISWNGEKVKV SSKEGHKYTA KLKGPSKVKL
PKLESWKYTD SLPEIKSDYK TSSSAWVVAD KKNTTNAVLV PDLKNPVLYV DEYNVHYGNH
IYRATFPTTD KAPTGVYLNL TGGLAFGYSV WLNSDYVGSY LGNATVGRSG QEFSFKNATL
SKKENVLVVL MDNSGHDLRD GALDPRGITN ATLIGSAKGG YKFSEWKIAG HAGSVEGEVI
DPVRGPLNEG GLYAERIGAH LPGFSDKKWK SFSSKQGTLV NPSAGVRAYR TTVDLDIPDG
VDVGISFKLT APSNTTFSPT KKGYSNRVRV LLFVNGYQYG RFNPYIGNQV SFPVPPGVLN
YSGENTIAVT VWSQSAEGGE VKVEWEVDYA HSSSFDVKFD SEYLRPEWTE DRLQYA
//
