ID F9FJH4_FUSOF Unreviewed; 1247 AA.
AC F9FJH4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=FOXB_06553 {ECO:0000313|EMBL:EGU83000.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU83000.1};
RN [1] {ECO:0000313|EMBL:EGU83000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83000.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001231};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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:EGU83000.1}.
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DR EMBL; AFQF01001995; EGU83000.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FJH4; -.
DR STRING; 660025.F9FJH4; -.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06564; GH20_DspB_LnbB-like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR015882; HEX_bac_N.
DR PANTHER; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1247
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383362"
FT DOMAIN 52..167
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 178..487
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REPEAT 919..955
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1034..1068
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1103..1131
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT ACT_SITE 336
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1247 AA; 136268 MW; 21BAB7E2562DF12F CRC64;
MLKEYLVAGI LLASPLLAVA QDLIPPILEN ADSFVEETWS VDSSPKVIYI DDGFASVSDK
DGLTLIPPTA HEFATTFQDD LAKITGSNWT LKRVNSLPTN ASGISLGSYT GEFSDLTYEN
GKSTSEGYEI IINSNRVFIG GSGARGMWWG TRTFLQLLLA GNGTITSTLG RDSPAYVTRG
YMLDAGRKWY SKDFLKELCS YASFFKMNEF HYHLSDNYPL NRGKNDSWRD VYSHFSLLPD
DKSLRGILHG RENETLSRDD FMELQSHCAS RGVTVIPEIE APGHSLYLTK WKPELALAKK
DLLNLTHPDT LPTVQSIWKE FLPWFKTKEV HIGADEYDAE LADDYITFVN KMSRFINSTT
NKRSRIWGTH EPSKRNQTID KNVIIQHWQY GQSDPVQLVK DGYDVINSED WWAYTSLKND
HMPILPARYP QFFNESRVFN FADKEEWQWT PADFNPVNTS LQLKSDEKRL RGATLAAWND
NGPDATTQLE AYYSMRRGIA VVGGRAWSGS RGPKLLEETS DTSVDFYSPR APDQNLDRVL
SLGANGTLVS WTRSGGDGKE VHLGHGSKGM NYTLTLSVTG PFTLSGLDST LSLDKSGNMV
FTADGWEYPL RKVTKDDALD LDPGAPGRIW VNTSSTHKPV KVSTPVNITL VTDALHGTVV
FSNGEVVGRF EVFVYGGRNT QFSWSQMAFV APLDKIEGGL ERLELSGSSN FTGAGETGGE
EPTDVPQGSD AARCVASSAF ITLGLVVGGL LLNQNGSRIC LGLRIATVYS GLQGIQSSPL
QPLTYRPRAV MDLWQVGQRK YNDIYCSQKA AIAHSGSHAT LLHPRIRCAG RRGHHPPPLV
SLPYATVKAR PGEACNFADE GRGEGTLSPV IARHEARLRS ILDSPRDSDY ESLSLEADRG
ESTTLIEHSG VNVNIWDEGG LTALHAAIQY SGPTACPHII DVLLRHSADI NALSKAVQHI
LRTVAQSGGT VEYLTRLAAK LLQRGAYANV VGSSGNPALY TGILNIACFP QAWERGLMDV
LLQGGAGAND LDGNGASALH LAVTHGVHAG VIISGLLRHC ADPRTRCRDG RCVLHHLAKF
MGPPGVAKQL RNLGLDPNAR DEHGQTPLLH ATVAGLVKMV RLLCESGVGV NTPIFDDDKT
AFFCAVRLKT VDAAQVLLQY GADLHHRGHS GRTVLHYHEA AYKAMSNGSA DAARINKLLI
ACGANVNAKR GCCRQGHGMS VLDAGGITRA QGEFALFLMA NGALRFR
//
