ID C6HNQ9_AJECH Unreviewed; 776 AA.
AC C6HNQ9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=HCDG_07840 {ECO:0000313|EMBL:EER38105.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER38105.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GG692432; EER38105.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HNQ9; -.
DR STRING; 544712.C6HNQ9; -.
DR VEuPathDB; FungiDB:HCDG_07840; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_010969_1_0_1; -.
DR OMA; GWQWTPA; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
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; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EER38105.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..776
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002966047"
FT DOMAIN 73..169
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 172..454
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 704..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 776 AA; 86521 MW; D21CF5D0D2FEFB2A CRC64;
MRLLLPLLAT AIAALQTLPP VDWPGSDNTP GSGFSISEAP KTVYIDEKFS ERRDENGLTL
IPPSGYEFAE TFLSDLEQAT GEKWTLKRIK EVPSDAKGII LGGFRQDADS LTYEDGTKSE
EGYELEIKNG QVFVGGTGAR GMYWGTHTFL QLLLVHGENE IPAGRIVDAP AYASRGYLLD
AGRKWYTPSF LKELCTYASF FKMSEFQYHS SDNYPLNRGL NDTWYEVYSQ FSLHPENEEL
KGVIQRANET LSRADFEDLQ QHCARRGVTI IPEIEAPGHC LFLTKWKPEL ALEKKDLLDL
TNPDSIPLVK SIWEEFLPWF QTKEVHIGAD EYDPTLADVY IHFVNEMAKF VKSKSGKDIR
IWGTYEPSDD MTISKDIIIQ HWQYGQSDPI LLNKDGYRYI NSEDWWGYMS LKSDHTPIFP
ATYPQFFNNT RTLNFANKPD WQWEPSLFNP VNVTEQVKPG VKGNKGAIIA AWNDNGPFAT
TQLEAFYAMR NGIPVVAARM WAGSRGNRLD AETLSATIEL LTNRAPGQNL DRRLPSEKGD
KKAGDTLLEW SREKGSKKLG QGSKGMNYTL ILDITGPFKL TSNDTSLSLD DGGNLVFNSD
NWAYPLRSVA EGDGYDPGHP GRIWTNVTSS THKPVTVPLT SQLTIKTDVI GGSRAWIDGK
FSGRFEVYIY GGKNTLFSWN QMALVAPLDT IEGDGLKSLT LKKDIKDTPD APDDPEHPSG
TPPAASSFVA KSFNRNTLLP QARMKGNSVC DAGCGSTGAS FRWSSLPEVT LAKILE
//
