ID C1GHJ2_PARBD Unreviewed; 754 AA.
AC C1GHJ2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=PADG_06728 {ECO:0000313|EMBL:EEH50649.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH50649.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH50649.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH50649.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275965; EEH50649.1; -; Genomic_DNA.
DR RefSeq; XP_010762211.1; XM_010763909.1.
DR AlphaFoldDB; C1GHJ2; -.
DR STRING; 502780.C1GHJ2; -.
DR GeneID; 22585385; -.
DR KEGG; pbn:PADG_06728; -.
DR VEuPathDB; FungiDB:PADG_06728; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_010969_1_0_1; -.
DR InParanoid; C1GHJ2; -.
DR OMA; GWQWTPA; -.
DR OrthoDB; 3202908at2759; -.
DR Proteomes; UP000001628; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 105..167
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 170..451
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 699..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 754 AA; 84037 MW; E3E827BED7FE4440 CRC64;
MFSPLLFIVT AASALQTLPP VRWPTSDGGS GFTFSATTNT VYIDETFATR SDQKGLTLIP
PSAYEFAETF LLDLEQVTGT KWDLRRTKEF PRDAKGILLG GFRDDADGLT YENGTPTEEG
YELEIKDGVV FIGGTGARGM YWGTQTLLQL FLINGEKEIP AGRTVDAPSY STRGFSLDAG
RKWYSPTFLK ELCTYASFFK MSEFQYHTSD NYPLNRGHNE TWNKVYSQFS LRPENEELHG
IVQRVNETLS RADFEDLQRH CARRGVTVIP EIEAPGHCLF ITKWKPELAL KKKDLLNLTH
PESIPVVKAI WEEFLPWFQT KEVHIGADEY DPTLADDYIN FVNEMAKFVK SKSGKDIRIW
GTHEPSENLT ISKDIIIQHW QYGQSDPLQL ERDGYRFINS QDWWAYMSIK NDHMPILPAR
YAQIFNNTRV LNFADQADWQ WEPSLYNPVN RTEQVKPDSK GNKGAIMAAW NDNGYDASTQ
LEAYYAMRDG IPVVAARAWA GSRGERLDSG SLSGTIELLT NRAPGQNLDR RILSLEKGGI
KAPDPLIKWS RETGAKTLGY GSKGMDYTLI LDTTGPFKLI SNDTTLSLSQ GGSLVFTSDN
CEYPLRSVSE HDGFDPGHPG RIWTNVSSST HEPVSVPLKS QLKIKTDVLS GSRVWLDGKF
VGRFEVFVFG GRNTLFSWSQ MAFVAPLDKI EGDGLESLTL RTDDDVPGGG GGGGDVPGGS
KPPNDSGSSR VGFMGLNEAT LLIFCSLVFL GMSC
//
