ID A0A1F5LRZ1_9EURO Unreviewed; 701 AA.
AC A0A1F5LRZ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=PENARI_c004G10049 {ECO:0000313|EMBL:OGE55709.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE55709.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE55709.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE55709.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE55709.1}.
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DR EMBL; LXJU01000004; OGE55709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LRZ1; -.
DR STRING; 1835702.A0A1F5LRZ1; -.
DR OrthoDB; 3202908at2759; -.
DR Proteomes; UP000177622; 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; 2.
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:UP000177622};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..701
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519830"
FT DOMAIN 63..163
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 166..327
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 335..471
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 701 AA; 78912 MW; FF94DCDBC9D9B79B CRC64;
MKWIVLSLAA VACALQTLPP VHLDPVAGRG FSLDTANRTI YLEADFASWR DQNGLTLIPP
SALEFATTFR DDLQELTNRS WDLQTVTRFP NASGVFLGRV PHSDRFTYED GRETEEGYEL
QVQDGSVSIR GSGARGMWWG TRTLLQQLIL TRSSIPAGRV EDAPAYKTRG FLLDAGRKWY
SLEFLKDLCT YASFFKLSEF HYHATDNYPL SRGPNATWNE VYSQFSLHPE DPKLQPLVQR
PNETLSRAQF EDFQRHCVQR GVTVMPEIES PGHCLSVTKW KPELALDSRD LLNLSHPDTI
PLMKSIWTEF LPWFHTKEVN IGADEYDSTL ADDYVKFVNE MSQFIQKTSG KSIRIWGTYE
PSNLTIDKGI TIQHWQYGQS DPIDLARNGY QIINSEDTWA YMSLKNDHVP IIPAPYPQFF
NNTRVLNFAD HDGWEWTPEL FNSVNITEQP DARAVQGAIL AAWNDNGPDA TTQLEAYYAI
RDGIPVVASR AWSGNRGPQL EQGKLGTSMA WLTSRAVGQN LDRQLIGESR SKSGTLLSWT
LDSRSNSDEH QLGHGSKGMD YTLELEVTGP FSLRSPDAIL TLSPDGQLTF TSDGWPYPLR
SVAEADGFDQ NQPGRIWANK TTSTHEIVKV PQQSRLTIST NKTTGSRVWV DGTFAGRFEV
FVYGGKNQVF SWSQMAFVAP LETLKGSGLH NLTLRHGSRH V
//
