HEXA_EMEND
ID HEXA_EMEND Reviewed; 603 AA.
AC Q9HGI3; Q5BD78;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Beta-hexosaminidase {ECO:0000255|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000255|PIRNR:PIRNR001093, ECO:0000269|PubMed:12450128};
DE AltName: Full=Beta-N-acetylglucosaminidase {ECO:0000303|PubMed:12450128};
DE AltName: Full=N-acetyl-beta-D-glucosaminidase NagA {ECO:0000303|PubMed:17455791};
DE Flags: Precursor;
GN Name=nagA {ECO:0000303|PubMed:12450128, ECO:0000312|EMBL:BAB13330.1};
OS Emericella nidulans (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425 {ECO:0000312|EMBL:BAB13330.1};
RN [1] {ECO:0000312|EMBL:BAB13330.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND BIOTECHNOLOGY.
RC STRAIN=A26 {ECO:0000303|PubMed:12450128};
RX PubMed=12450128; DOI=10.1271/bbb.66.2168;
RA Kim S., Matsuo I., Ajisaka K., Nakajima H., Kitamoto K.;
RT "Cloning and characterization of the nagA gene that encodes beta-n-
RT acetylglucosaminidase from Aspergillus nidulans and its expression in
RT Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 66:2168-2175(2002).
RN [2]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=FGSC 26 {ECO:0000303|PubMed:17455791};
RX PubMed=17455791; DOI=10.1007/bf02931619;
RA Pusztahelyi T., Molnar Z., Emri T., Klement E., Miskei M., Kerekgyarto J.,
RA Balla J., Pocsi I.;
RT "Comparative studies of differential expression of chitinolytic enzymes
RT encoded by chiA, chiB, chiC and nagA genes in Aspergillus nidulans.";
RL Folia Microbiol. (Praha) 51:547-554(2006).
CC -!- FUNCTION: Part of the binary chitinolytic system. Involved in
CC hydrolyzation of chitobiose and higher chito-oligomers (produced from
CC cell wall chitin by endochitinases), thus contributing to the formation
CC of germ tubes, fruit-bodies and septa during hyphenation (Probable).
CC Hydrolyzes synthetic substrates p-nitrophenyl-beta-N-acetyl-glucosamine
CC (pNP-beta-GlcNAc), p-nitrophenyl-beta-N-acetyl-galactosamine (pNP-beta-
CC GalNAc) and 5-bromo-4-chloro-3-indoyl-beta-D-N-glucosaminide (X-GlcNAc)
CC (PubMed:12450128). {ECO:0000269|PubMed:12450128, ECO:0000305}.
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:0000255|PIRNR:PIRNR001093,
CC ECO:0000269|PubMed:12450128};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4-5. {ECO:0000269|PubMed:12450128};
CC Temperature dependence:
CC Optimum temperature is 52 degrees Celsius.
CC {ECO:0000269|PubMed:12450128};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8J2T0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12450128}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during the stationary phase and
CC high levels remain in the autolytic stage.
CC {ECO:0000269|PubMed:17455791}.
CC -!- INDUCTION: Significantly up-regulated expression with colloidal chitin
CC and chito-oligomers, namely N-acetyl-D-glucosamine (GlcNAc), N,N'-
CC diacetylchitobiose (GlcNAc)2 and N,N',N''-triacetylchitotriose
CC (GlcNAc)3. Expression is unaffected by the oxidative-stress-generating
CC agents tested including menadione, hydrogen peroxide and diamide.
CC {ECO:0000269|PubMed:17455791}.
CC -!- DISRUPTION PHENOTYPE: Normal growth rate, cellular morphology and
CC efficiency of conidial formation when grown on easily metabolizable
CC carbon sources YG (complex) or MM-glucose (complete) media. Grows
CC poorly on a medium with chitobiose as a sole carbon source. Low level
CC of beta-N-acetylglucosaminidase activity.
CC {ECO:0000269|PubMed:12450128}.
CC -!- BIOTECHNOLOGY: This enzyme can be produced in large-scale and may be
CC used for the enzymatic synthesis of complex type sugar chains
CC containing GlcNAc and GalNAc as components.
CC {ECO:0000303|PubMed:12450128}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000255|PIRNR:PIRNR001093}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB039846; BAB13330.1; -; Genomic_DNA.
DR PIR; JC7900; JC7900.
DR AlphaFoldDB; Q9HGI3; -.
DR SMR; Q9HGI3; -.
DR CLAE; HEX20A_EMENI; -.
DR OMA; QYWVDHA; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:UniProtKB.
DR GO; GO:0015929; F:hexosaminidase activity; IDA:UniProtKB.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052781; P:chitobiose catabolic process; IMP:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.379.10; -; 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; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..603
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004330883"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT SITE 309
FT /note="Important determinant of glycosidic bond
FT specificity"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT SITE 485
FT /note="Essential for chitooligosaccharide substrate
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q06GJ0"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 293..354
FT /evidence="ECO:0000250|UniProtKB:Q8J2T0"
FT DISULFID 451..486
FT /evidence="ECO:0000250|UniProtKB:Q8J2T0"
FT DISULFID 586..593
FT /evidence="ECO:0000250|UniProtKB:Q8J2T0"
SQ SEQUENCE 603 AA; 67984 MW; 5C9B1EB726D7A3FD CRC64;
MAYFRLYAVL LAVASSVAAV KVNPLPAPRH ISWGHSGPKP LSDVSLRTER DTDDSILTNA
WNRAWETIVS LEWVPAGIEA PIPEFDEFPT STPSASAAAT RSKRANVPIQ FVDVDVEDWD
ADLQHGVDES YTLDAKAGSD AIDITAKTVW GALHAFTTLQ QLVISDGNGG LILEQPVHIK
DAPLYPYRGL MVDTGRNFIS VRKLHEQLDG MALSKLNVLH WHLDDTQSWP VHIDAYPEMT
KDAYSARETY SHDDLRNVVA YARARGIRVI PEIDMPAHSA SGWQQVDPDI VACANSWWSN
DNWPLHTAVQ PNPGQLDIIN PKTYEVVQDV YEELSSIFTD DWFHVGGDEI QPNCYNFSTY
VTEWFQEDPS RTYNDLMQHW VDKAVPIFRS VSDSRRLVMW EDVVLNTEHA DDVPTDIVMQ
SWNNGLENIN KLTERGYDVI VSSADFMYLD CGRGGYVTND DRYNEQTNPD PDTPSFNYGG
IGGSWCGPYK TWQRIYNYDF TLNLTNAQAK HVIGATAPLW SEQVDDVNIS NLFWPRAAAL
AELVWSGNRD AKGNKRTTLF TQRILNFREY LLANGVMAAT VVPKYCLQHP HACDLNYDQT
VLH
