ID K5WX86_PHACS Unreviewed; 559 AA.
AC K5WX86;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=PHACADRAFT_173171 {ECO:0000313|EMBL:EKM55102.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM55102.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM55102.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM55102.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(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 ECO:0000256|PIRNR:PIRNR001093};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR EMBL; JH930472; EKM55102.1; -; Genomic_DNA.
DR RefSeq; XP_007395446.1; XM_007395384.1.
DR AlphaFoldDB; K5WX86; -.
DR STRING; 650164.K5WX86; -.
DR GeneID; 18909624; -.
DR KEGG; pco:PHACADRAFT_173171; -.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; K5WX86; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000008370; 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; cd06562; GH20_HexA_HexB-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; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..559
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005687052"
FT DOMAIN 22..154
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 177..509
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 336
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 559 AA; 60847 MW; B43E542F4C7077AD CRC64;
MRLPIGLLVA LQPLFFRNVL AIWPAPRNIS SGEQTLLLSP EFSIVSDLPS TPQDLEDAVA
RTQARLFADG LGRLVVGRGA NDSVAFSSAE SLCTLRLALT SSSAAKSIAD EAVVPFEVRN
ESYALMVPAN GSEATLTAPT TLGLLRGLTT FEQLWYTYSE QVYAVNMPLV VHDSPAYPHR
GFGLDSARNF FPVPDIKRTL DAMSWVKLNA LYWHVVDSQS FPLEVSAFPE LSQQGAYSAM
QVYSEADVQD IISYAAARGI DVVLELDTPG HETAIGLSHP EHVACYLSTP WADFASEPPA
GQLRLATPAT VNFTVALVAS VSAKFRSALF STGGDEVNAN CYTQDTQTQA DLAQSGLSFD
EALNEFLLAT HAVIRAQGKT PIVKEDMILN HNTTLPNTTI AVVWISSQDA KNVTERGYRV
IHQPSDYFYL DCGGGGWVGD DILGNSWCDP FKTWQRIYSF DPLANLTAEE ASLVIGGQIP
IWSEQSGPEN LDPIVWPRAA SAAEVFWSGG YSNGAALNVT DALPRLHDMR FRMVQRGIKA
IPLQPEWCAL RPNACDLNS
//
