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Database: UniProt
Entry: A0A0Q9C090_9CELL
LinkDB: A0A0Q9C090_9CELL
Original site: A0A0Q9C090_9CELL 
ID   A0A0Q9C090_9CELL        Unreviewed;       853 AA.
AC   A0A0Q9C090;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=ASE27_13325 {ECO:0000313|EMBL:KRD35749.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD35749.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD35749.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD35749.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD35749.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD35749.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRD35749.1}.
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DR   EMBL; LMJG01000015; KRD35749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9C090; -.
DR   Proteomes; UP000051694; 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   Gene3D; 2.60.120.200; -; 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; IPR013320; ConA-like_dom_sf.
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; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT   DOMAIN          22..151
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          155..515
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   REGION          834..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   853 AA;  89719 MW;  3141EA90D0AA0809 CRC64;
     MATTAWSSAA PAAASEDEAP LALVPRPVSL ERGPGSGFRL GPTSVIVAPD DAAPVGEYLA
     DLLRPSTGFS LPVSDVSAAT GAITLTLTDA ASTDPEGYEL TVSEGAVAID APTAAGLFHG
     VQSLRQLLPA AVEATQVQDA DWVVPAVTIE DEPRFEYRSA MLDVARRFYP VDAVKRYIDQ
     IALYKLNTLH LHLTDDQGWR IAIDGLPALT EIGASTQSGW APGSNTGDPW FYTPADYAEI
     VEYAASRYIE VVPEIDGPGH TLAAQASVPG LTCDGVPTAP YYGFDVNLPM VCATEANSAN
     IRDYLEKVIS SVAAQNPGQY IHLGGDEVPN PPAGWYEAYT AMANEIATEH GKTIVGWHQW
     AQGATLPAGS LVQYWAEGRV NRPKIGVGAE SADIREVRAA LAAGARVVVS PADRSYTDMK
     YSSSTAYGLS WAGLVNLRRA YDWDPVTELS STDGTVKVVT EEQVAGVEAS LWADRAYRGS
     TSLPTSHSQF IPVEQYTDHM IFPRMPAIAE IAWSPAQDKD YTEFLSRLTQ HDDRWDALGY
     EWFRAPDVEW EPVVPVEPEL VHHWAFDETS GQSALDVVTG VRAAVDGGTW TPGQLGGAVS
     LDGVDDGVAL SAAPVSGPWT VASWVRRTGA RSSSALLSDT SSGVRTAIKL EQYKATAKVG
     FTQLGVADHR SEYATPLDEW VHLTLVSDGA TITVYADGAQ VSTVPGTATL GLAQLGRLMN
     APGWPGASDA AAVDVDDLRV YTGALDRAAV GALWDEVSPA PATVEVDATT RCVAGRVVIS
     VRAVNVGDVA VDLQVVTAAG KKSFSAVAPG AGAHQSFATR ASTIEAGTVT VTTGGAGGTE
     SEVTAGHPAL SCG
//
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