ID D2KW09_9BACL Unreviewed; 978 AA.
AC D2KW09;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00030512};
GN Name=hex1t {ECO:0000313|EMBL:BAI63641.1};
OS Paenibacillus sp. TS12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=192895 {ECO:0000313|EMBL:BAI63641.1};
RN [1] {ECO:0000313|EMBL:BAI63641.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TS12 {ECO:0000313|EMBL:BAI63641.1};
RA Sumida T., Ishii R., Yanagisawa T., Yokoyama S., Ito M.;
RT "Molecular cloning and crystal structural analysis of a novel
RT glycosphingolipis-degrading beta-N-acetylhexosaminidase from Paenibacillus
RT sp. TS12.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:3SUR, ECO:0007829|PDB:3SUS}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-502, AND DISULFIDE BONDS.
RX PubMed=22367352; DOI=10.1039/c2ob06636j;
RA Sumida T., Stubbs K.A., Ito M., Yokoyama S.;
RT "Gaining insight into the inhibition of glycoside hydrolase family 20 exo-
RT beta-N-acetylhexosaminidases using a structural approach.";
RL Org. Biomol. Chem. 10:2607-2612(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; AB490155; BAI63641.1; -; Genomic_DNA.
DR PDB; 3SUR; X-ray; 1.90 A; A=1-502.
DR PDB; 3SUS; X-ray; 1.80 A; A=1-502.
DR PDB; 3SUT; X-ray; 1.90 A; A=1-502.
DR PDB; 3SUU; X-ray; 1.60 A; A=1-502.
DR PDB; 3SUV; X-ray; 1.60 A; A=1-502.
DR PDB; 3SUW; X-ray; 1.90 A; A=1-502.
DR PDBsum; 3SUR; -.
DR PDBsum; 3SUS; -.
DR PDBsum; 3SUT; -.
DR PDBsum; 3SUU; -.
DR PDBsum; 3SUV; -.
DR PDBsum; 3SUW; -.
DR AlphaFoldDB; D2KW09; -.
DR SMR; D2KW09; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd14254; Dockerin_II; 1.
DR CDD; cd06568; GH20_SpHex_like; 1.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR016134; Dockerin_dom.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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; PF00963; Cohesin; 1.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF07554; FIVAR; 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; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51766; DOCKERIN; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3SUR, ECO:0007829|PDB:3SUS};
KW Glycosidase {ECO:0000313|EMBL:BAI63641.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAI63641.1}.
FT DOMAIN 917..978
FT /note="Dockerin"
FT /evidence="ECO:0000259|PROSITE:PS51766"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
FT DISULFID 372..427
FT /evidence="ECO:0007829|PDB:3SUR, ECO:0007829|PDB:3SUS"
SQ SEQUENCE 978 AA; 105214 MW; E9E4B54529D0055C CRC64;
MMSFIPESAS ASTSQPSILP KPVSYTVGSG QFVLTKNASI FVAGNNVGET DELFNIGQAL
AKKLNASTGY TISVVKSNQP TAGSIYLTTV GGNAALGNEG YDLITTSNQV TLTANKPEGV
FRGNQTLLQL LPAGIEKNTV VSGVQWVIPH SNISDKPEYE YRGLMLDVAR HFFTVDEVKR
QIDLASQYKI NKFHMHLSDD QGWRIEIKSW PDLIEIGSKG QVGGGPGGYY TQEQFKDIVS
YAAERYIEVI PEIDMPGHTN AALASYGELN PDGKRKAMRT DTAVGYSTLM PRAEITYQFV
EDVISELAAI SPSPYIHLGG DESNATSAAD YDYFFGRVTA IANSYGKKVV GWDPSDTSSG
ATSDSVLQNW TCSASTGTAA KAKGMKVIVS PANAYLDMKY YSDSPIGLQW RGFVNTNRAY
NWDPTDCIKG ANIYGVESTL WTETFVTQDH LDYMLYPKLL SNAEVGWTAR GDRNWDDFKE
RLIEHTPRLQ NKGIKFFADP IVWELPIVQI NSEWKMDEGT GTVVKDTSGY LNGTLVGGAK
WTAGKQGNGV SFDGSSGYIN LGGQDITGNW TAAVWVYGQP NTTNNETLLS GTTSAIKINQ
YNKTGKVGIT IYGTKDYTYN YSIPSNKWTH LTFVGTSTGT ALYENGVLKE TIAAKMNGPM
ALVGAEKTGG SGDLTSYFRG SLDELKIFNR ALSASEVVEL AKSPAPKASL TGPQSANPGQ
SFDVKMGLSD VSPSEFGQMY AQDWTINYDS AKLQLDSITS LQDKFQVIDQ KELAPGQIRI
VAANAAANQG VTPQGDLFAF KFTVKAGTDV KTTISADHIV IGNAQGKELE IAGATHEIQV
SIPVDKSQLN VLIANAQAKH DAAVEGNEDG LYAAGSKAQL QTAIHTAKAV ADNSNASQQQ
VDSAKSALEE AVQVFESKKI SADVNGDGQV SIGDLAIIAG AYGKEEGQAG WNKKADVNHD
GKVDIIDLTI VAKAILQI
//
