ID C6W1V4_DYAFD Unreviewed; 868 AA.
AC C6W1V4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN OrderedLocusNames=Dfer_4327 {ECO:0000313|EMBL:ACT95529.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT95529.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT95529.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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}.
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DR EMBL; CP001619; ACT95529.1; -; Genomic_DNA.
DR RefSeq; WP_015813772.1; NC_013037.1.
DR AlphaFoldDB; C6W1V4; -.
DR STRING; 471854.Dfer_4327; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR KEGG; dfe:Dfer_4327; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_4_1_10; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000002011; Chromosome.
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:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02847; E_set_Chitobiase_C; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004866; CHB/HEX_N_dom.
DR InterPro; IPR004867; CHB_C_dom.
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 InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF03173; CHB_HEX; 1.
DR Pfam; PF03174; CHB_HEX_C; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM01081; CHB_HEX; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:ACT95529.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACT95529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..868
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002970954"
FT DOMAIN 32..182
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 545
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 868 AA; 97096 MW; 6E748D3FACD4BDE1 CRC64;
MKKLFPLSLI LFGALLLASC NKSGNVSKEQ AEKIAVSWKL VSNFIEPEGR FEAQFTIRNG
SDFTLDGSNW RLFWNMSPRP IQSNQTPQPA VIEHINGDWY QMLAAKDFKL APGDSVVIKY
TGTEGVIKET DAPLGLYFVF YDNEGKEKDI VQVADYTIEP FTTKEQILRG KMDLKEVPTA
ETRFKANAGF TKIGEEQLLK IIPSPVKLIP GAGTFTMTGK TNVYYQEGLE TEARYLISKL
KTLTGTDLPI QAGLPNKPSS EEAAIVLKTG KVAVNGISSE AYTLNIAQTG ITIEGSDAAG
VFYGVQSLLQ LAPTDSYQKP VASIGFGFVQ VQDAPRFQFR SLHLDVARNF QTKESVKRII
DLLSSYKVNH LLLYTTEDEG WRIEIDGLPE LTQVGAQRQH TSGMNANALH PGYGSGPVAN
EKGKHGSGYY TKADFIEILK YAHERHIKII PELNFPGHAL AAIKSMEARY ERLMKEGKEK
EANEYRLIDP DDKSVYISAQ GYKNNVVSVA RESTYNFFVK VVDEIAKLYE QAGLKMDTFH
TGGDEVADGV WTKSPMAAKL LQEHPEIKGP RYLQSYFFGK LLPMLEKRNL KVHGWEEIAL
NKTEKGAYLA NPEFVGHQVY PYVWNNVYDV DLGNRLANAG YQVVLCNVTN FYFDMSYNND
PKEPGLYWGG FVDTRDNWAF APFNMFRTTE ETSMGKPMKE EFAGKQAMKP EARKNVYGIE
AQLWSETIKG RDMMEYSILP KLLGFSESAW AAERKWENVA DDAARKAMMA EGWNIFANSI
AQKHLPRLKY INGGYNYRLP QPGAVIENGM LKANVELPGL AIRYTTDGSE PTEQSQLYES
PVKVSGTVTL KSFDLAGRSS RSSVVTAR
//
