ID B1KIV5_SHEWM Unreviewed; 888 AA.
AC B1KIV5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 89.
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};
DE Flags: Precursor;
GN OrderedLocusNames=Swoo_1311 {ECO:0000313|EMBL:ACA85603.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA85603.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA85603.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP000961; ACA85603.1; -; Genomic_DNA.
DR RefSeq; WP_012323949.1; NC_010506.1.
DR AlphaFoldDB; B1KIV5; -.
DR STRING; 392500.Swoo_1311; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR KEGG; swd:Swoo_1311; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_007082_4_1_6; -.
DR OMA; DVIPRPY; -.
DR Proteomes; UP000002168; 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 CDD; cd06569; GH20_Sm-chitobiase-like; 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:SF52; N-ACETYL-BETA-GLUCOSAMINIDASE; 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:ACA85603.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACA85603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002168};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..888
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002766673"
FT DOMAIN 52..216
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 556
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 888 AA; 98451 MW; 98FEB87A8B1BB634 CRC64;
MKLKLLTAAI TLVLATSGCS DNSKVNDNKP VTQTKAQSAE AMTQAVLNQL GETLDVKYRL
LTNFPEGCPT EGVDGRCFSA QIDLTSKVDL SSADWAIYYS QMRPVQKVLS EEFEITRVKG
DLHKITPTAA FTGLKAGQTK TIDFRGELWQ LSEIDAMPNY YLISGDLTPA LIKSTTVTHD
PETGMELRPY VADFTDADTQ YKRSDTDLIK WATPEVLFQA NQGVELQTGA ATNTIIPTPL
KVEVTSENKP VSLGAGIKLV LNAQARGPID AALKRLARLG VTESDKGLPV VLNTLKDSTQ
AGAYQLAITE QGIELTAADD AGFSYGLSSL TSLIDSQDLS INTMLVEDAP RYDFRGMHID
VSRNFHSKQL ILDMLDQMAA YKLNKLHLHM ADDEGWRLEI DGLPELTDIG SKRCHDISET
TCLLPQLGSG PSADTQVSGY YSKADYIEIL KYASARQIQV IPSMDMPGHS RAAIKSMDAR
YKKFMAEGNE TAAKEYLLTD PDDKTVYSSI QYYDDNTLNV CLESTFHFVD KVIDEIAKLH
KDAGQPLTLY HIGADETAGA WLESPQCKAF VANNVQGVTS FDELGAYFVE RVSNTLNDKG
IEPAGWSDGM SHTRPDKMPK KSQSNLWDVI SHGGHNRAHE QVNLGWDAVL GTPEMLYFDF
PYEADPKEHG YYWASRNTNE RKLYGFMPDN LPANAEQWTD IQGQPFEVDD TEKLDDSGKR
ISGPIAQGKG FAGLQGQIWS ETLRSDELVE YMTFPRLLIL AEKAWHKASW EVPYQYTGAV
YNQTTEFFTQ EMRASQAKQW AVIANTLGQK ELIKLDMAGI DYRVPTVGAH IHEGELHTNI
IYPGLKIEYR IDGGKWEAFK SPVAVKGMVE VRALAADGTR KGRTLEVK
//