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Database: UniProt
Entry: B1KIV5_SHEWM
LinkDB: B1KIV5_SHEWM
Original site: B1KIV5_SHEWM 
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}.
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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
//
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