ID A0A0J8VF69_9GAMM Unreviewed; 881 AA.
AC A0A0J8VF69;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ORFNames=C9I94_06860 {ECO:0000313|EMBL:PSW25369.1};
OS Photobacterium swingsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW25369.1, ECO:0000313|Proteomes:UP000240481};
RN [1] {ECO:0000313|EMBL:PSW25369.1, ECO:0000313|Proteomes:UP000240481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW25369.1,
RC ECO:0000313|Proteomes:UP000240481};
RA Butler K.;
RT "Whole genome sequencing of Histamine producing bacteria.";
RL Submitted (JAN-2018) 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 -!- 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:PSW25369.1}.
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DR EMBL; PYLZ01000003; PSW25369.1; -; Genomic_DNA.
DR RefSeq; WP_048897425.1; NZ_PYLZ01000003.1.
DR AlphaFoldDB; A0A0J8VF69; -.
DR STRING; 680026.AB733_02930; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000240481; 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: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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..881
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030009179"
FT DOMAIN 33..194
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 533
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 881 AA; 97468 MW; A37B20E2B2AECD75 CRC64;
MLKRSLLSCV VIASLTACSS ISPAQSSVNQ LAENLDINYT VITNQGADDG LACKELQAEW
ASCNKVNMTL TNTGEAVNST DWTIYFHSIR LILDVENDQF KITRVTGDLH KLEPTDKFDG
FAAGEEVVIP LVAEYWQLFE TDFMPGAFVT APGAEVRNII SLDTQDTGEY VDEIIGVQLK
RTLADNNVVA TANTRFEKNA DVTAVDATAH IIPTPLKTTR TYKKVDLANG ISITASGIDA
DQIAALNQRA ELLGIETAGE YPVSVTVDKH QFKDGVSGAY KLDITQNKTS VVAFDTAGAF
YGVQSLLALV NLDTTEIPTL NIEDAPRFEY RGVMVDVARN FHSKAAILAT IDQMAAYKLN
KLHLHLTDDE GWRLEIPGLP ELTDIGGKRC FDESETRCLL PQLGSGADSN NFGSGFFTTE
DYVEILTYAK NRSIEVIPEI DMPAHSRAAV MSMEARYARL AAEGRMDEAN QYRLMDPKDE
SNVTTVQFYN KQSFINPCLD SSATFVDKVI TEVAAMHKAA GVPLSTWHFG GDEAKNIKLH
AGFQDINDKE KIAWKGDLDL SKQDFPFAKS PQCQSLIASG EVADFEHLPS HFAEQVSKIV
ADKGIPHFQA WQDGLKHSKD ADAFATESVR ANFWDTLYWG GGASAYEWAD KGYDVVISNP
DYVYMDFPYE VDAKERGYYW ATRATDTRKM FGFAPENLPQ NAETSVDRDG NGFESAGTVT
PKKPFYGLSA QLWSETVRTD EQYEYMVFPR VIAAAERAWH QASWENEYKA GIKYSQETNR
VNKQAQLSDW TKFASAMGQR ELAKLERAGI DYRLPIPGAE VANGELSMNI SFPGVTLQYS
VDGGKTWVEY NNANKPKVTG EVQIRSASFT GERVSRVTSV N
//
