ID C3QI61_9BACE Unreviewed; 836 AA.
AC C3QI61;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=BSAG_03357 {ECO:0000313|EMBL:EEO51645.1};
OS Bacteroides sp. D1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO51645.1, ECO:0000313|Proteomes:UP000003361};
RN [1] {ECO:0000313|EMBL:EEO51645.1, ECO:0000313|Proteomes:UP000003361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:EEO51645.1,
RC ECO:0000313|Proteomes:UP000003361};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. D1.";
RL Submitted (MAY-2011) 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:EEO51645.1}.
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DR EMBL; ACAB02000114; EEO51645.1; -; Genomic_DNA.
DR RefSeq; WP_004317285.1; NZ_JH114350.1.
DR AlphaFoldDB; C3QI61; -.
DR GeneID; 69481379; -.
DR HOGENOM; CLU_007082_4_1_10; -.
DR Proteomes; UP000003361; 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 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 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; 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, ECO:0000313|EMBL:EEO51645.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..836
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002931059"
FT DOMAIN 29..181
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 836 AA; 94082 MW; D92709D347BE5F86 CRC64;
MRNILYMIGG SLCLLLFMTG CKSADGAKAP VSLTWEMGAA EVQPGYYENS FILKNISDVP
LGKDWIIYYS QLPREILQDE SASVKVEVVN ANFFRMYPAE NFQPLAPGDS LIVTFCCTNG
LKKLSYAPEG TYWVSQAGGK QGTPLPVELT IQPLQGMETE DWYPAPDKIY ASNLALETTA
KLQQTDIFPS VKEAFPAIGK ENVIIENKVR LTFHPDFANE AGLLKEKLET LYGLEVISEA
PVTVHLDYLP QQETATNDEY YRMDTGNSLI NISAPTSHGI FNGTQTLLSL LKGQEKPFRL
EAVSIRDYPD LPYRGQMLDI ARNFTTADQL KKLIDAISSY KLNVLHFHFS DDEGWRLQIP
GLEELTSVGA RRGHTTDELE CLYPGYDGNY DPSAPTSGNG YYTREEFIDL LRYAAQRHVR
VIPEIESPGH ARAAIVSMKA RYHKYINTDP EKAVEYLLSD AQDTSRYVSA QSYTDNVMNV
ALPSTYRFME KVIRELMVMY EEAEVPLTTI HLGGDEVPDG AWMGSPVCRA FMDEHGMTSA
HELSEYYITK MADYLQQYHV QFSGWQEAAL GHSEATDLHL NRLAAGVYCW NTVPEWEADE
IPYQVANKGY PVILCNVNNF YLDLAYDAHP DERGLSWAGY VDESKGFSML PYHIYRSSRT
DMAGNPVDLG IAERGKTVLT ASGKERIQGV QAQLFAETIR DFKWVEYYTF PKILGLVERG
WNAFPAWSML AREKEQQAFN KALALFYSKA SEKEMPHWAS RNINFRLPHP GLCLKEGKLY
ANTPIRGGEI RYTTDGAEPT LDSALWEAPI ACDASVVKAK LFYLNKESVT STLKVN
//
