ID A0A2G3J646_9NEIS Unreviewed; 827 AA.
AC A0A2G3J646;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CSQ88_20040 {ECO:0000313|EMBL:PHU99905.1};
OS Iodobacter sp. BJB302.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Iodobacter.
OX NCBI_TaxID=1506510 {ECO:0000313|EMBL:PHU99905.1, ECO:0000313|Proteomes:UP000224670};
RN [1] {ECO:0000313|EMBL:PHU99905.1, ECO:0000313|Proteomes:UP000224670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJB302 {ECO:0000313|EMBL:PHU99905.1,
RC ECO:0000313|Proteomes:UP000224670};
RA Jude B.A., Perron G.P., O'Brien K., Doing G., Bettina A.M.;
RT "Draft genomes of phenotypically distinct violacein producing isolates
RT cultured from the Hudson Valley Watershed.";
RL Submitted (OCT-2017) 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:PHU99905.1}.
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DR EMBL; PDZG01000090; PHU99905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3J646; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000224670; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 7..151
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 827 AA; 90379 MW; E477B0038D2F80D0 CRC64;
MTQPAGAHIQ LKWECLTNHY EGDHFLAELT ITNLSDVALS GQDWAIYFNT CRKIKPETVQ
GGVVMEHVNG DVSRFIPAAD FAGLPAGASM VVRYQGIFWV INETDAPLGF YIVYGNAVAD
AIGDPQIVPF SRPEQCNRNL ADAVPLMTPA LRFAENQALT LLPSDAVGKI TPTPTEARWD
AGQYLITAAT LIVHDEVLAK EAAFLRAALR DVSGVELQRA SRGAGITLQL GKVDVAGSGA
PLEAYSLEVS AAGIVITGAS AAGVMNGIQS LRQLLPVDSY LNPQPGLAVP FGYVIDAPRF
AYRGMHLDVG RNFSSKETVL RLLDCMALYK LNKFHFHLTD DEGWRLEIPS LPVLTEIGSL
RGFSPNEESS LLPSFGSGAV VQGSAGTGFY SRADFIEILQ FATARHIEVI PEIDVPGHAR
AAIKAMELRY ERLKAAGDLA GAEEYLLSDF NDQSKYESVQ LWHDNVMCIG QESCYRFIET
VLVDMKAMFA EAGAPLTTMH TGGDEVPHGA WEGSPICQAF MQEQGITSIQ GLQNYFLARY
RTLLQKHNLV FGGWEEIALS KQDGKHGPNP EFVDAKFQPY VWNNVWGWGQ EDFAYQLANA
GYQVVLSNVT NLYFDLSYAK DPQEPGYYWG GFIETRGAYE FCPLDIYTTA TVNLFGQPLD
ADSLAKMQRL TAEGTKNVLG MQGQLWGENA RSQGRVEYLA MPRVIALAER AWAADPGWTK
ISDKAARAAK MDADWNQFAN RLGQRDMPRL DGFVGGYGYR IPLPGVQRVD GKVSLNVSAP
GLALRYTQDG SEPNAQSALY TGPFAAEGVI KAASFSRTGR KSKTVVA
//
