ID A0A143HP48_9GAMM Unreviewed; 907 AA.
AC A0A143HP48;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A3224_11175 {ECO:0000313|EMBL:AMX03052.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03052.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) 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; CP014864; AMX03052.1; -; Genomic_DNA.
DR RefSeq; WP_067154506.1; NZ_CP014864.1.
DR AlphaFoldDB; A0A143HP48; -.
DR STRING; 252514.A3224_11175; -.
DR GeneID; 76608610; -.
DR KEGG; mthd:A3224_11175; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000076077; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..907
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007509551"
FT DOMAIN 48..212
FT /note="Chitobiase/beta-hexosaminidases N-terminal"
FT /evidence="ECO:0000259|SMART:SM01081"
FT ACT_SITE 554
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 907 AA; 99919 MW; BE4C147954E5C63E CRC64;
MIRVPLISAL LLAALLSACD RSGGFPAPTG SERLSSAERI ARDFLVTQEV LTNFQGVDER
LRTECKRAGG SGAICSSYRI SLINQGEAIR PGEGDWAIYF HSIRRSLRLL NRDDFTLEHI
KGDLHRLTPT EAFTGIAEGE TLAFDLLAEY WMQSESDFMP RLFVVDGAGK AHVIASTDSD
SIEGLALPIT SHHPENWKRT ADDANTLATP ASRYAAFSTR QPDGGESWRT RIIPRPQLLE
VTGEPVRLRT GIAVDAGPLE SRSLHAFRQR LEQLGLAPSG PGAYPVRVDI EPEAFREKVA
GAYTLQTKAR GARIIGRDQA GAFYGLQSLL ALVDLRSQTL ARVRVEDAPR FPHRGFSLDV
GRNFHSKAVV LKLLDQMAAY KLNRFHFHLS DDEGWRLEIP GLSELTEVGA RRCFDPGETR
CLLPQLGSGP KSDNSGSGFF TVEDYIHIVR YAAARHIEVI PEFDMPAHAR AAVVAMEARY
RKLADESAQR AAEYRLIDPQ DDTQYLSVQF YDDSYINPCI DSTYHFIGKL IREVQAMHRA
AGAPLASWHF GGDEALNILA GNGFEDAPGS DPDKGDVASV KRQMPWSESP ACQKLVPKGE
VEDLGQLGAF FAKRVSRLVA EAGIPTLAAW SDGVKHIENA GEMLATKRNY ANAWTPLFWG
GGAESVRLAD AGFGVVQSHA DFLYFDMPYE LDPKESGYYW ASRSTDTRKA FSYAPLNTAQ
LAEISTDRDG RGWSAMSPAP EFEKSVQGIQ GQLWSEVVRT DAQVEYMLFP RLLALAERAW
HRAEWELPLA EGQNFSARTA AVDKASLDAD WNGFAAALGN RELLKLDLSG IAYRIPVPGV
VVEDGALKTA LPYPGLPLEY FDGERWRELE TSVSADAVWA VRARSADGRR TGRAAILRAL
PAANAQR
//
