ID K1Z0G8_9BACT Unreviewed; 732 AA.
AC K1Z0G8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=ACD_77C00369G0001 {ECO:0000313|EMBL:EKD31204.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD31204.1};
RN [1] {ECO:0000313|EMBL:EKD31204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD31204.1}.
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DR EMBL; AMFJ01033857; EKD31204.1; -; Genomic_DNA.
DR AlphaFoldDB; K1Z0G8; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06563; GH20_chitobiase-like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF02838; Glyco_hydro_20b; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..732
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023041276"
FT DOMAIN 22..152
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 156..500
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 329
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 732 AA; 82743 MW; 68C9A6DDD1ABB24D CRC64;
MKRAFFTVIV AIMASLSLYS QVSIIPKPNS VTTGEGVFIL NENTTIGTND KNLSDLNYLK
DILFRATGFP VIVSKTIQPF NSIFLDVSGN YQIPAEGYIL TINANGASIK ASASSGIFYG
IQSLLQLLPP TVFSGRATGH EVWSIPAVTI EDSPRFHYRG MMLDVSRTFF SADVVKNYID
WMAYHKLNVF HWHLTDDNGW RIEIKKYPDL TEKGAWRGPG EVLAPSFGSG NKRYGGFYTQ
KQIKEIVAYA AARHIEIVPE IDLPGHSKAV TATYPNVACD NPENTLSVQG EGQNVWCVGK
EENFKMLDNI IKEISKLFPG QYIHIGGDEV NYSAWDKCPH CQALMAKEGM KSHEELLNYF
VRRMEVIVEK HGKHMAGWDE ILEGGALNPK TRVYAWRSVE KGIESVKKGQ PTIMMPGAYR
YFDMKQSELE RGHNWAGIVS VEKAYSLDPI GTAFLDEEQS KLIEGVQGAL WTELLGWPSR
FIEYQTYPRL SANAEAAWTN QNLRNWEDFN DRLMKFHYDR MYHMGIAFRI TPPLAKFEDG
AVKVTLPYPW AVVRFTMDES EPNAQSPVYK GDVYTDKPLK FRFATFFRDE LKSITVKVSN
VEYEYQKPEL EIETNIEAGK GNPTVNLTDG KQNTYFRSSR KLQAGDYLTY RFKTPVSTQK
IIVETGIPNI AFYWVTDGYA EVSYDGISFL KVTDLNRGSA VIRPKEPVKA VRIVVTAPND
GHIGAFQDLK IE
//
