ID A0A0G1CX57_9BACT Unreviewed; 754 AA.
AC A0A0G1CX57;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=UV65_C0022G0005 {ECO:0000313|EMBL:KKS90012.1};
OS Parcubacteria group bacterium GW2011_GWF2_43_11.
OC Bacteria.
OX NCBI_TaxID=1618967 {ECO:0000313|EMBL:KKS90012.1, ECO:0000313|Proteomes:UP000034303};
RN [1] {ECO:0000313|EMBL:KKS90012.1, ECO:0000313|Proteomes:UP000034303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:KKS90012.1}.
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DR EMBL; LCFH01000022; KKS90012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1CX57; -.
DR Proteomes; UP000034303; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKS90012.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 185..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 439..749
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..95
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 754 AA; 83718 MW; 225846FD8B07D301 CRC64;
MLETNPNKIT NLSDQKEEKD LLAREEVKTM EKDTSHLREI EARRERERLA RIKTAEEIAR
EKEREGLAEK SALARDLAEQ EAKAREERII KMRETRAVEE SAQAQAKTEQ AEIATGEFRG
ALKETQAKEE ELRKKFLDRV EARAEGREEA PPLPPVPPTL PIVEEKKSPE IPKTFVKKPG
PGQKLWIRIV LGLLILAILA AAATFGYWYF VVRGGPETTA PVNRIPEQKE LVIPPPLFYV
ENTQTVKIAE TSEVPFVLAQ FVQTETALSS VNRILFEDTK NTEVLGLKGL FDSLGIITPN
GFYNKVADDP TFFIYSQEEG NRLGLVVKIN NQEGLAEMIK LWEGTMEENF QGLFGLLGKN
EPALSSSFKD AKYQEISFRF QTFTREDLGI VYAIFDDYFI LTTSWKSMEK ALDKLKEAPM
SHFFSPGIGA EFVLANMDLK GKIGQLFFIG INGTTLTQET ENLIASVQPG GILLLKKNIV
DEDQTKELIR GLQKVALENY GIPLFIGVDQ EGGVISPVNF IREKTGQSEI KTADQAYAVG
LGRGAELRDL GINLNLAPVL DVAQPGDFLF SRAFQATDSQ ADAFAKALIA GQKTASILTA
VKHFPGYGDI AFDPEDTLAT LDETPPIALF KTAAQAKPEF VMTSNVIYSK IDAELPFSFS
EKGIALLKES VGEEPLIMTD DLPQQSLIDT FALKGVVTLP IKAGADILTF SLNWETTLPE
AVRILQESVQ TGEISQERID GSVSKIIELK QAYY
//
