ID E3HZW2_RHOVT Unreviewed; 526 AA.
AC E3HZW2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, 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};
GN OrderedLocusNames=Rvan_0636 {ECO:0000313|EMBL:ADP69913.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP69913.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002292; ADP69913.1; -; Genomic_DNA.
DR AlphaFoldDB; E3HZW2; -.
DR STRING; 648757.Rvan_0636; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR KEGG; rva:Rvan_0636; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_517659_0_0_5; -.
DR Proteomes; UP000001399; Chromosome.
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; 2.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30480:SF15; BETA-HEXOSAMINIDASE LPQI; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADP69913.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..526
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003171852"
FT DOMAIN 195..508
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT REGION 79..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 54234 MW; 97A6A465F6C99C98 CRC64;
MGGSVRSRLV ALGVFGLSGA AAAAPIPLPL AAPSDAVAFV NDVEDAFPGT ATTRRLRSTP
ADCRARALQY SGGECVATVE KPPVASPQKP PLPPQPPKPK TATPAPAAAP KPNAPPKPNA
PVASATRPTN ESGRTPPAAK PVVMQTSRVL GPAPKTDVAK VSVAKVSVTK VGAPKGDAAK
ASAASAPPSL RAMTGQLLLS GFSGRRASDP DVVRVHAALA AGRLAGVVVA TSNISSSAQL
RELLHYLGDE TGAVPALVAV DQEGGPESAL GEEKGFAFYP SAKNVGRSRS LGEARALYRE
MAEEMSSLGI TLNIGPALGA CGDKRADFSA PCFATAEPRA RAFAAAFTRG HHDRAVLTAL
RAEAFSARRA ASLRRERAST AMLRAVARAD AADAAILRVK ASEQPISSAV TSVSQPSRPG
ESWLRRDMAF GGAIIVDLNL GNSGAPLHQG EAVVSALIAG ADLVLVRATP DVPQDLDETV
YEAVEEAVVA GRLPRARVED AWRHVLSLKA RLASFRQRMQ VATASR
//
