ID H6R8D0_NOCCG Unreviewed; 387 AA.
AC H6R8D0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN OrderedLocusNames=NOCYR_5328 {ECO:0000313|EMBL:CCF66077.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF66077.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF66077.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF66077.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(2012).
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; FO082843; CCF66077.1; -; Genomic_DNA.
DR RefSeq; WP_014353521.1; NC_016887.1.
DR AlphaFoldDB; H6R8D0; -.
DR STRING; 1127134.NOCYR_5328; -.
DR KEGG; ncy:NOCYR_5328; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_0_4_11; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000008190; 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; 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: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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCF66077.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008190};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..387
FT /note="beta-N-acetylhexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038695766"
FT DOMAIN 64..377
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 40278 MW; C285AEF3D2F99BEC CRC64;
MRKTPLVLFA VLAAIATGCS GGDAGNSTTT RPVATNATSA PTPGATTTAE RDCSADYLAK
FTPRQKLAQL LTVGVNSTAD ALAVVRDHQV GGIFIGGWTD ESLLADGQVE QVKAAANAPL
MVTIDEEGGR VSRVSDLIGP APSARQTAKT MTTEEFYTAT LERGKALKDL GVTVNFAPDV
DVSSQPDNSV IGDRSFSDDP MVVTEYAGAY IRAMREVGVG TVMKHFPGHG AGSGDSHLGA
VRTPPLDQLQ NRDLVPFRDL VGSGAGVMVG HLDVPGLTEP NVPASISPAA MELLRKGTGY
GAAPFDGPIF TDDLGGMAAI TDRMSIPEAV EAALVAGADN ALWITTDAVP QVLDRLEQAV
WSGRLPIAQV DASVLRMAWF KGAPLHC
//
