ID A0A1C5H017_9ACTN Unreviewed; 600 AA.
AC A0A1C5H017;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=GA0070609_0699 {ECO:0000313|EMBL:SCG39283.1};
OS Micromonospora echinaurantiaca.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47857 {ECO:0000313|EMBL:SCG39283.1, ECO:0000313|Proteomes:UP000198217};
RN [1] {ECO:0000313|EMBL:SCG39283.1, ECO:0000313|Proteomes:UP000198217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43904 {ECO:0000313|EMBL:SCG39283.1,
RC ECO:0000313|Proteomes:UP000198217};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; LT607750; SCG39283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5H017; -.
DR Proteomes; UP000198217; Chromosome i.
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; cd06568; GH20_SpHex_like; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
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; 2.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198217}.
FT DOMAIN 58..191
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 195..362
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT DOMAIN 366..510
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 600 AA; 63467 MW; 18CFE2148EEF2D34 CRC64;
MSTLPSAADQ DGPALSQQSA ADQGRLPLRE PAAADLARTA ARAAGDLLAP PAPVRLDDVV
PAPEQVRPDP GADYLLTPDA VIRVSTGPAA LAVAEQLAAL LRPATGYPLP VTDAARPEPA
GGIALVLVDD ETLGPEGYQL DITPAGVRIA AAGPAGLLHG VQTLRQLLPA AIESRTPVAE
RWALPGGSIT DRPRFAYRGA MLDVARHFFG VEDVLRVVDH LSRYKLNHLH LHLTDDQGWR
IAVDSWPRLA AVGGVGEVGD GPGGFYTKAD YQRIVAYAAE RHITVVPEID LPGHTNAALV
AYPELAPAGT VPTPYTGTEV GFSYVDPASE RTYDFVTDVL AEVTAMTPGP WLHIGGDEAF
KVKREAYTGF VERAQRIVAG LGKTVVGWHQ LAPAGHVDGR VLQWWGTDAD DPTTAEAARR
GARLLLSPGN HAYLDMKYAP DTPIGHDWAG LIDLRRSYEW DPGAHVTGVP ETAVLGVEAP
LWTESVTSLP EVEFMLFPRL PALAELGWSP RATHDWDRFR DRLAGHGPRW TAAGITFHRS
PEVSWPTEAP AEVPAEAPTA APAAAPAAAP VPAGPMPAGP RPAIPTQPGP DDAPATAPSV
//
