ID W5W487_9PSEU Unreviewed; 622 AA.
AC W5W487;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Beta-N-acetylhexosaminidase {ECO:0000313|EMBL:AHH95281.1};
DE EC=3.2.1.52 {ECO:0000313|EMBL:AHH95281.1};
GN ORFNames=KALB_1911 {ECO:0000313|EMBL:AHH95281.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH95281.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH95281.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH95281.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CP007155; AHH95281.1; -; Genomic_DNA.
DR RefSeq; WP_025355465.1; NZ_CP007155.1.
DR AlphaFoldDB; W5W487; -.
DR STRING; 1449976.KALB_1911; -.
DR KEGG; kal:KALB_1911; -.
DR PATRIC; fig|1449976.3.peg.1906; -.
DR eggNOG; COG3525; Bacteria.
DR HOGENOM; CLU_010969_0_1_11; -.
DR OrthoDB; 9763537at2; -.
DR Proteomes; UP000019225; Chromosome.
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; cd06564; GH20_DspB_LnbB-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; IPR000421; FA58C.
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; PTHR43678:SF1; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR PANTHER; PTHR43678; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00640)-RELATED; 1.
DR Pfam; PF00754; F5_F8_type_C; 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.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:AHH95281.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHH95281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..622
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038922540"
FT DOMAIN 480..622
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 622 AA; 67357 MW; 1D5D662345CFE544 CRC64;
MASTPARLSA AILLALTLIT PSAHAGAAPA ANTKPSTIPA LRQWTGGTGS FTFGPGSRVV
LGSTVLSSTA NTFAADLKSL YGRDFTPVVG TPRPGDVYLA LGGADPQEGY TLSITDRITI
TAPTDTGLFN GTRTVLQLLH QGTSVPQGSA RDWPSYPQRG LMVDDGRKFF TLDWLIDQVR
ELAYLKMNYL HLHLSDNEGF RVESTSHPEV VSTEHLSKAE VRTLLAVAAA YHVTVVPEID
MPGHLRAVLN AHPDLRLTGA DGSVSTDFID LSKDGSYALL KDLITEYAEL FPGPYFHIGA
DEYVGNYGNY PQVLAYAKQH YGANAVAKDT YLGFVNWADD LVRASGKTTR AWNDGLYGGS
AVTVHPDVLV EFWYNYGLSP QQLVDGGHQI MNSSYTPTYY VLGRGKASPA TTYEQWTPNL
FQGNQSLTDP SHNLGEKVHV WCDFPDAETE AHVASGIRDL LRVVAQQTWG SAKPADGYSA
FQDVIGLIGR NPAWPVGNLA ANRPITVSST ETPDFPGYNA VDGDYATRWS SAYGDGEWIT
VDLGSVHAVS RVKLSWETAY GKAYQVQTSV DGTNWNTIYS TNAGRGGTED LTGLTGSGRY
VRMQGVTRAT GWGYSLYEFE VY
//