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Database: UniProt
Entry: R1IGA5_9PSEU
LinkDB: R1IGA5_9PSEU
Original site: R1IGA5_9PSEU 
ID   R1IGA5_9PSEU            Unreviewed;       521 AA.
AC   R1IGA5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=H480_05734 {ECO:0000313|EMBL:EOD69474.1};
OS   Amycolatopsis vancoresmycina DSM 44592.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD69474.1, ECO:0000313|Proteomes:UP000014139};
RN   [1] {ECO:0000313|EMBL:EOD69474.1, ECO:0000313|Proteomes:UP000014139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD69474.1,
RC   ECO:0000313|Proteomes:UP000014139};
RA   Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT   "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285}.
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:EOD69474.1}.
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DR   EMBL; AOUO01000060; EOD69474.1; -; Genomic_DNA.
DR   RefSeq; WP_003062006.1; NZ_AOUO01000060.1.
DR   AlphaFoldDB; R1IGA5; -.
DR   PATRIC; fig|1292037.4.peg.1118; -.
DR   eggNOG; COG3525; Bacteria.
DR   OrthoDB; 9763537at2; -.
DR   Proteomes; UP000014139; Unassembled WGS sequence.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..521
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004361769"
FT   DOMAIN          37..167
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          171..485
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        333
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   521 AA;  56554 MW;  3410744B0DBE76E1 CRC64;
     MHLSRAVLTA AVVSLAAVAV PTSAVAAPAA PERSVTDVVP VPVSAKPDPH GDFRLTPSTV
     ITADRGAGQV ADYLRGLLRP ATGYPLPVVP HAAGLPAIAL QLGHDTRIGT EGYQLKVARD
     GVTLKANTAD GLFEGVQSLR QLLPSAIEAK RVQHRTWTVA GGTILDYPRF AERGAMLDVA
     RHFFRPDQVK LYLDQIAQYK VNTLHLHLAD DQGWRIEIKS WPKLATVGGK TAVDGDPGGY
     YTQAQYQDIV AYAASRHITV IPEIDMPGHT NAAQSTYAEL NCDGKAVPVR TDTEVGYSSL
     CISSPVTYKF VEDVVRELAA ITPGPYLHIG GDEAHSTPPA DYIAFEKKVQ PIVAKYGKKV
     TGWHEIAKSD PPASAVPQYW DFGGDNASVA AAAARGSKIL MSPANFAYLD MKYTESTPLG
     QDWAALVEVR DGYNWDPATL VNGVGESQVA GVEAPLWTET IRTSNDIEYM AFPRLPGIAE
     IGWSPRSTHN WDAYRLRLAK QAPRWVQQGI DFYRSPQVDW K
//
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