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Database: UniProt
Entry: A0A0N0GP09_9NEIS
LinkDB: A0A0N0GP09_9NEIS
Original site: A0A0N0GP09_9NEIS 
ID   A0A0N0GP09_9NEIS        Unreviewed;       513 AA.
AC   A0A0N0GP09;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   Name=ybbD {ECO:0000313|EMBL:KPC53256.1};
GN   ORFNames=WG78_09200 {ECO:0000313|EMBL:KPC53256.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC53256.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC53256.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC53256.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPC53256.1}.
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DR   EMBL; LAQT01000007; KPC53256.1; -; Genomic_DNA.
DR   RefSeq; WP_053937504.1; NZ_LAQT01000007.1.
DR   AlphaFoldDB; A0A0N0GP09; -.
DR   STRING; 857265.WG78_09200; -.
DR   PATRIC; fig|857265.3.peg.1895; -.
DR   OrthoDB; 9786661at2; -.
DR   Proteomes; UP000037939; Unassembled WGS sequence.
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:SF13; BETA-HEXOSAMINIDASE; 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};
KW   Lipoprotein {ECO:0000313|EMBL:KPC53256.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037939}.
FT   DOMAIN          9..332
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   513 AA;  54595 MW;  A50350490F94CC95 CRC64;
     MADLAHLSLK QKIGQLLMVG FDGLRANAHI ETLLRDHHVG GVILFRRNVD TPVQVAALNR
     QLQQINAEHS QIPLLIGVDQ EGGMVARVEE GVTPLPSAMA FRAAGSVDAC ETLTRYANAE
     LHALGFNINF APDLDVNNNP RNPVIGVRAF GDNPGDVIEY GMAALRGIQA AGMAATAKHF
     PGHGDTDVDS HLGLPRVPHA RARLDAIELA PFRAAIAAGV DTFMSSHVVF PAFEADVDTP
     ATMSHAVLTG LLRQQLGFEG VVFTDCMEMD AIAKGVGTVA GAVAAFKAGA DIVLVSHTQA
     LQQGALAALE HAVTTGEISE AQIDQSVARV LALKAKRAMA QWNTLNTDLL PLMLRQPAAV
     ALSEQVHAQA VTLAGRCAPL QPALSVLLIT LEVRMRSEID EVARRTDTLA APLRALGYTV
     EEVRLPASPE IVDLERVQRL ADAAAQVVCV SYNAVLNPAQ QRLIALLPTQ RLWLIAGRLP
     YDLDLAPGAA GRMTAYANRP AALQAVAQRL RAP
//
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