ID   A0A1Q3WD91_9BACT        Unreviewed;       835 AA.
AC   A0A1Q3WD91;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=BGO59_14560 {ECO:0000313|EMBL:OJW72361.1};
OS   Spirosoma sp. 48-14.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW72361.1, ECO:0000313|Proteomes:UP000186057};
RN   [1] {ECO:0000313|EMBL:OJW72361.1, ECO:0000313|Proteomes:UP000186057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=48-14 {ECO:0000313|EMBL:OJW72361.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJW72361.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MKUD01000063; OJW72361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3WD91; -.
DR   STRING; 1895854.BGO59_14560; -.
DR   Proteomes; UP000186057; 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   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   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, ECO:0000313|EMBL:OJW72361.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..835
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012298349"
FT   DOMAIN          26..156
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          159..391
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        298
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   835 AA;  92669 MW;  8BF110EB48F46F0F CRC64;
     MKRIKAILLG VLIGSGQNPA AATTVPVLPY PQQVTVGDPL PPIGTAIAFT GSGLESGVTK
     RLAANWQLAG LNQAAQALQQ TVTLIVSGKS AKANALVDAY TAGWSGKVGA EGYVLVLNAR
     HKFIAANTET GLFYGLQSLK QLVRSGWNQE ITITDWPSFA NRGIYDDISR GPTPKVSTIK
     KQIERLAELK INSLSFYIEH VVQPRSYPDF APADGKLTMD DIRELSAYAA QFHMQLVGSF
     QSFGHFANIL SQPRYQPMGE TSTMISPLDP KARAFLASVI TELCGAFNAP YFNVNCDETF
     DLGKGKSKAY VDRVGVAKYY ADHIKFLYDV VKKQHKQLMM WGDIALQHEE ILDLLPKDII
     YLTWEYGDQK SYDTWIQPFV KRGLPFVVCP GIVNSNRLFP DMVMARGNIN GFLKAGKQAG
     TAGVLTTIWD EGPMCFFHSD WYGVYTAAEK SWNISQAETG SFNERFERTA YNTDNGNYVK
     ALFTLMELRG IPLTYNLAEQ IWLQKLLPDS GKKLIINNQD VPKIQAIVNT GLTYIRTAEP
     QLNRTDAQFL EFTLQQYQLL MDSRLLLAQA ADTYRTAQSQ HHTAALQATI QAIESLQARY
     QSLKETYRSL WEAENQPYYL AINLNGFDGK ITQLQQLTTR LQTLISSSPP LPAIAAVGLD
     IKASNAFYFQ NWLLTGPFKT PTPPRFLYSE DPAYNVPPKP GDMAQFQGKS YRWQKYISQE
     GGIVDLSDYY KTASGAVAYA YCSITTDSAQ AVTAQVSAQA AELFVNGVQV KPGNAVDQDE
     TPFALNLTKG VNHVLLKLPA SASWNFAFRL DTRKPITNHK HKYSLNAKTS VHEAD
//