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Database: UniProt
Entry: A0A1Q4F361_9SPHI
LinkDB: A0A1Q4F361_9SPHI
Original site: A0A1Q4F361_9SPHI 
ID   A0A1Q4F361_9SPHI        Unreviewed;       689 AA.
AC   A0A1Q4F361;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=BGP14_00325 {ECO:0000313|EMBL:OJY85624.1};
OS   Sphingobacteriales bacterium 44-15.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY85624.1, ECO:0000313|Proteomes:UP000186250};
RN   [1] {ECO:0000313|EMBL:OJY85624.1, ECO:0000313|Proteomes:UP000186250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-15 {ECO:0000313|EMBL:OJY85624.1};
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:OJY85624.1}.
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DR   EMBL; MKWG01000030; OJY85624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4F361; -.
DR   STRING; 1895837.BGP14_00325; -.
DR   Proteomes; UP000186250; 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   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, ECO:0000313|EMBL:OJY85624.1}.
FT   DOMAIN          24..158
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          163..401
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        302
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   689 AA;  78978 MW;  10B45C5DAEC59E33 CRC64;
     MKHFLLIVIV VVTGARLRSQ STRELIPAPQ QIKYLPGKFL LSDLSVYTAT SDDEQVVFAL
     NDFVKATEKH SGITIRKASS AAAATLKYKV LHKGYELPDY DPSSADNRRE SYTMKITANK
     IYIEAYAATG LYYALKTLRQ MLEPNGKASC FPLAEIADEP KLKYRGVMMD FAHGGLLKPD
     EIKRQIDFLA AWKSNQYYFY NEVSIQLKGY AGLQYKQSYT QAEIKDIIAY GKERHIDVIP
     FVAFYGHLHD LLKNETYANL AIGNYGHELD PRKPEVAALL RNWIKQYANL FHSPFIHIGF
     DETWETNRIS TEKDPTIDAE KLWIDQLTLL SGELKKYNKT VLAWTDMTNY YPGLMAKVPE
     NVIPVIWEYS PDTAALHNFM NPVLKANKKF FIQPAVSGWG HIYPAATYTY NNIDLCLEEG
     LKKNTIGFIT SVWTDAVEPF VRPSWSFMAY GCISAWQGAS PDRKTFEQNF YRLLFDTAGA
     KVQQACTNLA AAIEDLKKCF GRNTGNMPGG TIIESWSNPF QPYYMNIVQS NPDALKQARI
     KCEEAEYLLV QSMPELNAAD KDFIESLRVT ARLMHYEATR FLWANVISKR WDEAMLGNKK
     NNFVFYDIGY ICHGLIQDVM DELGTLKDDY SAAWLSEYMP YRKNTILGRF DVEYGLWQKL
     LLKLIDFRIQ HPEDYIAPQS FTDTFKPDF
//
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