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Database: UniProt
Entry: A0A0F4RHQ5_9RHOB
LinkDB: A0A0F4RHQ5_9RHOB
Original site: A0A0F4RHQ5_9RHOB 
ID   A0A0F4RHQ5_9RHOB        Unreviewed;       548 AA.
AC   A0A0F4RHQ5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN   ORFNames=TW80_15380 {ECO:0000313|EMBL:KJZ18307.1};
OS   Loktanella sp. S4079.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ18307.1, ECO:0000313|Proteomes:UP000033741};
RN   [1] {ECO:0000313|EMBL:KJZ18307.1, ECO:0000313|Proteomes:UP000033741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4079 {ECO:0000313|EMBL:KJZ18307.1,
RC   ECO:0000313|Proteomes:UP000033741};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ18307.1}.
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DR   EMBL; JXYE01000007; KJZ18307.1; -; Genomic_DNA.
DR   RefSeq; WP_045998336.1; NZ_JXYE01000007.1.
DR   AlphaFoldDB; A0A0F4RHQ5; -.
DR   STRING; 579483.TW80_15380; -.
DR   PATRIC; fig|579483.3.peg.3162; -.
DR   OrthoDB; 9781691at2; -.
DR   Proteomes; UP000033741; 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; IPR019800; Glyco_hydro_3_AS.
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.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJZ18307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT   DOMAIN          79..343
FT                   /note="Glycoside hydrolase family 3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00933"
SQ   SEQUENCE   548 AA;  60499 MW;  B94D218068E9D5B3 CRC64;
     MQFEKFEQSP FSLDSEAIDW VKAAFSALSN DDKLRQLFNL RCPGDNAKLM AQAMAFRPGG
     ITRMLSGDAQ AERAFIAKFN KIVPTPLLVS ADLEGSRMGL PDGAEWPNPL SLAAIDDLDI
     TKEVSRRMAQ EAAASGINWS FTPVLDINHA FRSAIVATRG FGSDVDTIEK HAIAQMEVFQ
     EHGIGATVKH WPGEGYDDRD QHLVTTINPL SMDDWKQSFG RLYQAAIDRG AMSVMSAHIA
     LPAYANQGDN SPEAYRPASI SKLLTTQLLR VEMGFNGLVV SDATSMAGLG SWSHRKDYLP
     ELISSGCDVI LFSDNPEQDL GYLRAALEDG RLTWDRINDA VARQLAMKAA LGLHQKAAPL
     ARVDRQANIS YAADVALMAP TLVKDVQDNL PLSPKKHRRV LVFSGGIVFP FVPDPLPFVL
     PDLLVGAGFQ VTIYTPGMEV SPSQYDLVLY LFGDETLLTR GRIFLDWLSL TGDFGVAMQR
     FWHEIPTVMI SFGYPYMLYD APRVPTYINA YSTTETTQHA VFQLLLGKKD WNENNPVDPF
     VGLGDAKF
//
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