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Database: UniProt
Entry: I4VRX4_9GAMM
LinkDB: I4VRX4_9GAMM
Original site: I4VRX4_9GAMM 
ID   I4VRX4_9GAMM            Unreviewed;       736 AA.
AC   I4VRX4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE            EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
DE   AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|ARBA:ARBA00033000};
GN   ORFNames=UU7_16297 {ECO:0000313|EMBL:EIL89965.1};
OS   Rhodanobacter spathiphylli B39.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL89965.1, ECO:0000313|Proteomes:UP000003226};
RN   [1] {ECO:0000313|EMBL:EIL89965.1, ECO:0000313|Proteomes:UP000003226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B39 {ECO:0000313|EMBL:EIL89965.1,
RC   ECO:0000313|Proteomes:UP000003226};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
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 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:EIL89965.1}.
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DR   EMBL; AJXT01000055; EIL89965.1; -; Genomic_DNA.
DR   RefSeq; WP_007810245.1; NZ_AJXT01000055.1.
DR   AlphaFoldDB; I4VRX4; -.
DR   STRING; 1163407.UU7_16297; -.
DR   PATRIC; fig|1163407.3.peg.3275; -.
DR   eggNOG; COG3525; Bacteria.
DR   OrthoDB; 9763537at2; -.
DR   Proteomes; UP000003226; 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; cd06563; GH20_chitobiase-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PF00754; F5_F8_type_C; 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.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..736
FT                   /note="beta-N-acetylhexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003696078"
FT   DOMAIN          23..146
FT                   /note="Beta-hexosaminidase bacterial type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02838"
FT   DOMAIN          149..469
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   DOMAIN          598..711
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   ACT_SITE        314
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ   SEQUENCE   736 AA;  82241 MW;  854903E20FF76216 CRC64;
     MPRHLVALLL LAFPLCTQAT ATGVIPQPER IEAGRGSFAL GPNVRIVAPA DRRAQEIAAF
     LRDGIREDSG IALRIGAATR QPRIELRTDP SVQGEEAYRL TVTPQRVEIA SADDRGLFWG
     VQTLRQLLPP GHHATLAIAA VRIDDAPRYA WRGVMLDAAR HFIPVALVKQ QIDLLSRYKL
     NVLHWHLTDD QGWRIEIRKY PRLTSVGAWR TEADGSRSGG FYTRQDIRDI VEYARQRNVM
     IVPEIEMPGH ASAAVAAYPS LSCPQQPIVV PATWGVFTDI YCAGDEASFT FLHDVLSEVA
     ELFPAPYIHI GGDEVPKQQW AQSASSQQRM RDEHLAGVDA LQSWFVQRIQ RDLEARGKTL
     VGWDEILEGG ADRNAIVEMW RGDAEAAKAL ANGNRLIVAG PFYLDTPIEE LTTQDIYRIN
     PFASPAFAGH QDQVLGAEAP LWSEYVTPRN LEAMLYPRVI ALAERLWNPD ANDYADFQQR
     LRTQYPWLDA QHIAYGPEDR DLVDYKLDYN PLQHRWRVRA ARGFDDIALH YTVDGSEPTS
     QSPAFGDVLD RYVPATLKIA PFRHGVPYLP SQTFQSVDNK ALGKPINYLT APDPHYAGTA
     TQLVDGVIGD DDFNDGLWVG WRGSDLDATL DLQPVTPFHT IQMRFLQQSG SWALLPRRVT
     FAVSDDGKTW RTLQSTPIAV DPMDLRAMIR TVRFEAATPV TARYLRVTAQ NYGVLPPGHE
     GAGKPAHLFT DEILVQ
//
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