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
//