ID A0A2N4X8R9_9BACT Unreviewed; 699 AA.
AC A0A2N4X8R9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=C0V77_17975 {ECO:0000313|EMBL:PLK42814.1};
OS Emticicia sp. TH156.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Emticicia.
OX NCBI_TaxID=2067454 {ECO:0000313|EMBL:PLK42814.1, ECO:0000313|Proteomes:UP000234203};
RN [1] {ECO:0000313|EMBL:PLK42814.1, ECO:0000313|Proteomes:UP000234203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH156 {ECO:0000313|EMBL:PLK42814.1,
RC ECO:0000313|Proteomes:UP000234203};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in
CC the main chain of hardwood xylans.; EC=3.2.1.131;
CC Evidence={ECO:0000256|RuleBase:RU361198};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361198}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC ECO:0000256|RuleBase:RU361198}.
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:PLK42814.1}.
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DR EMBL; PKRS01000010; PLK42814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4X8R9; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000234203; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR GO; GO:0033939; F:xylan alpha-1,2-glucuronosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361198};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361198};
KW Reference proteome {ECO:0000313|Proteomes:UP000234203};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..699
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014982361"
FT DOMAIN 24..130
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 134..453
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 454..677
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 291
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 365
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 699 AA; 79482 MW; DEA863153B30EF19 CRC64;
MIKKIFVLLM VFSLAARADD GSRLWLKYDL LKDPVLRTSY TSSTRFIVAH DESPIIKTAV
TELQSGLGGL LGRRIQVYSK ADTRTGGIIL HLDNEAPLLI NDGFSIRSQK GNIVISARNP
SGILYGTFEL LRHIQTGKSL QNLNLVSNPK VKLRMLNHWD NANGTVERGY AGSSMWKWPE
LPFRIDPRYI QYARANASIG INAASINNVN ASSRFLTAEY LEKIKAVADV LRPYGISVFI
SVNFRSPRTL GGLKTSDPLD PEVRKWWNEK TKEIHQYIPD FGGFLVKANS EGEPGPQDYG
RTHADGANML AEAMRPYKGI VIWRAFVYKA DPNGDRFKEA YEQFKPLEGT FDPKVIVQVK
NGPIDFMPRE PFHPMFGAFP KTTLGMEFQI TQEYLGQSTH LTYLAPMFKE CLDADTYAKG
KGSTVAKVID GSLDGHQLSL MAGVANTGSD NNWTGHPFNQ ANWYAFGRLA WDYTLSSEQI
ASEWIAMTLT PNKFAQRKIN EMMMRSLPLY ISYTYPLGTA HMMGEGHHYG PEPWLEKSGR
PDWTSVYYHR ADTIGLGFDR TGKVSNALSL YQPDVQKIWG NPDNCPLDYL LWFHHVSWKK
KLSTGRTLWN ELCWRYYDGA EQVKALQADW ESIKPLIDKE TYENVKGRLM IQEKEALWWR
DACVLYFINY AKMPLPAPLK LPARSLDEVK KLVEIYHLR
//
