ID A0A1W2H637_9BACT Unreviewed; 713 AA.
AC A0A1W2H637;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=SAMN00777080_3028 {ECO:0000313|EMBL:SMD44407.1};
OS Aquiflexum balticum DSM 16537.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Aquiflexum.
OX NCBI_TaxID=758820 {ECO:0000313|EMBL:SMD44407.1, ECO:0000313|Proteomes:UP000192333};
RN [1] {ECO:0000313|EMBL:SMD44407.1, ECO:0000313|Proteomes:UP000192333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16537 {ECO:0000313|EMBL:SMD44407.1,
RC ECO:0000313|Proteomes:UP000192333};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT838813; SMD44407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2H637; -.
DR STRING; 758820.SAMN00777080_3028; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000192333; Chromosome i.
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:UP000192333};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..713
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012031941"
FT DOMAIN 25..143
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 147..466
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 467..692
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 406
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 713 AA; 81778 MW; 4CCFC5428D44E412 CRC64;
MKRLFTLVVI LLMSEYVNAN DGYKLWLQYF PFENKAVADY YRDYLENIHI VGISPTHEVI
KNELGIAIKG FLGKDYQALT GKSVESALCI ISKTDELPQE IKTAFAPNTV GLKDDGYLLK
YHQGKMYIIS NTNIGLLYGT FSFLKSIQTR AQLETMDILE NPQIQRRLLN HWDNLNRTVE
RGYAGFSIWN WHRLPHHIDQ QYIDYARANA SIGINGTSIT NVNANALVLT PEYLEKAAAL
ADAFRPYGIK IYLTARFNAP MVLDNLPTAD PLDPGVQKWW KDKTAEIYSY IPDFGGFLVK
ADSEGQPGPH NYGRTQADGA NILADAVQPF GGIVMWRAFV YNEKTPTDRI KQAYDEFKPL
DGEFRENVII QVKNGPLDFQ PREPFHPLFG AMPKTPIMME FQITKEYLGQ ETHWVNLASM
WEEVLQSDTY AKGKGSTVSK VIDGSLHGYK LTGMAGVANI GTDRNWTGHH TGQADWYAYG
KLAWNPDTKI DKIAEDWLKM TFSTDPDFVG TIKGVMLKSH EILVNYMTPI GLHHIMARSH
HWGPGPWVTG GSRDDWTATY YHKASKDSIG FDRTVTGSNA LGQYAPEWKQ ILGDPDKISL
DYLLWFHRVP WNKKLKTGNT LWHEMAIRYQ KGVEGARWMQ KKWEIQEGKI DTERFDHIRS
FLNIQVREAE WWRDSCLLYF QQFSQMPLPE GVEKPKYDLN YYLNFKRNFV PGI
//
