ID A0A226HYG5_9FLAO Unreviewed; 717 AA.
AC A0A226HYG5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=B0A75_12165 {ECO:0000313|EMBL:OXA99008.1};
OS Flavobacterium oncorhynchi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=728056 {ECO:0000313|EMBL:OXA99008.1, ECO:0000313|Proteomes:UP000198336};
RN [1] {ECO:0000313|EMBL:OXA99008.1, ECO:0000313|Proteomes:UP000198336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 59446 {ECO:0000313|EMBL:OXA99008.1,
RC ECO:0000313|Proteomes:UP000198336};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) 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:OXA99008.1}.
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DR EMBL; MUHA01000017; OXA99008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226HYG5; -.
DR Proteomes; UP000198336; 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}; 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..717
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013279809"
FT DOMAIN 25..146
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 150..469
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 470..694
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 717 AA; 81940 MW; 28857F64D0AC0431 CRC64;
MTSFRFVFLF LLISFSASAQ KDYKLWLQYN SVANSAIASE YKNNLKGIVI LGNSETLKIA
EKELKTGFLD MLGNIPETKQ DIKEENNLIV GSESNLNTEI QNELRSDFDK INTEGFIIKS
ISFKNKKQII IAGKNDVAVL YGVFNFLRIL QTNKSVKNLN IVDSPKTNIR ILNHWDNLDR
TVERGYAGFS LWNWQKLPDF IDQRYIDYAR ANASIGINGT VLTNVNANAL ILTPQYLEKV
EALANVFRPY GIKVYLTARF SAPIEIGNLK TADPKDPEVI NWWRNKSAEI YKRIPDFGGF
LVKANSEGQP GPQNYGRDHV DGANMLADAV APFGGVIMWR AFVYSEHDAN DRAKQAYAEF
QPYDGKFRKN VIVQVKNGAI DFQPREPFHP LFGAMPKTPL MMEFQITQEY LGFSTHLVFL
PKLFQEVLES DTYQKGKGST VAKVVDGTLY QNKLTGIAGV ANIGNDLNWT GHPFAQANWY
GFGRLAWNPY LDSETIADEW LRSTFSNDEN FIKPVKSMMI ESREAVVNYM TPLGLHHIMD
TGHHYGPGPW VSNLSRPEWN PNYYHKADKN GIGFDRSKSG TNAVSQYAPE VANIFDNLET
CPEKDLLWFH HVSWDYKLKN RQTLWNGLSL KYQEGVDQVK EMQNVWNRAG KYVDNERFNE
VKMLLEIQYK EAKWWRDACL LYFQQFSGKE LPNGVEKPTQ TLEYFKSLKF PFAPGNG
//
