ID A6DG58_9BACT Unreviewed; 703 AA.
AC A6DG58;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 28-JUN-2023, entry version 60.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=LNTAR_22334 {ECO:0000313|EMBL:EDM29175.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM29175.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM29175.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM29175.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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:EDM29175.1}.
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DR EMBL; ABCK01000002; EDM29175.1; -; Genomic_DNA.
DR RefSeq; WP_007276905.1; NZ_ABCK01000002.1.
DR AlphaFoldDB; A6DG58; -.
DR STRING; 313628.LNTAR_22334; -.
DR eggNOG; COG3661; Bacteria.
DR Proteomes; UP000004947; 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:UP000004947};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..703
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002691072"
FT DOMAIN 32..143
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 148..479
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 480..700
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT REGION 558..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 419
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 703 AA; 80239 MW; 2188167B784ECBDA CRC64;
MTKKAKMIYS LTCLFSLICT AHSSNAPSSY RAWLSYQKID KQKILNTYQN LFQELSVAGK
SPIIQSSINE LQIGLKAILQ TDLKISNSFS KGLIIGTAKE LSMKGIDLDV SNLSSEGFLL
QSDNQKLILS AKSDLGLLYG AFHILRLIQT QQALNTLDLK ENPKIQHRLL NHWDNPGTVP
EGRSYVERGY AGDSIFKWDE LSKHEQRYID YCRMLASTGI NGSVMNNVNT AKKGLEGWKL
LTPEYLPKLK YLAGIFRQYG IKMYISVNFF SPVIVGGLPE ANPNDPKVQK WWNDKANEIY
KEIPDFGGYL VKADSEGEPG PMKYGLTHAD GANLLARSLK PHGGIVMWRA FVYGHKKSNP
DRAAQPYDLF KPIDGKFDDN AIVQIKNGPH DFQVREPVST LFSAMPKTNQ MLELQITQEY
TGHERHVCYL VPQWKTIFDF DTHAKGKGTE IKKILSGQVY KYKHAGIAGV SNIGDDTNWT
GHLLAQANFY GFGRLSWNPD LSTEEITAEW IKQTFGHNKK IMKVVSKILN TSWRTYEDYT
MPLGIGFMSN GCPDNDESHF RPDPAKRKKY HKADKKGLGY DRTKNSKGHS HYAGQYHKPV
YDMYKNVETC PEELLLFFHH LPYTHKLKSG KTIIQHIYDA HNDGVKQVEN YYKEWQSLNG
LMDAERFEEV SLKLKEQIKY AAEWRDSINS YFYKLSKIKE INK
//
