ID Q1NAJ5_SPHSS Unreviewed; 713 AA.
AC Q1NAJ5;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 03-MAY-2023, entry version 62.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=SKA58_08604 {ECO:0000313|EMBL:EAT08011.1};
OS Sphingomonas sp. (strain SKA58).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT08011.1, ECO:0000313|Proteomes:UP000005395};
RN [1] {ECO:0000313|EMBL:EAT08011.1, ECO:0000313|Proteomes:UP000005395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA58 {ECO:0000313|EMBL:EAT08011.1,
RC ECO:0000313|Proteomes:UP000005395};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) 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:EAT08011.1}.
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DR EMBL; AAQG01000013; EAT08011.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1NAJ5; -.
DR STRING; 314266.SKA58_08604; -.
DR eggNOG; COG3661; Bacteria.
DR HOGENOM; CLU_007125_1_0_5; -.
DR Proteomes; UP000005395; 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:UP000005395};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..713
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004195011"
FT DOMAIN 28..142
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 147..465
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 467..690
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 303
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 405
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 713 AA; 78670 MW; F3962BB8C64B40D8 CRC64;
MARLFCYMMA MVMAMLALPV RAEDGYDLWL RYAPAEQARA ADISAHARTI VPVENGSTME
VATRELQRAV AHMTGRAPTL ATTPTAGALW LATPRSAPGI PLSLKGLGAE GYAIRSIDRG
GQPVTLIAAN SDIGLLHGAF HWLRLAQTNA PLDRLDIRSA PRIGLRLLNH WDNLDGTVER
GYAGMSIWDW WRLPDYKGPR YTDYARANAS IGINGTVLNN VNAKAESLSA PYIAKAAALA
DIFRPYGIKV YLSVKWTAPM ELDGLKTADP LDAQVAAWWK AKASEIYRAI PDFGGFLVKA
NSEGQPGPQD YDRTHADGAN MLAAAVKPHG GIVMWRAFVY AHDNPDDRAK QAYDDFKPLD
GQFADNVLVQ VKNGAIDFQP REPFHPLFGA MPKTPLMMEF QITKEYLGQS THLTYLGPLF
EEALDADTYA KGKGSTVAKV IDGSLDGHKL TGIAGVANIG VDRDWSGSIF NQADWYAFGR
LAWDPGLSAN AIAREWTAMT FSPDPRLVDP VVAMMMGSRE AAVDYMTPLG LAHVMATGHH
YGPAPWVSDL ARPEWNPVYY HKADADGIGF DRTKSGSNAI AQYAPVIARR LANPATTPES
ELLWFHHLPW DYRLKSGETL WNGLVHRYDH GVAYVAGMQR TWEGLRPLVD AERFAQTEAF
LAIQHREAQW WRDASIAYFQ SINHLPLPAD AMAPAHDLDW YKAQSFPYAP GHH
//
