ID A0A495JS85_9ACTN Unreviewed; 1152 AA.
AC A0A495JS85;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=BDK92_6255 {ECO:0000313|EMBL:RKR91833.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR91833.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR91833.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR91833.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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|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:RKR91833.1}.
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DR EMBL; RBKT01000001; RKR91833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495JS85; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000277671; 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; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51318; TAT; 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|RuleBase:RU361198};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361198};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361198};
KW Reference proteome {ECO:0000313|Proteomes:UP000277671};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|RuleBase:RU361198}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 37..1152
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019795690"
FT DOMAIN 101..194
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 199..553
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 555..776
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT DOMAIN 948..1145
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
SQ SEQUENCE 1152 AA; 126062 MW; CCE0EE1153916BB7 CRC64;
MNRGPVPRLR RTLIVLGTAL ATIAATLTVA TTPVAAAESR DDYSGSDLWL RYVPVSDTKL
LRDYRRTATA IVVENAEANQ VHRHTPHLAM APGSSEQLVE TTLGAARDEL VRGLGGLLDQ
PVPVTTVDGD NIPDGSVMVG TPTSSPLVDR VTSARDLAEI GDEGYLIRSV SRGKARFTVI
AGNTDLGALY GTFAFLRLMQ TQKPIEHLHI SESPKIKHRL LNNWETERLY AGNNASGLGG
LNGESGAIFN FAATGASTDR NLPVILDRYI VVARALASLG INGITINNVN ADNAYLTSSY
IAQEAALADA LRPYGIKLGL SIRYTAPTDG RFAPDTLTNS QLDPYGADFR GWWNRRAQQI
QTAIPDFMGL TVKANSEGQP GPQDFGYDHG DGANAIAAAV APLGMTVHWR TFVYNAEVDN
DRLKRAYLEF GPIDDEVQPD GARGRFADNV FLQTKNGPLD FQAREPIHPM FGRMENTNQA
LELQITQEYT GQNWMLAYLG PMYEEIVKTD TYATDENGKL LKKRLVGNIV DGTAQHHPDT
AIVGVANLGN ADNLTGHHFS QANLFAFGRQ AWNWTLSSAD IATDWVRMTW SNDKRVVDTI
QKMMMGSWEA LVSYQTPLGI GHQFAEGAHY RPDPADWAGR DDWSPIYYNK ADTVGLGFDR
SPNGSNLAAQ YFPRLQQRYG DIDSVPENLL MWFHHVPWGH RMDNGRTFWD ELVYRYQMGV
QYVTWMRETW DALQPDIDAR RFAEVRAKLA VHEADAADWR DTSVTYWKEF SGRDIPVDDG
PLSAKIVVNG TEFGGFNLSD SSYTIPVPAG ASPIITKVKT TDRKARYEII SQAAGVPGQA
VVKVTKESFF GPLVKNYVFN LVRDTRLTSL NVNGEPLASF APKVLHYSAL TPAGTTTVPT
VTAGAADPAA SVTVEQATSA SGQARITVTN GEASSVYTVD LNTTITGSDE FGSTQLGPQW
QWVRPDESRW RLADGSLVIS AQQGDLQGNA NTAKNLALQD VNGDWTAESR IVFSRPLANN
NEQGGVLGYA DDNNYVKLAW EMGSATAAVN RVRIVFLREQ NGASSTLEIT GADAQRIVGT
DGAIWLRLTK TGDSYRAYYS SDGSVYRFIG STTLNVEPTK AGLMAFNRAG TSTDLDVAFD
YFRVESLGDP IR
//
