ID A0A3M9MR65_9BACT Unreviewed; 721 AA.
AC A0A3M9MR65;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=EFA69_13610 {ECO:0000313|EMBL:RNI27198.1};
OS Rufibacter immobilis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1348778 {ECO:0000313|EMBL:RNI27198.1, ECO:0000313|Proteomes:UP000271010};
RN [1] {ECO:0000313|EMBL:RNI27198.1, ECO:0000313|Proteomes:UP000271010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCC P1 {ECO:0000313|EMBL:RNI27198.1,
RC ECO:0000313|Proteomes:UP000271010};
RA Yang Y.;
RT "Rufibacter latericius sp. nov., isolated from water in Baiyang Lake.";
RL Submitted (NOV-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|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:RNI27198.1}.
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DR EMBL; RJJE01000017; RNI27198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9MR65; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000271010; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..721
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018004995"
FT DOMAIN 30..151
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 155..474
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 475..699
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 312
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 721 AA; 81640 MW; 91A476724BCEF48C CRC64;
MRKKIISPLS FLCLFLWFTG AARAEDGYRL WQRYDLLQNK PLVKEYQKAL GQLVVQGSSP
TLSIIEDELS TGLSGLLGQP FSAAENPEKK NVLLVGTPAT SPVLKGLGLE DKLKAVGKDG
YLLLSRKAGG KNYTVVAANT EVGALYGSFH LLRLLQTQQR INNLDISSSP KTQHRILNHW
DNLDRTVERG YAGFSIWDWH KLPDYIDQRY LDYARANASI GINGTVLTNV NANSLVLSEE
YLKKVKALAD TFRPYGIKVY LTARFSSPIE LGKLKTADPL NPEVKAWWKN KVEEIYRHIP
DFGGFLVKAN SEGQPGPQNY NRSHADGANM LAEALAPKGG LVMWRAFVYD DKVPDDRHKQ
AYTEFKPLDG KFLPNVMVQV KNGAIDFQPR EPFHPLFGAM PKTPLMMEFQ ITQEYLGQGT
HLAYLAPMFK ETLMADTYAK GKGSTVAKVV DGSLDNHYHS GMAGVANIGN DRNWTSHPFG
QANWYTFGRL AWDYNLTSEA IADEWIKMTF SGSPTLVSTV KQMMMGSREA VVNYMTPLGL
HHLMGWSHHY GPGPWIKDKP RADWTSVYYH RADEKGIGFD RTRTGSNALS QYAPEVQALL
QNPATCPEDV LLWFHHLPWD WKMKSGRTLW DELCYKYSEG VDSVRAMQKD WDSLQGQVDK
ERYQQVKQYL AIQEKDARWW RDACLLYFQT FSKRPIPQAL EKPAGTLEEY MKIDPKFAPG
I
//
