ID A0A395LPB6_9SPHN Unreviewed; 705 AA.
AC A0A395LPB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Xylan alpha-1,2-glucuronidase {ECO:0000256|RuleBase:RU361198};
DE EC=3.2.1.131 {ECO:0000256|RuleBase:RU361198};
GN ORFNames=DL238_06705 {ECO:0000313|EMBL:RDS78575.1};
OS Alteriqipengyuania lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Alteriqipengyuania.
OX NCBI_TaxID=1538146 {ECO:0000313|EMBL:RDS78575.1, ECO:0000313|Proteomes:UP000254101};
RN [1] {ECO:0000313|EMBL:RDS78575.1, ECO:0000313|Proteomes:UP000254101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-5 {ECO:0000313|EMBL:RDS78575.1,
RC ECO:0000313|Proteomes:UP000254101};
RA Chen X., Liu J.;
RT "Erythrobacter nanhaiensis sp. nov., a novel member of the genus
RT Erythrobacter isolated from the South China Sea.";
RL Submitted (JUL-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:RDS78575.1}.
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DR EMBL; QRBB01000001; RDS78575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395LPB6; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000254101; 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; 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 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|RuleBase:RU361198};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361198};
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|RuleBase:RU361198}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..705
FT /note="Xylan alpha-1,2-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017466028"
FT DOMAIN 35..146
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 153..458
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 459..681
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
SQ SEQUENCE 705 AA; 77853 MW; 1246D232A8F72A48 CRC64;
MRVREVVNRV AAGAAILLLA VTAATPASAE DGYDLWLRYA PLEGEAAVYL QRGFAVEAEM
TPTVEVAADE LAVALGKMAG SSDRKLPAHP RIVIGTRDRL SPAYSDVTSR LEGLAANAFI
IGQSTDGRIV VASDDDLGLL YGVFALTRHL AVHGNLDDVD QASAPAMPLR LLNHWDNPDG
HVERGYAGRS IFDWWHLPEK LDPRMIDYAR ANASIGINGA VVNNVNARGF MLEPRYIAKL
QRLADAWRPY GIRVYLSARF SAPVDIGGLD TADPLDPQVA AWWQVKADEI YASIPDFGGF
LVKANSEGQP GPQDYGRTHA DGANMLAAAI GDRGTVIWRA FVYSAEDETD RAKQAYEEFV
PLDGQFADNV IVQVKNGPVD FQPREPFHPM FGAMPNTRLM LELQITREYL GQATGAVYLA
PMWTEVLDAR TGRGGSVARI VAPVGVAGVA NTGSARNWTG THFDQANWYA FGRLAWDPTL
TSKEIAREWV AQTFVREPGP RDAIAGSMEQ SRESVVRYMT PFGLAHLMAT GHHYGPAPWV
CDLARPEWNP CYYHRADADG IGFDRTANGS DALAQYAPEV ASQWADPAAI DEDYLLWFHH
VPWDHRMKSG RTLWEELVAS YGWGELRILA RIQGWQKLAP FIDAERHAAV AADLAIQLQE
ARWWRDASIA YWQSVNGLDL PPGTRPPEHD LEYYRKLDFP EAPGQ
//
