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Database: UniProt
Entry: A0A0Q5TR31_9SPHI
LinkDB: A0A0Q5TR31_9SPHI
Original site: A0A0Q5TR31_9SPHI 
ID   A0A0Q5TR31_9SPHI        Unreviewed;       323 AA.
AC   A0A0Q5TR31;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KQS37152.1};
GN   ORFNames=ASG14_09050 {ECO:0000313|EMBL:KQS37152.1};
OS   Pedobacter sp. Leaf194.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS37152.1, ECO:0000313|Proteomes:UP000051708};
RN   [1] {ECO:0000313|EMBL:KQS37152.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS37152.1,
RC   ECO:0000313|Proteomes:UP000051708};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS37152.1, ECO:0000313|Proteomes:UP000051708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf194 {ECO:0000313|EMBL:KQS37152.1,
RC   ECO:0000313|Proteomes:UP000051708};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KQS37152.1}.
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DR   EMBL; LMPU01000008; KQS37152.1; -; Genomic_DNA.
DR   RefSeq; WP_056870942.1; NZ_LMPU01000008.1.
DR   AlphaFoldDB; A0A0Q5TR31; -.
DR   STRING; 1736297.ASG14_09050; -.
DR   OrthoDB; 9803461at2; -.
DR   Proteomes; UP000051708; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd18618; GH43_Xsa43E-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            168
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   323 AA;  36696 MW;  F6940CF2CC71B34A CRC64;
     MAYCKRHFLT ASLVYLSFQG FSQEKLAVSK GNPIITNKYT ADPAAFVYGD SVYLYTGHDV
     APKSKNDYEM HEWLCYSSAD MVNWKEHKSP LNVKDFAWAK DDAWASQVIE RNGKFYWYVA
     TEHGSIKGKS IGVAVADNPR GPFKDALGKA LITNNMTTAV DITWDDIDPT VIIDDDGQAY
     LFWGNQRCYY AKLKANMIEL DGEIKTISVP EFTEAPWVHK HKNWYYLSYA SGFPEKIVYA
     MSKSINGPWD YKGILNEIAG NSNTNHQSII DFKGKSYFIY HNGAINNDGG SYRRSVCIDD
     LHYNNDGTIK RIIMTTEGVR KVR
//
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