ID A0A093X9W4_TALMA Unreviewed; 187 AA.
AC A0A093X9W4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590};
DE EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590};
GN ORFNames=GQ26_0510460 {ECO:0000313|EMBL:KFX41988.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX41988.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX41988.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX41988.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000256|ARBA:ARBA00007792, ECO:0000256|PROSITE-ProRule:PRU01097}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01097}.
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:KFX41988.1}.
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DR EMBL; JPOX01000051; KFX41988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X9W4; -.
DR eggNOG; ENOG502RXA7; Eukaryota.
DR HOGENOM; CLU_1448639_0_0_1; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR Pfam; PF00457; Glyco_hydro_11; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS51761; GH11_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KFX41988.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFX41988.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:KFX41988.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..187
FT /note="endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001893545"
FT DOMAIN 45..187
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
SQ SEQUENCE 187 AA; 20242 MW; DD4422BB1BD71899 CRC64;
MVAFSSLLVA FTAIVGALAA PTELVKDDNV LDLLSRGPSN FVLDTTNTTS LVRRAGINYN
QDYTTGGTVN YYHSSTGFQV NWNTQNDFVV GVGWNPGSNS PVNFGGQFSV SSGTGLLSVY
GWTTNPLVEY YIIEDYHNQP SFGTQKEYPV QPAFNPGYID VQSVYFCAPV AADAGHSHRA
ESFQCLG
//
