ID A0A093V8G1_TALMA Unreviewed; 315 AA.
AC A0A093V8G1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Arabinoxylan arabinofuranohydrolase {ECO:0000313|EMBL:KFX46279.1};
GN ORFNames=GQ26_0190400 {ECO:0000313|EMBL:KFX46279.1};
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:KFX46279.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX46279.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX46279.1,
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 -!- 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:KFX46279.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPOX01000019; KFX46279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V8G1; -.
DR eggNOG; ENOG502SHQG; Eukaryota.
DR HOGENOM; CLU_009397_4_2_1; -.
DR Proteomes; UP000029285; 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; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 148
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 315 AA; 35068 MW; A952FC733694DC95 CRC64;
MGGGNNWPSP RQIQNSSSST YSGNPIFPGW YADPDAHIFL NQYWIFPSLS LDYSQQTYFD
CFSSPDLIHW TKHSRILDFT NIPWSTNRAA WAPTVAFKNG DYFMYFSAGD GAGIGVAKST
TKRPEGPYED VLGKPLVADV LFGGQPIDPV VFVDDDARVY LLWGGWSHGL GAELGDDMVS
FKTHPIELTP PNYVEAPYMI KRKGVYYYMY SVGGWGDNSY GVEYVTSTTS PLGPFTKTSQ
HILSPDPDVA QGTGSNGVIH VPGTSEWYIV YHRRPLGDYD ANHRYVCIDR MEFDDGDGGI
KPIRITREGV KANPL
//
