ID G9MV09_HYPVG Unreviewed; 499 AA.
AC G9MV09;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN ORFNames=TRIVIDRAFT_53036 {ECO:0000313|EMBL:EHK21733.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK21733.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK21733.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC {ECO:0000256|ARBA:ARBA00006963}.
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:EHK21733.1}.
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DR EMBL; ABDF02000065; EHK21733.1; -; Genomic_DNA.
DR RefSeq; XP_013955927.1; XM_014100452.1.
DR AlphaFoldDB; G9MV09; -.
DR STRING; 413071.G9MV09; -.
DR EnsemblFungi; EHK21733; EHK21733; TRIVIDRAFT_53036.
DR GeneID; 25795269; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_53036; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR InParanoid; G9MV09; -.
DR OMA; WNYPTRY; -.
DR OrthoDB; 2573673at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHK21733.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 22..335
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 353..494
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 298
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 23..33
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 82..87
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 177..178
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 402..440
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 499 AA; 51093 MW; A9F6E30490F88A21 CRC64;
MLPPIRTALG LVATGSLATG GPCDIYSSGG TPCVAAHSTT RALYSAYTGP LYQVQRGSDG
ATTTISPLSS GVANAAAQDS FCAGTTCLIT IIYDQSGRGN HLTQAPPGGF NGPESNGYDN
LASAIGAPVT LNGQKAYGVF ISPGTGYRNN AASGTARGDA AEGMYAVLDG THYNGACCFD
YGNAETSSRD TGNGHMEAIY FGDSTVWGTG SGSGPWVMAD LENGLFSGSS AGNNAGDPSI
SYRFVTAAVK GQPNQWAIRG ANAASGSLST FYSGARPTVS GYNPMSKEGA IILGIGGDNS
NGAQGTFYEG VMTSGYPSDA TENSVQANIV AAKYAVTSLT SGPALTVGSS ISLRATTACC
TTRYIAHTGS TVNTQVVSSS SAAALKQSAS WTVRTGLGNS GCFSFESKDT PGSYIRHNNF
ALLLNANDGS KQFAEDATFC PQAGLNGQGS SLRAWGYPTR YFRHYNNILY IGSNGGVHTF
DATTSFNDDV SFVISASFA
//
