ID B2AFI2_PODAN Unreviewed; 659 AA.
AC B2AFI2;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=PODANS_5_11670 {ECO:0000313|EMBL:CAP62201.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP62201.1};
RN [1] {ECO:0000313|EMBL:CAP62201.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP62201.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP62201.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP62201.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP29615.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC {ECO:0000256|ARBA:ARBA00007186}.
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DR EMBL; CU633461; CAP62201.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP29615.1; -; Genomic_DNA.
DR RefSeq; XP_001904421.1; XM_001904386.1.
DR AlphaFoldDB; B2AFI2; -.
DR STRING; 515849.B2AFI2; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR GeneID; 6188578; -.
DR KEGG; pan:PODANSg1441; -.
DR VEuPathDB; FungiDB:PODANS_5_11670; -.
DR eggNOG; ENOG502QQEX; Eukaryota.
DR HOGENOM; CLU_010060_1_1_1; -.
DR OrthoDB; 1097767at2759; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000001197; Chromosome 5.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR010720; Alpha-L-AF_C.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR Pfam; PF06964; Alpha-L-AF_C; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDP29615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..659
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007638716"
FT DOMAIN 461..635
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 659 AA; 72029 MW; E3ACCBE2F6F55C2F CRC64;
MIHLKPALAA LLALSTQCVA IDLFVKSSGG NKTTDIMYGL MHEDINNSGD GGIYAELISN
RAFQGSEKFP SNLDNWSPVG GATLTLQKLA KPLSSALPYS VNVANPKEGK GKGKDTKGKK
VGLANAGFWG MDVKRQKYTG SFHVTGEYKG DFEVSLRSAI TGETFGKKVV KGGSKKGKWT
EKEFELVPFK DAPNSNNTFV VHLFPPTFKG RKNGLRIDLA QTMVELKPTF LRFPGGNMLE
GNTLDTWWKW YETIGPLKDR PGMAGVWEYQ QTLGLGLVEY MEWADDMNLE PIVGVFAGLA
LDGSFVPESE MGWVIQQALD EIEFLTGDAK TTKWGAVRAK LGHPKPWKVK WVEIGNEDWL
AGRPAGFESY INYRFPMMMK AFNEKYPDIK IIASPSIFDN MTIPAGAAGD HHPYLTPDEF
VERFAKFDNL SKDNVTLIGE AASTHPNGGI AWEGDLMPLP WWGGSVAEAI FLISTERNGD
KIIGATYAPG LRSLDRWQWS MTWVQHAADP ALTTRSTSWY VWRILAHHII RETLPVDAPA
GKPNFDPLFY VAGKSESGTG IFKAAVYNST ESIPVSLKFD GLNEGAVANL TVLTGPEDPY
GYNDPFTGIN VVKEKTTFIK AGKGGKFTFT LPGLSVAVLE TADAVKGGKG KGKGKGKGN
//
