ID B2AFC4_PODAN Unreviewed; 410 AA.
AC B2AFC4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Carboxylic ester hydrolase {ECO:0000256|RuleBase:RU367147};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU367147};
GN ORFNames=PODANS_5_12620 {ECO:0000313|EMBL:CAP62142.1};
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:CAP62142.1};
RN [1] {ECO:0000313|EMBL:CAP62142.1, 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:CAP62142.1};
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:CAP62142.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP62142.1};
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:CDP29214.1}
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 -!- FUNCTION: Esterase involved in the hydrolysis of xylan, a major
CC structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. {ECO:0000256|RuleBase:RU367147}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000256|ARBA:ARBA00001691};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367147}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC subfamily. {ECO:0000256|ARBA:ARBA00007052}.
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DR EMBL; CU633458; CAP62142.1; -; Genomic_DNA.
DR EMBL; FO904940; CDP29214.1; -; Genomic_DNA.
DR RefSeq; XP_001904363.1; XM_001904328.1.
DR AlphaFoldDB; B2AFC4; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR GeneID; 6188504; -.
DR KEGG; pan:PODANSg1382; -.
DR VEuPathDB; FungiDB:PODANS_5_12620; -.
DR eggNOG; ENOG502QTDU; Eukaryota.
DR HOGENOM; CLU_027551_1_1_1; -.
DR OrthoDB; 1740325at2759; -.
DR Proteomes; UP000001197; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR010126; Esterase_phb.
DR NCBIfam; TIGR01840; esterase_phb; 1.
DR PANTHER; PTHR43037:SF6; CARBOXYLIC ESTER HYDROLASE; 1.
DR PANTHER; PTHR43037; UNNAMED PRODUCT-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367147};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367147};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367147};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Secreted {ECO:0000256|RuleBase:RU367147};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487,
KW ECO:0000256|RuleBase:RU367147};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367147}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU367147"
FT CHAIN 17..410
FT /note="Carboxylic ester hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU367147"
FT /id="PRO_5007638560"
FT DOMAIN 373..408
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 410 AA; 43225 MW; EAB7E9B6F27E04B5 CRC64;
MKTVAVLSLL ASLASAASLT LVTENFGPNP RNNPFYIYVP DVLPPNPAIL VNPHWCHGTA
PAAFSGSQYA TLASQHGFIV IYPQSSPAQA NSDKCWDVSS KETLTHNGGG DSLGVVSMVK
WTINKYNADP KRVFVTGVSS GGMMTQVLLG SYPDVFAAGA AFAGVPFGCF APAGNNTGAF
GYWSDDCAKG RVTKTPAQWA DLVKSAYPGY DGWRPKLQLF HGTNDEILDY VNHQEGIKQW
AEVLGVGITP VSVTPNTPIS GWTKSVYGAE GWLEGYSAAG VPHDIRVQEA TVMAFFELAC
KGEDCFRWGD SEWCDAEPSA TTSSVVVSMT GAPVTTTSTS STSVRVTTPS ATSTSSRVTT
TFVTSTSTAA PVAGQPLWAQ CGGMGFNGPT ACAVGTCTIY NPYYAQVNPQ
//
