ID N1RZW6_FUSC4 Unreviewed; 276 AA.
AC N1RZW6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Feruloyl esterase C {ECO:0000256|RuleBase:RU367094};
DE EC=3.1.1.73 {ECO:0000256|RuleBase:RU367094};
DE AltName: Full=Ferulic acid esterase C {ECO:0000256|RuleBase:RU367094};
GN ORFNames=FOC4_g10005918 {ECO:0000313|EMBL:EMT67805.1};
OS Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT67805.1, ECO:0000313|Proteomes:UP000016929};
RN [1] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC methyl ferulate and wheat arabinoxylan. {ECO:0000256|ARBA:ARBA00025250,
CC ECO:0000256|RuleBase:RU367094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000256|ARBA:ARBA00034075,
CC ECO:0000256|RuleBase:RU367094};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367094}.
CC -!- SIMILARITY: Belongs to the faeC family. {ECO:0000256|ARBA:ARBA00010278,
CC ECO:0000256|RuleBase:RU367094}.
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; KB726570; EMT67805.1; -; Genomic_DNA.
DR AlphaFoldDB; N1RZW6; -.
DR STRING; 1229665.N1RZW6; -.
DR ESTHER; fuso4-a0a0c4diy4; FaeC.
DR HOGENOM; CLU_027551_2_0_1; -.
DR Proteomes; UP000016929; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-UniRule.
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; IPR043595; FaeB/C/D.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR38050; -; 1.
DR PANTHER; PTHR38050:SF1; FERULOYL ESTERASE C; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367094};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367094};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367094};
KW Reference proteome {ECO:0000313|Proteomes:UP000016929};
KW Secreted {ECO:0000256|RuleBase:RU367094};
KW Signal {ECO:0000256|RuleBase:RU367094};
KW Xylan degradation {ECO:0000256|RuleBase:RU367094}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367094"
FT CHAIN 21..276
FT /note="Feruloyl esterase C"
FT /evidence="ECO:0000256|RuleBase:RU367094"
FT /id="PRO_5027166041"
FT DOMAIN 122..214
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 276 AA; 29237 MW; FFDCBF1F1D4BE67A CRC64;
MRSLLTLTLA LFASAGLGDA ASAGCGKQPP SSGVKTMQVN GKNREYTLQL PNNYQNNKPH
RLVFGYHWLS GNMGNVVQGG YYGLRNLAGD STIFIAPNGL NAGWANQGGE DITFTDQMLA
FAKQNLCIDE KQVFATGFSY GGAMSHSVAC SRPNDFAAVA VISGALLSGC NGGNTPVSYL
HIHGSADNVL SIQQGRQLRD KWIGTNGCQQ KQVNDPAPGA QNYVKTSYTC SRKPVTWIGH
GGGHVADPTA NGQKFAPGET WTFFNAAAGK SAKLRC
//