FAEC_EMENI
ID FAEC_EMENI Reviewed; 270 AA.
AC Q5B2G3; C8VH20;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Feruloyl esterase C;
DE EC=3.1.1.73;
DE AltName: Full=Ferulic acid esterase C;
DE Short=FAEC;
DE Flags: Precursor;
GN Name=faeC; ORFNames=AN5267;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [4]
RP INDUCTION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(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:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC EC=3.1.1.73; Evidence={ECO:0000269|PubMed:16844780};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.1. {ECO:0000269|PubMed:16844780};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:16844780};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Induced during growth on suberin.
CC {ECO:0000269|PubMed:25043916}.
CC -!- SIMILARITY: Belongs to the faeC family. {ECO:0000305}.
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DR EMBL; AACD01000093; EAA62427.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF82209.1; -; Genomic_DNA.
DR RefSeq; XP_662871.1; XM_657779.1.
DR AlphaFoldDB; Q5B2G3; -.
DR SMR; Q5B2G3; -.
DR STRING; 162425.CADANIAP00003838; -.
DR CLAE; FAE1C_EMENI; -.
DR ESTHER; emeni-faec; FaeC.
DR EnsemblFungi; CBF82209; CBF82209; ANIA_05267.
DR EnsemblFungi; EAA62427; EAA62427; AN5267.2.
DR GeneID; 2871558; -.
DR KEGG; ani:AN5267.2; -.
DR VEuPathDB; FungiDB:AN5267; -.
DR eggNOG; ENOG502QU71; Eukaryota.
DR HOGENOM; CLU_027551_2_0_1; -.
DR InParanoid; Q5B2G3; -.
DR OMA; SSGCGKQ; -.
DR OrthoDB; 1257904at2759; -.
DR BRENDA; 3.1.1.73; 517.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030600; F:feruloyl esterase activity; IDA:UniProtKB.
DR GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR043595; FaeB/C/D.
DR InterPro; IPR034429; FaeC.
DR PANTHER; PTHR38050; PTHR38050; 1.
DR PANTHER; PTHR38050:SF1; PTHR38050:SF1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..270
FT /note="Feruloyl esterase C"
FT /id="PRO_0000394942"
SQ SEQUENCE 270 AA; 27977 MW; 89D4972DDDFC8C97 CRC64;
MLRAVLLPTL LAFGAFTPVH GANSPGCGKQ PTLTNGVNQI NGREYVLKIP DGYDPSKPHH
LIFGLHWRGG NMYNVVNGDS IQPWYGLEAR AQGSAIFVAP NGLNAGWANT NGEDVAFIDA
IMEQVEDDLC VDQASRFATG FSWGGGMSYA LACARAAEFR AVSVLSGGLI SGCDGGNDPI
AYLGIHGIND PVLPLDGGVT LANTFVSNNG CQPTDIGQPA SGSGGSVRTD FSGCSHPVSF
IAYDGGHDGA PLGVGSSLAP DATWEFFMAA
