ID   PELF1_ASPTN             Reviewed;         388 AA.
AC   Q0CFF7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Probable pectin lyase F-1;
DE            Short=PLF-1;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF-1; ORFNames=ATEG_07577;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC       pectin lyase, polygalacturonase, pectin methylesterase and
CC       rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC       most important in depolymerization of pectin, since it cleaves internal
CC       glycosidic bonds of highly methylated pectins (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC         ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC         galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CH476604; EAU31839.1; -; Genomic_DNA.
DR   RefSeq; XP_001216198.1; XM_001216198.1.
DR   AlphaFoldDB; Q0CFF7; -.
DR   SMR; Q0CFF7; -.
DR   EnsemblFungi; EAU31839; EAU31839; ATEG_07577.
DR   GeneID; 4323045; -.
DR   VEuPathDB; FungiDB:ATEG_07577; -.
DR   eggNOG; ENOG502RZWS; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; WSAGCNG; -.
DR   OrthoDB; 1267775at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR   GO; GO:0047490; F:pectin lyase activity; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0045490; P:pectin catabolic process; ISS:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR002022; Pec_lyase.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR045032; PEL.
DR   PANTHER; PTHR31683; PTHR31683; 1.
DR   Pfam; PF00544; Pectate_lyase_4; 1.
DR   SMART; SM00656; Amb_all; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Lyase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..388
FT                   /note="Probable pectin lyase F-1"
FT                   /id="PRO_0000394360"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        80..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        328..336
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  41339 MW;  92CF177CD4C15315 CRC64;
     MKTATFSTLL ALSASAVNAQ VSGTAFGFAA GTTGGGSAAP ETPSSIDELV EWLTDDTART
     IMIDRTWDFT GTEGTTDGQC CSTRTTTCEG GTSAGQAWIQ DTCDDGTWVS CTYDNAAKNP
     INVGSNKSIV GVGSDGVLKG KGLRITGGNS NVIIQNIHIT DLNPQYVWGG DAITLDDADL
     VWIDHNKISL IGRQFIVSGW GKAGRVTISN NEFDGVTDWS AGCNGKHYWT LLLIGEQDFY
     TFSDNWVHDV SGRAPHMGTD MTESTIFFHG VNNYFQNIGG HAFDIDTNTW ALLEGNYFES
     VDTPLTETSL TSGALIYNVP TVDSASACTS PLGYICEWNR LAGSGTWTER TDADVLTMAS
     QYIDSLIDHI PVADVPTTVV ANAGVGKL