ID   PELF_ASPFN              Reviewed;         428 AA.
AC   B8N316;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable pectin lyase F;
DE            Short=PLF;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF; ORFNames=AFLA_025400;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963473; EED55269.1; -; Genomic_DNA.
DR   RefSeq; XP_002374051.1; XM_002374010.1.
DR   AlphaFoldDB; B8N316; -.
DR   SMR; B8N316; -.
DR   EnsemblFungi; EED55269; EED55269; AFLA_025400.
DR   VEuPathDB; FungiDB:AFLA_025400; -.
DR   eggNOG; ENOG502QXM6; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; DWCGSYP; -.
DR   Proteomes; UP000001875; 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; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..428
FT                   /note="Probable pectin lyase F"
FT                   /id="PRO_0000394357"
FT   REGION          337..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..107
FT                   /evidence="ECO:0000250"
FT   DISULFID        324..332
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   428 AA;  44809 MW;  B328D549864FE773 CRC64;
     MVLLHPLLTA AALLGASARA QSVVGTPFGF ASGTTGGGNA APAAPKDTNE LKEWLADPNP
     RVIVIDKEFN FIGTEDTCTD CECCIPDSNT CGDAGQNAIK TEGSDWCGSY PATTCTYDNA
     GLEGMEVASD KTIIGVGDAG VIRGKGLRLV NGVSNIIIQN VHITELNPQY IWGGDAISLD
     GTDKIWVDHV KVSLVGRQMF VTGYESSGGV TVSNSEFDGQ TKWSASCDGH HYWSVLGYGK
     GDQITFANNY IHHTSGRSPK IEFDSHWHAY NNFWENNSGH AFDVGEGANV LIEGNVFSNV
     KTPMNPEDTP GSTFAVNAQD ASSCTSALGR PCIANELTSS GELSGNDEAV LSGWPKGEGD
     TKAMTTDKVP SYVKANAGVG KLGSGGSGAA SSSASITPSP TSSAIPSSSA TPSSSAYARR
     HYARHHHY