ID   PELF_NEOFI              Reviewed;         386 AA.
AC   A1DEH0;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Probable pectin lyase F;
DE            Short=PLF;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF; ORFNames=NFIA_077100;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW17777.1; -; Genomic_DNA.
DR   RefSeq; XP_001259674.1; XM_001259673.1.
DR   AlphaFoldDB; A1DEH0; -.
DR   SMR; A1DEH0; -.
DR   EnsemblFungi; EAW17777; EAW17777; NFIA_077100.
DR   GeneID; 4586256; -.
DR   KEGG; nfi:NFIA_077100; -.
DR   VEuPathDB; FungiDB:NFIA_077100; -.
DR   eggNOG; ENOG502RZWS; Eukaryota.
DR   HOGENOM; CLU_021980_0_1_1; -.
DR   OMA; WSAGCNG; -.
DR   OrthoDB; 1267775at2759; -.
DR   Proteomes; UP000006702; 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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..386
FT                   /note="Probable pectin lyase F"
FT                   /id="PRO_0000394363"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..334
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  41397 MW;  5DED61AB321AFAB4 CRC64;
     MKTAVLSLLL ALQAYARVTG SPSGFAAGTT GGGSATPAAP SSLDELVQWI TDDTPRVILI
     DRTWDFIGTE GTTTGKCCSM PSTTVCNGGT SKGQAWIQDH CDGGSWVSCK YDNAALTPMD
     VGSNKSIVGV GNKGVIKGKG LRVRNGNKNV IIQNIHITNL NPQYVWGGDA ITLDNADQVW
     IDHNKISLIG RQFIVSGWGK AGHVTISNNE FDGRTSWSAG CNGKHYWTLL LLGEQDYYTF
     EGNWLHDVSG RAPHMGTDHT KSQIFFHGVN NYFQNLGGHA FDVDTNTWVL LEGNYFENVK
     TPLTDTSLKA GGKLYTTSTV NAAGACLDKL GYICEWNRLA GSGAWQDRTD ADVKTKAATY
     KNSLVGHYPV ADVPAKVVAN AGVGKV