ID   PELF_ASPOR              Reviewed;         428 AA.
AC   Q2UJA7;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Probable pectin lyase F;
DE            Short=PLF;
DE            EC=4.2.2.10;
DE   Flags: Precursor;
GN   Name=pelF; ORFNames=AO090003001295;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE58358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007155; BAE58358.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001820360.2; XM_001820308.2.
DR   AlphaFoldDB; Q2UJA7; -.
DR   SMR; Q2UJA7; -.
DR   CAZy; PL1; Polysaccharide Lyase Family 1.
DR   Proteomes; UP000006564; Chromosome 2.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..428
FT                   /note="Probable pectin lyase F"
FT                   /id="PRO_0000394359"
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;  44837 MW;  B328CBA9685FE773 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 SSSVSITPSP TSSAIPSSSA TPSSSAYARR
     HYARHHHY