PELA_ASPNG
ID PELA_ASPNG Reviewed; 379 AA.
AC Q01172;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Pectin lyase A;
DE Short=PLA;
DE EC=4.2.2.10;
DE AltName: Full=Pectin lyase II;
DE Short=PLII;
DE Flags: Precursor;
GN Name=pelA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-40 AND
RP 115-125.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=1934134; DOI=10.1007/bf00318518;
RA Kusters-Van Someren M.A., Harmsen J.A.M., Kester H.C.M., Visser J.;
RT "Structure of the Aspergillus niger pelA gene and its expression in
RT Aspergillus niger and Aspergillus nidulans.";
RL Curr. Genet. 20:293-299(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=2225145; DOI=10.1007/bf00312604;
RA Harmsen J.A.M., Kurster-Van Sommeren M.A., Visser J.;
RT "Cloning and expression of a second Aspergillus niger pectin lyase gene
RT (pelA): indications of a pectin lyase gene family in A. niger.";
RL Curr. Genet. 18:161-166(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-379 FOR STRAIN N400, X-RAY
RP CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 21-379 FOR STRAIN 4M-147, AND VARIANTS
RP LYS-32; SER-39; THR-121; ALA-233; ALA-268; TRP-273; GLU-309; SER-316 AND
RP SER-337.
RC STRAIN=4M-147, and
RC ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=9195887; DOI=10.1016/s0969-2126(97)00222-0;
RA Mayans O., Scott M., Connerton I., Gravesen T., Benen J., Visser J.,
RA Pickersgill R., Jenkins J.;
RT "Two crystal structures of pectin lyase A from Aspergillus reveal a pH
RT driven conformational change and striking divergence in the substrate-
RT binding clefts of pectin and pectate lyases.";
RL Structure 5:677-689(1997).
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.
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:0000305}.
CC -!- PTM: N-glycosylated at Asn-129 and O-glycosylated at Thr-88 when
CC expressed in Aspergillus nidulans. The protein from strain 4M-147 is O-
CC glycosylated at Thr-88 and Ser-368. PubMed:9195887 modeled GalNAc at
CC the O-glycosylation site, a glycosylation not observed in fungi. The O-
CC linked saccharide is probably mannose.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
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DR EMBL; X60724; CAA43130.1; -; Genomic_DNA.
DR EMBL; X55784; CAA39305.1; -; Genomic_DNA.
DR PIR; S17979; S17979.
DR PDB; 1IDJ; X-ray; 2.40 A; A/B=21-379.
DR PDB; 1IDK; X-ray; 1.93 A; A=21-379.
DR PDBsum; 1IDJ; -.
DR PDBsum; 1IDK; -.
DR AlphaFoldDB; Q01172; -.
DR SMR; Q01172; -.
DR STRING; 5061.CADANGAP00011153; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR CLAE; PEL1A_ASPNG; -.
DR VEuPathDB; FungiDB:An14g04370; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1161674; -.
DR VEuPathDB; FungiDB:ATCC64974_3740; -.
DR VEuPathDB; FungiDB:M747DRAFT_327313; -.
DR eggNOG; ENOG502QXM6; Eukaryota.
DR BioCyc; MetaCyc:MON-20551; -.
DR BRENDA; 4.2.2.10; 518.
DR EvolutionaryTrace; Q01172; -.
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; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lyase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1934134"
FT CHAIN 21..379
FT /note="Pectin lyase A"
FT /id="PRO_0000024896"
FT ACT_SITE 256
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="O-linked (Man) threonine"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 368
FT /note="O-linked (Man) serine; in strain 4M-147"
FT DISULFID 83..102
FT DISULFID 92..226
FT DISULFID 322..330
FT VARIANT 32
FT /note="E -> K (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 39
FT /note="D -> S (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 121
FT /note="V -> T (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 233
FT /note="G -> A (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 268
FT /note="C -> A (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 273
FT /note="F -> W (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 309
FT /note="A -> E (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 316
FT /note="T -> S (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT VARIANT 337
FT /note="C -> S (in strain: 4M-147)"
FT /evidence="ECO:0000269|PubMed:9195887"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1IDK"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1IDK"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1IDK"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1IDJ"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 272..283
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 295..311
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1IDK"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1IDK"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:1IDK"
SQ SEQUENCE 379 AA; 39855 MW; 4DF1326BFFCA77B5 CRC64;
MKYSTIFSAA AAVFAGSAAA VGVSGSAEGF AEGVTGGGDA TPVYPDTIDE LVSYLGDDEA
RVIVLTKTFD FTDSEGTTTG TGCAPWGTAS ACQVAIDQDD WCENYEPDAP SVSVEYYNAG
VLGITVTSNK SLIGEGSSGA IKGKGLRIVS GAENIIIQNI AVTDINPKYV WGGDAITLDD
CDLVWIDHVT TARIGRQHYV LGTSADNRVS LTNNYIDGVS DYSATCDGYH YWGIYLDGDA
DLVTMKGNYI YHTSGRSPKV QDNTLLHCVN NYFYDISGHA FEIGEGGYVL AEGNVFQNVD
TVLETYEGAA FTVPSTTAGE VCSTYLGRDC VINGFGCSGT FSEDSTSFLS DFEGKNIASA
SAYTSVASRV VANAGQGNL
