PELB_ASPNG
ID PELB_ASPNG Reviewed; 378 AA.
AC Q00205;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Pectin lyase B;
DE Short=PLB;
DE EC=4.2.2.10;
DE Flags: Precursor;
GN Name=pelB;
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].
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=1495474; DOI=10.1007/bf00272352;
RA Kusters-Van Someren M., Flipphi M., de Graaff L., van den Broeck H.,
RA Kester H., Hinnen A., Visser J.;
RT "Characterization of the Aspergillus niger pelB gene: structure and
RT regulation of expression.";
RL Mol. Gen. Genet. 234:113-120(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9449837; DOI=10.1104/pp.116.1.69;
RA Vitali J., Schick B., Kester H.C., Visser J., Jurnak F.;
RT "The tree-dimensional structure of Aspergillus niger pectin lyase B at 1.7-
RT A resolution.";
RL Plant Physiol. 116:69-80(1998).
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:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000305}.
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DR EMBL; X65552; CAA46521.1; -; Genomic_DNA.
DR PIR; S23573; S23573.
DR PDB; 1QCX; X-ray; 1.70 A; A=21-378.
DR PDBsum; 1QCX; -.
DR AlphaFoldDB; Q00205; -.
DR SMR; Q00205; -.
DR STRING; 5061.CADANGAP00002970; -.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR CLAE; PEL1B_ASPNG; -.
DR VEuPathDB; FungiDB:An03g00190; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1219484; -.
DR VEuPathDB; FungiDB:ATCC64974_82630; -.
DR VEuPathDB; FungiDB:M747DRAFT_60678; -.
DR eggNOG; ENOG502QXM6; Eukaryota.
DR EvolutionaryTrace; Q00205; -.
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 Disulfide bond; Glycoprotein; Lyase; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /note="Or 21"
FT /evidence="ECO:0000255"
FT CHAIN 21..378
FT /note="Pectin lyase B"
FT /id="PRO_0000024897"
FT ACT_SITE 255
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..102
FT DISULFID 92..225
FT DISULFID 322..330
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1QCX"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1QCX"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 271..282
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1QCX"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:1QCX"
FT HELIX 366..373
FT /evidence="ECO:0007829|PDB:1QCX"
SQ SEQUENCE 378 AA; 39703 MW; 4FF321AF2B0B72FF CRC64;
MHYKLLFAAA AASLASAVSA AGVVGAAEGF AHGVTGGGSA SPVYPTTTDE LVSYLGDNEP
RVIILDRTFD FTGTEGTETT TGCAPWGTAS QCQVAINLHS WCDNYQASAP KVSVTDKAGI
LPITVNSNKS IVGQGTKGVI KGKGLRVVSG AKNVIIQNIA VTDINPKYVW GGDAITVDDS
DLVWIDHVTT ARIGRQHIVL GTSADNRVTI SYSLIDGRSD YSATCNGHHY WGVYLDGSND
MVTLKGNYFY NLSGRMPKVQ GNTLLHAVNN LFHNFDGHAF EIGTGGYVLA EGNVFQDVNI
VVETPISGQL FSSPDANTNQ QCASVFGRSC QLNAFGNSGS MSGSDTSIIS KFAGKTIAAA
HPPGNIAQWT MKNAGQGK
