Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ligninase LG2

Gene

GLG2

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.By similarity

Catalytic activityi

1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O.By similarity
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.By similarity

Pathwayi: lignin degradation

This protein is involved in the pathway lignin degradation, which is part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the pathway lignin degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei71Transition state stabilizer1
Active sitei75Proton acceptor1
Metal bindingi76Calcium 11
Metal bindingi94Calcium 1; via carbonyl oxygen1
Metal bindingi96Calcium 11
Metal bindingi98Calcium 11
Metal bindingi204Iron (heme axial ligand)1
Metal bindingi205Calcium 21
Metal bindingi222Calcium 21
Metal bindingi224Calcium 21
Metal bindingi227Calcium 2; via carbonyl oxygen1
Metal bindingi229Calcium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.11.1.14. 1380.
UniPathwayiUPA00892.

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
PeroxiBasei2409. PcLiP05_RP78.

Names & Taxonomyi

Protein namesi
Recommended name:
Ligninase LG2 (EC:1.11.1.14By similarity)
Alternative name(s):
Diarylpropane peroxidase
Lignin peroxidase
Gene namesi
Name:GLG2
Synonyms:LIP2
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
PropeptideiPRO_000002376222 – 281 Publication7
ChainiPRO_000002376329 – 371Ligninase LG2Add BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 43
Disulfide bondi42 ↔ 313
Disulfide bondi62 ↔ 148
Modified residuei1993-hydroxytryptophan1 Publication1
Disulfide bondi277 ↔ 345
Glycosylationi285N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Hydroxylation, Zymogen

Expressioni

Developmental stagei

Ligninases are expressed during secondary metabolism, and are triggered by nutrient limitation.

Structurei

Secondary structure

1371
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 43Combined sources4
Helixi44 – 55Combined sources12
Turni58 – 60Combined sources3
Helixi64 – 77Combined sources14
Helixi82 – 86Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi94 – 97Combined sources4
Helixi98 – 101Combined sources4
Helixi103 – 106Combined sources4
Helixi110 – 112Combined sources3
Helixi115 – 129Combined sources15
Helixi133 – 146Combined sources14
Helixi179 – 190Combined sources12
Helixi194 – 200Combined sources7
Helixi201 – 206Combined sources6
Beta strandi208 – 213Combined sources6
Beta strandi219 – 223Combined sources5
Helixi231 – 235Combined sources5
Beta strandi255 – 257Combined sources3
Helixi264 – 269Combined sources6
Turni273 – 275Combined sources3
Helixi276 – 280Combined sources5
Turni281 – 284Combined sources4
Helixi286 – 301Combined sources16
Turni302 – 304Combined sources3
Helixi307 – 309Combined sources3
Beta strandi310 – 312Combined sources3
Helixi314 – 316Combined sources3
Beta strandi324 – 327Combined sources4
Helixi338 – 340Combined sources3
Beta strandi346 – 348Combined sources3
Beta strandi357 – 359Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGAX-ray2.03A/B29-371[»]
1LLPX-ray1.70A29-371[»]
ProteinModelPortaliP49012.
SMRiP49012.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49012.

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Ligninase subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.
OMAiHTIARDP.

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD
60 70 80 90 100
DIQANMFHGG QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM
110 120 130 140 150
IFDTIETAFH PNIGLDEVVA MQKPFVQKHG VTPGDFIAFA GAVALSNCPG
160 170 180 190 200
APQMNFFTGR KPATQPAPDG LVPEPFHTVD QIIARVNDAG EFDELELVWM
210 220 230 240 250
LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG TLFPGSGGNQ
260 270 280 290 300
GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL
310 320 330 340 350
TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF
360 370
PSLVTLPGPA TSVARIPPHK A
Length:371
Mass (Da):39,329
Last modified:February 1, 1996 - v1
Checksum:iF6AAB123EDC92123
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74229 mRNA. Translation: AAA33735.1.
M92644 Genomic DNA. Translation: AAA33738.1.
PIRiJC1268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74229 mRNA. Translation: AAA33735.1.
M92644 Genomic DNA. Translation: AAA33738.1.
PIRiJC1268.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LGAX-ray2.03A/B29-371[»]
1LLPX-ray1.70A29-371[»]
ProteinModelPortaliP49012.
SMRiP49012.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA2. Auxiliary Activities 2.
PeroxiBasei2409. PcLiP05_RP78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410II1B. Eukaryota.
ENOG410ZS1R. LUCA.
OMAiHTIARDP.

Enzyme and pathway databases

UniPathwayiUPA00892.
BRENDAi1.11.1.14. 1380.

Miscellaneous databases

EvolutionaryTraceiP49012.

Family and domain databases

CDDicd00692. ligninase. 1 hit.
InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 1 hit.
PF11895. Peroxidase_ext. 1 hit.
[Graphical view]
PRINTSiPR00462. LIGNINASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIG2_PHACH
AccessioniPrimary (citable) accession number: P49012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.