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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.

Catalytic activityi

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

Cofactori

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei71 – 711Transition state stabilizer
Active sitei75 – 751Proton acceptor
Metal bindingi76 – 761Calcium 1
Metal bindingi94 – 941Calcium 1; via carbonyl oxygen
Metal bindingi96 – 961Calcium 1
Metal bindingi98 – 981Calcium 1
Metal bindingi204 – 2041Iron (heme axial ligand)
Metal bindingi205 – 2051Calcium 2
Metal bindingi222 – 2221Calcium 2
Metal bindingi224 – 2241Calcium 2
Metal bindingi227 – 2271Calcium 2; via carbonyl oxygen
Metal bindingi229 – 2291Calcium 2

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

PeroxiBasei2409. PcLiP05_RP78.

Names & Taxonomyi

Protein namesi
Recommended name:
Ligninase LG2 (EC:1.11.1.14)
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Propeptidei22 – 2871 PublicationPRO_0000023762
Chaini29 – 371343Ligninase LG2PRO_0000023763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 43
Disulfide bondi42 ↔ 313
Disulfide bondi62 ↔ 148
Modified residuei199 – 19913-hydroxytryptophan1 Publication
Disulfide bondi277 ↔ 345
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence analysis

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

1
371
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 434Combined sources
Helixi44 – 5512Combined sources
Turni58 – 603Combined sources
Helixi64 – 7714Combined sources
Helixi82 – 865Combined sources
Beta strandi87 – 893Combined sources
Beta strandi94 – 974Combined sources
Helixi98 – 1014Combined sources
Helixi103 – 1064Combined sources
Helixi110 – 1123Combined sources
Helixi115 – 12915Combined sources
Helixi133 – 14614Combined sources
Helixi179 – 19012Combined sources
Helixi194 – 2007Combined sources
Helixi201 – 2066Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi219 – 2235Combined sources
Helixi231 – 2355Combined sources
Beta strandi255 – 2573Combined sources
Helixi264 – 2696Combined sources
Turni273 – 2753Combined sources
Helixi276 – 2805Combined sources
Turni281 – 2844Combined sources
Helixi286 – 30116Combined sources
Turni302 – 3043Combined sources
Helixi307 – 3093Combined sources
Beta strandi310 – 3123Combined sources
Helixi314 – 3163Combined sources
Beta strandi324 – 3274Combined sources
Helixi338 – 3403Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi357 – 3593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGAX-ray2.03A/B29-371[»]
1LLPX-ray1.70A29-371[»]
ProteinModelPortaliP49012.
SMRiP49012. Positions 29-371.
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

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 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
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGAX-ray2.03A/B29-371[»]
1LLPX-ray1.70A29-371[»]
ProteinModelPortaliP49012.
SMRiP49012. Positions 29-371.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

InterProiIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR001621. Ligninase.
IPR024589. Ligninase_C.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF11895. DUF3415. 1 hit.
PF00141. peroxidase. 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...

Publicationsi

  1. "Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme."
    Ritch T.G. Jr., Nipper V.J., Akileswaran L., Smith A.J., Pribnow D.G., Gold M.H.
    Gene 107:119-126(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-48.
    Strain: ATCC 201542 / OGC101.
  2. "Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporium."
    Ritch T.G. Jr., Gold M.H.
    Gene 118:73-80(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 201542 / OGC101.
  3. "Crystallographic refinement of lignin peroxidase at 2 A."
    Poulos T.L., Edwards S.L., Wariishi H., Gold M.H.
    J. Biol. Chem. 268:4429-4440(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  4. "The crystal structure of lignin peroxidase at 1.70-A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle."
    Choinowski T., Blodig W., Winterhalter K.H., Piontek K.
    J. Mol. Biol. 286:809-827(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), HYDROXYLATION AT TRP-199.
    Strain: ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM F-1767.

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: May 11, 2016
This is version 107 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.