LSDX3_SPHPI
ID LSDX3_SPHPI Reviewed; 490 AA.
AC Q52008;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Lignostilbene-alpha,beta-dioxygenase isozyme III {ECO:0000312|EMBL:AAB35856.2};
DE Short=LSD-III {ECO:0000303|PubMed:8534977};
DE EC=1.13.11.43 {ECO:0000269|PubMed:8534977};
GN Name=lsdB {ECO:0000312|EMBL:AAB35856.2};
OS Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=13689;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB35856.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=TMY1009 {ECO:0000312|EMBL:AAB35856.2};
RX PubMed=8534977; DOI=10.1271/bbb.59.1866;
RA Kamoda S., Saburi Y.;
RT "Cloning of a lignostilbene-alpha,beta-dioxygenase isozyme gene from
RT Pseudomonas paucimobilis TMY1009.";
RL Biosci. Biotechnol. Biochem. 59:1866-1868(1995).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=TMY1009 {ECO:0000269|PubMed:7763880};
RX PubMed=7763880; DOI=10.1271/bbb.57.931;
RA Kamoda S., Saburi Y.;
RT "Structural and enzymatical comparison of lignostilbene-alpha,beta-
RT dioxygenase isozymes, I, II, and III, from Pseudomonas paucimobilis
RT TMY1009.";
RL Biosci. Biotechnol. Biochem. 57:931-934(1993).
CC -!- FUNCTION: Catalyzes the cleavage of the interphenyl double bond (C
CC alpha-C beta) of lignin-derived polyphenolic diaryl-propane type
CC compounds (Stilbene). {ECO:0000269|PubMed:7763880,
CC ECO:0000269|PubMed:8534977}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin;
CC Xref=Rhea:RHEA:21340, ChEBI:CHEBI:15379, ChEBI:CHEBI:17501,
CC ChEBI:CHEBI:18346; EC=1.13.11.43;
CC Evidence={ECO:0000269|PubMed:7763880, ECO:0000269|PubMed:8534977};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q53353};
CC Note=1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q53353};
CC -!- ACTIVITY REGULATION: Activity is high with beta-5 type stilbene and
CC minimal with beta-1 type stilbene. A 4-hydroxyl group and trans-
CC stilbene structure is essential for the binding of substrates to the
CC enzyme. {ECO:0000269|PubMed:7763880}.
CC -!- SUBUNIT: Homodimer of two beta subunits. {ECO:0000269|PubMed:7763880}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; S80637; AAB35856.2; -; Genomic_DNA.
DR PIR; JC4324; JC4324.
DR AlphaFoldDB; Q52008; -.
DR SMR; Q52008; -.
DR PRIDE; Q52008; -.
DR BioCyc; MetaCyc:MON-18892; -.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0050054; F:lignostilbene alpha beta-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046274; P:lignin catabolic process; IDA:UniProtKB.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Direct protein sequencing; Iron; Lignin degradation;
KW Metal-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7763880"
FT CHAIN 2..490
FT /note="Lignostilbene-alpha,beta-dioxygenase isozyme III"
FT /evidence="ECO:0000269|PubMed:7763880"
FT /id="PRO_0000416941"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 490 AA; 55126 MW; 32EC3A4E03A52DA9 CRC64;
MAHFPDTSGM TGVLRPLRIE GDILDLEVEG EIPAQLDGTF HRVHPDAQFP PRFEDDQFFN
GDGMVSLFRF HDGKIDFRQR YAQTDKWKVE RKAGKSLFGA YRNPLTDDAS VQGMIRGTAN
TNVMVHAGKL YAMKEDSPCL IMDPLTLETE GYTNFDGKLK NQTFSAHAKI DPVTGNFCNF
GYAATGLLTT DCSYFEIDPA GNLLFETEFQ VPYYCMMHDY GLTEHYAIFH IVPCSPNWDR
LKAGLPHFGF DTTLPVWLGV VPRGPGVTNK DVRWFKAPKT IFASHVMNAF EEGSKIHFDT
PQAENNAFPF FPDIHGAPFD PVAARPYLHR WTVDLGSNSE DFAEVRQLTS WIDEFPRVDA
RYVGQPYRHG WGLVMDPEME MEFARGRASG FKMNRIGHWD HATGKEDSWW CGPQSIIQEP
CFVPRMADSA EGDGYIIALV DNLITNYSDL VVLDALNLKD GPIGRAKLPI RLRSGLHGNW
ADASKLPIAA
