LIGF_SPHSK
ID LIGF_SPHSK Reviewed; 257 AA.
AC P30347;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein LigF;
GN Name=ligF;
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=1744051; DOI=10.1128/jb.173.24.7950-7955.1991;
RA Masai E., Katayama Y., Kawai S., Nishikawa S., Yamasaki M., Morohoshi N.;
RT "Cloning and sequencing of the gene for a Pseudomonas paucimobilis enzyme
RT that cleaves beta-aryl ether.";
RL J. Bacteriol. 173:7950-7955(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=8495726; DOI=10.1016/0014-5793(93)81465-c;
RA Masai E., Katayama Y., Kubota S., Kawai S., Yamasaki M., Morohoshi N.;
RT "A bacterial enzyme degrading the model lignin compound beta-etherase is a
RT member of the glutathione-S-transferase superfamily.";
RL FEBS Lett. 323:135-140(1993).
CC -!- FUNCTION: Lignin degradation enzyme.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; D11473; BAA02031.1; -; Genomic_DNA.
DR PIR; S33314; S33314.
DR RefSeq; WP_014075191.1; NC_015976.1.
DR PDB; 4XT0; X-ray; 2.07 A; A=1-243.
DR PDBsum; 4XT0; -.
DR AlphaFoldDB; P30347; -.
DR SMR; P30347; -.
DR STRING; 627192.SLG_08650; -.
DR BioCyc; MetaCyc:MON-15129; -.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lignin degradation.
FT CHAIN 1..257
FT /note="Protein LigF"
FT /id="PRO_0000186042"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT DOMAIN 89..257
FT /note="GST C-terminal"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4XT0"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:4XT0"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4XT0"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:4XT0"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 158..179
FT /evidence="ECO:0007829|PDB:4XT0"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:4XT0"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4XT0"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:4XT0"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:4XT0"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:4XT0"
SQ SEQUENCE 257 AA; 29686 MW; 900E30C3BB3AE08B CRC64;
MTLKLYSFGP GANSLKPLAT LYEKGLEFEQ VFVDPSKFEQ HSDWFKKINP RGQVPALWHD
GKVVTESTVI CEYLEDVFPE SGNSLRPADP FKRAEMRVWT KWVDEYFCWC VSTIGWAFGI
KAIAQKMSDE EFEEHINKNV PIPEQQLKWR RARNGFPQEM LDEEFRKVGV SVARLEETLS
KQDYLVDTGY SLADICNFAI ANGLQRPGGF FGDYVNQEKT PGLCAWLDRI NARPAIKEMF
EKSKREDLLK RQNEKVA