ID   LIGE_SPHSK              Reviewed;         281 AA.
AC   P27457;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Beta-etherase;
DE   AltName: Full=Beta-aryl ether cleaving enzyme;
GN   Name=ligE;
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], AND PROTEIN SEQUENCE OF 2-11.
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: Able to degrade various dimeric lignin compounds. Catalyzes
CC       the unique and reductive cleavage of arylglycerol-beta-aryl ether.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; M69107; AAA25878.1; -; Genomic_DNA.
DR   EMBL; D11473; BAA02032.1; -; Genomic_DNA.
DR   PIR; A43749; A43749.
DR   RefSeq; WP_014075192.1; NC_015976.1.
DR   PDB; 4YAM; X-ray; 1.91 A; A/B/C/D=1-281.
DR   PDBsum; 4YAM; -.
DR   AlphaFoldDB; P27457; -.
DR   SMR; P27457; -.
DR   STRING; 627192.SLG_08660; -.
DR   BioCyc; MetaCyc:MON-15130; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane;
KW   Direct protein sequencing; Hydrolase; Lignin degradation; Membrane.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1744051"
FT   CHAIN           2..281
FT                   /note="Beta-etherase"
FT                   /id="PRO_0000084420"
FT   DOMAIN          11..87
FT                   /note="GST N-terminal"
FT   REGION          244..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   STRAND          57..59
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           72..82
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           111..125
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           131..141
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           148..152
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           167..173
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           186..201
FT                   /evidence="ECO:0007829|PDB:4YAM"
FT   HELIX           214..226
FT                   /evidence="ECO:0007829|PDB:4YAM"
SQ   SEQUENCE   281 AA;  32070 MW;  694CA47B8BD008AB CRC64;
     MARNNTITLY DLQLESGCTI SPYVWRTKYA LKHKGFDIDI VPGGFTGILE RTGGRSERVP
     VIVDDGEWVL DSWVIAEYLD EKYPDRPMLF EGPTQKNLMK FLDNWLWSTA VGPWFRCYIL
     DYHDLSLPQD RDYVRWSREQ WFLGGQRLED VQAGREDRLP LVPPTLEPFR RILAETKWLG
     GDQPNFADYS ALAVFLWTAS VARTPPLTED DPLRDWLDRG FDLFDGLGRH PGMNPLFGLK
     LREGDPEPFV RQTGPAGAGG QALNKGPQTT KMPPRVAEKA D