ID   DESA_SPHSK              Reviewed;         462 AA.
AC   G2IJ05; Q7WST1;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Syringate O-demethylase {ECO:0000303|PubMed:15090517};
DE            EC=2.1.1.- {ECO:0000269|PubMed:15090517};
DE   AltName: Full=Tetrahydrofolate-dependent syringate O-demethylase {ECO:0000303|PubMed:15090517};
DE            Short=H(4)folate-dependent syringate O-demethylase {ECO:0000303|PubMed:15090517};
GN   Name=desA {ECO:0000303|PubMed:15090517};
GN   ORFNames=SLG_25000 {ECO:0000312|EMBL:BAK67175.1};
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], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=15090517; DOI=10.1128/jb.186.9.2757-2765.2004;
RA   Masai E., Sasaki M., Minakawa Y., Abe T., Sonoki T., Miyauchi K.,
RA   Katayama Y., Fukuda M.;
RT   "A novel tetrahydrofolate-dependent O-demethylase gene is essential for
RT   growth of Sphingomonas paucimobilis SYK-6 with syringate.";
RL   J. Bacteriol. 186:2757-2765(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=22207743; DOI=10.1128/jb.06254-11;
RA   Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA   Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA   Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA   Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT   lignin-derived biaryls and monoaryls.";
RL   J. Bacteriol. 194:534-535(2012).
CC   -!- FUNCTION: Involved in the catabolism of syringate. Catalyzes the
CC       conversion of syringate to 3-O-methylgallate (3MGA) in the presence of
CC       tetrahydrofolate. Has weak activity with vanillate and 3-O-
CC       methylgallate. {ECO:0000269|PubMed:15090517}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + syringate = (6S)-5-methyl-
CC         5,6,7,8-tetrahydrofolate + 3-O-methylgallate; Xref=Rhea:RHEA:59840,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:19950, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:132111; Evidence={ECO:0000269|PubMed:15090517};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0 (in the presence of 1 mM tetrahydrofolate).
CC         {ECO:0000269|PubMed:15090517};
CC   -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC       {ECO:0000305|PubMed:15090517}.
CC   -!- INDUCTION: Induced by growth on syringate.
CC       {ECO:0000269|PubMed:15090517}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cannot grow on syringate, but grows on
CC       vanillate. {ECO:0000269|PubMed:15090517}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB110975; BAC79257.1; -; Genomic_DNA.
DR   EMBL; AP012222; BAK67175.1; -; Genomic_DNA.
DR   RefSeq; WP_014076820.1; NC_015976.1.
DR   AlphaFoldDB; G2IJ05; -.
DR   SMR; G2IJ05; -.
DR   STRING; 627192.SLG_25000; -.
DR   EnsemblBacteria; BAK67175; BAK67175; SLG_25000.
DR   KEGG; ssy:SLG_25000; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_046852_1_0_5; -.
DR   OrthoDB; 282830at2; -.
DR   BRENDA; 2.1.1.341; 2280.
DR   UniPathway; UPA00892; -.
DR   Proteomes; UP000001275; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
PE   1: Evidence at protein level;
KW   Lignin degradation; Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..462
FT                   /note="Syringate O-demethylase"
FT                   /id="PRO_0000447210"
SQ   SEQUENCE   462 AA;  50778 MW;  6DA09308F31FF3E1 CRC64;
     MAKSLQDVLD NAGNAVDFLR NQQTGPNVYP GVPAEYSNWR NEQRAWAKTA VLFNQSYHMV
     ELMVEGPDAF AFLNYLGINS FKNFAPGKAK QWVPVTAEGY VIGDVILFYL AENQFNLVGR
     APAIEWAEFH AATGKWNVTL TRDERTALRT DGVRRHYRFQ LQGPNAMAIL TDAMGQTPPD
     LKFFNMADIQ IAGKTVGALR HGMAGQPGYE LYGPWADYEA VHSALVAAGK NHGLALVGGR
     AYSSNTLESG WVPSPFPGYL FGEGSADFRK WAGENSYGAK CSIGGSYVPE SLEGYGLTPW
     DIGYGIIVKF DHDFIGKEAL EKMANEPHLE KVTLALDDED MLRVMSSYFS DSGRAKYFEF
     PSAVYSMHPY DSVLVDGKHV GVSTWVGYSS NEGKMLTLAM IDPKYAKPGT EVSLLWGEPN
     GGTSKPTVEP HEQTEIKAVV APVPYSAVAR TGYADSWRTK KA