ID   LIGD_SPHSK              Reviewed;         305 AA.
AC   Q01198;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=C alpha-dehydrogenase;
DE            EC=1.-.-.-;
GN   Name=ligD;
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 103272 / SYK-6;
RX   PubMed=7764263; DOI=10.1271/bbb.57.1655;
RA   Masai E., Kubota S., Katayama Y., Kawai S., Yamasaki M., Morohoshi N.;
RT   "Characterization of the C alpha-dehydrogenase gene involved in the
RT   cleavage of beta-aryl ether by Pseudomonas paucimobilis.";
RL   Biosci. Biotechnol. Biochem. 57:1655-1659(1993).
CC   -!- FUNCTION: Catalyzes the C alpha dehydrogenation of arylglycerol-beta-
CC       aryl ether (C alpha alcohol type) (compound IV).
CC   -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; S67975; AAC60455.1; -; Genomic_DNA.
DR   EMBL; D11473; BAA02030.1; -; Genomic_DNA.
DR   EMBL; D11341; BAA01953.1; -; Genomic_DNA.
DR   PIR; S35991; S35991.
DR   RefSeq; WP_014075190.1; NC_015976.1.
DR   AlphaFoldDB; Q01198; -.
DR   SMR; Q01198; -.
DR   STRING; 627192.SLG_08640; -.
DR   BioCyc; MetaCyc:MON-15126; -.
DR   UniPathway; UPA00892; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Lignin degradation; Oxidoreductase.
FT   CHAIN           1..305
FT                   /note="C alpha-dehydrogenase"
FT                   /id="PRO_0000054717"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         10..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  32344 MW;  6071D1451A928900 CRC64;
     MKDFQDQVAF ITGGASGAGF GQAKVFGQAG AKIVVADVRA EAVEKAVAEL EGLGITAHGI
     VLDIMDREAY ARAADEVEAV FGQAPTLLSN TAGVNSFGPI EKTTYDDFDW IIGVNLNGVI
     NGMVTFVPRM IASGRPGHIV TVSSLGGFMG SALAGPYSAA KAASINLMEG YRQGLEKYGI
     GVSVCTPANI KSNIAEASRL RPAKYGTSGY VENEESIASL HSIHQHGLEP EKLAEAIKKG
     VEDNALYIIP YPEVREGLEK HFQAIIDSVA PMESDPEGAR QRVEALMAWG RDRTRVFAEG
     DKKGA