LIGC_SPHSK
ID LIGC_SPHSK Reviewed; 315 AA.
AC Q9KWL3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase;
DE Short=CHMS dehydrogenase;
DE EC=1.1.1.312;
DE AltName: Full=2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase;
GN Name=ligC;
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=2185230; DOI=10.1128/jb.172.5.2704-2709.1990;
RA Noda Y., Nishikawa S., Shiozuka K., Kadokura H., Nakajima H., Yoda K.,
RA Katayama Y., Morohoshi N., Haraguchi T., Yamasaki M.;
RT "Molecular cloning of the protocatechuate 4,5-dioxygenase genes of
RT Pseudomonas paucimobilis.";
RL J. Bacteriol. 172:2704-2709(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=9864312; DOI=10.1128/jb.181.1.55-62.1999;
RA Masai E., Shinohara S., Hara H., Nishikawa S., Katayama Y., Fukuda M.;
RT "Genetic and biochemical characterization of a 2-pyrone-4, 6-dicarboxylic
RT acid hydrolase involved in the protocatechuate 4, 5-cleavage pathway of
RT Sphingomonas paucimobilis SYK-6.";
RL J. Bacteriol. 181:55-62(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION AS A
RP CHMS DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP DISRUPTION PHENOTYPE, ACTIVITY REGULATION, SUBUNIT, AND NOMENCLATURE.
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=11073908; DOI=10.1128/jb.182.23.6651-6658.2000;
RA Masai E., Momose K., Hara H., Nishikawa S., Katayama Y., Fukuda M.;
RT "Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-
RT semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage
RT pathway in Sphingomonas paucimobilis SYK-6.";
RL J. Bacteriol. 182:6651-6658(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=11092855; DOI=10.1128/jb.182.24.6950-6957.2000;
RA Hara H., Masai E., Katayama Y., Fukuda M.;
RT "The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-
RT cleavage pathway, is essential to vanillate and syringate degradation in
RT Sphingomonas paucimobilis SYK-6.";
RL J. Bacteriol. 182:6950-6957(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=12486039; DOI=10.1128/jb.185.1.41-50.2003;
RA Hara H., Masai E., Miyauchi K., Katayama Y., Fukuda M.;
RT "Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and
RT operon structure of the protocatechuate 4,5-cleavage pathway genes in
RT Sphingomonas paucimobilis SYK-6.";
RL J. Bacteriol. 185:41-50(2003).
CC -!- FUNCTION: Involved in the degradation of protocatechuate (PCA) via the
CC PCA 4,5-cleavage pathway. Catalyzes the oxidation of the hemiacetal
CC form of 4-carboxy-2-hydroxymuconate-6-semialdehyde (CHMS) to produce 2-
CC pyrone-4,6-dicarboxylate (PDC). LigC has 10-times-higher affinity to
CC NADP than to NAD. {ECO:0000269|PubMed:11073908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP(+)
CC = 2-oxo-2H-pyran-4,6-dicarboxylate + H(+) + NADPH;
CC Xref=Rhea:RHEA:29587, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58304, ChEBI:CHEBI:58349, ChEBI:CHEBI:61985;
CC EC=1.1.1.312; Evidence={ECO:0000269|PubMed:11073908};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate (10 mM),
CC HgCl2 (10 mM), or 5,5-dithiobis(2-nitrobenzoate) (100 mM).
CC {ECO:0000269|PubMed:11073908}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.6 uM for NAD (with CHMS as substrate at 25 degrees Celsius and
CC pH 8) {ECO:0000269|PubMed:11073908};
CC KM=24.6 uM for CHMS (with NADP as cofactor at 25 degrees Celsius and
CC pH 8) {ECO:0000269|PubMed:11073908};
CC KM=26 uM for NADP (with CHMS as substrate at 25 degrees Celsius and
CC pH 8) {ECO:0000269|PubMed:11073908};
CC KM=252 uM for CHMS (with NAD as cofactor at 25 degrees Celsius and pH
CC 8) {ECO:0000269|PubMed:11073908};
CC Vmax=363 umol/min/mg enzyme with CHMS as substrate (with NADP as
CC cofactor at 25 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11073908};
CC Vmax=449 umol/min/mg enzyme with CHMS as substrate (with NAD as
CC cofactor at 25 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:11073908};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11073908};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:11073908};
CC -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11073908}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene prevents growth with
CC vanillate. Only PCA is accumulated during the incubation of vanillate
CC with the whole cells of the ligC insertion mutant. A repression of PCA
CC 4,5-dioxygenase (LigAB) activity is also observed.
CC {ECO:0000269|PubMed:11073908}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA 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; AB035122; BAA97119.1; -; Genomic_DNA.
DR EMBL; AB073227; BAB88744.1; -; Genomic_DNA.
DR RefSeq; WP_014075575.1; NC_015976.1.
DR AlphaFoldDB; Q9KWL3; -.
DR SMR; Q9KWL3; -.
DR STRING; 627192.SLG_12490; -.
DR KEGG; ag:BAA97119; -.
DR BioCyc; MetaCyc:MON-3466; -.
DR UniPathway; UPA00892; -.
DR GO; GO:0050606; F:4-carboxy-2-hydroxymuconate semialdehyde hemiacetal dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IDA:UniProtKB.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR045560; LigC_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF19858; OxRdtase_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; NADP; Oxidoreductase.
FT CHAIN 1..315
FT /note="4-carboxy-2-hydroxymuconate-6-semialdehyde
FT dehydrogenase"
FT /id="PRO_0000418616"
SQ SEQUENCE 315 AA; 34629 MW; 58077E4EE667DCE1 CRC64;
MRIALAGAGA FGEKHLDGLK NIDGVEIVSI ISRKAEQAAE VAAKYGAKHS GTDLSEALAR
DDVDAVILCT PTQMHAEQAI ACMNAGKHVQ VEIPLADSWA DAEAVMKKSQ ETGLVCMVGH
TRRFNPSHQY IHNKIVAGEL AIQQMDVQTY FFRRKNMNAK GEPRSWTDHL LWHHAAHTVD
LFAYQAGKIV QANAVQGPIH PELGIAMDMS IQLKSETGAI CTLSLSFNND GPLGTFFRYI
CDNGTWIARY DDLVTGKEEP VDVSKVDVSM NGIELQDREF IAAIREGREP NSSVARVLDC
YRVLGELEVQ LEKQG
