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4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (CHMS dehydrogenase) (EC 1.1.1.312) (2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase)

 LIGC_SPHPI              Reviewed;         315 AA.
Q9KWL3;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 58.
RecName: Full=4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase;
Short=CHMS dehydrogenase;
EC=1.1.1.312;
AltName: Full=2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase;
Name=ligC;
Sphingomonas paucimobilis (Pseudomonas paucimobilis).
Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
Sphingomonadaceae; Sphingomonas.
NCBI_TaxID=13689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SYK-6;
PubMed=2185230; DOI=10.1128/jb.172.5.2704-2709.1990;
Noda Y., Nishikawa S., Shiozuka K., Kadokura H., Nakajima H., Yoda K.,
Katayama Y., Morohoshi N., Haraguchi T., Yamasaki M.;
"Molecular cloning of the protocatechuate 4,5-dioxygenase genes of
Pseudomonas paucimobilis.";
J. Bacteriol. 172:2704-2709(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SYK-6;
PubMed=9864312;
Masai E., Shinohara S., Hara H., Nishikawa S., Katayama Y., Fukuda M.;
"Genetic and biochemical characterization of a 2-pyrone-4, 6-
dicarboxylic acid hydrolase involved in the protocatechuate 4, 5-
cleavage pathway of Sphingomonas paucimobilis SYK-6.";
J. Bacteriol. 181:55-62(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION
AS A CHMS DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, DISRUPTION PHENOTYPE, ENZYME REGULATION, SUBUNIT, AND
NOMENCLATURE.
STRAIN=SYK-6;
PubMed=11073908; DOI=10.1128/JB.182.23.6651-6658.2000;
Masai E., Momose K., Hara H., Nishikawa S., Katayama Y., Fukuda M.;
"Genetic and biochemical characterization of 4-carboxy-2-
hydroxymuconate-6-semialdehyde dehydrogenase and its role in the
protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-
6.";
J. Bacteriol. 182:6651-6658(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11092855; DOI=10.1128/JB.182.24.6950-6957.2000;
Hara H., Masai E., Katayama Y., Fukuda M.;
"The 4-oxalomesaconate hydratase gene, involved in the protocatechuate
4,5-cleavage pathway, is essential to vanillate and syringate
degradation in Sphingomonas paucimobilis SYK-6.";
J. Bacteriol. 182:6950-6957(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12486039; DOI=10.1128/JB.185.1.41-50.2003;
Hara H., Masai E., Miyauchi K., Katayama Y., Fukuda M.;
"Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase
gene and operon structure of the protocatechuate 4,5-cleavage pathway
genes in Sphingomonas paucimobilis SYK-6.";
J. Bacteriol. 185:41-50(2003).
-!- FUNCTION: Involved in the degradation of protocatechuate (PCA) via
the PCA 4,5-cleavage pathway. Catalyzes the oxidation of the
hemiacetal form of 4-carboxy-2-hydroxymuconate-6-semialdehyde
(CHMS) to produce 2-pyrone-4,6-dicarboxylate (PDC). LigC has 10-
times-higher affinity to NADP than to NAD.
{ECO:0000269|PubMed:11073908}.
-!- CATALYTIC ACTIVITY: 4-carboxy-2-hydroxymuconate semialdehyde
hemiacetal + NADP(+) = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH.
{ECO:0000269|PubMed:11073908}.
-!- ENZYME REGULATION: Inhibited by p-chloromercuribenzoate (10 mM),
HgCl2 (10 mM), or 5,5-dithiobis(2-nitrobenzoate) (100 mM).
{ECO:0000269|PubMed:11073908}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20.6 uM for NAD (with CHMS as substrate at 25 degrees Celsius
and pH 8) {ECO:0000269|PubMed:11073908};
KM=24.6 uM for CHMS (with NADP as cofactor at 25 degrees Celsius
and pH 8) {ECO:0000269|PubMed:11073908};
KM=26 uM for NADP (with CHMS as substrate at 25 degrees Celsius
and pH 8) {ECO:0000269|PubMed:11073908};
KM=252 uM for CHMS (with NAD as cofactor at 25 degrees Celsius
and pH 8) {ECO:0000269|PubMed:11073908};
Vmax=363 umol/min/mg enzyme with CHMS as substrate (with NADP as
cofactor at 25 degrees Celsius and pH 8)
{ECO:0000269|PubMed:11073908};
Vmax=449 umol/min/mg enzyme with CHMS as substrate (with NAD as
cofactor at 25 degrees Celsius and pH 8)
{ECO:0000269|PubMed:11073908};
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:11073908};
Temperature dependence:
Optimum temperature is 25 degrees Celsius.
{ECO:0000269|PubMed:11073908};
-!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11073908}.
-!- DISRUPTION PHENOTYPE: Disruption of this gene prevents growth with
vanillate. Only PCA is accumulated during the incubation of
vanillate with the whole cells of the ligC insertion mutant. A
repression of PCA 4,5-dioxygenase (LigAB) activity is also
observed. {ECO:0000269|PubMed:11073908}.
-!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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EMBL; AB035122; BAA97119.1; -; Genomic_DNA.
EMBL; AB073227; BAB88744.1; -; Genomic_DNA.
ProteinModelPortal; Q9KWL3; -.
SMR; Q9KWL3; -.
KEGG; ag:BAA97119; -.
KO; K10219; -.
BioCyc; MetaCyc:MONOMER-3466; -.
UniPathway; UPA00892; -.
GO; GO:0050606; F:4-carboxy-2-hydroxymuconate semialdehyde hemiacetal dehydrogenase activity; IDA:UniProtKB.
GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IDA:UniProtKB.
GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000683; Oxidoreductase_N.
Pfam; PF01408; GFO_IDH_MocA; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Direct protein sequencing; NAD; NADP; Oxidoreductase.
CHAIN 1 315 4-carboxy-2-hydroxymuconate-6-
semialdehyde dehydrogenase.
/FTId=PRO_0000418616.
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


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