LIGK_SPHSK
ID LIGK_SPHSK Reviewed; 228 AA.
AC G2IQQ8; Q8RQW0;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=4-carboxy-4-hydroxy-2-oxoadipate aldolase {ECO:0000303|PubMed:12486039};
DE Short=CHA aldolase {ECO:0000303|PubMed:12486039};
DE EC=4.1.3.17 {ECO:0000269|PubMed:12486039};
DE AltName: Full=Oxaloacetate decarboxylase {ECO:0000305|PubMed:12486039};
DE Short=OAA decarboxylase;
DE EC=4.1.1.112 {ECO:0000269|PubMed:12486039};
GN Name=ligK {ECO:0000303|PubMed:12486039, ECO:0000312|EMBL:BAB88738.1,
GN ECO:0000312|EMBL:BAK65930.1};
GN ORFNames=SLG_12550 {ECO:0000312|EMBL:BAK65930.1};
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, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, DISRUPTION
RP PHENOTYPE, AND PATHWAY.
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).
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).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=29658701; DOI=10.1021/acs.biochem.8b00295;
RA Hogancamp T.N., Raushel F.M.;
RT "Functional annotation of LigU as a 1,3-allylic isomerase during the
RT degradation of lignin in the protocatechuate 4,5-cleavage pathway from the
RT soil bacterium Sphingobium sp. SYK-6.";
RL Biochemistry 57:2837-2845(2018).
CC -!- FUNCTION: Contributes to the degradation of lignin, being involved in
CC the final step of the protocatechuate 4,5-cleavage pathway. Catalyzes
CC the conversion of 4-carboxy-4-hydroxy-2-oxoadipate (CHA, also named 2-
CC hydroxy-4-oxobutane-1,2,4-tricarboxylate) to pyruvate and oxaloacetate
CC but also the decarboxylation of oxaloacetate to pyruvate and CO2. Is
CC essential for catabolism and utilization of vanillate and syringate
CC (PubMed:12486039). Is also able to catalyze the formation of 4-hydroxy-
CC 4-methyl-2-oxoglutarate (HMG) from two molecules of pyruvate
CC (PubMed:29658701). {ECO:0000269|PubMed:12486039,
CC ECO:0000269|PubMed:29658701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate;
CC Xref=Rhea:RHEA:22748, ChEBI:CHEBI:15361, ChEBI:CHEBI:58276;
CC EC=4.1.3.17; Evidence={ECO:0000269|PubMed:29658701};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate +
CC pyruvate; Xref=Rhea:RHEA:28935, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:58075; EC=4.1.3.17;
CC Evidence={ECO:0000269|PubMed:12486039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28936;
CC Evidence={ECO:0000269|PubMed:12486039};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:16526; EC=4.1.1.112;
CC Evidence={ECO:0000269|PubMed:12486039};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15642;
CC Evidence={ECO:0000269|PubMed:12486039};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12486039};
CC -!- ACTIVITY REGULATION: Both CHA aldolase and oxaloacetate decarboxylase
CC activity are activated in the presence of phosphate ion, and inhibited
CC by N-ethylmaleimide. CHA aldolase activity is also inhibited by
CC oxaloacetate with a Ki value of 23 uM; thus, the amount of oxaloacetate
CC in the cells might control the production of oxaloacetate from CHA.
CC {ECO:0000269|PubMed:12486039}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.2 uM for 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
CC {ECO:0000269|PubMed:12486039};
CC KM=136 uM for oxaloacetate {ECO:0000269|PubMed:12486039};
CC Vmax=265 umol/min/mg enzyme for CHA aldol cleavage
CC {ECO:0000269|PubMed:12486039};
CC Vmax=13.2 umol/min/mg enzyme for oxaloacetate decarboxylation
CC {ECO:0000269|PubMed:12486039};
CC pH dependence:
CC Optimum pH is 8.0 for CHA aldolase activity, and 7.0 for oxaloacetate
CC decarboxylase activity. {ECO:0000269|PubMed:12486039};
CC -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC {ECO:0000305|PubMed:12486039}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12486039}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC on both vanillate and syringate. {ECO:0000269|PubMed:12486039}.
CC -!- SIMILARITY: Belongs to the LigK/PcmE 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; AB073227; BAB88738.1; -; Genomic_DNA.
DR EMBL; AP012222; BAK65930.1; -; Genomic_DNA.
DR AlphaFoldDB; G2IQQ8; -.
DR SMR; G2IQQ8; -.
DR STRING; 627192.SLG_12550; -.
DR EnsemblBacteria; BAK65930; BAK65930; SLG_12550.
DR KEGG; ssy:SLG_12550; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_3_2_5; -.
DR UniPathway; UPA00892; -.
DR Proteomes; UP000001275; Chromosome.
DR GO; GO:0047443; F:4-hydroxy-4-methyl-2-oxoglutarate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019617; P:protocatechuate catabolic process, meta-cleavage; IDA:CACAO.
DR CDD; cd16841; RraA_family; 1.
DR InterPro; IPR014165; LigK_PcmE.
DR InterPro; IPR005493; RraA/RraA-like.
DR InterPro; IPR036704; RraA/RraA-like_sf.
DR Pfam; PF03737; RraA-like; 1.
DR SUPFAM; SSF89562; SSF89562; 1.
DR TIGRFAMs; TIGR02798; ligK_PcmE; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..228
FT /note="4-carboxy-4-hydroxy-2-oxoadipate aldolase"
FT /id="PRO_0000446302"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
SQ SEQUENCE 228 AA; 24159 MW; 0D0C283D21D521F6 CRC64;
MRGAAMGVVV QNIERAPLEV IDGLAACGVA TVHEAQGRTG LLASYMRPIY RGARVAGSAL
TISAPPGDNW MVHVAIEQLK AGDILLLAPT SPCEDGYFGD LLATSAQARG CRGLVIDAGV
RDVRDLTEMN FPVWSKAIYA QGTVKNTLGS VNVPVVCANA LVNPGDVIVA DDDGVCVVPL
ANAEKVLEAA RAREANEGDK REKMANGVLG LDLYKMRERL EKEGLKYV
