GALC_PSEPK
ID GALC_PSEPK Reviewed; 238 AA.
AC Q88JX9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=4-carboxy-4-hydroxy-2-oxoadipic acid aldolase;
DE AltName: Full=CHA aldolase;
DE EC=4.1.3.17 {ECO:0000269|PubMed:21219457};
DE AltName: Full=Gallate degradation protein C;
GN Name=galC; OrderedLocusNames=PP_2514;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=21219457; DOI=10.1111/j.1365-2958.2010.07448.x;
RA Nogales J., Canales A., Jimenez-Barbero J., Serra B., Pingarron J.M.,
RA Garcia J.L., Diaz E.;
RT "Unravelling the gallic acid degradation pathway in bacteria: the gal
RT cluster from Pseudomonas putida.";
RL Mol. Microbiol. 79:359-374(2011).
CC -!- FUNCTION: Catalyzes the conversion of 4-carboxy-4-hydroxy-2-oxoadipic
CC acid (CHA) to pyruvate and oxaloacetate, the last step of gallate
CC degradation pathway. {ECO:0000269|PubMed:21219457}.
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:21219457};
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:21219457};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:21219457};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to grow in gallate.
CC {ECO:0000269|PubMed:21219457}.
CC -!- SIMILARITY: Belongs to the LigK/PcmE family. {ECO:0000305}.
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DR EMBL; AE015451; AAN68126.1; -; Genomic_DNA.
DR RefSeq; NP_744662.1; NC_002947.4.
DR RefSeq; WP_010953448.1; NC_002947.4.
DR AlphaFoldDB; Q88JX9; -.
DR SMR; Q88JX9; -.
DR STRING; 160488.PP_2514; -.
DR EnsemblBacteria; AAN68126; AAN68126; PP_2514.
DR KEGG; ppu:PP_2514; -.
DR PATRIC; fig|160488.4.peg.2669; -.
DR eggNOG; COG0684; Bacteria.
DR HOGENOM; CLU_072626_3_2_6; -.
DR OMA; VNVPVVC; -.
DR PhylomeDB; Q88JX9; -.
DR BioCyc; MetaCyc:MON-3481; -.
DR BioCyc; PPUT160488:G1G01-2698-MON; -.
DR Proteomes; UP000000556; 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:0016833; F:oxo-acid-lyase activity; IDA:UniProtKB.
DR GO; GO:0019396; P:gallate catabolic process; IDA:UniProtKB.
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..238
FT /note="4-carboxy-4-hydroxy-2-oxoadipic acid aldolase"
FT /id="PRO_0000418487"
FT BINDING 101..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:A5W059"
SQ SEQUENCE 238 AA; 25110 MW; 05A95BA277B42372 CRC64;
MSGLIGKTGI VVRNIPRVEP HMIDALGRLG VATVHEAQGR KGLLNTAVRP IQQGVAVAGS
AVTVLVAPGD NWMFHVAVEQ CRPGDVLVVA PSSPCSDGYF GDLLATSLQA RGVLGLVIDA
GVRDSQTLRD MGFAVWSRAI NAQGTVKEVL GSVNLPLLCA GQLVNAGDIV VADDDGVVVV
RHGEAQAVLE AATQRADLEE RKRLRLAAGE LGLDIYEMRP RLAAKGLRYV DHLTDLEG
