GALB_PSEPK
ID GALB_PSEPK Reviewed; 258 AA.
AC Q88JX8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=4-oxalmesaconate hydratase;
DE Short=OMA hydratase;
DE EC=4.2.1.83;
DE AltName: Full=Gallate degradation protein B;
GN Name=galB; OrderedLocusNames=PP_2515;
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, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 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 oxalomesaconic acid enol
CC (OMAenol) to 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). Mediates the
CC third step of gallate degradation pathway.
CC {ECO:0000269|PubMed:21219457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = 4-carboxy-2-
CC hydroxy-cis,cis-muconate + H2O; Xref=Rhea:RHEA:17401,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58075, ChEBI:CHEBI:58142; EC=4.2.1.83;
CC Evidence={ECO:0000269|PubMed:21219457};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=85 uM for (1E,3E)-4-hydroxybuta-1,3-diene-1,2,4-tricarboxylate
CC {ECO:0000269|PubMed:21219457};
CC Vmax=76 umol/min/mg enzyme {ECO:0000269|PubMed:21219457};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21219457};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:21219457};
CC -!- DISRUPTION PHENOTYPE: Lacks 4-oxalmesaconate hydratase activity.
CC {ECO:0000269|PubMed:21219457}.
CC -!- SIMILARITY: Belongs to the MshB deacetylase family. {ECO:0000305}.
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DR EMBL; AE015451; AAN68127.1; -; Genomic_DNA.
DR RefSeq; NP_744663.1; NC_002947.4.
DR RefSeq; WP_010953449.1; NC_002947.4.
DR PDB; 5CGZ; X-ray; 2.10 A; A/B=20-258.
DR PDBsum; 5CGZ; -.
DR AlphaFoldDB; Q88JX8; -.
DR SMR; Q88JX8; -.
DR STRING; 160488.PP_2515; -.
DR EnsemblBacteria; AAN68127; AAN68127; PP_2515.
DR KEGG; ppu:PP_2515; -.
DR PATRIC; fig|160488.4.peg.2670; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_1_0_6; -.
DR OMA; DPFNPDH; -.
DR PhylomeDB; Q88JX8; -.
DR BioCyc; MetaCyc:G1G01-2699-MON; -.
DR BioCyc; PPUT160488:G1G01-2699-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0047584; F:4-oxalmesaconate hydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019396; P:gallate catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993; PTHR12993; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..258
FT /note="4-oxalmesaconate hydratase"
FT /id="PRO_0000418497"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5CGZ"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 74..92
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5CGZ"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:5CGZ"
FT HELIX 211..230
FT /evidence="ECO:0007829|PDB:5CGZ"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:5CGZ"
SQ SEQUENCE 258 AA; 29071 MW; 40D2E5E9190C4A24 CRC64;
MTSCAHPHCR SQRNMNTPQK SALVVSAHSA DFVWRAGGAI ALHAEQGYAM HVVCLSFGER
GESAKLWRKG EMTEAKVKDA RREEAMAAAE ILGASVEFFD IGDYPMRADK DTLFRLADVY
RRVQPEFVLS HSLKDPYNYD HPLAMHLAQE ARIIAQAEGY KPGEKIVGAP PVYAFEPHQP
EQCEWRPDTF LDITSVWDKK YAAIQCMAGQ EHLWEYYTRV ALQRGVQAKR NVGITSARNI
VYAEGLQSVF PRVTENLA
