OADC_PSEAE
ID OADC_PSEAE Reviewed; 287 AA.
AC Q9HUU1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Oxaloacetate decarboxylase;
DE EC=4.1.1.112;
GN OrderedLocusNames=PA4872;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH OXALATE AND
RP MAGNESIUM, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-212 AND HIS-235.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18081320; DOI=10.1021/bi701954p;
RA Narayanan B.C., Niu W., Han Y., Zou J., Mariano P.S., Dunaway-Mariano D.,
RA Herzberg O.;
RT "Structure and function of PA4872 from Pseudomonas aeruginosa, a novel
RT class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase
RT superfamily.";
RL Biochemistry 47:167-182(2008).
CC -!- FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate
CC with high efficiency. Is also able to decarboxylate 3-
CC methyloxaloacetate. Seems to play a role in maintaining cellular
CC concentrations of bicarbonate and pyruvate.
CC {ECO:0000269|PubMed:18081320}.
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:18081320};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18081320};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:18081320};
CC -!- ACTIVITY REGULATION: Not inhibited by 3,3-difluoroxaloacetate.
CC {ECO:0000269|PubMed:18081320}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for oxaloacetate {ECO:0000269|PubMed:18081320};
CC KM=0.63 mM for 3-methyloxaloacetate {ECO:0000269|PubMed:18081320};
CC Note=The turnover number for the oxaloacetate decarboxylation is
CC equal to 7500 per second.;
CC pH dependence:
CC There is nearly no change in activity from pH 5 to 10.
CC {ECO:0000269|PubMed:18081320};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:18081320}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Oxaloacetate decarboxylase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08257.1; -; Genomic_DNA.
DR PIR; D83038; D83038.
DR RefSeq; NP_253559.1; NC_002516.2.
DR RefSeq; WP_003121125.1; NZ_QZGE01000002.1.
DR PDB; 3B8I; X-ray; 1.90 A; A/B/C/D/E/F=1-287.
DR PDBsum; 3B8I; -.
DR AlphaFoldDB; Q9HUU1; -.
DR SMR; Q9HUU1; -.
DR STRING; 287.DR97_2223; -.
DR BindingDB; Q9HUU1; -.
DR PaxDb; Q9HUU1; -.
DR PRIDE; Q9HUU1; -.
DR EnsemblBacteria; AAG08257; AAG08257; PA4872.
DR GeneID; 878100; -.
DR KEGG; pae:PA4872; -.
DR PATRIC; fig|208964.12.peg.5105; -.
DR PseudoCAP; PA4872; -.
DR HOGENOM; CLU_027389_3_2_6; -.
DR InParanoid; Q9HUU1; -.
DR OMA; IAHACSY; -.
DR PhylomeDB; Q9HUU1; -.
DR BioCyc; PAER208964:G1FZ6-4986-MON; -.
DR BRENDA; 4.1.1.112; 5087.
DR EvolutionaryTrace; Q9HUU1; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR HAMAP; MF_01299; OadC; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR023687; Oxaloacetate_deCOase_bac.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..287
FT /note="Oxaloacetate decarboxylase"
FT /id="PRO_0000364058"
FT BINDING 50
FT /ligand="substrate"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18081320"
FT BINDING 159
FT /ligand="substrate"
FT BINDING 235
FT /ligand="substrate"
FT MUTAGEN 212
FT /note="Y->F: 25-fold increase in substrate affinity and 23-
FT fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:18081320"
FT MUTAGEN 235
FT /note="H->A: 2-fold increase in substrate affinity and 15-
FT fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:18081320"
FT MUTAGEN 235
FT /note="H->Q: No change in substrate affinity and 3-fold
FT decrease in activity."
FT /evidence="ECO:0000269|PubMed:18081320"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3B8I"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:3B8I"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3B8I"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 236..253
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:3B8I"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:3B8I"
SQ SEQUENCE 287 AA; 31321 MW; 807D13799A49CE0B CRC64;
MHRASHHELR AMFRALLDSS RCYHTASVFD PMSARIAADL GFECGILGGS VASLQVLAAP
DFALITLSEF VEQATRIGRV ARLPVIADAD HGYGNALNVM RTVVELERAG IAALTIEDTL
LPAQFGRKST DLICVEEGVG KIRAALEARV DPALTIIART NAELIDVDAV IQRTLAYQEA
GADGICLVGV RDFAHLEAIA EHLHIPLMLV TYGNPQLRDD ARLARLGVRV VVNGHAAYFA
AIKATYDCLR EERGAVASDL TASELSKKYT FPEEYQAWAR DYMEVKE
