ID F6AJU8_PSEF1 Unreviewed; 290 AA.
AC F6AJU8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Oxaloacetate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01299};
DE EC=4.1.1.112 {ECO:0000256|HAMAP-Rule:MF_01299};
GN OrderedLocusNames=Psefu_4085 {ECO:0000313|EMBL:AEF24040.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF24040.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF24040.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate.
CC Seems to play a role in maintaining cellular concentrations of
CC bicarbonate and pyruvate. {ECO:0000256|HAMAP-Rule:MF_01299}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01299};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01299};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01299};
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase family. Oxaloacetate
CC decarboxylase subfamily. {ECO:0000256|HAMAP-Rule:MF_01299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Oxaloacetate decarboxylase family. {ECO:0000256|ARBA:ARBA00005838}.
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DR EMBL; CP002727; AEF24040.1; -; Genomic_DNA.
DR AlphaFoldDB; F6AJU8; -.
DR STRING; 743720.Psefu_4085; -.
DR KEGG; pfv:Psefu_4085; -.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_3_2_6; -.
DR Proteomes; UP000000686; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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 PANTHER; PTHR42905:SF3; OXALOACETATE DECARBOXYLASE; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01299};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01299};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01299};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01299}; Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299"
SQ SEQUENCE 290 AA; 31560 MW; 1407C9AA0C308011 CRC64;
MTNMQRASHH ELRRAFRALL ASGSCYHTAS VFDPMSARIA GDLGFEVGIL GGSVASLQVL
AAPDFALITL SEFVEQATRI HRVSRLPVIA DADHGYGNAL NVMRTVVELE RAGISALTIE
DTLLPAQFNR KSTDLISVAE GVGKVRAALE ARVDPDLAII ARTNAGVLSV DEVIKRTVAY
QKAGADAICM VGVEDFEHLE KIAEHLSVPL MLVTYGNPKL RDNERLAKLG VRIVVNGHAA
YFAAIKATYD CLREQRNAVA SDLSASELAH KYTQPEDYVA WADEFMNVKE
//
