ID A0AAI8MD00_9BRAD Unreviewed; 288 AA. AC A0AAI8MD00; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 27-NOV-2024, entry version 3. DE RecName: Full=Oxaloacetate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01299}; DE EC=4.1.1.112 {ECO:0000256|HAMAP-Rule:MF_01299}; GN ORFNames=S23_30220 {ECO:0000313|EMBL:BAL76229.1}; OS Bradyrhizobium cosmicum. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=1404864 {ECO:0000313|EMBL:BAL76229.1, ECO:0000313|Proteomes:UP000007886}; RN [1] {ECO:0000313|EMBL:BAL76229.1, ECO:0000313|Proteomes:UP000007886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S23321 {ECO:0000313|EMBL:BAL76229.1, RC ECO:0000313|Proteomes:UP000007886}; RX PubMed=22452844; DOI=10.1264/jsme2.ME11321; RA Okubo T., Tsukui T., Maita H., Okamoto S., Oshima K., Fujisawa T., RA Saito A., Futamata H., Hattori R., Shimomura Y., Haruta S., Morimoto S., RA Wang Y., Sakai Y., Hattori M., Aizawa S., Nagashima K.V.P., Masuda S., RA Hattori T., Yamashita A., Bao Z., Hayatsu M., Kajiya-Kanegae H., RA Yoshinaga I., Sakamoto K., Toyota K., Nakao M., Kohara M., Anda M., RA Niwa R., Jung-Hwan P., Sameshima-Saito R., Tokuda S., Yamamoto S., RA Yamamoto S., Yokoyama T., Akutsu T., Nakamura Y., Nakahira-Yanaka Y., RA Takada Hoshino Y., Hirakawa H., Mitsui H., Terasawa K., Itakura M., RA Sato S., Ikeda-Ohtsubo W., Sakakura N., Kaminuma E., Minamisawa K.; RT "Complete genome sequence of Bradyrhizobium sp. S23321: insights into RT symbiosis evolution in soil oligotrophs."; RL Microbes Environ. 27:306-315(2012). 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=oxaloacetate + H(+) = pyruvate + CO2; 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}. 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; AP012279; BAL76229.1; -; Genomic_DNA. DR RefSeq; WP_015685531.1; NZ_CP041656.2. DR KEGG; brs:S23_30220; -. DR Proteomes; UP000007886; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:TreeGrafter. 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; IEA:TreeGrafter. 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}. FT BINDING 47 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299" FT BINDING 85 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01299" SQ SEQUENCE 288 AA; 30239 MW; D7EAC8FCBCBDC57E CRC64; MAFRSRREKL RIILSGSACV HPGSVYDAIS IRIAEDLGFP LGMFGGSVAS LAVLGDPDIT LITLTELAEQ MRRMSRAASL PVLVDADHGY GNALNVRRTV QELETAGAAG LTIEDTLLPA GFGEAKAQLI SLEEGVGKMK AALDGRGDPS LVIMGRTGAA SITSVEDAIR RAKAYEAVGV DALFFTGIKS RAELEAVAAA THLPIVLGGA PEDMNALDYL AGQRVRIALQ GHAPIAAAMQ AVYETQKALR EGTPPKALKG LPSAELTNRV TREADVKARS ADVLGLKK //