OIAX_AGRRK
ID OIAX_AGRRK Reviewed; 419 AA.
AC B9JK73;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=3-oxo-isoapionate-4-phosphate decarboxylase {ECO:0000303|PubMed:29867142};
DE EC=4.1.1.121 {ECO:0000269|PubMed:29867142};
GN Name=oiaX {ECO:0000303|PubMed:29867142};
GN OrderedLocusNames=Arad_9230 {ECO:0000312|EMBL:ACM30315.1};
OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=311403;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K84 / ATCC BAA-868;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA Andersen H.M., Almo S.C., Gerlt J.A.;
RT "Functional assignment of multiple catabolic pathways for D-apiose.";
RL Nat. Chem. Biol. 14:696-705(2018).
CC -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the
CC decarboxylation of 3-oxo-isoapionate 4-phosphate to L-erythrulose 1-
CC phosphate. {ECO:0000269|PubMed:29867142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxoisoapionate 4-phosphate + H(+) = CO2 + L-erythrulose 1-
CC phosphate; Xref=Rhea:RHEA:57072, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58002, ChEBI:CHEBI:141357;
CC EC=4.1.1.121; Evidence={ECO:0000269|PubMed:29867142};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O93627};
CC -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. {ECO:0000305}.
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DR EMBL; CP000629; ACM30315.1; -; Genomic_DNA.
DR RefSeq; WP_015917643.1; NC_011983.1.
DR AlphaFoldDB; B9JK73; -.
DR SMR; B9JK73; -.
DR STRING; 311403.Arad_9230; -.
DR EnsemblBacteria; ACM30315; ACM30315; Arad_9230.
DR KEGG; ara:Arad_9230; -.
DR eggNOG; COG1850; Bacteria.
DR HOGENOM; CLU_031450_3_0_5; -.
DR OMA; IHGHPDG; -.
DR OrthoDB; 848380at2; -.
DR BioCyc; MetaCyc:MON-20966; -.
DR BRENDA; 4.1.1.121; 200.
DR Proteomes; UP000001600; Chromosome 2.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..419
FT /note="3-oxo-isoapionate-4-phosphate decarboxylase"
FT /id="PRO_0000446043"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:O93627"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O93627"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O93627"
FT MOD_RES 179
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:O93627"
SQ SEQUENCE 419 AA; 45085 MW; CD2DF34EFD8EF5C4 CRC64;
MSITITYRIE TPGSIEAMAD KIASDQSTGT FVPVPGETEE LKSRVAARVL GIRQLEDAKR
PTWPEVAEGH GPLRRADVDI AFPLDAIGTD LSALMTIAIG GVFSIKGMTG IRIVDMKLPN
AFRGAHPGPQ FGVAGSKRLT GVEGRPIIGT IVKPALGLRP VETAELVGEL INSGVDFIKD
DEKLMSPAYS PLKERVAAIM PRILDHEQKT GKKVMYAFGI SHADPDEMMR NHDLVLEAGG
NCAVVNINSI GFGGMSFLRK RSGLVLHAHR NGWDVLTRDP GAGMDFKVYQ QFWRLLGVDQ
FQINGIRVKY WEPDESFIES FKAVSTPLFD PSDCPLPVAG SGQWGGQAPE TYQRTGRTTD
LLYLCGGGIV SHPSGPAAGV RAVQQAWEAA VADIPLANYA KDHPELAASI AKFSDGKGA
