ID   OIAX_RHIR8              Reviewed;         419 AA.
AC   B9JK73;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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   Rhizobium rhizogenes (strain K84 / ATCC BAA-868) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
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   AlphaFoldDB; B9JK73; -.
DR   SMR; B9JK73; -.
DR   STRING; 311403.Arad_9230; -.
DR   KEGG; ara:Arad_9230; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_0_5; -.
DR   BioCyc; MetaCyc:MONOMER-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   CDD; cd08207; RLP_NonPhot; 1.
DR   Gene3D; 3.20.20.110; Ribulose bisphosphate carboxylase, large subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.150; RuBisCO large subunit, N-terminal domain; 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; RIBULOSE BISPHOSPHATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42704:SF9; RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN; 1.
DR   Pfam; PF00016; RuBisCO_large; 1.
DR   Pfam; PF02788; RuBisCO_large_N; 1.
DR   SFLD; SFLDS00014; RuBisCO; 1.
DR   SFLD; SFLDG00301; RuBisCO-like_proteins; 1.
DR   SUPFAM; SSF51649; RuBisCo, C-terminal domain; 1.
DR   SUPFAM; SSF54966; RuBisCO, large subunit, small (N-terminal) domain; 1.
DR   PROSITE; PS00157; RUBISCO_LARGE; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding.
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
//