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OIAX_RHIEC
ID   OIAX_RHIEC              Reviewed;         417 AA.
AC   Q2JZQ0;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=RHE_PF00042 {ECO:0000312|EMBL:ABC93936.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42f.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=CFN 42 / ATCC 51251;
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; CP000138; ABC93936.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2JZQ0; -.
DR   SMR; Q2JZQ0; -.
DR   EnsemblBacteria; ABC93936; ABC93936; RHE_PF00042.
DR   KEGG; ret:RHE_PF00042; -.
DR   HOGENOM; CLU_031450_3_0_5; -.
DR   OMA; IHGHPDG; -.
DR   Proteomes; UP000001936; Plasmid p42f.
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   Plasmid; Reference proteome.
FT   CHAIN           1..417
FT                   /note="3-oxo-isoapionate-4-phosphate decarboxylase"
FT                   /id="PRO_0000450939"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
FT   MOD_RES         177
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
SQ   SEQUENCE   417 AA;  44833 MW;  508F61FEB05F85DF CRC64;
     MITLTYRIET PGSVETMADK IASDQSTGTF VPVPGETEEL KSRVAARVLA IRPLENARHP
     TWPESAPDTL LHRADVDIAF PLEAIGTDLS ALMTIAIGGV YSIKGMTGIR IVDMKLPEAF
     RSAHPGPQFG IAGSRRLTGV EGRPIIGTIV KPALGLRPHE TAELVGELIG SGVDFIKDDE
     KLMSPAYSPL KERVAAIMPR ILDHEQKTGK KVMYAFGISH ADPDEMMRNH DIVAAAGGNC
     AVVNINSIGF GGMSFLRKRS SLVLHAHRNG WDVLTRDPGA GMDFKVYQQF WRLLGVDQFQ
     INGIRIKYWE PDESFVSSFK AVSTPLFDAA DCPLPVAGSG QWGGQAPETY ERTGRTIDLL
     YLCGGGIVSH PGGPAAGVRA VQQAWQAAVA GIPLEVYAKD HPELAASIAK FSDGKGA
 
 
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