ID   OIAT_XANP2              Reviewed;         414 AA.
AC   A7IJG7;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=3-oxo-isoapionate-4-phosphate transcarboxylase/hydrolase {ECO:0000303|PubMed:29867142};
DE            EC=3.7.1.- {ECO:0000269|PubMed:29867142};
GN   Name=oiaT {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=Xaut_2924 {ECO:0000312|EMBL:ABS68160.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 conversion
CC       of 3-oxo-isoapionate 4-phosphate to 3-phosphoglycerate and glycolate.
CC       {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoisoapionate 4-phosphate + H2O = (2R)-3-phosphoglycerate +
CC         glycolate + H(+); Xref=Rhea:RHEA:57076, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58272,
CC         ChEBI:CHEBI:141357; 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; CP000781; ABS68160.1; -; Genomic_DNA.
DR   RefSeq; WP_012114910.1; NC_009720.1.
DR   AlphaFoldDB; A7IJG7; -.
DR   SMR; A7IJG7; -.
DR   STRING; 78245.Xaut_2924; -.
DR   EnsemblBacteria; ABS68160; ABS68160; Xaut_2924.
DR   KEGG; xau:Xaut_2924; -.
DR   eggNOG; COG1850; Bacteria.
DR   HOGENOM; CLU_031450_3_0_5; -.
DR   OMA; ATYWMET; -.
DR   OrthoDB; 848380at2; -.
DR   PhylomeDB; A7IJG7; -.
DR   BioCyc; MetaCyc:MON-20969; -.
DR   BRENDA; 3.7.1.28; 1641.
DR   Proteomes; UP000002417; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..414
FT                   /note="3-oxo-isoapionate-4-phosphate
FT                   transcarboxylase/hydrolase"
FT                   /id="PRO_0000446042"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
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   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
FT   MOD_RES         180
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:O93627"
SQ   SEQUENCE   414 AA;  44329 MW;  FB254C926BBD27C2 CRC64;
     MSERVYATYW METGGDPART AEVIAGEQSS GTFVALATET AELKERSGAR VERLDILDTA
     DIPSLPGGMA SDRYTRAILE LSWPVENFGP SLPNLMSTIA GNLFELHQVS GLRLIDLKLP
     PSFTNAFAGP AFGIAGTRKL AGVAQGPIIG TIIKPSIGLT PEETAQQVRE LIAGDIDFIK
     DDELQADGAR CPFEARVKAV MRVVNDAADR RGRKVMVAFN ITGDLDEMRR RHDLVLAEGG
     TCVMVCLNSI GLVGVREIRR HTQLPIHGHR AGWGYLYRCP SLGWDYAPWQ QLWRLAGVDH
     LHVNGLDNKF SEANASVIAA ARAVLSPLNH AAPMGAMPVF SSGQTGRQAA ETYAAIGCAD
     LIHTAGGGIF GHPAGVPAGV EALRAAWRAA MAGASLEDEA TRSPALRSAL GFWR