ID   FRBC_STRR3              Reviewed;         373 AA.
AC   Q0ZQ46;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=2-phosphonomethylmalate synthase {ECO:0000303|PubMed:18721747};
DE            EC=2.3.3.19 {ECO:0000269|PubMed:18721747};
GN   Name=frbC {ECO:0000303|PubMed:18721747};
GN   ORFNames=VM95_23205 {ECO:0000312|EMBL:KJS60087.1};
OS   Streptomyces rubellomurinus (strain ATCC 31215).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=359131;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ATCC 31215 {ECO:0000312|EMBL:ABB90392.1};
RX   PubMed=18721747; DOI=10.1016/j.chembiol.2008.07.010;
RA   Eliot A.C., Griffin B.M., Thomas P.M., Johannes T.W., Kelleher N.L.,
RA   Zhao H., Metcalf W.W.;
RT   "Cloning, expression, and biochemical characterization of Streptomyces
RT   rubellomurinus genes required for biosynthesis of antimalarial compound
RT   FR900098.";
RL   Chem. Biol. 15:765-770(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31215 {ECO:0000312|EMBL:KJS60087.1,
RC   ECO:0000312|Proteomes:UP000033699};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the phosphonic acid
CC       antibiotic FR900098, a potential anti-malarial drug, which acts as a
CC       potent inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase
CC       (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid
CC       biosynthesis. Catalyzes the condensation between acetyl-CoA and
CC       phosphonopyruvate to yield (R)-2-(phosphonomethyl)malate.
CC       {ECO:0000269|PubMed:18721747}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphonopyruvate + acetyl-CoA + H2O = (R)-2-
CC         (phosphonomethyl)malate + CoA + H(+); Xref=Rhea:RHEA:52144,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:71402, ChEBI:CHEBI:136541;
CC         EC=2.3.3.19; Evidence={ECO:0000269|PubMed:18721747};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:18721747}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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; DQ267750; ABB90392.1; -; Genomic_DNA.
DR   EMBL; JZKH01000051; KJS60087.1; -; Genomic_DNA.
DR   RefSeq; WP_045699990.1; NZ_JZKH01000051.1.
DR   AlphaFoldDB; Q0ZQ46; -.
DR   SMR; Q0ZQ46; -.
DR   EnsemblBacteria; KJS60087; KJS60087; VM95_23205.
DR   KEGG; ag:ABB90392; -.
DR   PATRIC; fig|359131.3.peg.5648; -.
DR   OMA; SNMFAHE; -.
DR   BioCyc; MetaCyc:MON-18399; -.
DR   BRENDA; 2.3.3.19; 15041.
DR   Proteomes; UP000033699; Unassembled WGS sequence.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07939; DRE_TIM_NifV; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013477; NifV/FrbC.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..373
FT                   /note="2-phosphonomethylmalate synthase"
FT                   /id="PRO_0000443947"
FT   DOMAIN          5..256
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   373 AA;  40381 MW;  C273D081908C1BFB CRC64;
     MRNDLVLEDT TLRDGEQTPG VAFSKETKTA ILNALIEAGV TSIEIGIPAM GGEELDFIKS
     VVDRQDEARL VVWHRGVRED VERSLDLGFT SVHVGLPTSA GHLKASVRKD RTWLLATARD
     MVKMAKDRGA FVSISAEDIA RTEISFLQEY AGVVAEAGAD RLRLSDTVGL LGPEAYGERV
     AAVLSAADID VQCHAHNDFG LATANTLAGL KAGARYFHVT VNAIGERAGM ADLAQVVVAL
     KKLYDRDLGI DLTKLKKVSR LVAEAAGHQV LPWQPITGDN VFAHESGIHA NGMFRDTSSF
     EPFPPEHVGG ERRYVLGKHS GRALVAWALE QEGITPREEL LPHCLEEVRA LSIRIGGAVS
     HEQLVEIYNK AAA