PMMS_STRHY
ID PMMS_STRHY Reviewed; 440 AA.
AC Q9LCB4; A0A0M3N086;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=2-phosphinomethylmalate synthase {ECO:0000303|PubMed:3781934};
DE Short=PMS {ECO:0000303|PubMed:3781934};
DE EC=2.3.3.18 {ECO:0000269|PubMed:3170341, ECO:0000269|PubMed:3781934};
DE AltName: Full=PMM synthase {ECO:0000303|PubMed:3170341};
GN Name=Pmms {ECO:0000303|PubMed:3170341};
OS Streptomyces hygroscopicus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1912;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293 {ECO:0000312|EMBL:BAA90528.1};
RX PubMed=1368511; DOI=10.1271/bbb1961.54.463;
RA Shimotohno K.W., Imai S., Murakami T., Seto H.;
RT "Purification and characterization of citrate synthase from Streptomyces
RT hygroscopicus SF-1293 and comparison of its properties with those of 2-
RT phosphinomethylmalic acid synthase.";
RL Agric. Biol. Chem. 54:463-470(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293 {ECO:0000312|EMBL:BAA90528.1};
RA Hidaka T., Shimotohno K.W., Morishita T., Seto H.;
RT "Nucleotide sequence of 2-phosphinomethylmalic acid synthase of bialaphos
RT producing Streptomyces hygroscopicus.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293 {ECO:0000312|EMBL:AKN91125.1};
RX PubMed=26328935; DOI=10.1038/ja.2015.77;
RA Blodgett J.A., Zhang J.K., Yu X., Metcalf W.W.;
RT "Conserved biosynthetic pathways for phosalacine, bialaphos and newly
RT discovered phosphonic acid natural products.";
RL J. Antibiot. 69:15-25(2016).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3781934; DOI=10.7164/antibiotics.39.1356;
RA Shimotohno K., Seto H., Otake N., Imai S., Satoh A.;
RT "Studies on the biosynthesis of bialaphos (SE-1293). 7. The absolute
RT configuration of 2-phosphinomethylmalic acid, a biosynthetic intermediate
RT of bialaphos.";
RL J. Antibiot. 39:1356-1359(1986).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX PubMed=3170341; DOI=10.7164/antibiotics.41.1057;
RA Shimotohno K.W., Seto H., Otake N., Imai S., Murakami T.;
RT "Studies on the biosynthesis of bialaphos (SF-1293). 8. Purification and
RT characterization of 2-phosphinomethylmalic acid synthase from Streptomyces
RT hygroscopicus SF-1293.";
RL J. Antibiot. 41:1057-1065(1988).
CC -!- FUNCTION: Involved in the biosynthesis of the herbicide bialaphos (BA).
CC Catalyzes the condensation berween phosphinopyruvic acid (PPA), an
CC analog of oxalacetic acid, and acetyl-CoA to form R-2-
CC phosphinomethylmalic acid (PMM) (PubMed:3781934, PubMed:3170341). Can
CC also act on oxaloacetate, but shows no activity when acetyl-CoA is
CC substituted by propionyl-CoA or butyryl-CoA (PubMed:3170341).
CC {ECO:0000269|PubMed:3170341, ECO:0000269|PubMed:3781934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(hydrohydroxyphosphoryl)pyruvate + acetyl-CoA + H2O = CoA +
CC H(+) + phosphinomethylmalate; Xref=Rhea:RHEA:26068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58348, ChEBI:CHEBI:91181; EC=2.3.3.18;
CC Evidence={ECO:0000269|PubMed:3170341, ECO:0000269|PubMed:3781934};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3170341};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:3170341};
CC Note=Can also use magnesium, calcium and iron ions with lower
CC efficiency. {ECO:0000269|PubMed:3170341};
CC -!- ACTIVITY REGULATION: Strongly inhibited by p-chloromercuribenzoate
CC (pCMB), iodoacetamide (IA) and EDTA. {ECO:0000269|PubMed:3170341}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for acetyl-CoA {ECO:0000269|PubMed:3170341};
CC KM=130 uM for oxaloacetate {ECO:0000269|PubMed:3170341};
CC KM=390 uM for phosphinopyruvic acid (PPA)
CC {ECO:0000269|PubMed:3170341};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:3170341};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:3170341};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3170341}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000305}.
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DR EMBL; AB029822; BAA90528.1; -; Genomic_DNA.
DR EMBL; KP026916; AKN91125.1; -; Genomic_DNA.
DR PIR; PS0106; PS0106.
DR AlphaFoldDB; Q9LCB4; -.
DR SMR; Q9LCB4; -.
DR KEGG; ag:BAA90528; -.
DR BioCyc; MetaCyc:MON-15047; -.
DR BRENDA; 2.3.3.18; 6043.
DR BRENDA; 2.3.3.19; 6043.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Cobalt; Manganese; Transferase.
FT CHAIN 1..440
FT /note="2-phosphinomethylmalate synthase"
FT /id="PRO_0000443948"
FT DOMAIN 39..313
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT CONFLICT 73
FT /note="G -> D (in Ref. 3; AKN91125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49199 MW; 2441B859FE03F3D1 CRC64;
MTVQNPQEPE YFPEVFPQDA FPQYAWDEGM RPITLPHEVW LSETTHRDGQ QGGLPLSLDT
SRRIYDILCE ITGDSTAIRH AEFFPYRDSD RNALIYALER HRDGAPIEPT TWIRARREDV
ELIKRIGVIE TGLLSSSSDY HTFHKFGSGG RTQAASMYLD AVTMALDHGI RPRVHLEDTT
RSSPDFVRAL VEEVLKTAER YPAELQPRFR VCDTLGIGLP YDDVSLPRSI PRWIRLLRGF
GLSPSQIELH PHNDTWLVVA NCLAAIREGC GVISGTTLGT GERTGNAPLE AVMVHLLGMG
YWSGARVNLP AVNKLVELYE GIGAGPSQKY PFFGRDAYVT RAGIHADGLN KFWWMYAPFN
APLLTGRELD VALTKDSGQA GLLFVLNKRL GLQLEKGDPR VAEVLAWMDR QWDAGRVSAV
EWSELEPVVE KAFATEEGVG
