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Formate-dependent phosphoribosylglycinamide formyltransferase (5'-phosphoribosylglycinamide transformylase 2) (Formate-dependent GAR transformylase) (EC 2.1.2.-) (GAR transformylase 2) (GART 2) (Non-folate glycinamide ribonucleotide transformylase) (Phosphoribosylglycinamide formyltransferase 2)

 PURT_ECOLI              Reviewed;         392 AA.
P33221;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 171.
RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000305|PubMed:8117714};
AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000303|PubMed:8117714};
AltName: Full=Formate-dependent GAR transformylase {ECO:0000305|PubMed:8117714};
EC=2.1.2.- {ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151};
AltName: Full=GAR transformylase 2 {ECO:0000303|PubMed:8117714};
Short=GART 2 {ECO:0000303|PubMed:8117714};
AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000303|PubMed:8117714};
AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000303|PubMed:8117714};
Name=purT {ECO:0000303|PubMed:8117714};
OrderedLocusNames=b1849, JW1838;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE
SPECIFICITY, REACTION MECHANISM, AND PATHWAY.
STRAIN=K12;
PubMed=8117714; DOI=10.1021/bi00175a023;
Marolewski A., Smith J.M., Benkovic S.J.;
"Cloning and characterization of a new purine biosynthetic enzyme: a
non-folate glycinamide ribonucleotide transformylase from E. coli.";
Biochemistry 33:2531-2537(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
MUTAGENESIS OF GLY-162, SUBSTRATE SPECIFICITY, PATHWAY, AND REACTION
MECHANISM.
PubMed=9184151; DOI=10.1021/bi962961p;
Marolewski A.E., Mattia K.M., Warren M.S., Benkovic S.J.;
"Formyl phosphate: a proposed intermediate in the reaction catalyzed
by Escherichia coli PurT GAR transformylase.";
Biochemistry 36:6709-6716(1997).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[7]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG;
BETA-FORMYL GLYCINAMIDE RIBONUCLEOTIDE AND MAGNESIUM ION, AND SUBUNIT.
PubMed=10913290; DOI=10.1021/bi000926j;
Thoden J.B., Firestine S., Nixon A., Benkovic S.J., Holden H.M.;
"Molecular structure of Escherichia coli PurT-encoded glycinamide
ribonucleotide transformylase.";
Biochemistry 39:8791-8802(2000).
[8]
X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH BETA-FORMYL
GLYCINAMIDE RIBONUCLEOTIDE; ATP AND MAGNESIUM ION, AND SUBUNIT.
PubMed=11953435; DOI=10.1074/jbc.M202251200;
Thoden J.B., Firestine S.M., Benkovic S.J., Holden H.M.;
"PurT-encoded glycinamide ribonucleotide transformylase. Accommodation
of adenosine nucleotide analogs within the active site.";
J. Biol. Chem. 277:23898-23908(2002).
-!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
PurT is also able to cleave acetyl phosphate and carbamoyl
phosphate to produce ATP with acetate and carbamate, respectively.
{ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151}.
-!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide
= 5'-phosphoribosyl-N-formylglycinamide + ADP + phosphate.
{ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.1 uM for GAR (at pH 8) {ECO:0000269|PubMed:8117714,
ECO:0000269|PubMed:9184151};
KM=45 uM for ATP (with formate) {ECO:0000269|PubMed:9184151};
KM=77.4 uM for ATP (with acetate at pH 8)
{ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151};
KM=319 uM for formate (at pH 8) {ECO:0000269|PubMed:8117714,
ECO:0000269|PubMed:9184151};
KM=3.68 mM for acetate (at pH 8) {ECO:0000269|PubMed:8117714};
Note=Kcat is 37.6 sec(-1) for transformylase activity (at pH 8).
Kcat is 0.309 sec(-1) for acetate kinase activity (at pH 8).
{ECO:0000269|PubMed:8117714};
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
phospho-D-ribosyl)glycinamide (formate route): step 1/1.
{ECO:0000255|HAMAP-Rule:MF_01643, ECO:0000305|PubMed:8117714,
ECO:0000305|PubMed:9184151}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435, ECO:0000305|PubMed:8117714}.
-!- INTERACTION:
P22939:ispA; NbExp=4; IntAct=EBI-553029, EBI-553011;
-!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
Rule:MF_01643}.
-----------------------------------------------------------------------
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EMBL; L20897; AAA23861.1; -; Genomic_DNA.
EMBL; U00096; AAC74919.1; -; Genomic_DNA.
EMBL; AP009048; BAA15657.1; -; Genomic_DNA.
PIR; A54227; A54227.
RefSeq; NP_416363.1; NC_000913.3.
RefSeq; WP_000173484.1; NZ_LN832404.1.
PDB; 1EYZ; X-ray; 1.75 A; A/B=1-392.
PDB; 1EZ1; X-ray; 1.75 A; A/B=1-392.
PDB; 1KJ8; X-ray; 1.60 A; A/B=2-392.
PDB; 1KJ9; X-ray; 1.60 A; A/B=2-392.
PDB; 1KJI; X-ray; 1.60 A; A/B=2-392.
PDB; 1KJJ; X-ray; 1.75 A; A/B=2-392.
PDB; 1KJQ; X-ray; 1.05 A; A/B=2-392.
PDB; 1NFE; Model; -; A=1-392.
PDBsum; 1EYZ; -.
PDBsum; 1EZ1; -.
PDBsum; 1KJ8; -.
PDBsum; 1KJ9; -.
PDBsum; 1KJI; -.
PDBsum; 1KJJ; -.
PDBsum; 1KJQ; -.
PDBsum; 1NFE; -.
ProteinModelPortal; P33221; -.
SMR; P33221; -.
BioGrid; 4260365; 7.
DIP; DIP-10618N; -.
IntAct; P33221; 7.
STRING; 316385.ECDH10B_1990; -.
DrugBank; DB03434; 3[N-Morpholino]Propane Sulfonic Acid.
DrugBank; DB02236; Glycinamide Ribonucleotide.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB02930; Phosphothiophosphoric Acid-Adenylate Ester.
iPTMnet; P33221; -.
PaxDb; P33221; -.
PRIDE; P33221; -.
EnsemblBacteria; AAC74919; AAC74919; b1849.
EnsemblBacteria; BAA15657; BAA15657; BAA15657.
GeneID; 946368; -.
KEGG; ecj:JW1838; -.
KEGG; eco:b1849; -.
PATRIC; fig|1411691.4.peg.400; -.
EchoBASE; EB1757; -.
EcoGene; EG11809; purT.
eggNOG; ENOG4108HH9; Bacteria.
eggNOG; COG0027; LUCA.
HOGENOM; HOG000072820; -.
InParanoid; P33221; -.
KO; K08289; -.
OMA; GMVTMIT; -.
PhylomeDB; P33221; -.
BioCyc; EcoCyc:GARTRANSFORMYL2-MONOMER; -.
BioCyc; MetaCyc:GARTRANSFORMYL2-MONOMER; -.
UniPathway; UPA00074; UER00127.
EvolutionaryTrace; P33221; -.
PRO; PR:P33221; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0008776; F:acetate kinase activity; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.1490.20; -; 1.
HAMAP; MF_01643; PurT; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR003135; ATP-grasp_carboxylate-amine.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR005862; PurT.
InterPro; IPR011054; Rudment_hybrid_motif.
Pfam; PF02222; ATP-grasp; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
TIGRFAMs; TIGR01142; purT; 1.
PROSITE; PS50975; ATP_GRASP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Magnesium; Metal-binding;
Nucleotide-binding; Purine biosynthesis; Reference proteome;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8117714}.
CHAIN 2 392 Formate-dependent
phosphoribosylglycinamide
formyltransferase.
/FTId=PRO_0000074956.
DOMAIN 119 308 ATP-grasp. {ECO:0000255|HAMAP-
Rule:MF_01643}.
NP_BIND 160 165 ATP. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
NP_BIND 195 198 ATP. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
REGION 22 23 5'-phosphoribosylglycinamide binding.
{ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
REGION 362 363 5'-phosphoribosylglycinamide binding.
{ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
METAL 267 267 Magnesium. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
METAL 279 279 Magnesium. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 82 82 5'-phosphoribosylglycinamide.
{ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 114 114 ATP. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 155 155 ATP. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 203 203 ATP. {ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 286 286 5'-phosphoribosylglycinamide.
{ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
BINDING 355 355 5'-phosphoribosylglycinamide.
{ECO:0000269|PubMed:10913290,
ECO:0000269|PubMed:11953435}.
MOD_RES 179 179 N6-acetyllysine. {ECO:0000255|HAMAP-
Rule:MF_01643,
ECO:0000269|PubMed:18723842}.
MUTAGEN 162 162 G->I: Strong decrease in the reaction
rate for the conversion of formate to
FGAR and in the affinity for formate.
3- and 2-fold decrease in the affinity
for ATP and GAR, respectively.
{ECO:0000269|PubMed:9184151}.
STRAND 14 19 {ECO:0000244|PDB:1KJQ}.
HELIX 22 32 {ECO:0000244|PDB:1KJQ}.
TURN 33 35 {ECO:0000244|PDB:1KJQ}.
STRAND 37 44 {ECO:0000244|PDB:1KJQ}.
HELIX 48 52 {ECO:0000244|PDB:1KJQ}.
STRAND 53 58 {ECO:0000244|PDB:1KJQ}.
HELIX 64 74 {ECO:0000244|PDB:1KJQ}.
STRAND 77 81 {ECO:0000244|PDB:1KJQ}.
HELIX 88 96 {ECO:0000244|PDB:1KJQ}.
STRAND 100 103 {ECO:0000244|PDB:1KJQ}.
HELIX 105 112 {ECO:0000244|PDB:1KJQ}.
HELIX 114 122 {ECO:0000244|PDB:1KJQ}.
STRAND 132 137 {ECO:0000244|PDB:1KJQ}.
HELIX 138 148 {ECO:0000244|PDB:1KJQ}.
STRAND 150 157 {ECO:0000244|PDB:1KJQ}.
TURN 161 164 {ECO:0000244|PDB:1KJ8}.
STRAND 166 168 {ECO:0000244|PDB:1KJQ}.
HELIX 171 173 {ECO:0000244|PDB:1KJQ}.
HELIX 174 184 {ECO:0000244|PDB:1KJQ}.
HELIX 186 188 {ECO:0000244|PDB:1KJQ}.
STRAND 192 196 {ECO:0000244|PDB:1KJQ}.
STRAND 201 211 {ECO:0000244|PDB:1KJQ}.
STRAND 214 217 {ECO:0000244|PDB:1KJQ}.
STRAND 221 226 {ECO:0000244|PDB:1KJQ}.
STRAND 229 235 {ECO:0000244|PDB:1KJQ}.
HELIX 241 258 {ECO:0000244|PDB:1KJQ}.
STRAND 260 271 {ECO:0000244|PDB:1KJQ}.
STRAND 274 283 {ECO:0000244|PDB:1KJQ}.
HELIX 286 290 {ECO:0000244|PDB:1KJQ}.
HELIX 291 294 {ECO:0000244|PDB:1KJQ}.
STRAND 295 297 {ECO:0000244|PDB:1KJQ}.
HELIX 299 307 {ECO:0000244|PDB:1KJQ}.
STRAND 319 326 {ECO:0000244|PDB:1KJQ}.
STRAND 329 334 {ECO:0000244|PDB:1KJQ}.
STRAND 336 338 {ECO:0000244|PDB:1KJQ}.
HELIX 340 342 {ECO:0000244|PDB:1KJQ}.
STRAND 348 352 {ECO:0000244|PDB:1KJQ}.
STRAND 358 361 {ECO:0000244|PDB:1KJQ}.
STRAND 365 370 {ECO:0000244|PDB:1KJQ}.
HELIX 374 387 {ECO:0000244|PDB:1KJQ}.
STRAND 389 391 {ECO:0000244|PDB:1KJQ}.
SEQUENCE 392 AA; 42434 MW; 276B3883E7403EA9 CRC64;
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL
AAEELQLPTS TYRFADSESL FREAVADIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG
SRRLGVALAT AESVVDAIER AKHAAGQVKV QG


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