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Database: UniProt
Entry: B1JDF0
LinkDB: B1JDF0
Original site: B1JDF0 
ID   PURT_PSEPW              Reviewed;         393 AA.
AC   B1JDF0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   16-JAN-2019, entry version 77.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE            EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000255|HAMAP-Rule:MF_01643};
GN   OrderedLocusNames=PputW619_4162;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Taghavi S., Vangronsveld D.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
CC       the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
CC       producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
CC       provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide +
CC         phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58426, ChEBI:CHEBI:58457, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC       phospho-D-ribosyl)glycinamide (formate route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
DR   EMBL; CP000949; ACA74642.1; -; Genomic_DNA.
DR   RefSeq; WP_012315976.1; NC_010501.1.
DR   ProteinModelPortal; B1JDF0; -.
DR   SMR; B1JDF0; -.
DR   STRING; 390235.PputW619_4162; -.
DR   EnsemblBacteria; ACA74642; ACA74642; PputW619_4162.
DR   KEGG; ppw:PputW619_4162; -.
DR   eggNOG; ENOG4108EF9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; PPUT390235:G1GBA-4273-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000000720; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01643; PurT; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01142; purT; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Transferase.
FT   CHAIN         1    393       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_1000186889.
FT   DOMAIN      119    308       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     160    165       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     195    198       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       22     23       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      363    364       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       267    267       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       279    279       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      82     82       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     114    114       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     155    155       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     203    203       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     286    286       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     356    356       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   393 AA;  42558 MW;  A44694E9AE8FF303 CRC64;
     MTRIGTPLSP TATRVLLCGC GELGKEVVIE LQRLGVEVIA VDRYANAPAM QVAHRSHVVN
     MLDGVALRAV IEAEKPHYIV PEIEAIATAT LVELENEGFN VVPTARATQL TMNREGIRRL
     AAEELDLPTS PYHFADTFED YAKAVADVGY PCVVKPVMSS SGKGQSLLRS DADLQKSWDY
     AQEGGRAGKG RVIIEGFIDF DYEITLLTVR HVGGTTYLEP VGHRQEKGDY QESWQPQAMS
     PKALAESQRV AKAVTDALGG RGLFGVELFV KGDQVWFSEV SPRPHDTGLV TLISQDLSQF
     ALHARAILGL PIPVVRQFGP SASAVILPEG QSQQTSFANL GAALSEPDTA IRLFGKPEIN
     GQRRMGVCLA RDESIEAARA KATRAAQAVK VEF
//
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