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Database: UniProt
Entry: A3NT04
LinkDB: A3NT04
Original site: A3NT04 
ID   PURT_BURP0              Reviewed;         404 AA.
AC   A3NT04;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   05-DEC-2018, entry version 75.
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=BURPS1106A_1196;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) 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; CP000572; ABN89214.1; -; Genomic_DNA.
DR   RefSeq; WP_004522466.1; NC_009076.1.
DR   ProteinModelPortal; A3NT04; -.
DR   SMR; A3NT04; -.
DR   PRIDE; A3NT04; -.
DR   EnsemblBacteria; ABN89214; ABN89214; BURPS1106A_1196.
DR   KEGG; bpl:BURPS1106A_1196; -.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   BioCyc; BPSE357348:G1G89-1215-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000006738; Chromosome I.
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   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51246; SSF51246; 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    404       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000319142.
FT   DOMAIN      123    318       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     164    169       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     199    202       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       25     26       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      372    373       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       277    277       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       289    289       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      85     85       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     118    118       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     159    159       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     207    207       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     296    296       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     365    365       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   404 AA;  43083 MW;  8DBB650E67D908AD CRC64;
     MQIGQRLGTP LSPSATRVML LGAGELGKEV IIALQRLGVE VIAVDRYPNA PGHQVAHRAH
     VIDMTDPDAL RALVDAERPH LVVPEIEAIA TDALAAIEAA GVCEVIPTAR ATQLTMNREG
     IRRLAAEELG LPTSPYAFAQ SFDEFAAAVA RIGFPCVVKP VMSSSGKGQS VVRSEADIEP
     AWRYAMAGGR VNHGRVIVEG FIRFDYEITQ LTVRAIDPAS GQTRTSFCAP IGHLQVAGDY
     VESWQPQPMS AKALERSRDI AHRVTSALGG RGIFGVELFV RGDDVWFSEV SPRPHDTGLV
     TLASQRQSEF ELHARAILGL PVEPALATPA ASAVIYGGLD EAGIAFEGVR DALAVPGADL
     RLFGKPESFA KRRMGVALAT GANVDEARER AKRAAAAVRP VSAR
//
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