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Database: UniProt
Entry: A5GX22
LinkDB: A5GX22
Original site: A5GX22 
ID   PURT_SYNR3              Reviewed;         393 AA.
AC   A5GX22;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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=SynRCC307_2528;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK29431.1; -; Genomic_DNA.
DR   RefSeq; WP_011936940.1; NC_009482.1.
DR   ProteinModelPortal; A5GX22; -.
DR   SMR; A5GX22; -.
DR   STRING; 316278.SynRCC307_2528; -.
DR   PRIDE; A5GX22; -.
DR   EnsemblBacteria; CAK29431; CAK29431; SynRCC307_2528.
DR   KEGG; syr:SynRCC307_2528; -.
DR   eggNOG; ENOG4108HH9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; SSP316278:G1GJL-2450-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02222; ATP-grasp; 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; Reference proteome;
KW   Transferase.
FT   CHAIN         1    393       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000319250.
FT   DOMAIN      114    304       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     155    160       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     190    193       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       17     18       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      361    362       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       263    263       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       275    275       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      77     77       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     109    109       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     150    150       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     198    198       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     282    282       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     354    354       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   393 AA;  41447 MW;  B2E9D48C12A0A4A9 CRC64;
     MTSTHLPATL LLLGSGELGK EVAIAAQRLG CRVVAVDRYA NAPAMQVADT AVVIPMTDAE
     ALKQVIREHQ PALVIPEIEA LAVDALAELE AEGITVIPTA RATAITMNRD RIRDLAAGEL
     GLRTARFGYA SSAEELSSAA EPLGWPVVVK PVMSSSGKGQ SVATNPEELQ QAWTAATQGA
     RGSASLVIVE EFLRFEQEIT LLTVRQKDGP TLFCPPIGHI QERGDYQCSW QPAELQQSQL
     LEAQRMARQV TDALGGAGIF GVEFFIASGE VIFSELSPRP HDTGLVTLRG QNLSEFELHL
     RAVLGLPIPS ITSTGAAASR VVLAGADQQG GPVHYRGVAE ALAVPESELL LFGKPEARPM
     RRMGVALASG SSLAEARGRA DTAAQAVALE IGG
//
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