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Database: UniProt
Entry: B2FTB9
LinkDB: B2FTB9
Original site: B2FTB9 
ID   PURT_STRMK              Reviewed;         395 AA.
AC   B2FTB9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   16-JAN-2019, 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=Smlt1264;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N.,
RA   Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R.,
RA   Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C.,
RA   Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by
RT   drug resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44816.1; -; Genomic_DNA.
DR   RefSeq; WP_012479445.1; NC_010943.1.
DR   ProteinModelPortal; B2FTB9; -.
DR   SMR; B2FTB9; -.
DR   STRING; 522373.Smlt1264; -.
DR   PRIDE; B2FTB9; -.
DR   EnsemblBacteria; CAQ44816; CAQ44816; Smlt1264.
DR   GeneID; 6395429; -.
DR   KEGG; sml:Smlt1264; -.
DR   PATRIC; fig|522373.3.peg.1225; -.
DR   eggNOG; ENOG4108HH9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 1677960at2; -.
DR   BioCyc; SMAL522373:SMLT_RS06125_4-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000008840; 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   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    395       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_1000186899.
FT   DOMAIN      120    309       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     161    166       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     196    199       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       268    268       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       280    280       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      82     82       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     115    115       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     156    156       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     204    204       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     287    287       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     356    356       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   395 AA;  42333 MW;  C4FF7F3E7B2701BB CRC64;
     MAKLGTPLSP SATRVLLLGS GELGKEVAIE LQRLGVEVIA ADRYADAPAM QVAHRSHVID
     MLDAMALRAL IAQEQPHLVV PEIEAIHTET LVQLEQEQGL RVIPTARAAR LTMDREGIRR
     LAAETLGLPT SPYRFVDTEA EYRAAVAAIG LPCVVKPVMS SSGKGQSTLR SEAEIAPAWE
     YAQTGGRAGA GRCIVEGFID FDYEITLLTV RHAGGTSFCA PIGHLQKDGD YRESWQPQPM
     SSAALARAEE ISRAITDDLG GWGLFGVELF VKGDEVWFSE VSPRPHDTGL VTLVSQELSE
     FALHARAILG LPIPVIRQSG PSASCALLAH GEGVPYFNNV AAALQVPDTA VRLFGKPSVH
     GHRRVGVTLA RAETIDEARA IARDAAEAIG VELRP
//
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