GenomeNet

Database: UniProt
Entry: Q8PBI2
LinkDB: Q8PBI2
Original site: Q8PBI2 
ID   PURT_XANCP              Reviewed;         400 AA.
AC   Q8PBI2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   05-DEC-2018, entry version 112.
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=XCC1137;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 /
OS   NCPPB 528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM40436.1; -; Genomic_DNA.
DR   RefSeq; NP_636512.1; NC_003902.1.
DR   RefSeq; WP_011036337.1; NC_003902.1.
DR   ProteinModelPortal; Q8PBI2; -.
DR   SMR; Q8PBI2; -.
DR   STRING; 190485.XCC1137; -.
DR   EnsemblBacteria; AAM40436; AAM40436; XCC1137.
DR   GeneID; 35544534; -.
DR   GeneID; 998725; -.
DR   KEGG; xcc:XCC1137; -.
DR   PATRIC; fig|190485.4.peg.1216; -.
DR   eggNOG; ENOG4108EF9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   BioCyc; XCAM190485:XCC1137-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome;
KW   Transferase.
FT   CHAIN         1    400       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000319265.
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      368    369       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     361    361       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
SQ   SEQUENCE   400 AA;  42926 MW;  4E52930C6AF5353D CRC64;
     MTTLGTPLSP SATRVLLLGS GELGKEVAIE LQRFGVEVIA ADRYANAPAM QVAHRSHVLD
     MLDPQALRAL IAQEQPHLIV PEIEAIHTET LVALEHEQGQ KVIPTARAAR LTMDREGIRR
     LAAETLGLPT SPYRFVDTAA EYREAIATVG LPCVVKPVMS SSGKGQSTLR SEADIDAAWD
     YAQTGGRAGA GRCIVEGFID FDYEITLLTV RHAGGTSFCD PIGHWQKDGD YRESWQPQPM
     SAAALRRSQE IAQAITDELG GWGLFGVELF VKGDEVWFSE VSPRPHDTGL VTLVSQELSE
     FALHARAILG LPVGAENGGV IRQSGPSASC ALLAHGNGVP VFDNVAEALR DPDTALRLFG
     KPRVDGHRRV GVTLARAGSI DAAREKARVA AAALTIQLRD
//
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