ID PURT_XANC8 Reviewed; 400 AA.
AC Q4US21;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 16-JAN-2019, entry version 106.
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=XC_3106;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(2005).
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; CP000050; AAY50152.1; -; Genomic_DNA.
DR RefSeq; WP_011036337.1; NC_007086.1.
DR ProteinModelPortal; Q4US21; -.
DR SMR; Q4US21; -.
DR STRING; 314565.XC_3106; -.
DR EnsemblBacteria; AAY50152; AAY50152; XC_3106.
DR GeneID; 35544534; -.
DR KEGG; xcb:XC_3106; -.
DR eggNOG; ENOG4108EF9; Bacteria.
DR eggNOG; COG0027; LUCA.
DR HOGENOM; HOG000072820; -.
DR KO; K08289; -.
DR OMA; GMVTMIT; -.
DR OrthoDB; 1677960at2; -.
DR BioCyc; XCAM314565:XC_RS15655-MONOMER; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000000420; 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 1 400 Formate-dependent
FT phosphoribosylglycinamide
FT formyltransferase.
FT /FTId=PRO_0000319266.
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
//
