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PURT_XANCB
ID   PURT_XANCB              Reviewed;         400 AA.
AC   B0RY47;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01643};
DE            EC=6.3.1.21 {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   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=xcc-b100_3202;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the
CC       transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing
CC       5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by
CC       PurU via hydrolysis of 10-formyl-tetrahydrofolate. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-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:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:456216;
CC         EC=6.3.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24830;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (formate route): step 1/1. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; AM920689; CAP52567.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RY47; -.
DR   SMR; B0RY47; -.
DR   KEGG; xca:xcc-b100_3202; -.
DR   HOGENOM; CLU_011534_1_3_6; -.
DR   OMA; GMVTMIT; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Purine biosynthesis.
FT   CHAIN           1..400
FT                   /note="Formate-dependent phosphoribosylglycinamide
FT                   formyltransferase"
FT                   /id="PRO_1000186902"
FT   DOMAIN          120..309
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         22..23
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         82
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         161..166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         196..199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         287
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         361
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         368..369
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="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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