PURT_NOSS1
ID PURT_NOSS1 Reviewed; 391 AA.
AC Q8YXB6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=alr1299;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB73256.1; -; Genomic_DNA.
DR PIR; AH1968; AH1968.
DR RefSeq; WP_010995471.1; NZ_RSCN01000021.1.
DR AlphaFoldDB; Q8YXB6; -.
DR SMR; Q8YXB6; -.
DR STRING; 103690.17130646; -.
DR EnsemblBacteria; BAB73256; BAB73256; BAB73256.
DR KEGG; ana:alr1299; -.
DR eggNOG; COG0027; Bacteria.
DR OMA; GMVTMIT; -.
DR OrthoDB; 1677960at2; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000002483; 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; 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; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..391
FT /note="Formate-dependent phosphoribosylglycinamide
FT formyltransferase"
FT /id="PRO_0000319119"
FT DOMAIN 115..305
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 18..19
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 78
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 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 156..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 191..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 283
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 353
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 360..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"
SQ SEQUENCE 391 AA; 42898 MW; 36F13E8860D918DF CRC64;
MSKAIKLPQK LMLLGSGELG KEFVIAAQRL GNYVIAVDRY ANAPAMQVSD CCEVISMLSA
DDLEAVVTKY EPDFIIPEIE AIRTEKLQEF EDRGITVIPT AAATNYTMNR DRIRELAHEE
LGIRTAKYGY AVTLEELIAV SDNIGFPNVV KPVMSSSGKG QSVVATKEEV EKAWDYAIAN
SRGDSQKVIV EEFINFEIEI TLLTIKQWNA PTIFCSPIGH RQERGDYQES WQPAGISEDK
ILEAQAIAKT VTDALGGAGI FGVEFFITKD EVIFSELSPR PHDTGMVTLI SQNLNEFELH
LRAILGLPIP KIEQLGFCAS AVILASEKLD APLFTGVAEA LAEPDVDIRL FGKPTAHPYR
RMGVALAKAE NVETAREKAT DAASKIHISS Q
