ID A0A2R5FWV6_NOSCO Unreviewed; 387 AA.
AC A0A2R5FWV6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01643};
DE EC=6.3.1.21 {ECO:0000256|HAMAP-Rule:MF_01643};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE AltName: Full=Formate-dependent GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE AltName: Full=GAR transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE Short=GART 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
GN Name=purT {ECO:0000256|HAMAP-Rule:MF_01643};
GN ORFNames=NIES4072_56370 {ECO:0000313|EMBL:GBG21948.1};
OS Nostoc commune NIES-4072.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG21948.1, ECO:0000313|Proteomes:UP000245124};
RN [1] {ECO:0000313|EMBL:GBG21948.1, ECO:0000313|Proteomes:UP000245124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG21948.1,
RC ECO:0000313|Proteomes:UP000245124};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01643}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01643}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC Rule:MF_01643}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG21948.1}.
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DR EMBL; BDUD01000001; GBG21948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5FWV6; -.
DR OrthoDB; 9804625at2; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000245124; Unassembled WGS sequence.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR048740; PurT_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01142; purT; 1.
DR PANTHER; PTHR43055; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR PANTHER; PTHR43055:SF1; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF21244; PurT_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01643}; Ligase {ECO:0000256|HAMAP-Rule:MF_01643};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01643};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01643};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01643}; Reference proteome {ECO:0000313|Proteomes:UP000245124};
KW Transferase {ECO:0000313|EMBL:GBG21948.1}.
FT DOMAIN 113..303
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 16..17
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 76
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 154..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 189..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 281
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 351
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 358..359
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
SQ SEQUENCE 387 AA; 42502 MW; 3FEBED9061ED0C92 CRC64;
MSIKLPQKLM LLGSGELGKE FAIAAQRLGN YVIAVDRYAN APAMQVADAY EVISMLSADD
LEAVVTKYQP DIIIPEIEAI RTKKLIEFEQ QGITVIPTAA ATNYTMNRDR IRELAHQQLG
IRTAKYGYAT TLEELIAVSD EIGFSNVVKP VMSSSGKGQS VVQEKSEVEK AWNYAIANSR
GDSQKVIVEE FINFEIEITL LTIKQWNAPT IFCSPIGHRQ ERGDYQESWQ PAEISEDKIL
KAQEIAIKVT DALGGAGIFG VEFFITKDEV IFSELSPRPH DTGMVTLISQ NLNEFELHLR
AILGLPIPHI EQLGASASAV ILASEKSDSI AFSGVADALS EKDVDIKLFG KPNAHPYRRM
GVALAKGINV QEAREKATKA ASKIQII
//