PURT_PYRFU
ID PURT_PYRFU Reviewed; 429 AA.
AC Q8U3M7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=PF0430;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80554.1; -; Genomic_DNA.
DR RefSeq; WP_011011545.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3M7; -.
DR SMR; Q8U3M7; -.
DR STRING; 186497.PF0430; -.
DR EnsemblBacteria; AAL80554; AAL80554; PF0430.
DR GeneID; 41712226; -.
DR KEGG; pfu:PF0430; -.
DR PATRIC; fig|186497.12.peg.447; -.
DR eggNOG; arCOG01598; Archaea.
DR HOGENOM; CLU_011534_1_3_2; -.
DR OMA; GMVTMIT; -.
DR OrthoDB; 57699at2157; -.
DR PhylomeDB; Q8U3M7; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000001013; 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..429
FT /note="Formate-dependent phosphoribosylglycinamide
FT formyltransferase"
FT /id="PRO_0000319284"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 26..27
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 86
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 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 199..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT BINDING 295
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 375
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 382..383
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 429 AA; 48231 MW; ECE8B37904B75D72 CRC64;
MIKLRDELGT ATTDSAQKIL LLGSGELGKE IAIEAQRLGV EVVAVDRYAN APAMQVAHRS
YVGNMMDKDF LWSVVEREKP DAIIPEIEAI NLDALFEFEK EGYFVVPNAK ATWIAMHRER
LRETLVKEAK VPTSRYMYAT TLDELYEACE KIGYPCHTKA IMSSSGKGSY FVRGPEDIPK
AWEEAKTKAR GSAEKIIVEE HIDFDVEITE LAVRHFDENG EIVTTFPKPV GHYQIDGDYH
ASWQPAEISE KAEREVYRIA KRITDVLGGL GLFGVEMFVK GDKVWANEVS PRPHDTGMVT
LASHPPGFSE FGLHLRAVLG LPIPGEWVDG YRLFPMLIPA ATHVIKAKVS GYSPRFRGLA
KALSVPNATI RLFGKPEAYP GRRLGVVLAW DKDVQEAKKR AEMVAHMIEL RTRSSDWHSQ
DYEKRKHLL
