PURT_PYRHO
ID PURT_PYRHO Reviewed; 430 AA.
AC O58056;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=PH0318;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), AND SUBUNIT.
RA Yoshikawa S., Arai R., Kamo-Uchikubo T., Shirouzu M., Yokoyama S.;
RT "Crystal structure of Probable phosphoribosylglycinamide formyl transferase
RT (PH0318) from Pyrococcus horikoshii OT3.";
RL Submitted (JUL-2005) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ADP, AND SUBUNIT.
RA Yoshikawa S., Arai R., Kamo-Uchikubo T., Shirouzu M., Yokoyama S.;
RT "Crystal structure of Probable phosphoribosylglycinamide formyl transferase
RT from Pyrococcus horikoshii OT3 complexed with ADP.";
RL Submitted (AUG-2006) to the PDB data bank.
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 ECO:0000305|Ref.2, ECO:0000305|Ref.3}.
CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC Rule:MF_01643}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29392.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29392.1; ALT_INIT; Genomic_DNA.
DR PIR; C71138; C71138.
DR RefSeq; WP_048053086.1; NC_000961.1.
DR PDB; 2CZG; X-ray; 2.35 A; A/B=1-430.
DR PDB; 2DWC; X-ray; 1.70 A; A/B=1-430.
DR PDBsum; 2CZG; -.
DR PDBsum; 2DWC; -.
DR AlphaFoldDB; O58056; -.
DR SMR; O58056; -.
DR STRING; 70601.3256709; -.
DR EnsemblBacteria; BAA29392; BAA29392; BAA29392.
DR GeneID; 1444201; -.
DR KEGG; pho:PH0318; -.
DR eggNOG; arCOG01598; Archaea.
DR OrthoDB; 57699at2157; -.
DR UniPathway; UPA00074; UER00127.
DR EvolutionaryTrace; O58056; -.
DR Proteomes; UP000000752; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..430
FT /note="Formate-dependent phosphoribosylglycinamide
FT formyltransferase"
FT /id="PRO_0000319285"
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 ECO:0000269|Ref.3"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT ECO:0000269|Ref.3"
FT BINDING 199..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT ECO:0000269|Ref.3"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT ECO:0000269|Ref.3"
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"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 230..245
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 283..292
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:2DWC"
FT HELIX 394..406
FT /evidence="ECO:0007829|PDB:2DWC"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2DWC"
SQ SEQUENCE 430 AA; 48374 MW; C2835B8D3CC2B679 CRC64;
MIKLRDELGT ATTDSAQKIL LLGSGELGKE IAIEAQRLGV EVVAVDRYAN APAMQVAHRS
YVGNMMDKDF LWSVVEREKP DAIIPEIEAI NLDALFEFEK DGYFVVPNAR ATWIAMHRER
LRETLVKEAK VPTSRYMYAT TLDELYEACE KIGYPCHTKA IMSSSGKGSY FVKGPEDIPK
AWEEAKTKAR GSAEKIIVEE HIDFDVEVTE LAVRHFDENG EIVTTFPKPV GHYQIDGDYH
ASWQPAEISE KAEREVYRIA KRITDVLGGL GIFGVEMFVK GDKVWANEVS PRPHDTGMVT
LASHPPGFSE FALHLRAVLG LPIPGEWVDG YRLFPMLIPA ATHVIKAKVS GYSPRFRGLV
KALSVPNATV RLFGKPEAYV GRRLGIALAW DKDVEVAKRK AEMVAHMIEL RTRSSDWHDQ
NYEKRKHLLR
