ID E4TWR3_SULKY Unreviewed; 387 AA.
AC E4TWR3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Sulku_0076 {ECO:0000313|EMBL:ADR32744.1};
OS Sulfuricurvum kujiense (strain ATCC BAA-921 / DSM 16994 / JCM 11577 /
OS YK-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfuricurvum.
OX NCBI_TaxID=709032 {ECO:0000313|EMBL:ADR32744.1, ECO:0000313|Proteomes:UP000008721};
RN [1] {ECO:0000313|EMBL:ADR32744.1, ECO:0000313|Proteomes:UP000008721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-921 / DSM 16994 / JCM 11577 / YK-1
RC {ECO:0000313|Proteomes:UP000008721};
RX PubMed=22675602; DOI=10.4056/sigs.2456004;
RA Han C., Kotsyurbenko O., Chertkov O., Held B., Lapidus A., Nolan M.,
RA Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Brambilla E.M., Rohde M., Spring S.,
RA Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of the sulfur compounds oxidizing
RT chemolithoautotroph Sulfuricurvum kujiense type strain (YK-1(T)).";
RL Stand. Genomic Sci. 6:94-103(2012).
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}.
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DR EMBL; CP002355; ADR32744.1; -; Genomic_DNA.
DR RefSeq; WP_013458941.1; NC_014762.1.
DR AlphaFoldDB; E4TWR3; -.
DR STRING; 709032.Sulku_0076; -.
DR KEGG; sku:Sulku_0076; -.
DR eggNOG; COG0027; Bacteria.
DR HOGENOM; CLU_011534_1_3_7; -.
DR OrthoDB; 9804625at2; -.
DR UniPathway; UPA00074; UER00127.
DR Proteomes; UP000008721; 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; 3.40.50.20; -; 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};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000313|EMBL:ADR32744.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01643};
KW Metal-binding {ECO:0000256|HAMAP-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:UP000008721}.
FT DOMAIN 118..306
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 21..22
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 81
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 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 159..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 193..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT BINDING 284
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 352
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 359..360
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; 42706 MW; 6BAD3D6A86B15728 CRC64;
MLFSAPLKNN SKKIMLLGSG ELGKEVAIEA QRLGIEVIAV DRYNHAPAHL VANRSHVVNM
QDKEAVLKLI RKEKPDYILP EIEAISIDAL FAAEAEGFCV IPNAEAVNKT MNRKNIRRFA
AEDLGLKTSR YHFVSTYEDM CASAEDVGFP CVIKPVMSSS GHGQSIARTR EDLAASWEIA
KEARGDASEL IVEEFIRFDY EITLLTARNG VETVFCEPIG HIQKDGDYIY SWQPMEMSKK
ALKRSQKIAK AITDGLGGKG LFGVELFVAG DEVYFSEVSP RPHDTGMVTL ITQSQSEFAL
HVRAVLGLPL GFTFYGDGAS AAFKSVVEST EPVVDVADEV FDDNSFVRVF GKPEAHVGRR
MAVVLVFDKV NKAMKKAKKL IKKIKDA
//
