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Database: UniProt
Entry: A0A0S3F4D1_9SPHN
LinkDB: A0A0S3F4D1_9SPHN
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ID   A0A0S3F4D1_9SPHN        Unreviewed;       390 AA.
AC   A0A0S3F4D1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   ECO:0000313|EMBL:ALR22554.1};
GN   ORFNames=ATN00_10960 {ECO:0000313|EMBL:ALR22554.1};
OS   Sphingobium baderi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR22554.1, ECO:0000313|Proteomes:UP000056968};
RN   [1] {ECO:0000313|EMBL:ALR22554.1, ECO:0000313|Proteomes:UP000056968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DE-13 {ECO:0000313|EMBL:ALR22554.1,
RC   ECO:0000313|Proteomes:UP000056968};
RA   Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT   "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT   para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT   Sphingobium baderi DE-13.";
RL   Submitted (NOV-2015) 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}.
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DR   EMBL; CP013264; ALR22554.1; -; Genomic_DNA.
DR   RefSeq; WP_062068691.1; NZ_CP013264.1.
DR   AlphaFoldDB; A0A0S3F4D1; -.
DR   STRING; 1332080.ATN00_10960; -.
DR   KEGG; sbd:ATN00_10960; -.
DR   OrthoDB; 9804625at2; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000056968; 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}; 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:UP000056968};
KW   Transferase {ECO:0000313|EMBL:ALR22554.1}.
FT   DOMAIN          111..300
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         14..15
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         74
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         106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         152..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         187..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         278
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         350
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         357..358
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   390 AA;  42744 MW;  9B50B771708785FF CRC64;
     MAFTAKILLL GSGELGREFV ISAKRLGCQV IACDSYAGAP AMQVADGYEV FSMLDGDALK
     AAIHQHRPDF VVPEIEAIRT ETLAEVEAHG VEVVPSARAT MMTMNRDAIR EVAAVELGLR
     TSRYRYAESL EEVRAGAEHT GLPCVIKPVM SSSGKGQSTV RNANELESAW TYAVANMRGD
     RQRVIVEEFI PFDYEITLLT VRTRDGVLFC PPIGHRQERG DYQESWQPTP MSAKALADAQ
     DMSRKVVDNL GGYGLFGVEF FVKGEEVIFS ELSPRPHDTG MVTLISQKLS EFDLHARAIL
     GLPIPEIRLY GAATSAVILA DRESDNFRFE GLADALATTG AEVDVRLFGK PTTRPYRRMG
     VALARAETVE EARRVAAEAA AKVRIVYDKG
//
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