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Protein

Phosphoribosylglycinamide formyltransferase

Gene

purN

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.UniRule annotation

Catalytic activityi

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Phosphoribosylglycinamide formyltransferase (purN)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 65110-formyltetrahydrofolateUniRule annotation
Binding sitei107 – 107110-formyltetrahydrofolateUniRule annotation
Active sitei109 – 1091Proton donorUniRule annotation
Sitei145 – 1451Raises pKa of active site HisUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Enzyme and pathway databases

BioCyciBHAL272558:GJC5-690-MONOMER.
UniPathwayiUPA00074; UER00126.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.2UniRule annotation)
Alternative name(s):
5'-phosphoribosylglycinamide transformylaseUniRule annotation
GAR transformylaseUniRule annotation
Gene namesi
Name:purNUniRule annotationImported
Ordered Locus Names:BH0632Imported
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)Imported
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi272558.BH0632.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P9XX-ray1.90A/B1-188[»]
ProteinModelPortaliQ9KF54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 181180Formyl_trans_NInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 1435'-phosphoribosylglycinamide bindingUniRule annotation
Regioni90 – 93410-formyltetrahydrofolate bindingUniRule annotation

Sequence similaritiesi

Belongs to the GART family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108V3E. Bacteria.
COG0299. LUCA.
KOiK11175.
OMAiGITIHLV.
OrthoDBiEOG615VP4.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
HAMAPiMF_01930. PurN.
InterProiIPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR004607. PurN_trans.
[Graphical view]
PfamiPF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00639. PurN. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KF54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRVAIFASG SGTNAEAIIQ SQKAGQLPCE VALLITDKPG AKVVERVKVH
60 70 80 90 100
EIPVCALDPK TYPSKEAYEI EVVQQLKEKQ IDFVVLAGYM RLVGPTLLGA
110 120 130 140 150
YEGRIVNIHP SLLPAFPGLH AIEQAIRANV KVTGVTIHYV DEGMDTGPII
160 170 180
AQEAVSIEEE DTLETLTTKI QAVEHRLYPA TLHKLLSK
Length:188
Mass (Da):20,503
Last modified:October 1, 2000 - v1
Checksum:i908871F1942147C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04351.1.
PIRiH83728.
RefSeqiWP_010896808.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB04351; BAB04351; BAB04351.
KEGGibha:BH0632.
PATRICi18938254. VBIBacHal18977_0665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04351.1.
PIRiH83728.
RefSeqiWP_010896808.1. NC_002570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P9XX-ray1.90A/B1-188[»]
ProteinModelPortaliQ9KF54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH0632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB04351; BAB04351; BAB04351.
KEGGibha:BH0632.
PATRICi18938254. VBIBacHal18977_0665.

Phylogenomic databases

eggNOGiENOG4108V3E. Bacteria.
COG0299. LUCA.
KOiK11175.
OMAiGITIHLV.
OrthoDBiEOG615VP4.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00126.
BioCyciBHAL272558:GJC5-690-MONOMER.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
HAMAPiMF_01930. PurN.
InterProiIPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR004607. PurN_trans.
[Graphical view]
PfamiPF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00639. PurN. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125Imported.
  2. "Crystal structure of phosphoribosylglycinamide formyltransferase from Bacillus Halodurans."
    Patskovsky Y., Toro R., Foti R., Seidel R.D., Almo S.C.
    Submitted (OCT-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).

Entry informationi

Entry nameiQ9KF54_BACHD
AccessioniPrimary (citable) accession number: Q9KF54
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.