Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6D238 (PUR4_ERWCT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosylformylglycinamidine synthase
Short name=FGAM synthase
Short name=FGAMS
EC=6.3.5.3
Alternative name(s):
Formylglycinamide ribotide amidotransferase
Short name=FGARAT
Formylglycinamide ribotide synthetase
Gene names
Name:purL
Ordered Locus Names:ECA3258
OrganismErwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]
Taxonomic identifier29471 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length1294 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. HAMAP MF_00419

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. HAMAP MF_00419

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP MF_00419.

Sequence similarities

In the N-terminal section; belongs to the FGAMS family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12941294Phosphoribosylformylglycinamidine synthase HAMAP MF_00419
PRO_0000264572

Regions

Domain1041 – 1294254Glutamine amidotransferase type-1
Nucleotide binding305 – 31612ATP Potential

Sites

Active site11341Nucleophile By similarity
Active site12591 By similarity
Active site12611 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6D238 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: F85AF988A5F34950

FASTA1,294142,126
        10         20         30         40         50         60 
MEILRGSPAL SAFRINKLLV RCKEHLLPVS DIYAEYVHFA DVSTPLNNDE QAKLTRLLKY 

        70         80         90        100        110        120 
GPSLAEHEPQ GHLLLVTPRP GTISPWSSKA TDIAHNCGLS KVLRLERGLA FYIHAPTLND 

       130        140        150        160        170        180 
EQWQQLGALL HDRMMESVFS DLKQAAALFS HHQPAPFKRI EILLQGRQAL EEANVRLGLA 

       190        200        210        220        230        240 
LAEDEIDYLL EAFNNLGRNP TDIELYMFAQ ANSEHCRHKI FNADWVIDGV TQPKSLFKMI 

       250        260        270        280        290        300 
KNTFEHTPDH VLSAYKDNAA VMEGSAVGRF YTDANGQYDY HQEDAHILMK VETHNHPTAI 

       310        320        330        340        350        360 
SPWPGAATGS GGEIRDEGAT GRGSKPKAGL VGFSVSNLRI PGFIQPWEEE FGKPDRIVSA 

       370        380        390        400        410        420 
LDIMTEGPLG GAAFNNEFGR PALTGYFRTY EERVDSHNGE ELRGYHKPIM LAGGIGNIRG 

       430        440        450        460        470        480 
DHVKKGEIIV GAKLIVLGGP SMNIGLGGGA ASSMASGQSD ADLDFASVQR DNPEMERRCQ 

       490        500        510        520        530        540 
EVIDRCWQLG EANPILFIHD VGAGGLSNAM PELVSDGGRG GRFELRDILN DEPGMSPLEV 

       550        560        570        580        590        600 
WCNESQERYV LAVAPEQLAQ FDEICRRERA PYAVIGEATE ELHLTMNDRH FNNQPIDLPL 

       610        620        630        640        650        660 
DVLLGKTPKM LRDVERKQVE GTPLQRDDIY LAEAVERVLH LPVVAEKTFL ITIGDRSVTG 

       670        680        690        700        710        720 
MVARDQMVGP WQVPVADCAV TTASLDSYYG EAMSIGERAP VALRNFAASA RLAVGEALTN 

       730        740        750        760        770        780 
IAATHIGPLT RVKLSANWMA AAGHPGEDAG LYDAVKAVGE ELCPALGLTI PVGKDSMSMK 

       790        800        810        820        830        840 
TRWQEEGEDR AVTSPMSLVI SAFARVEDVR NTVTPQLRTG QDNALLLIDL GAGNKALGAT 

       850        860        870        880        890        900 
ALAQVYRQLG RKTADVHSPE QLAGFFNAIQ ELVAAKALLA YHDRSDGGLI VTLAEMAFAG 

       910        920        930        940        950        960 
HCGVTVDIAS QGEDTLATLF NEELGAVIQI PAARRAEVDA ILALHGLADC VHYLGQAEEG 

       970        980        990       1000       1010       1020 
TRFTINQGAE AVYQESRSTL RRWWAETSWQ MQRLRDNPQC ADQEHIARQD DNDPGLNVSL 

      1030       1040       1050       1060       1070       1080 
TFDPKEDIAA PYIAKNVRPK VAVLREQGVN SHVEMAAAFH RAGFDAIDIH MSDLLANRRN 

      1090       1100       1110       1120       1130       1140 
LQDFQALVAC GGFSYGDVLG AGEGWAKSIL FNARVRDEFA EFFLRPQTLA LGVCNGCQMM 

      1150       1160       1170       1180       1190       1200 
SNLRELIPGA DLWPRFVRNK SDRFEARFSL VEVDKSPSLF MNDMAGSRMP IAVSHGEGQV 

      1210       1220       1230       1240       1250       1260 
EVRDDAHLAA IEEHGLVALR YINHYGQVTE NYPANPNGSS NGITAVTSTS GRATVMMPHP 

      1270       1280       1290 
ERVFRTVSNS WHPEEWGEDG PWMRMFRNAR RQLG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX950851 Genomic DNA. Translation: CAG76156.1.
RefSeqYP_051347.1. NC_004547.2.

3D structure databases

HSSPHSSP built from PDB template 1T3T based on UniProtKB P74881.
ProteinModelPortalQ6D238.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2881272.
GenomeReviewsGene locus ECA3258 in contig BX950851_GR.
KEGGeca:ECA3258.
NMPDRfig|218491.3.peg.1960.
PATRIC20481853. VBIPecAtr54885_3302.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG335309.
OMAVKAVGME.
ProtClustDBPRK05297.

Enzyme and pathway databases

BioCycECAR218491:ECA3258-MONOMER.

Family and domain databases

HAMAPMF_00419. PurL_1.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR017926. GATASE_1.
IPR010073. PRibForGlyAmidine_synth.
IPR022940. PRibForGlyAmidine_synth_bac.
IPR016188. PurM_N-like.
[Graphical view]
KOK01952.
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMSSF56042. AIR_synth_C. 2 hits.
SSF55326. PurM_N-like. 2 hits.
TIGRFAMsTIGR01735. FGAM_synt. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR4_ERWCT
AccessionPrimary (citable) accession number: Q6D238
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents