Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q1C5E7 (PUR4_YERPA)

Last modified September 1, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: YPA_2360
OrganismYersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]
Taxonomic identifier360102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length1296 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. HAMAP MF_00419

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: HAMAP

phosphoribosylformylglycinamidine synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12961296Phosphoribosylformylglycinamidine synthase HAMAP MF_00419
PRO_0000264602

Regions

Domain1043 – 1296254Glutamine amidotransferase type-1
Nucleotide binding306 – 31712ATP Potential

Sites

Active site11361Nucleophile By similarity
Active site12611 By similarity
Active site12631 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1C5E7-1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: 338EB52821A8888A

FASTA1,296142,048
        10         20         30         40         50         60 
MEILRGSPAL SAFRITKLLS RCQDAHLLVS DIYAEYVHFA DVSAPLSADE HARLQRLLQY 

        70         80         90        100        110        120 
GPSLPEHPPA GRLLLVTPRP GTISPWSSKA TDIAHNCGLS QILRLERGLA FSIQGPDLNE 

       130        140        150        160        170        180 
SQWKQLAALL HDRMMEAVFT DLQQAEQLFS HHQPAPVQRV DILGQGRSAL EQANIKLGLA 

       190        200        210        220        230        240 
LAQDEIDYLL TAFTGLGRNP TDIELYMFAQ ANSEHCRHKI FNADWVIDGV VQPKTLFKMI 

       250        260        270        280        290        300 
KNTFEHTPDY VLSAYKDNAA VMEGSQVGRF YATAEKGIYD YHQEEAHILM KVETHNHPTA 

       310        320        330        340        350        360 
ISPWPGAATG SGGEIRDEGA TGRGAKPKAG LVGFSVSNLR IPGFEQPWEE NFGKPDRIVT 

       370        380        390        400        410        420 
ALDIMTEGPL GGAAFNNEFG RPALLGYFRT YEERVNSHNG IELRGYHKPI MLAGGLGNIR 

       430        440        450        460        470        480 
ADHVQKGEIT VGAKLVVLGG PSMNIGLGGG AASSMASGQS DADLDFASVQ RDNPEMERRC 

       490        500        510        520        530        540 
QEVIDRCWQL GEYNPILFIH DVGAGGLSNA MPELVNDGGR GGRFELRDIL NDEPGMSPLE 

       550        560        570        580        590        600 
VWCNESQERY VLAVAPAQMA LFDEICRRER APYAVIGEAT EEKHLLLNDR HFGNQPIDMP 

       610        620        630        640        650        660 
LDVLLGKTPK MLRDVTRLQA KGDALQRADI SLAEAVKRIM HLPAVAEKTF LITIGDRTVT 

       670        680        690        700        710        720 
GMVTRDQMVG PWQIPVADCA VTSASLDSYY GEAMSLGERA PVALLDFAAS ARLAVGEALT 

       730        740        750        760        770        780 
NIAATQIGEL KRIKLSANWM SAAGHPGEDA GLYDAVRAVG EELCPALEIT IPVGKDSMSM 

       790        800        810        820        830        840 
KTRWQEGHEQ REMTSPLSLV ITAFARIEDV RRTVTPQLRT DKGDNALLLI DLGAGHNALG 

       850        860        870        880        890        900 
ATALTQVYRQ LGDKPADVRN VQQLAGFFNA MQRLVADQHL LAYHDRSDGG LLVTLAEMAF 

       910        920        930        940        950        960 
AGHCGVTVDI QSLGNDALAA LFNEELGAVI QVRAEQRADV EKLLADHGLA NCVHYLGRAV 

       970        980        990       1000       1010       1020 
AGDTFDIRSG TDVVYSEKRS TLRLWWAETS WQMQRLRDNP DCADQEHQAK QDESDPGLNV 

      1030       1040       1050       1060       1070       1080 
KLTFDPAEDI AAPFILKQAR PKVAVLREQG VNSHVEMAAA FHRAGFDAVD VHMSDLLAGR 

      1090       1100       1110       1120       1130       1140 
TDLQSFQTLV ACGGFSYGDV LGAGEGWAKS ILFNDRVRDE FEAFFHRPTT LALGVCNGCQ 

      1150       1160       1170       1180       1190       1200 
MMSNLRELIP GAEHWPRFVR NLSDSFEARF SLVEVASSPS LFMQDMVGSR MPIAVSHGEG 

      1210       1220       1230       1240       1250       1260 
QVEVRDAAHL AALEQSHLVA LRFVNNHGVV TEQYPANPNG SANGITAVTS VSGRATVMMP 

      1270       1280       1290 
HPERVFRTVS NSWHPEEWGE DSPWMRMFRN ARKQLG 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed: 16740952] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000308 Genomic DNA. Translation: ABG14325.1. Different initiation.
RefSeqYP_652270.1.

3D structure databases

SMRQ1C5E7. Positions 1-1296.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1C5E7.

Genome annotation databases

GeneID4121241.
GenomeReviewsGene locus YPA_2360 in contig CP000308_GR.
KEGGypa:YPA_2360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1C5E7.

Enzyme and pathway databases

BioCycYPES360102:YPA_2360-MON.

Family and domain databases

HAMAPMF_00419.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR017926. GATASE_1.
IPR010073. PRibForGlyAmidine_synth.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
TIGRFAMsTIGR01735. FGAM_synt. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR4_YERPA
AccessionPrimary (citable) accession number: Q1C5E7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: September 1, 2009
This is version 28 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents