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Q2SK05 (PUR4_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:HCH_02192
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella

Protein attributes

Sequence length1298 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 – 12981298Phosphoribosylformylglycinamidine synthase HAMAP MF_00419
PRO_0000264577

Regions

Domain1046 – 1298253Glutamine amidotransferase type-1
Nucleotide binding307 – 31812ATP Potential

Sites

Active site11391Nucleophile By similarity
Active site12631 By similarity
Active site12651 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2SK05 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 06E16745026E6254

FASTA1,298141,107
        10         20         30         40         50         60 
MFELRGAPAL SPFRREKLLK NIQEQAPEVQ SVYAEYMHFV DLEGDLSAEQ RTVLDRLLQY 

        70         80         90        100        110        120 
GPQGQSEMPS GTLFLVVPRP GTISPWSSKA TDIAHNCGLT AIRRIERGVA YHVGSSEQLS 

       130        140        150        160        170        180 
SERRAAIAAI LHDRMTQSVF HEIAGAELLF AHAEPKPMTT VDILADGRDA LAEANRSMGL 

       190        200        210        220        230        240 
ALAEDEIDYL TSAFTELGRN PTDVELMMFA QANSEHCRHK IFNATWEIDG EVQSHSLFGM 

       250        260        270        280        290        300 
IRNTYEQGGQ DVLSAYCDNA AVIKGGQGGR FFPDHRTKIY GYNVEDIHIL MKVETHNHPT 

       310        320        330        340        350        360 
AISPFAGAST GSGGEIRDEG ATGIGAKPKA GLTGFTVSNL NIPGYKQPWE GDYGKPERIV 

       370        380        390        400        410        420 
SALQIMLDGP IGGAAFNNEF GRPALCGYFR TYEEQVPGVN GLEWRGYHKP IMIAGGMGNI 

       430        440        450        460        470        480 
RASHVEKKDI SVDAKLIVLG GPAMLIGLGG GAASSMDSGA GQEDLDFASV QRDNPEMERR 

       490        500        510        520        530        540 
CQEVIDRCWQ LGDDNPILFI HDVGAGGLSN ALPELVKDGG RGGLFELRDV PNDEPGMSPL 

       550        560        570        580        590        600 
EIWCNESQER YVMAVAEQDM ELFDQLCRRE RCPYAVVGSA TEELKIQVSD EYFANSPVDL 

       610        620        630        640        650        660 
PMSVLFGKPP KMHRTIERKS FTKPIFDSTT LDLKEAAERI LRLPSVASKS FLITIGDRSV 

       670        680        690        700        710        720 
TGMVSRDQMV GPWQAPVSDV AVTTASFDTY RGEAMAMGER TPIALIDPPS SGRMAVGEAI 

       730        740        750        760        770        780 
TNLAAAKIEK LSDIKLSANW MAAAGHPGED EALFETVKAV GMELCPELGI TIPVGKDSMS 

       790        800        810        820        830        840 
MKTVWEEGEK QKSVTAPLSL IISGFAPVED VRKTLTPQMD LSTPSKLLLI DLGSGKNRLG 

       850        860        870        880        890        900 
GSALAQVYRS VGAVAPDLDN PEELAAFFAC IQKLNNEGKL KAYHDRSDGG VFTTLCEMAF 

       910        920        930        940        950        960 
ASRCGMTICF DGLVKDRTHI ARELFNEELG AVVQVSEEHV DEVKTCFADA GLADHVVVLG 

       970        980        990       1000       1010       1020 
EPHADQSVKF QHEGQTVLGY SRGALQKIWA ETSYRMQSMR DNSECAAEEF AAIDDDNDPG 

      1030       1040       1050       1060       1070       1080 
LSAKLTYDVN EDIAAPFINR GAKPKIVVLR EQGVNSQAEM AAAFDRAGFS AVDVHMSDIL 

      1090       1100       1110       1120       1130       1140 
SGAVSLSQFK ALAACGGFSF GDVLGAGEGW AKSILFNARA RDQFEAFFHR KDTFALGVCN 

      1150       1160       1170       1180       1190       1200 
GCQMISNLKE LIPGADAWPR FVRNRSEQYE ARVAMVEVLD SPSILLQGMA GSMMPIAVAH 

      1210       1220       1230       1240       1250       1260 
GEGLAEVGPE GAAALMAQKN VALRFVDNYG RPTMSHPFNP NGSPLGITSV CNDDGRITVM 

      1270       1280       1290 
MPHPERVFRA VANSWRPSAW SEDGAWMRMF RNARVWLG

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000155 Genomic DNA. Translation: ABC29019.1.
RefSeqYP_433444.1. NC_007645.1.

3D structure databases

HSSPHSSP built from PDB template 1VK3 based on UniProtKB Q9X0X3.
ProteinModelPortalQ2SK05.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SK05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3841188.
GenomeReviewsGene locus HCH_02192 in contig CP000155_GR.
KEGGhch:HCH_02192.
NMPDRfig|349521.5.peg.1970.
PATRIC22085282. VBIHahChe29232_2024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0046.
HOGENOMHBG335309.
OMAVKAVGME.
PhylomeDBQ2SK05.
ProtClustDBPRK05297.

Enzyme and pathway databases

BioCycHCHE349521:HCH_02192-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_HAHCH
AccessionPrimary (citable) accession number: Q2SK05
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 45 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

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