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Q2YNG6

- PURL_BRUA2

UniProt

Q2YNG6 - PURL_BRUA2

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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene
purL, BAB1_0857
Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL By similarity.

Catalytic activityi

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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501 By similarity
Binding sitei53 – 531ATP By similarity
Binding sitei92 – 921ATP By similarity
Metal bindingi94 – 941Magnesium 1 By similarity
Active sitei96 – 961Proton acceptor By similarity
Binding sitei117 – 1171Substrate By similarity
Metal bindingi118 – 1181Magnesium 2 By similarity
Binding sitei241 – 2411Substrate By similarity
Metal bindingi269 – 2691Magnesium 2 By similarity
Binding sitei495 – 4951ATP By similarity
Binding sitei532 – 5321ATP; via carbonyl oxygen and amide nitrogen By similarity
Metal bindingi533 – 5331Magnesium 1 By similarity
Binding sitei535 – 5351Substrate By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBABO359391:GKDV-871-MONOMER.
BMEL359391:GJOQ-871-MONOMER.
UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase subunit PurL (EC:6.3.5.3)
Short name:
FGAM synthase
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase subunit II
Short name:
FGAR amidotransferase II
Short name:
FGAR-AT II
Glutamine amidotransferase PurL
Phosphoribosylformylglycinamidine synthase subunit II
Gene namesi
Name:purL
Ordered Locus Names:BAB1_0857
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000002719: Chromosome I

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Phosphoribosylformylglycinamidine synthase subunit PurLUniRule annotationPRO_0000236649Add
BLAST

Interactioni

Subunit structurei

Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits By similarity.

Protein-protein interaction databases

STRINGi359391.BAB1_0857.

Structurei

3D structure databases

ProteinModelPortaliQ2YNG6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 984Substrate binding By similarity
Regioni313 – 3153Substrate binding By similarity

Sequence similaritiesi

Belongs to the FGAMS family.

Phylogenomic databases

eggNOGiCOG0046.
HOGENOMiHOG000238227.
KOiK01952.
OMAiQAVVFKI.
OrthoDBiEOG6FNHHR.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
HAMAPiMF_00420. PurL_2.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR010074. PRibForGlyAmidine_synth_II.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01736. FGAM_synth_II. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YNG6-1 [UniParc]FASTAAdd to Basket

« Hide

MTISNTRDIT PELIEAHGLK PDEYQRILEL IGREPTFTEL GIFSAMWNEH    50
CSYKSSKKWL RTLPTSGPRV IQGPGENAGV VDIGDGDCVV FKMESHNHPS 100
YIEPYQGAAT GVGGILRDVF TMGARPVAAM NALRFGEPDH PKTRHLVSGV 150
VSGVGGYGNA FGVPTVGGEV NFDKRYNGNI LVNAFAAGLA RHDGIFLSEA 200
EGVGLPVVYL GAKTSRDGVG GATMASAEFD ESIEEKRPTV QVGDPFTEKC 250
LLEACLELMA SGAVIAIQDM GAAGLTCSAV EMGAKGDLGI ELILDHVPVR 300
EENMTAYEMM LSESQERMLM VLKPEKEAEA QAIFRKWGLD FAIVGKTTDD 350
LRFRVIHQGE EVANLPIKDL GDEAPEYDRP WMEPGKHAPL PASNVPQVED 400
YSAALLKLIG SPDLSSRRWV YEQYDTLIQG NSLQVPGGDA GVIRVEGHET 450
KALAFSSDVT PRYCEADPFE GGKQAVAECW RNITATGAEP LASTDNLNFG 500
NPEKPEIMGQ LVKAIEGIGE ACRALDFPIV SGNVSLYNET NGQAILPTPT 550
IAGVGLLPDW SQMAKIGGMQ DGDTLVLLGG DGTHLGQSVY LRDLFDRADG 600
PAPFVDLALE KRNGEFVRSA IRNGQVTACH DLSDGGLAIA VAEMAIKSGK 650
GATLDAGDGL PHALLFGEDQ ARYVISATPE MAKLIALNAE GAGVPFRILG 700
TVGGDRLKIS KNVDVSVADL TQAYEGWFPN FMNGELTGNN 740
Length:740
Mass (Da):79,148
Last modified:February 7, 2006 - v1
Checksum:iC59E25D61D763D78
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ10813.1.
RefSeqiYP_414285.1. NC_007618.1.

Genome annotation databases

EnsemblBacteriaiCAJ10813; CAJ10813; BAB1_0857.
GeneIDi3787541.
KEGGibmf:BAB1_0857.
PATRICi17844627. VBIBruMel86222_0892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM040264 Genomic DNA. Translation: CAJ10813.1 .
RefSeqi YP_414285.1. NC_007618.1.

3D structure databases

ProteinModelPortali Q2YNG6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 359391.BAB1_0857.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ10813 ; CAJ10813 ; BAB1_0857 .
GeneIDi 3787541.
KEGGi bmf:BAB1_0857.
PATRICi 17844627. VBIBruMel86222_0892.

Phylogenomic databases

eggNOGi COG0046.
HOGENOMi HOG000238227.
KOi K01952.
OMAi QAVVFKI.
OrthoDBi EOG6FNHHR.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00128 .
BioCyci BABO359391:GKDV-871-MONOMER.
BMEL359391:GJOQ-871-MONOMER.

Miscellaneous databases

PROi Q2YNG6.

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
HAMAPi MF_00420. PurL_2.
InterProi IPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR010074. PRibForGlyAmidine_synth_II.
IPR016188. PurM_N-like.
[Graphical view ]
Pfami PF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view ]
SUPFAMi SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsi TIGR01736. FGAM_synth_II. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2308.

Entry informationi

Entry nameiPURL_BRUA2
AccessioniPrimary (citable) accession number: Q2YNG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: September 3, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In Gram-negative bacteria and most eukaryotes, FGAM synthase is only formed by PurL, a single polypeptide of 140 kDa (large PurL). However in Gram-positive bacteria and archaebacteria, phosphoribosylformylglycinamidine synthase is composed of three separate proteins: PurL (small PurL), PurQ and PurS By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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