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Q7VEK9

- PURL_PROMA

UniProt

Q7VEK9 - PURL_PROMA

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Protein
Phosphoribosylformylglycinamidine synthase subunit PurL
Gene
purL, Pro_0003
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
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 sitei53 – 531 By similarity
Binding sitei56 – 561ATP By similarity
Binding sitei95 – 951ATP By similarity
Metal bindingi97 – 971Magnesium 1 By similarity
Active sitei99 – 991Proton acceptor By similarity
Binding sitei120 – 1201Substrate By similarity
Metal bindingi121 – 1211Magnesium 2 By similarity
Binding sitei244 – 2441Substrate By similarity
Metal bindingi272 – 2721Magnesium 2 By similarity
Binding sitei523 – 5231ATP By similarity
Binding sitei560 – 5601ATP; via carbonyl oxygen and amide nitrogen By similarity
Metal bindingi561 – 5611Magnesium 1 By similarity
Binding sitei563 – 5631Substrate By similarity

GO - Molecular functioni

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

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

BioCyciPMAR167539:GJN2-3-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:Pro_0003
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001420: Chromosome

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 – 793793Phosphoribosylformylglycinamidine synthase subunit PurLUniRule annotation
PRO_0000100477Add
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

STRINGi167539.Pro0003.

Structurei

3D structure databases

ProteinModelPortaliQ7VEK9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1014Substrate binding By similarity
Regioni316 – 3183Substrate binding By similarity

Sequence similaritiesi

Belongs to the FGAMS family.

Phylogenomic databases

eggNOGiCOG0046.
KOiK01952.
OMAiQAVVFKI.
OrthoDBiEOG6FNHHR.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
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.

Q7VEK9-1 [UniParc]FASTAAdd to Basket

« Hide

MIKSKDYLVD YNVELALKKE GLTKADYIEI CNRLKRSPNR TELGMFGVMW    50
SEHCCYRNSR SLLSNFPTTG KNILVGPGEN AGVVDLGEGQ RLAFKIESHN 100
HPSAIEPFQG AATGVGGILR DIFTMGARPI ALLNSLRFGP LDTPINVGLL 150
EGVVSGIAHY GNCVGVPTVG GEVAFDKSYS GNPLVNAMAL GIMETKEIVC 200
SGAKGIDFPV IYVGSTTGRD GMGGASFASS ELTQASIDDR PAVQVGDPFL 250
EKGLIEGCLE AFKTGYVVAA QDMGAAGLTC SCSEMAAKGG VGIELDLDLV 300
PAREKNMTAY EFLLSESQER MLFVVEPGKE ELIMNKFRKW GLQAKVVGKV 350
LEENIVRVIH EKQIVVNLPA DSLAEDTPVN KHELLEEPPG FIKDHWKWDE 400
TSLPKVSIKG VHFKENNTIL DWNQIILRLL DDPTIASKRW IYNQYDYQVQ 450
NNTIIAPGIG DAALIRLREI ENQNQNSNRG IAAVVDCPNR WVALDPERGA 500
IAAVAEASRN ISCVGAKPLA VTDNLNFSSP EDPIGYWQLA KACKGLSKAC 550
VVLETPVTGG NVSLYNETAL PNGLKQPIQP TPVVGMIGLI QDINSATRQG 600
WKDQGDQIYL LGTSIDPSIL NNQNISLAAT SYLENIYGLK TGRPPLIDLE 650
FEKLVQLFLR ESIANNLIKS AHDISDGGLV IGLAESCISS GLGIECNLPE 700
IDNRLDKLLF AEGGSRVLVS VSPNNIHNIK NSLNNFNIAN SEQISFNYLG 750
TVTDNKYFQI NINQTKIIDL SVNEITNKFE RSIPRRINST IVS 793
Length:793
Mass (Da):86,331
Last modified:June 7, 2005 - v2
Checksum:iDA470F1FED396B31
GO

Sequence cautioni

The sequence AAP99049.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017126 Genomic DNA. Translation: AAP99049.1. Different initiation.
RefSeqiNP_874397.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99049; AAP99049; Pro_0003.
GeneIDi1461381.
KEGGipma:Pro_0003.
PATRICi23026575. VBIProMar8617_0003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017126 Genomic DNA. Translation: AAP99049.1 . Different initiation.
RefSeqi NP_874397.1. NC_005042.1.

3D structure databases

ProteinModelPortali Q7VEK9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 167539.Pro0003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP99049 ; AAP99049 ; Pro_0003 .
GeneIDi 1461381.
KEGGi pma:Pro_0003.
PATRICi 23026575. VBIProMar8617_0003.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00128 .
BioCyci PMAR167539:GJN2-3-MONOMER.

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
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: SARG / CCMP1375 / SS120.

Entry informationi

Entry nameiPURL_PROMA
AccessioniPrimary (citable) accession number: Q7VEK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: September 3, 2014
This is version 76 of the entry and version 2 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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