Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7VEK9

- PURL_PROMA

UniProt

Q7VEK9 - PURL_PROMA

Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.UniRule annotation

    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 – 531UniRule annotation
    Binding sitei56 – 561ATPUniRule annotation
    Binding sitei95 – 951ATPUniRule annotation
    Metal bindingi97 – 971Magnesium 1UniRule annotation
    Active sitei99 – 991Proton acceptorUniRule annotation
    Binding sitei120 – 1201SubstrateUniRule annotation
    Metal bindingi121 – 1211Magnesium 2UniRule annotation
    Binding sitei244 – 2441SubstrateUniRule annotation
    Metal bindingi272 – 2721Magnesium 2UniRule annotation
    Binding sitei523 – 5231ATPUniRule annotation
    Binding sitei560 – 5601ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
    Metal bindingi561 – 5611Magnesium 1UniRule annotation
    Binding sitei563 – 5631SubstrateUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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 PurLUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferase subunit IIUniRule annotation
    Short name:
    FGAR amidotransferase IIUniRule annotation
    Short name:
    FGAR-AT IIUniRule annotation
    Glutamine amidotransferase PurLUniRule annotation
    Phosphoribosylformylglycinamidine synthase subunit IIUniRule annotation
    Gene namesi
    Name:purLUniRule annotation
    Ordered Locus Names:Pro_0003
    OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
    Taxonomic identifieri167539 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001420: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 793793Phosphoribosylformylglycinamidine synthase subunit PurLPRO_0000100477Add
    BLAST

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    STRINGi167539.Pro0003.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VEK9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1014Substrate bindingUniRule annotation
    Regioni316 – 3183Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the FGAMS family.UniRule annotation

    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...
    MobiDBi 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: October 1, 2014
    This is version 77 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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