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)

Q14GZ5

- GLYA_FRAT1

UniProt

Q14GZ5 - GLYA_FRAT1

Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.UniRule annotation

    Catalytic activityi

    5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361Pyridoxal phosphateUniRule annotation
    Binding sitei56 – 561Pyridoxal phosphateUniRule annotation
    Binding sitei58 – 581SubstrateUniRule annotation
    Binding sitei65 – 651SubstrateUniRule annotation
    Binding sitei66 – 661Pyridoxal phosphateUniRule annotation
    Binding sitei100 – 1001Pyridoxal phosphateUniRule annotation
    Binding sitei122 – 1221Substrate; via carbonyl oxygenUniRule annotation
    Binding sitei176 – 1761Pyridoxal phosphateUniRule annotation
    Binding sitei204 – 2041Pyridoxal phosphateUniRule annotation
    Binding sitei229 – 2291Pyridoxal phosphateUniRule annotation
    Binding sitei236 – 2361Pyridoxal phosphateUniRule annotation
    Binding sitei263 – 2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygenUniRule annotation
    Binding sitei363 – 3631Pyridoxal phosphateUniRule annotation

    GO - Molecular functioni

    1. glycine hydroxymethyltransferase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. glycine biosynthetic process from serine Source: UniProtKB-HAMAP
    2. tetrahydrofolate interconversion Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, One-carbon metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciFTUL393115:GJUT-1259-MONOMER.
    UniPathwayiUPA00193.
    UPA00288; UER01023.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine hydroxymethyltransferaseUniRule annotation (EC:2.1.2.1UniRule annotation)
    Short name:
    SHMTUniRule annotation
    Short name:
    Serine methylaseUniRule annotation
    Gene namesi
    Name:glyAUniRule annotation
    Ordered Locus Names:FTF1241
    OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
    Taxonomic identifieri393115 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
    ProteomesiUP000001821: 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 – 417417Serine hydroxymethyltransferasePRO_1000006250Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei230 – 2301N6-(pyridoxal phosphate)lysineUniRule annotation

    Proteomic databases

    PRIDEiQ14GZ5.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi393115.FTF1241.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14GZ5.
    SMRiQ14GZ5. Positions 8-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni126 – 1283Substrate bindingUniRule annotation
    Regioni355 – 3573Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the SHMT family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0112.
    HOGENOMiHOG000239404.
    KOiK00600.
    OMAiHLMLVDV.
    OrthoDBiEOG6Z0QB2.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00051. SHMT.
    InterProiIPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR001085. Ser_HO-MeTrfase.
    IPR019798. Ser_HO-MeTrfase_PLP_BS.
    [Graphical view]
    PANTHERiPTHR11680. PTHR11680. 1 hit.
    PfamiPF00464. SHMT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000412. SHMT. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00096. SHMT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q14GZ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSFEKNSLK NTDKEIFDAI ELEVKRQHEH VELIASENYA SPAVMEAQGS    50
    QLTNKYAEGY HGKRYYGGCE FVDIAEKLAI ERAQQLFGVD YANVQPHSGS 100
    QANAAVYNAV LKPGDTVLGM DLGAGGHLTH GSKVNFSGKI YNSIQYGLDE 150
    NGDIDYKQVA QLAKEHKPKM IIAGFSAFSG IINWQKFREI ADSVDAVLMA 200
    DIAHVAGLVA AGVYPNPFPY VYVATTTTHK TLRGPRGGLI LCNNNPELAK 250
    KFQSAIFPGI QGGPLMHVIA AKAVAFKEAL EPSFVDYQKQ VLKNAKAMEK 300
    VLKQRGINII SGGTSNHLLL LDITNTGFSG KEAEAALGRA NITVNKNSIP 350
    NDPRSPFVTS GLRIGSPAIT TRGFKEKECE LVANLLADVV FNCGDEKVEN 400
    ETAAKVLDLC DKFPVYK 417
    Length:417
    Mass (Da):45,316
    Last modified:August 22, 2006 - v1
    Checksum:i419A2B83E0C8DB03
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL09257.1.
    RefSeqiYP_667331.1. NC_008245.1.

    Genome annotation databases

    EnsemblBacteriaiCAL09257; CAL09257; FTF1241.
    GeneIDi4200288.
    KEGGiftf:FTF1241.
    PATRICi17961544. VBIFraTul133500_1434.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL09257.1 .
    RefSeqi YP_667331.1. NC_008245.1.

    3D structure databases

    ProteinModelPortali Q14GZ5.
    SMRi Q14GZ5. Positions 8-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 393115.FTF1241.

    Proteomic databases

    PRIDEi Q14GZ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL09257 ; CAL09257 ; FTF1241 .
    GeneIDi 4200288.
    KEGGi ftf:FTF1241.
    PATRICi 17961544. VBIFraTul133500_1434.

    Phylogenomic databases

    eggNOGi COG0112.
    HOGENOMi HOG000239404.
    KOi K00600.
    OMAi HLMLVDV.
    OrthoDBi EOG6Z0QB2.

    Enzyme and pathway databases

    UniPathwayi UPA00193 .
    UPA00288 ; UER01023 .
    BioCyci FTUL393115:GJUT-1259-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_00051. SHMT.
    InterProi IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR001085. Ser_HO-MeTrfase.
    IPR019798. Ser_HO-MeTrfase_PLP_BS.
    [Graphical view ]
    PANTHERi PTHR11680. PTHR11680. 1 hit.
    Pfami PF00464. SHMT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000412. SHMT. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00096. SHMT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
      Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
      PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FSC 198.

    Entry informationi

    Entry nameiGLYA_FRAT1
    AccessioniPrimary (citable) accession number: Q14GZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

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

    External Data

    Dasty 3