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Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate.1 Publication

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=7 µM for tetrahydrofolate2 Publications
  2. KM=140 µM for serine2 Publications
  3. KM=300 µM for serine2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351Pyridoxal phosphate2 Publications
    Binding sitei55 – 551Pyridoxal phosphate2 Publications
    Sitei55 – 551Transaldimination and stability
    Binding sitei57 – 571Substrate
    Binding sitei64 – 641Substrate
    Binding sitei65 – 651Pyridoxal phosphate2 Publications
    Binding sitei99 – 991Pyridoxal phosphate2 Publications
    Binding sitei121 – 1211Substrate; via carbonyl oxygen
    Binding sitei175 – 1751Pyridoxal phosphate2 Publications
    Binding sitei203 – 2031Pyridoxal phosphate2 Publications
    Binding sitei228 – 2281Pyridoxal phosphate2 Publications
    Binding sitei235 – 2351Pyridoxal phosphate2 Publications
    Sitei235 – 2351Transaldimination and stability
    Binding sitei246 – 2461Substrate
    Binding sitei263 – 2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei363 – 3631Pyridoxal phosphate2 Publications

    GO - Molecular functioni

    • glycine hydroxymethyltransferase activity Source: EcoCyc
    • identical protein binding Source: IntAct
    • pyridoxal phosphate binding Source: EcoCyc
    • zinc ion binding Source: EcoliWiki

    GO - Biological processi

    • glycine biosynthetic process from serine Source: EcoCyc
    • glycine catabolic process Source: EcoCyc
    • L-serine catabolic process Source: EcoCyc
    • tetrahydrofolate interconversion Source: UniProtKB-UniPathway
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, One-carbon metabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:GLYOHMETRANS-MONOMER.
    ECOL316407:JW2535-MONOMER.
    MetaCyc:GLYOHMETRANS-MONOMER.
    BRENDAi2.1.2.1. 2026.
    4.1.2.48. 2026.
    UniPathwayiUPA00193.
    UPA00288; UER01023.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine hydroxymethyltransferase (EC:2.1.2.1)
    Short name:
    SHMT
    Short name:
    Serine methylase
    Gene namesi
    Name:glyA
    Ordered Locus Names:b2551, JW2535
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10408. glyA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551Y → F: 50 and 15-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 4-fold decrease in the catalytic efficiency. 1 Publication
    Mutagenesisi65 – 651Y → F: Decrease in catalytic activity. 1 Publication
    Mutagenesisi85 – 851L → A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-276. 1 Publication
    Mutagenesisi214 – 2141P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication
    Mutagenesisi214 – 2141P → G: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication
    Mutagenesisi216 – 2161P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. Alteration in the folding rate. 1 Publication
    Mutagenesisi216 – 2161P → G: Important decrease in affinity and catalytic efficiency. Severely compromised in folding into a catalytically competent enzyme. 1 Publication
    Mutagenesisi218 – 2181P → A: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication
    Mutagenesisi218 – 2181P → G: No significant difference in catalytic efficiency and affinity compared to the wild-type. 1 Publication
    Mutagenesisi235 – 2351R → K: 1500- and 20-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 15-fold decrease in the catalytic efficiency. 1 Publication
    Mutagenesisi235 – 2351R → L: 450- and 11-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 60-fold decrease in the catalytic efficiency. 1 Publication
    Mutagenesisi235 – 2351R → Q: 900- and 17-fold increase in the affinity for serine and tetrahydrofolate, respectively, and 30-fold decrease in the catalytic efficiency. 1 Publication
    Mutagenesisi258 – 2581P → A: Important decrease in affinity and catalytic efficiency. Reduced thermal stability. 1 Publication
    Mutagenesisi258 – 2581P → G: Important decrease in affinity and catalytic efficiency. 1 Publication
    Mutagenesisi264 – 2641P → A: Important decrease in affinity and catalytic efficiency. 1 Publication
    Mutagenesisi264 – 2641P → G: Important decrease in affinity and catalytic efficiency. 1 Publication
    Mutagenesisi276 – 2761L → A: Alteration of the dimer-monomer equilibrium accompanied by minor changes in the catalytic properties and whitout any significant change of tertiary structure. In the monomeric state; when associated with A-85. 1 Publication
    Mutagenesisi363 – 3631R → A: It does not bind serine and glycine and shows no activity with serine as the substrate. 1 Publication
    Mutagenesisi363 – 3631R → K: Exhibits only 0.03% of the catalytic activity of the wild-type and a 15-fold reduction in affinity for glycine and serine. 1 Publication
    Mutagenesisi372 – 3721R → A: No significant difference compared to the wild-type. 1 Publication
    Mutagenesisi372 – 3721R → K: No significant difference compared to the wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Serine hydroxymethyltransferasePRO_0000113573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541N6-acetyllysine1 Publication
    Modified residuei62 – 621N6-succinyllysine1 Publication
    Modified residuei229 – 2291N6-(pyridoxal phosphate)lysine
    Modified residuei242 – 2421N6-succinyllysine1 Publication
    Modified residuei250 – 2501N6-acetyllysine; alternate1 Publication
    Modified residuei250 – 2501N6-succinyllysine; alternate1 Publication
    Modified residuei277 – 2771N6-succinyllysine1 Publication
    Modified residuei285 – 2851N6-acetyllysine1 Publication
    Modified residuei293 – 2931N6-succinyllysine1 Publication
    Modified residuei331 – 3311N6-succinyllysine1 Publication
    Modified residuei346 – 3461N6-succinyllysine1 Publication
    Modified residuei354 – 3541N6-acetyllysine; alternate1 Publication
    Modified residuei354 – 3541N6-succinyllysine; alternate1 Publication
    Modified residuei375 – 3751N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A825.
    PRIDEiP0A825.

    2D gel databases

    SWISS-2DPAGEP0A825.

    Expressioni

    Inductioni

    By CsgD.1 Publication

    Gene expression databases

    GenevestigatoriP0A825.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-909080,EBI-909080

    Protein-protein interaction databases

    DIPiDIP-36205N.
    IntActiP0A825. 7 interactions.
    MINTiMINT-7293373.
    STRINGi511145.b2551.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Helixi13 – 2816Combined sources
    Beta strandi29 – 313Combined sources
    Helixi41 – 477Combined sources
    Helixi50 – 534Combined sources
    Beta strandi62 – 665Combined sources
    Helixi69 – 8618Combined sources
    Beta strandi89 – 924Combined sources
    Helixi98 – 10912Combined sources
    Beta strandi115 – 1195Combined sources
    Turni121 – 1244Combined sources
    Helixi127 – 1293Combined sources
    Helixi135 – 1395Combined sources
    Beta strandi140 – 1456Combined sources
    Beta strandi149 – 1524Combined sources
    Helixi155 – 16511Combined sources
    Beta strandi168 – 1736Combined sources
    Helixi183 – 19210Combined sources
    Beta strandi196 – 2005Combined sources
    Turni202 – 2043Combined sources
    Helixi205 – 2095Combined sources
    Turni217 – 2193Combined sources
    Beta strandi220 – 22910Combined sources
    Beta strandi237 – 2437Combined sources
    Helixi246 – 25611Combined sources
    Turni257 – 2604Combined sources
    Helixi266 – 27813Combined sources
    Helixi282 – 30423Combined sources
    Helixi310 – 3123Combined sources
    Beta strandi315 – 3228Combined sources
    Helixi324 – 3263Combined sources
    Helixi330 – 33910Combined sources
    Turni356 – 3583Combined sources
    Beta strandi360 – 3656Combined sources
    Helixi367 – 3715Combined sources
    Helixi376 – 39116Combined sources
    Turni392 – 3943Combined sources
    Helixi396 – 41217Combined sources
    Beta strandi415 – 4173Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DFOX-ray2.40A/B/C/D1-417[»]
    1EQBX-ray2.70A/B/C/D1-417[»]
    3G8MX-ray3.30A1-417[»]
    ProteinModelPortaliP0A825.
    SMRiP0A825. Positions 1-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A825.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni125 – 1273Substrate binding
    Regioni355 – 3573Substrate binding

    Sequence similaritiesi

    Belongs to the SHMT family.Curated

    Phylogenomic databases

    eggNOGiCOG0112.
    HOGENOMiHOG000239404.
    InParanoidiP0A825.
    KOiK00600.
    OMAiICAKLPV.
    OrthoDBiEOG6Z0QB2.
    PhylomeDBiP0A825.

    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.

    P0A825-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ
    60 70 80 90 100
    LTNKYAEGYP GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ
    110 120 130 140 150
    ANFAVYTALL EPGDTVLGMN LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT
    160 170 180 190 200
    GHIDYADLEK QAKEHKPKMI IGGFSAYSGV VDWAKMREIA DSIGAYLFVD
    210 220 230 240 250
    MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL AKGGSEELYK
    260 270 280 290 300
    KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE
    310 320 330 340 350
    VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP
    360 370 380 390 400
    NDPKSPFVTS GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE
    410
    RIKGKVLDIC ARYPVYA
    Length:417
    Mass (Da):45,317
    Last modified:July 21, 1986 - v1
    Checksum:i13E5558E99938539
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00283 Genomic DNA. Translation: CAA23547.1.
    U00096 Genomic DNA. Translation: AAC75604.1.
    AP009048 Genomic DNA. Translation: BAA16459.1.
    J01620 Genomic DNA. Translation: AAA23912.1.
    PIRiA00559. XYECS.
    RefSeqiNP_417046.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC75604; AAC75604; b2551.
    BAA16459; BAA16459; BAA16459.
    GeneIDi947022.
    KEGGiecj:Y75_p2504.
    eco:b2551.
    PATRICi32120501. VBIEscCol129921_2653.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    V00283 Genomic DNA. Translation: CAA23547.1.
    U00096 Genomic DNA. Translation: AAC75604.1.
    AP009048 Genomic DNA. Translation: BAA16459.1.
    J01620 Genomic DNA. Translation: AAA23912.1.
    PIRiA00559. XYECS.
    RefSeqiNP_417046.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DFOX-ray2.40A/B/C/D1-417[»]
    1EQBX-ray2.70A/B/C/D1-417[»]
    3G8MX-ray3.30A1-417[»]
    ProteinModelPortaliP0A825.
    SMRiP0A825. Positions 1-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-36205N.
    IntActiP0A825. 7 interactions.
    MINTiMINT-7293373.
    STRINGi511145.b2551.

    2D gel databases

    SWISS-2DPAGEP0A825.

    Proteomic databases

    PaxDbiP0A825.
    PRIDEiP0A825.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75604; AAC75604; b2551.
    BAA16459; BAA16459; BAA16459.
    GeneIDi947022.
    KEGGiecj:Y75_p2504.
    eco:b2551.
    PATRICi32120501. VBIEscCol129921_2653.

    Organism-specific databases

    EchoBASEiEB0403.
    EcoGeneiEG10408. glyA.

    Phylogenomic databases

    eggNOGiCOG0112.
    HOGENOMiHOG000239404.
    InParanoidiP0A825.
    KOiK00600.
    OMAiICAKLPV.
    OrthoDBiEOG6Z0QB2.
    PhylomeDBiP0A825.

    Enzyme and pathway databases

    UniPathwayiUPA00193.
    UPA00288; UER01023.
    BioCyciEcoCyc:GLYOHMETRANS-MONOMER.
    ECOL316407:JW2535-MONOMER.
    MetaCyc:GLYOHMETRANS-MONOMER.
    BRENDAi2.1.2.1. 2026.
    4.1.2.48. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP0A825.
    PROiP0A825.

    Gene expression databases

    GenevestigatoriP0A825.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-19.
      Strain: K12 / EMG2.
    6. "Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12."
      Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., Poole R.K.
      Mol. Gen. Genet. 226:49-58(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-17.
      Strain: K12.
    7. Cited for: PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Characterization of the Escherichia coli gene for serine hydroxymethyltransferase."
      Plamann M.D., Stauffer G.V.
      Gene 22:9-18(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7, FUNCTION AS A SERINE HYDROXYMETHYLTRANSFERASE.
    9. "The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase."
      Delle Fratte S., Iurescia S., Angelaccio S., Bossa F., Schirch V.
      Eur. J. Biochem. 225:395-401(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ARG-363 AND ARG-372.
    10. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    11. "Role of proline residues in the folding of serine hydroxymethyltransferase."
      Fu T.F., Boja E.S., Safo M.K., Schirch V.
      J. Biol. Chem. 278:31088-31094(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-214; PRO-216; PRO-218; PRO-258 AND PRO-264, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "CsgD, a regulator of curli and cellulose synthesis, also regulates serine hydroxymethyltransferase synthesis in Escherichia coli K-12."
      Chirwa N.T., Herrington M.B.
      Microbiology 149:525-535(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "The mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli apo-serine hydroxymethyltransferase."
      Malerba F., Bellelli A., Giorgi A., Bossa F., Contestabile R.
      Biochem. J. 404:477-485(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHANISM.
    14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-250; LYS-285; LYS-354 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    15. "The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase."
      Florio R., Chiaraluce R., Consalvi V., Paiardini A., Catacchio B., Bossa F., Contestabile R.
      FEBS J. 276:132-143(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LEU-85 AND LEU-276, SUBUNIT.
    16. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-62; LYS-242; LYS-250; LYS-277; LYS-293; LYS-331; LYS-346 AND LYS-354.
      Strain: K12.
    17. "Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase."
      Contestabile R., Angelaccio S., Bossa F., Wright H.T., Scarsdale N., Kazanina G., Schirch V.
      Biochemistry 39:7492-7500(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND PYRIDOXAL PHOSPHATE, MUTAGENESIS OF TYR-65.
    18. "Crystal structure at 2.4-A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate."
      Scarsdale J.N., Radaev S., Kazanina G., Schirch V., Wright H.T.
      J. Mol. Biol. 296:155-168(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
    19. "Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase."
      Vivoli M., Angelucci F., Ilari A., Morea V., Angelaccio S., di Salvo M.L., Contestabile R.
      Biochemistry 48:12034-12046(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF MUTANT PHE-55 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, MUTAGENESIS OF TYR-55 AND ARG-235, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGLYA_ECOLI
    AccessioniPrimary (citable) accession number: P0A825
    Secondary accession number(s): P00477
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: May 27, 2015
    This is version 96 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.