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P0A825

- GLYA_ECOLI

UniProt

P0A825 - GLYA_ECOLI

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Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Pyridoxal phosphate.

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

  1. glycine hydroxymethyltransferase activity Source: EcoCyc
  2. identical protein binding Source: IntAct
  3. pyridoxal phosphate binding Source: EcoCyc
  4. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. glycine biosynthetic process from serine Source: EcoCyc
  2. glycine catabolic process Source: EcoCyc
  3. L-serine catabolic process Source: EcoCyc
  4. 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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10408. glyA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. 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 – 114
Helixi13 – 2816
Beta strandi29 – 313
Helixi41 – 477
Helixi50 – 534
Beta strandi62 – 665
Helixi69 – 8618
Beta strandi89 – 924
Helixi98 – 10912
Beta strandi115 – 1195
Turni121 – 1244
Helixi127 – 1293
Helixi135 – 1395
Beta strandi140 – 1456
Beta strandi149 – 1524
Helixi155 – 16511
Beta strandi168 – 1736
Helixi183 – 19210
Beta strandi196 – 2005
Turni202 – 2043
Helixi205 – 2095
Turni217 – 2193
Beta strandi220 – 22910
Beta strandi237 – 2437
Helixi246 – 25611
Turni257 – 2604
Helixi266 – 27813
Helixi282 – 30423
Helixi310 – 3123
Beta strandi315 – 3228
Helixi324 – 3263
Helixi330 – 33910
Turni356 – 3583
Beta strandi360 – 3656
Helixi367 – 3715
Helixi376 – 39116
Turni392 – 3943
Helixi396 – 41217
Beta strandi415 – 4173

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDANNPAV.
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:
EMBL
GenBank
DDBJ
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.
YP_490779.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75604; AAC75604; b2551.
BAA16459; BAA16459; BAA16459.
GeneIDi12932320.
947022.
KEGGiecj:Y75_p2504.
eco:b2551.
PATRICi32120501. VBIEscCol129921_2653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A00559. XYECS.
RefSeqi NP_417046.1. NC_000913.3.
YP_490779.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DFO X-ray 2.40 A/B/C/D 1-417 [» ]
1EQB X-ray 2.70 A/B/C/D 1-417 [» ]
3G8M X-ray 3.30 A 1-417 [» ]
ProteinModelPortali P0A825.
SMRi P0A825. Positions 1-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36205N.
IntActi P0A825. 7 interactions.
MINTi MINT-7293373.
STRINGi 511145.b2551.

2D gel databases

SWISS-2DPAGE P0A825.

Proteomic databases

PaxDbi P0A825.
PRIDEi P0A825.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75604 ; AAC75604 ; b2551 .
BAA16459 ; BAA16459 ; BAA16459 .
GeneIDi 12932320.
947022.
KEGGi ecj:Y75_p2504.
eco:b2551.
PATRICi 32120501. VBIEscCol129921_2653.

Organism-specific databases

EchoBASEi EB0403.
EcoGenei EG10408. glyA.

Phylogenomic databases

eggNOGi COG0112.
HOGENOMi HOG000239404.
InParanoidi P0A825.
KOi K00600.
OMAi DANNPAV.
OrthoDBi EOG6Z0QB2.
PhylomeDBi P0A825.

Enzyme and pathway databases

UniPathwayi UPA00193 .
UPA00288 ; UER01023 .
BioCyci EcoCyc:GLYOHMETRANS-MONOMER.
ECOL316407:JW2535-MONOMER.
MetaCyc:GLYOHMETRANS-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A825.
PROi P0A825.

Gene expression databases

Genevestigatori P0A825.

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

« 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: October 29, 2014
This is version 92 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