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Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 5'-phosphateUniRule 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
Complete GO annotation...

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 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm 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 – 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.
OMAiAAWANVQ.
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

        10         20         30         40         50
MFSFEKNSLK NTDKEIFDAI ELEVKRQHEH VELIASENYA SPAVMEAQGS
60 70 80 90 100
QLTNKYAEGY HGKRYYGGCE FVDIAEKLAI ERAQQLFGVD YANVQPHSGS
110 120 130 140 150
QANAAVYNAV LKPGDTVLGM DLGAGGHLTH GSKVNFSGKI YNSIQYGLDE
160 170 180 190 200
NGDIDYKQVA QLAKEHKPKM IIAGFSAFSG IINWQKFREI ADSVDAVLMA
210 220 230 240 250
DIAHVAGLVA AGVYPNPFPY VYVATTTTHK TLRGPRGGLI LCNNNPELAK
260 270 280 290 300
KFQSAIFPGI QGGPLMHVIA AKAVAFKEAL EPSFVDYQKQ VLKNAKAMEK
310 320 330 340 350
VLKQRGINII SGGTSNHLLL LDITNTGFSG KEAEAALGRA NITVNKNSIP
360 370 380 390 400
NDPRSPFVTS GLRIGSPAIT TRGFKEKECE LVANLLADVV FNCGDEKVEN
410
ETAAKVLDLC DKFPVYK
Length:417
Mass (Da):45,316
Last modified:August 22, 2006 - v1
Checksum:i419A2B83E0C8DB03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL09257.1.
RefSeqiYP_667331.1. NC_008245.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286280 Genomic DNA. Translation: CAL09257.1.
RefSeqiYP_667331.1. NC_008245.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi393115.FTF1241.

Proteomic databases

PRIDEiQ14GZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0112.
HOGENOMiHOG000239404.
KOiK00600.
OMAiAAWANVQ.
OrthoDBiEOG6Z0QB2.

Enzyme and pathway databases

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

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

  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: April 29, 2015
This is version 63 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

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.