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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: tetrahydrofolate interconversion

This protein is involved in the pathway tetrahydrofolate interconversion, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolate interconversion and in One-carbon metabolism.

Pathwayi: glycine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes glycine from L-serine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Serine hydroxymethyltransferase (glyA)
This subpathway is part of the pathway glycine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycine from L-serine, the pathway glycine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei36Pyridoxal phosphateUniRule annotation1
Binding sitei56Pyridoxal phosphateUniRule annotation1
Binding sitei58SubstrateUniRule annotation1
Binding sitei65SubstrateUniRule annotation1
Binding sitei66Pyridoxal phosphateUniRule annotation1
Binding sitei100Pyridoxal phosphateUniRule annotation1
Binding sitei122Substrate; via carbonyl oxygenUniRule annotation1
Binding sitei176Pyridoxal phosphateUniRule annotation1
Binding sitei204Pyridoxal phosphateUniRule annotation1
Binding sitei229Pyridoxal phosphateUniRule annotation1
Binding sitei236Pyridoxal phosphateUniRule annotation1
Binding sitei263Pyridoxal phosphate; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei363Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000062501 – 417Serine hydroxymethyltransferaseAdd BLAST417

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei230N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ14GZ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 128Substrate bindingUniRule annotation3
Regioni355 – 357Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the SHMT family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000239404.
KOiK00600.
OMAiAAWANVQ.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
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.
RefSeqiWP_003021543.1. 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.
RefSeqiWP_003021543.1. NC_008245.1.

3D structure databases

ProteinModelPortaliQ14GZ5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000239404.
KOiK00600.
OMAiAAWANVQ.

Enzyme and pathway databases

UniPathwayiUPA00193.
UPA00288; UER01023.

Family and domain databases

CDDicd00378. SHMT. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT. 1 hit.
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...

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: November 2, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

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 one 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.