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Protein

Serine hydroxymethyltransferase

Gene

glyA

Organism
Synechococcus sp. (strain WH8102)
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 sitei40 – 401Pyridoxal phosphateUniRule annotation
Binding sitei60 – 601Pyridoxal phosphateUniRule annotation
Binding sitei62 – 621SubstrateUniRule annotation
Binding sitei69 – 691SubstrateUniRule annotation
Binding sitei70 – 701Pyridoxal phosphateUniRule annotation
Binding sitei126 – 1261Substrate; via carbonyl oxygenUniRule annotation
Binding sitei181 – 1811Pyridoxal phosphateUniRule annotation
Binding sitei209 – 2091Pyridoxal phosphateUniRule annotation
Binding sitei234 – 2341Pyridoxal phosphateUniRule annotation
Binding sitei241 – 2411Pyridoxal phosphateUniRule annotation
Binding sitei267 – 2671Pyridoxal phosphate; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei367 – 3671Pyridoxal 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

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:SYNW0259
OrganismiSynechococcus sp. (strain WH8102)
Taxonomic identifieri84588 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001422 Componenti: Chromosome

Subcellular locationi

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 – 429429Serine hydroxymethyltransferasePRO_0000113682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei235 – 2351N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi84588.SYNW0259.

Structurei

3D structure databases

ProteinModelPortaliQ7U9J7.
SMRiQ7U9J7. Positions 11-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 1323Substrate bindingUniRule annotation
Regioni359 – 3613Substrate 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.

Q7U9J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSTASSIN KGLAAADPAI AALIEKEQQR QETHLELIAS ENFASRAVMD
60 70 80 90 100
AQGSVLTNKY AEGLPSKRYY GGCEHVDAIE ELAIERAKEL FGAAWANVQP
110 120 130 140 150
HSGAQANFAV FLALLQPGDT IMGLDLSHGG HLTHGSPVNV SGKWFNVVQY
160 170 180 190 200
GVDRETQRLD MEAIRQLALE HKPKLIVCGF SAYPRTIDFA AFRAIADEVG
210 220 230 240 250
AFLLADMAHI AGLVAAGVHP SPVPHCDVVT TTTHKTLRGP RGGLILCRDA
260 270 280 290 300
DFAKKFDKAV FPGSQGGPLE HVIAAKAVAF GEALQPAFKT YSQHVVANAA
310 320 330 340 350
ALAERLIARG IDVVSGGTDN HVVLLDLRSV GMTGKVADLL VSDVHITANK
360 370 380 390 400
NTVPFDPESP FVTSGLRLGT AALTTRGFDA GAFREVADVI ADRLLNPEDD
410 420
AVQQQCLRRV EALCQRFPLY AAARQPALA
Length:429
Mass (Da):45,756
Last modified:September 30, 2003 - v1
Checksum:i8177A683A10E3D6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX569689 Genomic DNA. Translation: CAE06774.1.
RefSeqiNP_896354.1. NC_005070.1.
WP_011127135.1. NC_005070.1.

Genome annotation databases

KEGGisyw:SYNW0259.
PATRICi23831899. VBISynSp27240_0262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX569689 Genomic DNA. Translation: CAE06774.1.
RefSeqiNP_896354.1. NC_005070.1.
WP_011127135.1. NC_005070.1.

3D structure databases

ProteinModelPortaliQ7U9J7.
SMRiQ7U9J7. Positions 11-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi84588.SYNW0259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGisyw:SYNW0259.
PATRICi23831899. VBISynSp27240_0262.

Phylogenomic databases

eggNOGiCOG0112.
HOGENOMiHOG000239404.
KOiK00600.
OMAiAAWANVQ.
OrthoDBiEOG6Z0QB2.

Enzyme and pathway databases

UniPathwayiUPA00193.
UPA00288; UER01023.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH8102.

Entry informationi

Entry nameiGLYA_SYNPX
AccessioniPrimary (citable) accession number: Q7U9J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 25, 2004
Last sequence update: September 30, 2003
Last modified: March 31, 2015
This is version 78 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, Reference 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.