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A5N7P5 (GLYA_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine hydroxymethyltransferase
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:CKL_1284
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium ›

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00051

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
One-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine biosynthetic process from serine

Inferred from electronic annotation. Source: HAMAP

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglycine hydroxymethyltransferase activity

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_1000074891

Regions

Region123 – 1253Substrate binding By similarity

Sites

Binding site331Pyridoxal phosphate By similarity
Binding site531Pyridoxal phosphate By similarity
Binding site551Substrate By similarity
Binding site621Substrate By similarity
Binding site631Pyridoxal phosphate By similarity
Binding site971Pyridoxal phosphate By similarity
Binding site1191Substrate; via carbonyl oxygen By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2591Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3591Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5N7P5 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 626466A21D11E446

FASTA41145,809
        10         20         30         40         50         60 
MDFNELKNTD KDIYGIIEEE WERQKNGIEL IASENFTSKS VMEAMGSFLT NKYAEGYPGK 

        70         80         90        100        110        120 
RYYGGCYIVD KAEDLARDRM KKLFNAEHVN VQPHSGSQAN MAVYMSVLKP GDTVLGMSLN 

       130        140        150        160        170        180 
HGGHLTHGSK VSFSGKLYNF VSYGLNSDTE IIDYDEMREL ALKHKPKMIV SGASAYPRKI 

       190        200        210        220        230        240 
DFKKIREICD EVGAYMMVDM AHIAGIIAAG RHESPVPYAD FVTTTTHKTL RGPRGGAIIC 

       250        260        270        280        290        300 
KEKYGAALDK TIFPGIQGGP LMHIIAAKAV CFGEALKDEY KEYIDQIIKN AKVFGEELVK 

       310        320        330        340        350        360 
YGFRLVSGGT DNHLLLVDLT NKNITGKDLE ELLDKVNITV NKNAIPFDKL KPNVTSGIRV 

       370        380        390        400        410 
GTPAVTTRGF KEEEMKKVAY FINKAVENRE GDLSAIKREV IELCEAFPLY E

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000673 Genomic DNA. Translation: EDK33326.1.
RefSeqYP_001394674.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N7P5.
SMRA5N7P5. Positions 6-388.
ModBaseSearch...

Protein-protein interaction databases

STRING431943.CKL_1284.

Proteomic databases

PRIDEA5N7P5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEDK33326; EDK33326; CKL_1284.
GeneID5392545.
KEGGckl:CKL_1284.
PATRIC19464019. VBICloKlu111549_1344.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAIAKLQWA.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycCKLU431943:GJF1-1284-MONOMER.
UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. 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]
PANTHERPTHR11680. PTHR11680. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_CLOK5
AccessionPrimary (citable) accession number: A5N7P5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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