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A7GX48 (GLYA_CAMC5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Ccur92_04860
ORF Names:CCV52592_1350
OrganismCampylobacter curvus (strain 525.92) [Complete proteome] [HAMAP]
Taxonomic identifier360105 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter ›

Protein attributes

Sequence length414 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 – 414414Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_1000006229

Regions

Region120 – 1223Substrate binding By similarity
Region348 – 3503Substrate binding By similarity

Sites

Binding site301Pyridoxal phosphate By similarity
Binding site501Pyridoxal phosphate By similarity
Binding site521Substrate By similarity
Binding site591Substrate By similarity
Binding site601Pyridoxal phosphate By similarity
Binding site941Pyridoxal phosphate By similarity
Binding site1161Substrate; via carbonyl oxygen By similarity
Binding site1701Pyridoxal phosphate By similarity
Binding site1981Pyridoxal phosphate By similarity
Binding site2231Pyridoxal phosphate By similarity
Binding site2301Pyridoxal phosphate By similarity
Binding site2561Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3561Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2241N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GX48 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C2BBFEE1A8FE4D11

FASTA41445,400
        10         20         30         40         50         60 
MSLQSYDKEI FDLVNLELKR QCDHLEMIAS ENFTYPEVME VMGSILTNKY AEGYPGKRYY 

        70         80         90        100        110        120 
GGCEYVDGIE QLAIDRCKQL FGCEFANVQP NSGSQANQGV YGALLNPGDK ILGMDLSHGG 

       130        140        150        160        170        180 
HLTHGAKVSS SGKIYESFFY GVELDGRINY ERILDIAKIV KPKMIVCGAS AYTREIEFDK 

       190        200        210        220        230        240 
FRAIADEVGA LLFADVAHIA GLVVAGEHQN PFPHCDVVSS TTHKTLRGPR GGIIMTNNEE 

       250        260        270        280        290        300 
YAKKINASIF PGIQGGPLVH VIAAKAVGFK HNLSPEWKIY AKQVKANAKK LSEILISRGF 

       310        320        330        340        350        360 
DLVSGGTDNH LILMSFLNRE FSGKDADIAL GNAGITVNKN TVPGEKRSPF VTSGIRVGSP 

       370        380        390        400        410 
ALTARGMKEA EFEIIANKIA DVLSDINNTD LQEKIKAELK ELAHKFIIYD RATF

« Hide

References

[1]"Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 525.92.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000767 Genomic DNA. Translation: EAT99552.1.
RefSeqYP_001407790.1. NC_009715.1.

3D structure databases

ProteinModelPortalA7GX48.
SMRA7GX48. Positions 1-410.
ModBaseSearch...

Protein-protein interaction databases

STRING360105.CCV52592_1350.

Proteomic databases

PRIDEA7GX48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAT99552; EAT99552; CCV52592_1350.
GeneID5407183.
KEGGccv:CCV52592_1350.
PATRIC20031398. VBICamCur47627_0518.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAAICAKFP.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycCCUR360105:GJ9P-530-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_CAMC5
AccessionPrimary (citable) accession number: A7GX48
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: May 1, 2013
This is version 43 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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