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B7GMG4 (GLYA_ANOFW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 33. 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:Aflv_2713
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP]
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Anoxybacillus ›

Protein attributes

Sequence length413 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. HAMAP-Rule MF_00051

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. HAMAP-Rule MF_00051

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00051.

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 – 413413Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_0000369898

Regions

Region123 – 1253Substrate binding By similarity
Region351 – 3533Substrate 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 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
B7GMG4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 4B6CDFA4CAFF5C39

FASTA41345,352
        10         20         30         40         50         60 
MSMSRLSQQD PQVFQAIQDE LKRQQTKIEL IASENFVSEA VMEAQGSVLT NKYAEGYPGR 

        70         80         90        100        110        120 
RYYGGCEHVD VVEELARERA KQLFGAEHAN VQPHSGAQAN MAVYFTILQH GDTVLGMNLS 

       130        140        150        160        170        180 
HGGHLTHGSP VNFSGIQYNF IEYGVDPETH RINYDDVREK ALKHKPKLIV AGASAYPRTI 

       190        200        210        220        230        240 
DFAKFREIAD EVGAYFMVDM AHIAGLVAAG LHPNPVPYAH FVTTTTHKTL RGPRGGMILC 

       250        260        270        280        290        300 
QEQFAKQIDK AIFPGIQGGP LMHVIAAKAV ALGEALQDDF KTYAQNIVNN AKRLAEALVA 

       310        320        330        340        350        360 
EGFTLVSGGT DNHLLLIDLR SIGLTGKVAE KVLDEIGITV NKNTIPYDPE SPFVTSGIRI 

       370        380        390        400        410 
GTAAVTSRGF GLEEMDEIAR IISIALKHKD DEQKLDEARR RVAALTEKFP LYV

« Hide

References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:R161.1-R161.16(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21510 / WK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000922 Genomic DNA. Translation: ACJ35066.1.
RefSeqYP_002317051.1. NC_011567.1.

3D structure databases

ProteinModelPortalB7GMG4.
ModBaseSearch...

Protein-protein interaction databases

STRING491915.Aflv_2713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ35066; ACJ35066; Aflv_2713.
GeneID7038986.
KEGGafl:Aflv_2713.
PATRIC20957424. VBIAnoFla45531_2797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239403.
KOK00600.
OMAFRRGVRS.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycAFLA491915:GHEO-2802-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_ANOFW
AccessionPrimary (citable) accession number: B7GMG4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 33 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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