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Q2W4T2 (GLYA_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:amb2339
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Magnetospirillum ›

Protein attributes

Sequence length427 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 – 427427Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_0000234985

Regions

Region131 – 1333Substrate binding By similarity

Sites

Binding site411Pyridoxal phosphate By similarity
Binding site611Pyridoxal phosphate By similarity
Binding site631Substrate By similarity
Binding site701Substrate By similarity
Binding site711Pyridoxal phosphate By similarity
Binding site1051Pyridoxal phosphate By similarity
Binding site1271Substrate; via carbonyl oxygen By similarity
Binding site1821Pyridoxal phosphate By similarity
Binding site2101Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2421Pyridoxal phosphate By similarity
Binding site2681Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3681Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2W4T2 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 871C5B053691AFCA

FASTA42745,736
        10         20         30         40         50         60 
MSSAPTDAFF RTPLSERDPE VFAAITQELK RQQDQIELIA SENIVSRAVL EAQGSVMTNK 

        70         80         90        100        110        120 
YAEGYPGKRY YGGCEFVDIA ESLAISRACQ IFGCSYANVQ PSSGSQANQG VFMALLQPGD 

       130        140        150        160        170        180 
TIMGMSLAAG GHLTHGAAPN QSGKWFKAVQ YGVRQQDSQI DFAEVEELAR THRPKLIIAG 

       190        200        210        220        230        240 
GSAYPRTIDF ARFRKIADEV GAFFMVDMAH FAGLVAGGVY PNPLPHAHVV TTTTHKTLRG 

       250        260        270        280        290        300 
PRGGMILSND ADIGKKINSA IFPGIQGGPL MHVIAGKAVA FGEALKPEFK LYAKQVVDNA 

       310        320        330        340        350        360 
RALADTLVRR GLDIVSGGTD SHLMLVDLRP KKLTGKAAEA SLEHAGMTCN KNGIPFDPEK 

       370        380        390        400        410        420 
PTITSGVRLG TPAATTRGFG VEEFKKVGEL IGDVLDGLAA NPEDNSAAEA RARAEVAELC 


RRFPIYQ

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP007255 Genomic DNA. Translation: BAE51143.1.
RefSeqYP_421702.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W4T2.
SMRQ2W4T2. Positions 14-413.
ModBaseSearch...

Protein-protein interaction databases

STRING342108.amb2339.

Proteomic databases

PRIDEQ2W4T2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE51143; BAE51143; amb2339.
GeneID3803877.
KEGGmag:amb2339.
PATRIC22438933. VBIMagMag129836_2309.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAQIDFARM.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-2366-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_MAGSA
AccessionPrimary (citable) accession number: Q2W4T2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 10, 2006
Last modified: May 1, 2013
This is version 58 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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