Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3MBD8 (GLYA_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:Ava_2076
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

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. 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: UniProtKB-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: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_0000234944

Regions

Region126 – 1283Substrate binding By similarity
Region355 – 3573Substrate binding By similarity

Sites

Binding site361Pyridoxal phosphate By similarity
Binding site561Pyridoxal phosphate By similarity
Binding site581Substrate By similarity
Binding site651Substrate By similarity
Binding site661Pyridoxal phosphate By similarity
Binding site1221Substrate; via carbonyl oxygen By similarity
Binding site1771Pyridoxal phosphate By similarity
Binding site2051Pyridoxal phosphate By similarity
Binding site2301Pyridoxal phosphate By similarity
Binding site2371Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2311N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MBD8 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 11EF119715721354

FASTA42746,272
        10         20         30         40         50         60 
MTRTNSDFLT NSDPAIAGLI NQELQRQRDH LELIASENFT SAAVLAAQGS VLTNKYAEGL 

        70         80         90        100        110        120 
PGKRYYGGCE FIDKIEQIAI DRAKQLFGAA HANVQPHSGA QANFAVFLTL LAPGDKIMGM 

       130        140        150        160        170        180 
DLSHGGHLTH GSPVNVSGKW FQVCHYGVSQ QTEQLDYDQI RELALRERPK LLICGYSAYP 

       190        200        210        220        230        240 
RIIDFEKFRS IADEVGAYLL ADIAHIAGLV ASGLHPDPIP YCHVVTTTTH KTLRGPRGGL 

       250        260        270        280        290        300 
ILTGDAELGK KLDKSVFPGS QGGPLEHVIA GKAVAFGEAL KPEFQGYSAQ VIENARALAN 

       310        320        330        340        350        360 
QLQNRGLKLV SDGTDNHLML VDLRSVNMTG KRADQLVSEV NITANKNTVP FDPQSPFVTS 

       370        380        390        400        410        420 
GLRLGSPAMT TRGMGEAEFT EIGNIIADRL LNPDSDTVAQ DCKRRVAALC DRFPLYPHLE 


IPVPVLA 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA21698.1.
RefSeqYP_322593.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3MBD8.
SMRQ3MBD8. Positions 8-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_2076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA21698; ABA21698; Ava_2076.
GeneID3680549.
KEGGava:Ava_2076.
PATRIC35424891. VBIAnaVar43351_3000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAMLIDLRN.
OrthoDBEOG6Z0QB2.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-2099-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. SSF53383. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_ANAVT
AccessionPrimary (citable) accession number: Q3MBD8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 25, 2005
Last modified: February 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways