Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0IDD8 (GLYA_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:
Pyridoxal-phosphate-dependent serine hydroxymethyltransferase

Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:sync_0300
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate serving as the one-carbon carrier By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_00051

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_00051

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00051.

Sequence similarities

Belongs to the SHMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006339

Regions

Region130 – 1323Substrate binding By similarity

Sites

Binding site401Pyridoxal phosphate By similarity
Binding site601Pyridoxal phosphate By similarity
Binding site621Substrate By similarity
Binding site691Substrate binding By similarity
Binding site701Pyridoxal phosphate By similarity
Binding site1261Substrate By similarity
Binding site1811Pyridoxal phosphate By similarity
Binding site2091Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2411Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3671Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2351N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0IDD8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: AAD67F3BFD82EFF8

FASTA42946,185
        10         20         30         40         50         60 
MTDRSAAPIN ASLKAADPAI AGLIDQEQMR QETHLELIAS ENFTSKAVME AQGSVLTNKY 

        70         80         90        100        110        120 
AEGLPHKRYY GGCEHVDAIE ELAITRAKQL FGAAWANVQP HSGAQANFAV FLALLQPGDT 

       130        140        150        160        170        180 
ILGMDLSHGG HLTHGSPVNV SGKWFNVVQY GVDKETQRLD MEAIRKLALE HKPKLIICGY 

       190        200        210        220        230        240 
SAYPRSIDFA AFRSIADEVG AYLLADMAHI AGLVAAGVHA SPVPHCDVVT TTTHKTLRGP 

       250        260        270        280        290        300 
RGGLILCRDA EFARRFDKAV FPGSQGGPLE HVIAAKAVAF GEALQPDFKA YSRQVVANAQ 

       310        320        330        340        350        360 
ALAARLQERK IDVVSGGTDN HVVLLDLRSI GMTGKVADLL VSDVHITANK NTVPFDPESP 

       370        380        390        400        410        420 
FVTSGLRLGT AALTTRGFDE KAFHEVADVI ADRLQNPEDD AIQARCLERV SDLCKRFPLY 


APALEPALA 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed: 16938853] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI46562.1.
RefSeqYP_729534.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0IDD8.
SMRQ0IDD8. Positions 13-413.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0IDD8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4259129.
GenomeReviewsGene locus sync_0300 in contig CP000435_GR.
KEGGsyg:sync_0300.
PATRIC23791454. VBISynSp88089_0309.
TIGRsync_0300.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGTSNHLM.
PhylomeDBQ0IDD8.
ProtClustDBPRK00011.

Family and domain databases

HAMAPMF_00051. SHMT.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00600.
PANTHERPTHR11680. Gly_HO-Metrfase. 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_SYNS3
AccessionPrimary (citable) accession number: Q0IDD8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 41 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