Skip Header

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

A1WVG6 (GLYA_HALHL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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
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:Hhal_0902
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Halorhodospira

Protein attributes

Sequence length416 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 – 416416Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006261

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2621Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3621Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WVG6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0B09D53810C87A9B

FASTA41645,196
        10         20         30         40         50         60 
MFSRDMTIAG YDPELAAAIE DERQRQEDHI ELIASENYAS PRVMEAQGSV LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDVAEQLAID RAKQLFGADY ANVQPHSGSQ ANAAVFHALL KPGDTILGMS 

       130        140        150        160        170        180 
LDHGGHLTHG AKVNFSGKLF NAVQYGINDD GQIDYDEIQR LATEHQPKMV IGGFSAYSQV 

       190        200        210        220        230        240 
VDWARLRQIA DSVGAYLVVD MAHIAGLVAA GVYPSPIPHA DAVTSTTHKT LRGPRGGIIL 

       250        260        270        280        290        300 
ARSNPDLEKK FQSLVFPGTQ GGPLMHAIAG KAVAFKEALE PDFKQYQEQV VANARAMARR 

       310        320        330        340        350        360 
VIERGYNVVS GGTDNHLFLM DLTPKNLTGK DADAALGRAN ITVNKNTVPN DPQSPFVTSG 

       370        380        390        400        410 
LRIGTPAITT RGFKEAEATR LADWICDVLD NMGDESVVER VRGEVEQICR EFPVYG

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000544 Genomic DNA. Translation: ABM61678.1.
RefSeqYP_001002480.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WVG6.
SMRA1WVG6. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1WVG6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4709320.
GenomeReviewsGene locus Hhal_0902 in contig CP000544_GR.
KEGGhha:Hhal_0902.
PATRIC22096105. VBIHalHal112047_0896.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMANEADAST.
PhylomeDBA1WVG6.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycHHAL349124:HHAL_0902-MONOMER.

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_HALHL
AccessionPrimary (citable) accession number: A1WVG6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 38 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents