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Reviewed, UniProtKB/Swiss-Prot Q6N622 (GLYA2_RHOPA)

Last modified February 9, 2010. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine hydroxymethyltransferase 2
      Short name=Serine methylase 2
      Short name=SHMT 2
    EC=2.1.2.1
Gene names
Name: glyA2
Ordered Locus Names: RPA2796
OrganismRhodopseudomonas palustris [Complete proteome] [HAMAP]
Taxonomic identifier1076 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Interconversion of serine and glycine. HAMAP MF_00051

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00051

Subcellular location

Cytoplasm By similarity HAMAP MF_00051.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine metabolic process

Inferred from electronic annotation. Source: InterPro

glycine metabolic process

Inferred from electronic annotation. Source: InterPro

one-carbon metabolic process

Inferred from electronic annotation. Source: HAMAP

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Serine hydroxymethyltransferase 2 HAMAP MF_00051
PRO_0000113652

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6N622-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3477D211B1B1EE1C

FASTA43445,360
        10         20         30         40         50         60 
MGPSVAPHAV HTIANPGVSA AGLVAADHAV AAAIADEETR QRDSIELIAS ENFVSRAVLD 

        70         80         90        100        110        120 
AQGSVLTNKY AEGYPHRRYY GGCANVDAIE DLVIARVNQL FGSAYANVQP HSGSQANQAV 

       130        140        150        160        170        180 
FLALLAPGDT ILGLDLKAGG HLTHGAPVNM SGRWFKAVSY GVDPETHRID MDQVAVQARQ 

       190        200        210        220        230        240 
HRPRLLIAGG SAYPRIIDFG RFRQIADEVG AILMVDMAHF AGLVAGGVYP SPVPFADVVT 

       250        260        270        280        290        300 
STTHKTLRGP RGGFVLTNDA NIAKKINSAT FPGLQGGPLM HVIAAKAVAF GEALQPEFGA 

       310        320        330        340        350        360 
YAQAVVENCR VLAQALADGG LTITSGGTDC HLAVVDLRPF GVTGNIAEQA LESVGITLNK 

       370        380        390        400        410        420 
NAIPNDPEKP MVTSGIRVGT AAGTSRGFGA DQYREIAGLV LETLHAVRAG TLDAAGQEIN 

       430 
KSVRRLAASF PLPY 

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References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed: 14704707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572602 Genomic DNA. Translation: CAE28238.1.
RefSeqNP_948139.1.

3D structure databases

SMRQ6N622. Positions 27-419.
ModBaseSearch...

Genome annotation databases

GeneID2693327.
KEGGrpa:RPA2796.
NMPDRfig|258594.1.peg.2782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAVTMSGKW.

Enzyme and pathway databases

BioCycRPAL258594:RPA2796-MONOMER.
BRENDA2.1.2.1. 373.

Family and domain databases

HAMAPMF_00051_B. SHMT_B.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11680. Gly_HO-Metrfase. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA2_RHOPA
AccessionPrimary (citable) accession number: Q6N622
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents