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Q6N622 (GLYA2_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:
Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2

Short name=SHMT 2
Short name=Serine methylase 2
EC=2.1.2.1
Gene names
Name:glyA2
Ordered Locus Names:RPA2796
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length434 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 – 434434Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000113652

Regions

Region140 – 1423Substrate binding By similarity

Sites

Binding site501Pyridoxal phosphate By similarity
Binding site701Pyridoxal phosphate By similarity
Binding site721Substrate By similarity
Binding site791Substrate binding By similarity
Binding site801Pyridoxal phosphate By similarity
Binding site1141Pyridoxal phosphate By similarity
Binding site1361Substrate By similarity
Binding site1911Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3771Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6N622 [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. NC_005296.1.

3D structure databases

ProteinModelPortalQ6N622.
SMRQ6N622. Positions 27-419.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2693327.
GenomeReviewsGene locus RPA2796 in contig BX571963_GR.
KEGGrpa:RPA2796.
NMPDRfig|258594.1.peg.2782.
PATRIC23290013. VBIRhoPal84835_2933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMADICADIR.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycRPAL258594:RPA2796-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 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: January 25, 2012
This is version 53 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