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Q2RVA2 (GLYA1_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 1
Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Ordered Locus Names:Rru_A1142
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

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 1
PRO_0000235015

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
Q2RVA2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: DB5DBEBEB26652E3

FASTA43445,849
        10         20         30         40         50         60 
MEASVAPPAL RNAPCAGVNA ACLSAADDAV AIAIAQETTR QRESIELIAS ENFVSKAVLE 

        70         80         90        100        110        120 
AQGSVLTNKY AEGYPQRRYY GGCANVDRVE DLAIARLNQL FGSTYANVQP HSGSQANQAV 

       130        140        150        160        170        180 
FLALLAPGDT ILGLDLKAGG HLTHGAPVNI SGRWFTAVSY GVDPRTHLID MEQMADLARR 

       190        200        210        220        230        240 
HRPKLLIAGG SAYPRLLDFA RFRQIADEVG AILMVDMAHF AGLVAGGVYP SPVPFADVIT 

       250        260        270        280        290        300 
STTHKTLRGP RGGFVLTNDA AIAKKINSAV FPGLQGGPLM HIIAAKAVAF GEALDPSFKI 

       310        320        330        340        350        360 
YARRVVENCR VLAQTLLDGG LAITSGGTDC HLAVVDLRPL GVTGTIAEQA LESIGITLNK 

       370        380        390        400        410        420 
NAIPNDPEKP MVTSGIRVGS AAGTSRGFGP EEYRRIAALI LETLHAVRAG TLEADREGIR 

       430 
TRVRSLVAGF PLPY

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / NCIB 8255.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000230 Genomic DNA. Translation: ABC21943.1.
RefSeqYP_426230.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RVA2.
SMRQ2RVA2. Positions 27-433.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2RVA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3834652.
GenomeReviewsGene locus Rru_A1142 in contig CP000230_GR.
KEGGrru:Rru_A1142.
NMPDRfig|1085.1.peg.3228.
PATRIC23325888. VBIRhoRub82919_1202.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAVMTSTTH.
PhylomeDBQ2RVA2.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycRRUB269796:RRU_A1142-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 nameGLYA1_RHORT
AccessionPrimary (citable) accession number: Q2RVA2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 47 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

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