Skip Header

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

Q6N693 (GLYA1_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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 1

Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Ordered Locus Names:RPA2724
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length432 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 – 432432Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 1
PRO_0000113651

Regions

Region135 – 1373Substrate binding By similarity

Sites

Binding site451Pyridoxal phosphate By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site671Substrate By similarity
Binding site741Substrate binding By similarity
Binding site751Pyridoxal phosphate By similarity
Binding site1091Pyridoxal phosphate By similarity
Binding site1311Substrate By similarity
Binding site1861Pyridoxal phosphate By similarity
Binding site2141Pyridoxal phosphate By similarity
Binding site2391Pyridoxal phosphate By similarity
Binding site2461Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6N693 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 25FBBB1820357471

FASTA43246,185
        10         20         30         40         50         60 
MSTANPASAP DSFFSASLEQ ADPEIAAAIR GELGRQRHEV ELIASENIVS RAVLEAQGSV 

        70         80         90        100        110        120 
MTNKYAEGYP GNRYYGGCEF VDVAENLAID RAKKLFGANF ANVQPNSGSQ MNQAVFLALL 

       130        140        150        160        170        180 
QPGDTFMGLD LAAGGHLTHG APVNMSGKWF KPVHYTVRRE DQMIDMDAVA KLAEEAKPKL 

       190        200        210        220        230        240 
IIAGGSAYPR AWDFKRFREI ADSVGAYFMV DMAHFAGLVA GGVHASPVPH AHVTTTTTHK 

       250        260        270        280        290        300 
SLRGPRGGLI LTNDEALAKK FNSAIFPGLQ GGPLMHVIAA KAVAFKEALQ PDFKVYTKNV 

       310        320        330        340        350        360 
VENAKALAET LRSAGFDLVS GGTDNHLMLV DLRPKGLKGN VSEKALVRAG ITCNKNGIPF 

       370        380        390        400        410        420 
DPEKPFVTSG LRLGTPAATT RGFGVAEFQQ VGHLIAEVLN AIAQSSDGAA PLVEASVKQR 

       430 
VKELTDRFPI YQ 

« Hide

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
BX572601 Genomic DNA. Translation: CAE28166.1.
RefSeqNP_948067.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ6N693.
SMRQ6N693. Positions 18-426.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2693455.
GenomeReviewsGene locus RPA2724 in contig BX571963_GR.
KEGGrpa:RPA2724.
NMPDRfig|258594.1.peg.2710.
PATRIC23289865. VBIRhoPal84835_2860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAIFNAGYA.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycRPAL258594:RPA2724-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_RHOPA
AccessionPrimary (citable) accession number: Q6N693
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 54 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