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Q46HB6 (GLYA_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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

Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:PMN2A_1624
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length411 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 – 411411Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000234999

Regions

Region117 – 1193Substrate binding By similarity

Sites

Binding site271Pyridoxal phosphate By similarity
Binding site471Pyridoxal phosphate By similarity
Binding site491Substrate By similarity
Binding site561Substrate binding By similarity
Binding site571Pyridoxal phosphate By similarity
Binding site1131Substrate By similarity
Binding site1681Pyridoxal phosphate By similarity
Binding site1961Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2541Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3541Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2221N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46HB6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D3169D5EBFFB0410

FASTA41144,723
        10         20         30         40         50         60 
MKCDPSIAKL INNELSRQET HLELIASENF ASKAVMEAQG SVLTNKYAEG LPNKRYYGGC 

        70         80         90        100        110        120 
EYVDGVEQLA IDRAKNLFGA NWANVQPHSG AQANFAVFLS LLKPGDTIMG MDLSHGGHLT 

       130        140        150        160        170        180 
HGSPVNVSGK WFKTCHYEVD KKTEMLDMDA IRKKAIENQP KLIICGFSAY PRKIDFKAFR 

       190        200        210        220        230        240 
SIADEVNAYL LADIAHIAGL VASGLHPSPI PYCDVVTTTT HKTLRGPRGG LILSKDKEIG 

       250        260        270        280        290        300 
KKLDKAVFPG TQGGPLEHVI AAKAVAFKEA SAPEFKIYSQ KVISNAKVLS NQLQKRGISI 

       310        320        330        340        350        360 
VSKGTDNHIV LLDLRSIGMT GKVADQLVSD IKITANKNTV PFDPESPFVT SGLRLGSAAL 

       370        380        390        400        410 
TTRGFNEQAF GDVGNVIADR LLNPNDEDIK EKSINKVSEL CNKFPLYSEN I 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59112.1.
RefSeqYP_292815.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46HB6.
SMRQ46HB6. Positions 2-392.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ46HB6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3607023.
GenomeReviewsGene locus PMN2A_1624 in contig CP000095_GR.
KEGGpmn:PMN2A_1624.
PATRIC23022731. VBIProMar14922_0323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMANRGINIV.
PhylomeDBQ46HB6.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycPMAR59920:PMN2A_1624-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_PROMT
AccessionPrimary (citable) accession number: Q46HB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 45 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