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A9KSH6 (GLYA_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Cphy_3274
OrganismClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]
Taxonomic identifier357809 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length412 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 – 412412Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000369913

Regions

Region124 – 1263Substrate binding By similarity

Sites

Binding site341Pyridoxal phosphate By similarity
Binding site541Pyridoxal phosphate By similarity
Binding site561Substrate By similarity
Binding site631Substrate binding By similarity
Binding site641Pyridoxal phosphate By similarity
Binding site1201Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3611Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KSH6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 903EA4D4CED4D70A

FASTA41244,730
        10         20         30         40         50         60 
MYSFEDIKVF DPELADSITM EIARQNDHIE LIASENFVSK AVMAAMGSPL TNKYAEGYPG 

        70         80         90        100        110        120 
KRYYGGCEFV DIAENLAIER AKKLFGCTYA NVQPHSGAQA NMAVFFALLQ PGDTVMGMNL 

       130        140        150        160        170        180 
AHGGHLTHGS PVNFSGSYFN IVPYGVDDNG FIDYEEVEKI AKECKPKLIV AGASAYARKI 

       190        200        210        220        230        240 
DFKRFREIAD LVGAYLMVDM AHIAGLVAAG YHQSPIPYAH VTTTTTHKTL RGPRGGMILS 

       250        260        270        280        290        300 
SEEFAEEHKL NKSIFPGTQG GPLMHVIAAK AICFKEALDD SFKDYAGKII SNAGALANEL 

       310        320        330        340        350        360 
TARGFNLVSG GTDNHLMLID LQNMNITGKE AEHILDEANI TCNKNTVPND PASPFVTSGI 

       370        380        390        400        410 
RLGTPAITTR GFNEKDMAVV AEAISLVVKD VDKNKEQAKA LVKMLTDAYP LY

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References

[1]"Complete genome sequence of Clostridium phytofermentans ISDg."
Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. expand/collapse author list , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000885 Genomic DNA. Translation: ABX43628.1.
RefSeqYP_001560367.1. NC_010001.1.

3D structure databases

ProteinModelPortalA9KSH6.
SMRA9KSH6. Positions 11-407.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9KSH6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5741553.
GenomeReviewsGene locus Cphy_3274 in contig CP000885_GR.
KEGGcpy:Cphy_3274.
PATRIC19506398. VBICloPhy16213_3422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMADIAHTAG.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycCPHY357809:CPHY_3274-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_CLOPH
AccessionPrimary (citable) accession number: A9KSH6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 34 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents