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Q824C8 (GLYA_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:CCA_00224
OrganismChlamydophila caviae [Complete proteome] [HAMAP]
Taxonomic identifier83557 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length497 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 – 497497Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000234965

Regions

Region180 – 1823Substrate binding By similarity

Sites

Binding site591Pyridoxal phosphate By similarity
Binding site791Pyridoxal phosphate By similarity
Binding site811Substrate By similarity
Binding site881Substrate binding By similarity
Binding site891Pyridoxal phosphate By similarity
Binding site1761Substrate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2601Pyridoxal phosphate By similarity
Binding site2881Pyridoxal phosphate By similarity
Binding site2951Pyridoxal phosphate By similarity
Binding site3191Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site4191Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2891N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q824C8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0022A8078019AE75

FASTA49754,205
        10         20         30         40         50         60 
MASLLHKFLE NASGKKGQDL ASTAYLAALD HLLHSFPSIG KSVIDELKGQ RSRLKMIASE 

        70         80         90        100        110        120 
NYASISVQLA MGNLLTDKYC EGSPFKRFYS CCENVDAIEW ECAETAKELF GAESAFVQPH 

       130        140        150        160        170        180 
SGADANLLAM MAIITQKIQG PAVKRLGYKT INDLTDKEYA ELKAEIGSHV CLGPSLNSGG 

       190        200        210        220        230        240 
HLTHGTVRMN VMSKLMRCLP YEVNKKTERF DYAEIARLVR THKPTVLVAG YSSYSRRLNF 

       250        260        270        280        290        300 
STLKQIADDC GAVLWVDMAH FAGLVAGGVF VEEENPIPFA DIVTTTTHKT LRGPRGGLVL 

       310        320        330        340        350        360 
ASKEYDGIIN RACPLMMGGP LPHVIAAKAV ALKEALTVDF KKYAHQVVDN ARTLAEHFQK 

       370        380        390        400        410        420 
QGLRLLTGGT DNHMLIIDLT SLGISGRIAE DILSSIGIAV NRNTIPSDAV GKWDTSGIRL 

       430        440        450        460        470        480 
GTPALTTLGM GSDEMEEVAN IIVKVLRNIT LRRNADDSFS KSEGELPENI AQEARARVAD 

       490 
LLSRFPLYPE IDLETLV 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP04975.1.
RefSeqNP_829097.1. NC_003361.3.

3D structure databases

ProteinModelPortalQ824C8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1217909.
GenomeReviewsGene locus CCA_00224 in contig AE015925_GR.
KEGGcca:CCA00224.
PATRIC20269474. VBIChlCav107360_0236.
TIGRCCA_00224.

Phylogenomic databases

HOGENOMHBG301263.
OMAMILTNHE.
ProtClustDBPRK13580.

Enzyme and pathway databases

BioCycCCAV227941:CCA_00224-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. 2 hits.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00600.
PANTHERPTHR11680. Gly_HO-Metrfase. 1 hit.
PfamPF00464. SHMT. 2 hits.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_CHLCV
AccessionPrimary (citable) accession number: Q824C8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 57 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