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B0BC69 (GLYA_CHLTB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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
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
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:CTLon_0687
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP]
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

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_1000091528

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
B0BC69 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: C1DC9DCA17C2C533

FASTA49754,249
        10         20         30         40         50         60 
MASLLDRYLR NISDKSQQNL ASVAYLASLD HLLHAFPSIG QSIVQELKSQ RSRLKMIASE 

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

       130        140        150        160        170        180 
SGADANLLAI MSIITQKIQS PAVQQLGYKT INDLPEQEYE ALKAEMAQHK CLGPSLNSGG 

       190        200        210        220        230        240 
HLTHGTVRMN IMSKLMHCLP YEVNLDTELF DYDEIAKIAK EHKPTVLIAG YSSYSRRFNF 

       250        260        270        280        290        300 
ATLKQIAEDC GAVLWVDMAH FAGLVAGGVF VGEENPMPYA DIVTTTTHKT LRGPRGGLVL 

       310        320        330        340        350        360 
AKKEYANTLN KACPLMMGGP LPHVIAAKAI ALKEAMTINF RKYAHKVVEN AQTLAEVFQR 

       370        380        390        400        410        420 
NGLRLLTGGT DNHMLIIDLT SLGVPGRIAE DMLTSVGIAV NRNTIPSDAS GQWKTSGIRL 

       430        440        450        460        470        480 
GTPALTTLGM GSAEMEEVAN IIVKVLRNIT VRSNAESGSS KSEGELSEGI AQEARQRVAD 

       490 
LLGRFPLYPE IDLETLV

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed: 18032721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCH-1/proctitis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM884177 Genomic DNA. Translation: CAP07084.1.
RefSeqYP_001653775.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BC69.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0BC69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5859328.
GenomeReviewsGene locus CTLon_0687 in contig AM884177_GR.
KEGGctl:CTLon_0687.
PATRIC20383037. VBIChlTra68089_0744.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAMILTNHE.
ProtClustDBPRK13580.

Enzyme and pathway databases

BioCycCTRA471473:CTLON_0687-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_CHLTB
AccessionPrimary (citable) accession number: B0BC69
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 33 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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