Q183G0 (GLYA_CLOD6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 50.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyridoxal-phosphate-dependent serine hydroxymethyltransferase Short name=SHMT Short name=Serine methylase EC=2.1.2.1 | ||||
| Gene names |
| ||||
| Organism | Clostridium difficile (strain 630) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272563 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 414 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis One-carbon metabolism |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-serine metabolic process Inferred from electronic annotation. Source: InterPro glycine metabolic processInferred from electronic annotation. Source: InterPro one-carbon metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | glycine hydroxymethyltransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 414 | 414 | Pyridoxal-phosphate-dependent serine hydroxymethyltransferase | PRO_0000369912 | |||||
Regions | |||||||||
| Region | 122 – 124 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 32 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 52 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 54 | 1 | Substrate By similarity | ||||||
| Binding site | 61 | 1 | Substrate binding By similarity | ||||||
| Binding site | 62 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 118 | 1 | Substrate By similarity | ||||||
| Binding site | 173 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 201 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 226 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 233 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 258 | 1 | Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 358 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 227 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. Parkhill J.Nat. Genet. 38:779-786(2006) [PubMed: 16804543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM180355 Genomic DNA. Translation: CAJ69613.1. |
| RefSeq | YP_001089238.1. NC_009089.1. |
3D structure databases | |
| ProteinModelPortal | Q183G0. |
| SMR | Q183G0. Positions 5-402. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q183G0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4912877. |
| GenomeReviews | Gene locus CD2726 in contig AM180355_GR. |
| KEGG | cdf:CD2726. |
| NMPDR | fig|1496.1.peg.2308. |
| PATRIC | 19443939. VBICloDif38397_2853. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0112. |
| HOGENOM | HBG301263. |
| OMA | KAICAKF. |
| ProtClustDB | CLSK2535392. |
Family and domain databases | |
| HAMAP | MF_00051. SHMT. [Tree] |
| InterPro | IPR015424. 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] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| KO | K00600. |
| PANTHER | PTHR11680. Gly_HO-Metrfase. 1 hit. |
| Pfam | PF00464. SHMT. 1 hit. [Graphical view] |
| PIRSF | PIRSF000412. SHMT. 1 hit. |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| PROSITE | PS00096. SHMT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLYA_CLOD6 | ||||||||
| Accession | Primary (citable) accession number: Q183G0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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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