Q3IZN2 (GLYA_RHOS4) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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 |
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| Organism | Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) | ||||||
| Taxonomic identifier | 272943 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter |
Protein attributes
| Sequence length | 431 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 Reference 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 – 431 | 431 | Pyridoxal-phosphate-dependent serine hydroxymethyltransferase | PRO_0000235014 | |||||
Regions | |||||||||
| Region | 132 – 134 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 42 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 62 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 64 | 1 | Substrate By similarity | ||||||
| Binding site | 71 | 1 | Substrate binding By similarity | ||||||
| Binding site | 72 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 106 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 128 | 1 | Substrate By similarity | ||||||
| Binding site | 183 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 211 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 236 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 243 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 269 | 1 | Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 369 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 237 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000143 Genomic DNA. Translation: ABA80002.1. |
| RefSeq | YP_353903.1. NC_007493.1. |
3D structure databases | |
| ProteinModelPortal | Q3IZN2. |
| SMR | Q3IZN2. Positions 15-421. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q3IZN2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3718402. |
| GenomeReviews | Gene locus RHOS4_24340 in contig CP000143_GR. |
| KEGG | rsp:RSP_0823. |
| NMPDR | fig|272943.3.peg.2455. |
| PATRIC | 23154829. VBIRhoSph57909_2784. |
Phylogenomic databases | |
| eggNOG | COG0112. |
| HOGENOM | HBG301263. |
| OMA | IFNAGYA. |
| PhylomeDB | Q3IZN2. |
| ProtClustDB | PRK00011. |
Enzyme and pathway databases | |
| BioCyc | RSPH272943:RSP_0823-MONOMER. |
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_RHOS4 | ||||||||
| Accession | Primary (citable) accession number: Q3IZN2 | ||||||||
| 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 |

Clusters with