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E8YN90 (E8YN90_9BURK) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine hydroxymethyltransferase HAMAP-Rule MF_00051
Short name=SHMT HAMAP-Rule MF_00051
Short name=Serine methylase HAMAP-Rule MF_00051
EC=2.1.2.1 HAMAP-Rule MF_00051
Gene names
Name:glyA HAMAP-Rule MF_00051
ORF Names:BC1001_0475 EMBL ADX53937.1
OrganismBurkholderia sp. CCGE1001 EMBL ADX53937.1
Taxonomic identifier640510 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism By similarity. HAMAP-Rule MF_00051

Interconversion of serine and glycine By similarity. RuleBase RU000585

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051 RuleBase RU000585

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00051 RuleBase RU000585

Pathway

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051 RuleBase RU000585

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00051

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00051.

Sequence similarities

Belongs to the SHMT family. HAMAP-Rule MF_00051 RuleBase RU004104

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site361Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site561Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site581Substrate By similarity HAMAP-Rule MF_00051
Binding site651Substrate By similarity HAMAP-Rule MF_00051
Binding site661Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site1001Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site1221Substrate; via carbonyl oxygen By similarity HAMAP-Rule MF_00051
Binding site1761Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2041Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2291Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2361Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site2611Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00051
Binding site3611Pyridoxal phosphate By similarity HAMAP-Rule MF_00051

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00051

Sequences

Sequence LengthMass (Da)Tools
E8YN90 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: E2738B6E75DBD6D3

FASTA41545,022
        10         20         30         40         50         60 
MFDRAQSTIA NVDPELWKVI ELENRRQEEH IELIASENYT SPAVMAAQGS QLTNKYAEGY 

        70         80         90        100        110        120 
PGKRYYGGCE YVDVAEQLAI DRVKQLFGAE AANVQPNSGS QANQGVFFAM LRPGDTIMGM 

       130        140        150        160        170        180 
SLAHGGHLTH GSPVNMSGKW FKVVSYGLNE AEDIDYDAAE KLAQEHKPKL IVAGASAFAL 

       190        200        210        220        230        240 
RIDFERLSKI AKSVGAYFMV DMAHYAGLVA AGVYPNPVPH ADFVTTTTHK SLRGPRGGVI 

       250        260        270        280        290        300 
LMKAEFEKQI NSAIFPGIQG GPLMHVIAAK AVAFKEALSP EFKAYQQQVV ENARALAETL 

       310        320        330        340        350        360 
VKRGLRIVSG RTESHVMLVD LRAKKITGKA AEAALGAAHI TVNKNAIPND PEKPFVTSGI 

       370        380        390        400        410 
RLGSPAMTTR GFGTKEAEQV GNLIADVLDN PEDAATIERV RGQVAELTQR FPVYR

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References

[1]"Complete sequence of chromosome1 of Burkholderia sp. CCGE1001."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Martinez-Romero E. expand/collapse author list , Rogel M.A., Auchtung J., Tiedje J., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CCGE1001 EMBL ADX53937.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002519 Genomic DNA. Translation: ADX53937.1.
RefSeqYP_004226997.1. NC_015136.1.

3D structure databases

ProteinModelPortalE8YN90.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX53937; ADX53937; BC1001_0475.
GeneID10222003.
KEGGbug:BC1001_0475.
PATRIC46893433. VBIBurSp1058_0496.

Phylogenomic databases

KOK00600.

Enzyme and pathway databases

BioCycBSP640510:GI28-2969-MONOMER.
UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 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 nameE8YN90_9BURK
AccessionPrimary (citable) accession number: E8YN90
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: April 3, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info