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B1JEA0 (B1JEA0_PSEPW) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 49. 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
Ordered Locus Names:PputW619_4885 EMBL ACA75361.1
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP] EMBL ACA75361.1
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length417 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

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00051

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

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 site351Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site551Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site571Substrate By similarity HAMAP-Rule MF_00051
Binding site641Substrate By similarity HAMAP-Rule MF_00051
Binding site651Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site991Pyridoxal phosphate By similarity HAMAP-Rule MF_00051
Binding site1211Substrate; 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 site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00051
Binding site3631Pyridoxal 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
B1JEA0 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 52435C0B30809816

FASTA41744,719
        10         20         30         40         50         60 
MFSKQDQIQG YDDALLAAMN AEEQRQEDHI ELIASENYTS KRVMQAQGSG LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDKVEALAIE RAKQLFGADY ANVQPHSGSS ANSAVYLALL QAGDTILGMS 

       130        140        150        160        170        180 
LAHGGHLTHG AKVSSSGKLY NAVQYGIDTN TGLIDYDEVE RLAVEHKPKM IVAGFSAYSK 

       190        200        210        220        230        240 
TLDFPRFRAI ADKVGALLFV DMAHVAGLVA AGLYPNPIPF ADVVTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LAKSNEEIEK KLNAAVFPGA QGGPLMHVIA AKAVCFKEAQ EPEFKSYQKQ VIENAQAMAQ 

       310        320        330        340        350        360 
VFIDRGYDVV SGGTDNHLFL VSLIRQGLTG KDADAALGRA HITVNKNAVP NDPQSPFVTS 

       370        380        390        400        410 
GLRIGTPAVT TRGFKVAQCV ALAGWICDIL DNLGDADVEA DVAKNVAALC TDFPVYR 

« Hide

References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000949 Genomic DNA. Translation: ACA75361.1.
RefSeqYP_001751730.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1JEA0.
SMRB1JEA0. Positions 1-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390235.PputW619_4885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA75361; ACA75361; PputW619_4885.
GeneID6113875.
KEGGppw:PputW619_4885.
PATRIC19959721. VBIPsePut93764_4916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAQVIDNAQ.
OrthoDBEOG6Z0QB2.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycPPUT390235:GHHJ-4968-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. SSF53383. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB1JEA0_PSEPW
AccessionPrimary (citable) accession number: B1JEA0
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)