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Q4ZM83 (GLYA2_PSEU2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2

Short name=SHMT 2
Short name=Serine methylase 2
EC=2.1.2.1
Gene names
Name:glyA2
Ordered Locus Names:Psyr_4712
OrganismPseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]
Taxonomic identifier205918 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

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 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 – 417417Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000235010

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4ZM83 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 004FD60AEBBE4D16

FASTA41744,874
        10         20         30         40         50         60 
MFSKQDQIQG YDDALLSAMN AEEQRQEDHI ELIASENYTS KRVMQAQGSG LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDKVEQLAIE RARQLFGADY ANVQPHSGSQ ANAAVYLALL QAGDTVLGMS 

       130        140        150        160        170        180 
LAHGGHLTHG AKVSFSGKLY NAVQYGIDTA TGLIDYDEVE RIAVECQPKM IIAGFSAYSK 

       190        200        210        220        230        240 
TLDFPRFRAI ADKVGAYLFV DMAHVAGLVA AGLYPNPLPY ADVVTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LARANEELEK KFNSAVFPGG QGGPLMHVIA AKAVCFKEAM EPGFKAYQQQ VIDNAQAMAQ 

       310        320        330        340        350        360 
VFIDRGFDVV SGGTDNHLFL VSLIRQGLTG KDADAALGRA HITVNKNSVP NDPQSPFVTS 

       370        380        390        400        410 
GLRIGTPAVT TRGFKVTQCV ELAGWICDIL DNLGDADVEA DVASQVAALC ADFPVYR 

« Hide

References

[1]"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000."
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E.
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed: 16043691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B728a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000075 Genomic DNA. Translation: AAY39739.1.
RefSeqYP_237777.1. NC_007005.1.

3D structure databases

ProteinModelPortalQ4ZM83.
SMRQ4ZM83. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4ZM83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3370262.
GenomeReviewsGene locus Psyr_4712 in contig CP000075_GR.
KEGGpsb:Psyr_4712.
PATRIC19990245. VBIPseSyr42314_4859.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAADVEANV.
PhylomeDBQ4ZM83.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycPSYR205918:PSYR_4712-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. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00600.
PANTHERPTHR11680. Gly_HO-Metrfase. 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 nameGLYA2_PSEU2
AccessionPrimary (citable) accession number: Q4ZM83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 49 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