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Q129K3 (GLYA_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:Bpro_2874
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Polaromonas

Protein attributes

Sequence length414 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 – 414414Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006292

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 site1211Substrate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2601Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3601Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q129K3 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: BD6E30F54D2F53B0

FASTA41444,920
        10         20         30         40         50         60 
MYHRNILVEQ TDPEIFAAIQ AENARQEHHI ELIASENYAS PAVMAAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
GRRYYGGCEY VDVAEQLAID RIKQIFGADA ANVQPHCGAS ANEAVFLAFL KPGDTIMGMS 

       130        140        150        160        170        180 
LAEGGHLTHG MALNMSGKWF NVVSYGLNDK EEIDYDAMER KAHETRPKLI IAGASAYSLR 

       190        200        210        220        230        240 
IDFERFAKVA KAVGAIFMVD IAHYAGLVAA GVYPNPVPHA DVVTSTTHKS LRGPRGGIIL 

       250        260        270        280        290        300 
MKAEHEKAIN SAIFPGLQGG PLMHVIAAKA VAFKEALSPE FKTYQQQVLT NARIVAETLT 

       310        320        330        340        350        360 
QRGLRIVSGR TESHLMLVDL RAKGITGKEA EAVLGSAHMT INKNAIPNDP EKPMVTSGVR 

       370        380        390        400        410 
IGTPAMTTRG FKDEEARVTA NLIADVLDNP RDAANIEAVR AKVNALTSRF PVYR

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000316 Genomic DNA. Translation: ABE44789.1.
RefSeqYP_549687.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ129K3.
SMRQ129K3. Positions 1-413.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ129K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4014449.
GenomeReviewsGene locus Bpro_2874 in contig CP000316_GR.
KEGGpol:Bpro_2874.
NMPDRfig|296591.1.peg.5465.
PATRIC22958920. VBIPolSp102244_2919.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAAHMTINK.
PhylomeDBQ129K3.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycPSP296591:BPRO_2874-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 nameGLYA_POLSJ
AccessionPrimary (citable) accession number: Q129K3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 42 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

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