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Q6LHN7 (GLYA2_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:PBPRB1322
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Photobacterium

Protein attributes

Sequence length431 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 – 431431Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000113632

Regions

Region135 – 1373Substrate binding By similarity

Sites

Binding site451Pyridoxal phosphate By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site671Substrate By similarity
Binding site741Substrate binding By similarity
Binding site751Pyridoxal phosphate By similarity
Binding site1311Substrate By similarity
Binding site1861Pyridoxal phosphate By similarity
Binding site2141Pyridoxal phosphate By similarity
Binding site2391Pyridoxal phosphate By similarity
Binding site2461Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LHN7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 117E9E9634859D4E

FASTA43146,611
        10         20         30         40         50         60 
MKASYQNHDL EMFFSTNLAQ VDGAVNAGIE AELNRQNQQI ELIASENIVS KAVMQAQGTC 

        70         80         90        100        110        120 
LTNKYAEGYA GHRYYGGCEH VDEVEKIAIA RAKQLFQCEY VNVQPHSGAQ ANGAVMLALL 

       130        140        150        160        170        180 
QPGDTILGMS LDAGGHLTHG ARPALSGKWF DAVQYGVNKD TLEIDYNQVR ELAIEHKPKM 

       190        200        210        220        230        240 
IIAGGSAIPR IINFAKFREI ADEVGAFLMV DMAHIAGLIA AGEHPSPIPH AHVITTTTHK 

       250        260        270        280        290        300 
TLRGPRGGMI LTNLEDINKK INSAVFPGLQ GGPLMHVIAG KAVAFGEALE PDFKIYIKNV 

       310        320        330        340        350        360 
ISNAKVLAEV LQNRGCDIVT NGTDTHLMLV DLRPKGLKGN AAENALERAG ITCNKNGIPF 

       370        380        390        400        410        420 
DTEKPMVTSG IRLGTPAGTS RGFGNDEFKQ IGEWIGDVLD GLAANPEDNS EVEKHVKQQV 

       430 
QKLCSRFPLY Q

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed: 15746425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR378679 Genomic DNA. Translation: CAG23193.1.
RefSeqYP_132993.1. NC_006371.1.

3D structure databases

ProteinModelPortalQ6LHN7.
SMRQ6LHN7. Positions 18-404.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3121443.
GenomeReviewsGene locus PBPRB1322 in contig CR354532_GR.
KEGGppr:PBPRB1322.
NMPDRfig|298386.1.peg.1427.
PATRIC22941266. VBIPhoPro109272_5199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAAAPNISG.
PhylomeDBQ6LHN7.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycPPRO298386:PBPRB1322-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_PHOPR
AccessionPrimary (citable) accession number: Q6LHN7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 54 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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