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B0UWS8 (GLYA_HAES2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:HSM_0382
OrganismHaemophilus somnus (strain 2336) (Histophilus somni (strain 2336)) [Complete proteome] [HAMAP]
Taxonomic identifier228400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length419 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 – 419419Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000074899

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 site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2621Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3621Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0UWS8 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 84E336677A28AEBF

FASTA41945,596
        10         20         30         40         50         60 
MLKRSMNIAD YDPVLWQAIQ DENLRQEEHI ELIASENYAS PRVMEAQGCQ FTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEY ADIVEQLAID RAKALFGADY ANVQPHSGSQ ANAAVYMALL NPGDTILGMS 

       130        140        150        160        170        180 
LAHGGHLTHG ASVSFSGKIY KAEQYGITSE GLIDYDALRK QAHEVKPKMI VGGFSAYSQI 

       190        200        210        220        230        240 
VDWAKMREIA DEVGAYLFVD MAHVAGLIAA GVYPSPMPHA HVVTTTTHKT LAGPRGGLIL 

       250        260        270        280        290        300 
ANGNEELYKK LNSAVFPAGQ GGPLVHVIAA KAVCFKEALE PEFKTYQAQV VKNAKAMVKV 

       310        320        330        340        350        360 
FKQRGYNVVS NGTENHLFLV DLVNHGLTGK AADAALSRAN ITVNKNAVPN DPQKPFVTSG 

       370        380        390        400        410 
IRVGTPAVTR RGFNEEDVAE LAGWMCDILD SMNKDNHEQV IADTKEKVLA ICKRLPVYP 

« Hide

References

[1]"Complete sequence of Haemophilus somnus 2336."
US DOE Joint Genome Institute
Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F., Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M., Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S., Dyer D.W., Inzana T.J.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2336.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000947 Genomic DNA. Translation: ACA32021.1.
RefSeqYP_001783731.1. NC_010519.1.

3D structure databases

ProteinModelPortalB0UWS8.
SMRB0UWS8. Positions 1-418.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0UWS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6108162.
GenomeReviewsGene locus HSM_0382 in contig CP000947_GR.
KEGGhsm:HSM_0382.
PATRIC20197777. VBIHaeSom93646_0398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAFSASYEM.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycHSOM228400:HSM_0382-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_HAES2
AccessionPrimary (citable) accession number: B0UWS8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 27 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