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Q0I555 (GLYA_HAES1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:HS_1627
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus

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_1000006260

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
Q0I555 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 3C23D6699AD650A3

FASTA41945,570
        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 VKNAKAMVEV 

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

       370        380        390        400        410 
IRVGTPAVTR RGFNEEDVAE LAGWMCDILD SMNKDNHEQV IADTKEKVLA ICKRLPVYP

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000436 Genomic DNA. Translation: ABI25895.1.
RefSeqYP_719832.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I555.
SMRQ0I555. Positions 1-418.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0I555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4241154.
GenomeReviewsGene locus HS_1627 in contig CP000436_GR.
KEGGhso:HS_1627.
NMPDRfig|205914.1.peg.977.
PATRIC20283411. VBIHaeSom53361_1705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGANANIA.
PhylomeDBQ0I555.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycHSOM205914:HS_1627-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_HAES1
AccessionPrimary (citable) accession number: Q0I555
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 44 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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