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B0TI64 (GLYA_HELMI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:Helmi_08590
ORF Names:HM1_1090
OrganismHeliobacterium modesticaldum (strain ATCC 51547 / Ice1) [Complete proteome] [HAMAP]
Taxonomic identifier498761 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacterium

Protein attributes

Sequence length413 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 – 413413Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000369927

Regions

Region124 – 1263Substrate binding By similarity

Sites

Binding site341Pyridoxal phosphate By similarity
Binding site541Pyridoxal phosphate By similarity
Binding site561Substrate By similarity
Binding site631Substrate binding By similarity
Binding site641Pyridoxal phosphate By similarity
Binding site1201Substrate 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
B0TI64 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: F62FFCC54730C1EE

FASTA41344,522
        10         20         30         40         50         60 
MSEWKHLHQV DPEVAAAMDR EKKRQKNNIE LIASENFVSE AVMEAAGSVL TNKYAEGYPG 

        70         80         90        100        110        120 
KRYYGGCEFV DQVERLAIER AKRLFGAEHA NVQPHSGANA NMGVYFACLE PGDTVLGMNL 

       130        140        150        160        170        180 
AHGGHLTHGS PVNISGKYFR FVAYGVDAHT GRIDYDEVAR IARETKPKLI VAGASAYPRV 

       190        200        210        220        230        240 
LDFARFRAIA DEVGAMLMVD MAHIAGLVAA GLHPSPVPYA EFVTTTTHKT LRGPRGGMIL 

       250        260        270        280        290        300 
CKQEWAAKVD KAIFPGLQGG PLMHIIAAKA VAFQEAMAPA FTAYQKQIAA NAAALAKGLT 

       310        320        330        340        350        360 
DRGFQLVSGG TDNHLMLVDL RNKQLTGKEA EKRLDECRIT VNKNAIPFDP QSPFVTSGIR 

       370        380        390        400        410 
IGTPAATSRG MDEAAMDQVA EAIHLCLSDG SEGAMQKAVA IVDALCARFP LYA 

« Hide

References

[1]"The genome of Heliobacterium modesticaldum, a phototrophic representative of the Firmicutes containing the simplest photosynthetic apparatus."
Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.
J. Bacteriol. 190:4687-4696(2008) [PubMed: 18441057] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51547 / Ice1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000930 Genomic DNA. Translation: ABZ83484.1.
RefSeqYP_001679495.1. NC_010337.2.

3D structure databases

ProteinModelPortalB0TI64.
SMRB0TI64. Positions 5-405.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0TI64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5911383.
GenomeReviewsGene locus Helmi_08590 in contig CP000930_GR.
KEGGhmo:HM1_1090.
PATRIC22105969. VBIHelMod36755_0786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMADIAHTAG.

Enzyme and pathway databases

BioCycHMOD498761:HM1_1090-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_HELMI
AccessionPrimary (citable) accession number: B0TI64
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 32 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