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A1USI0 (GLYA_BARBK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. 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:
Serine hydroxymethyltransferase
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:BARBAKC583_0629
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella ›

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism By similarity. HAMAP-Rule MF_00051

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
One-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine biosynthetic process from serine

Inferred from electronic annotation. Source: HAMAP

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglycine hydroxymethyltransferase activity

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_1000006223

Regions

Region134 – 1363Substrate binding By similarity

Sites

Binding site441Pyridoxal phosphate By similarity
Binding site641Pyridoxal phosphate By similarity
Binding site661Substrate By similarity
Binding site731Substrate By similarity
Binding site741Pyridoxal phosphate By similarity
Binding site1081Pyridoxal phosphate By similarity
Binding site1301Substrate; via carbonyl oxygen By similarity
Binding site1851Pyridoxal phosphate By similarity
Binding site2131Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2451Pyridoxal phosphate By similarity
Binding site2711Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3711Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1USI0 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 6F049C4C1D58622C

FASTA43246,996
        10         20         30         40         50         60 
MIKRENDLQQ CFFNDTLQTV DAAVFDAVSG ELRRQCDEIE LIASGNIVSR AVLEAQGSVL 

        70         80         90        100        110        120 
TNKYAEGYPG KRYYGGCHFV DRIEELAIER AKNLFGAAFA NVQPNSGSQM NQAVFLALLQ 

       130        140        150        160        170        180 
PGDTFMGLDL SSGGHLTHGS PVNMSGKWFN RIAYGLRQED QLLDIESVER LAKEHKPKLI 

       190        200        210        220        230        240 
FAGGTAYSRI WDWKRFREIS DEVGAYLVVD MAHIAGLVAG GVHPSPIPHA HIVTTTTHKS 

       250        260        270        280        290        300 
LRGPRGGMIL TNDEVLAKKI NSAVFPGLQG GPLMHVIAAK AVALGEALQP AFKDYAAKVV 

       310        320        330        340        350        360 
ANAKILAENL QNNGFTIVSG GTDNHLLLVD LRNKSLTGKH AELALERASI ICNKNNIPFD 

       370        380        390        400        410        420 
PQLPSITSGI RLGTPAATTR GFAENEFIQI SDLISEVLDG LTIAKNDDEN FLVEAAVKKK 

       430 
VKNITDNFPF YS

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35685 / KC583.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000524 Genomic DNA. Translation: ABM45302.1.
RefSeqYP_988933.1. NC_008783.1.

3D structure databases

ProteinModelPortalA1USI0.
SMRA1USI0. Positions 21-426.
ModBaseSearch...

Protein-protein interaction databases

STRING360095.BARBAKC583_0629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM45302; ABM45302; BARBAKC583_0629.
GeneID4683891.
KEGGbbk:BARBAKC583_0629.
PATRIC20537545. VBIBarBac6912_0613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAFKAYAHQ.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycBBAC360095:GHRY-658-MONOMER.
UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 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_BARBK
AccessionPrimary (citable) accession number: A1USI0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 50 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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