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B3E1Z8 (GLYA_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Glov_1932
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length415 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 – 415415Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000091544

Regions

Region121 – 1233Substrate binding By similarity

Sites

Binding site311Pyridoxal phosphate By similarity
Binding site511Pyridoxal phosphate By similarity
Binding site531Substrate By similarity
Binding site601Substrate binding By similarity
Binding site611Pyridoxal phosphate By similarity
Binding site951Pyridoxal phosphate By similarity
Binding site1171Substrate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site2001Pyridoxal phosphate By similarity
Binding site2251Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3571Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3E1Z8 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 303765B7F975DA03

FASTA41544,916
        10         20         30         40         50         60 
MSILSQFDPA VAEAIQHETE RQEYNLELIA SENFVSEAVL EAQGSVMTNK YAEGYPGKRY 

        70         80         90        100        110        120 
YGGCHHVDVV ENLAIERAKE LFGAEHANVQ PHAGSQANMA VYNAVCQPGD TILGMNLSHG 

       130        140        150        160        170        180 
GHLTHGSPVN FSGRFYNVVP YGVSPDTETI DYNEVERLAL EHKPKMIVVG ASAYPRIIDF 

       190        200        210        220        230        240 
PAFRAIADKV GAKVMVDMAH IAGLVAAGVH PNPVPYAEFV TTTTHKTLRG PRGGMILCRE 

       250        260        270        280        290        300 
EYAKTINSQI FPGIQGGPLM HVIAAKAVAF KEALQPEFKT YQQQIVKNAA KLAECLMAKG 

       310        320        330        340        350        360 
FKLTSGGTDN HLMLINFTGT EITGKAAEEA LDKAGITVNK NTVPFETRSP FVTSGIRVGT 

       370        380        390        400        410 
PACTSHGLKE TEMEQVAGFI ADAVANIGND EALAAIQKRV NELMKKFPLY ASRLK 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD95648.1.
RefSeqYP_001952168.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3E1Z8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3E1Z8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6368033.
GenomeReviewsGene locus Glov_1932 in contig CP001089_GR.
KEGGglo:Glov_1932.
PATRIC21995551. VBIGeoLov31523_1874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAAHMTINK.
ProtClustDBPRK00011.

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_GEOLS
AccessionPrimary (citable) accession number: B3E1Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 28 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