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A8FSQ9 (GLYA_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Ssed_1271
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length418 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 – 418418Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000074910

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 site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3641Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FSQ9 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 1B5180C2B523B598

FASTA41845,262
        10         20         30         40         50         60 
MLKKDMNIAD FDPQLFQAIA DETRRQEEHI ELIASENYTS PRVLEAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDIAEELAIS RAKELFGATY ANVQPHSGSQ ANSAVFMALL QGGDTVLGMS 

       130        140        150        160        170        180 
LAHGGHLTHG SHVSFSGKLY NAVQYGIDEA TGKIDYAEVE RLAVEHKPKM IIAGFSAYSG 

       190        200        210        220        230        240 
IIDWGKFREI ADKVGAYLFV DMAHVAGLVA AGIYPNPLPH AHVVTTTTHK TLAGPRGGLI 

       250        260        270        280        290        300 
LSACDDEAIY KKLNSAVFPG GQGGPLMHVI AAKAVAFKEA LEPEFTAYQE QVVVNAKAMA 

       310        320        330        340        350        360 
KTFIERGYDV VSGGTDNHLF LLDLISKDIT GKDADAALGL ANITVNKNSV PNDPRSPFVT 

       370        380        390        400        410 
SGLRIGSPAI TRRGFKEEQS VELTNWMCDV LDDITDQGTI ERVKNQVLEL CARFPVYG 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV35882.1.
RefSeqYP_001473010.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FSQ9.
SMRA8FSQ9. Positions 1-418.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FSQ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5614044.
GenomeReviewsGene locus Ssed_1271 in contig CP000821_GR.
KEGGsse:Ssed_1271.
NMPDRfig|425104.3.peg.1114.
PATRIC23559870. VBISheSed62411_1341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGTSNHLM.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycSSED425104:SSED_1271-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_SHESH
AccessionPrimary (citable) accession number: A8FSQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 34 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