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O66776 (GLYA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. 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:aq_479
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length428 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 HAMAP MF_00051.

Sequence similarities

Belongs to the SHMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113522

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
O66776 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 883E1196CF472EE5

FASTA42847,454
        10         20         30         40         50         60 
MEHLLKTDPE VFDAVVKEYE RQFYNLEMIA SENFTSLAVM EATGSVLTNK YAEGLPGKRY 

        70         80         90        100        110        120 
YGGCEYVDVV ENLAIERAKK LFGAEHANVQ PHSGSQANMA VYFAVLNPGD TIMGMDLAHG 

       130        140        150        160        170        180 
GHLTHGAKVN FSGKLYNVIH YGVNPETELI DYDQLYKLAK EHKPKLIVGG ASAYPRVFDW 

       190        200        210        220        230        240 
AKMREIADEV GALFMVDMAH YAGLIAGGVY PNPVPYAQFV TSTTHKTLRG PRSGFILTTK 

       250        260        270        280        290        300 
EYAKAVDKSV FPGIQGGPLM HVIAAKAVAF KEAMSEEFKE YAKQVVENAR VLAEELKKYG 

       310        320        330        340        350        360 
FKIVTGGTDS HIVLVDLRNK NIIGKDAEKA LEKAGITVNK NAVPFDPLPP TKTSGIRIGT 

       370        380        390        400        410        420 
AALTTRGMKE DEMRKIAGWI NEVLSNMDDE KTIQRVRQEV RELCETFPLY PELKRRIDEL 


RSGKATDL 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06734.1.
PIRD70343.
RefSeqNP_213336.1. NC_000918.1.

3D structure databases

ProteinModelPortalO66776.
SMRO66776. Positions 1-405.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193194.
GenomeReviewsGene locus aq_479 in contig AE000657_GR.
KEGGaae:aq_479.
NMPDRfig|224324.1.peg.351.
PATRIC20958520. VBIAquAeo85532_0395.

Phylogenomic databases

HOGENOMHBG301263.
OMAFETFPYR.
PhylomeDBO66776.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycAAEO224324:AQ_479-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_AQUAE
AccessionPrimary (citable) accession number: O66776
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 77 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