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Q6FA66 (GLYA_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ACIAD2255
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length417 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 – 417417Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113517

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 site981Pyridoxal 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 site2621Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3621Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FA66 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 8B25FCE385257709

FASTA41744,943
        10         20         30         40         50         60 
MFANISLSEF DPELAKSIEA EDARQEAHIE LIASENYCSP AVMEAQGSKL TNKYAEGYPG 

        70         80         90        100        110        120 
KRYYGGCEYV DVIEQLAIDR AKALFGADYA NVQPHAGSQA NSAVYLALLN AGDTVLGMSL 

       130        140        150        160        170        180 
AHGGHLTHGA KVNFSGKTYN AVQYGLNPET GEIDYDEVER LAIEHKPRMI VAGFSAYSRI 

       190        200        210        220        230        240 
VDWQRFRDIA DKVGAYLFVD MAHVAGLVAA GVYPSPVQIA DVTTTTTHKT LRGPRSGLIL 

       250        260        270        280        290        300 
AKANEEIEKK LQSAVFPGNQ GGPLVHAIAA KAVCFKEAMA PEYKAYQQQV VKNAQAMAEV 

       310        320        330        340        350        360 
LIARGYDIVS GGTDNHLFLL SLIKQDVTGK EADAWLGNAN ITVNKNAVPN DPRSPFVTSG 

       370        380        390        400        410 
IRIGTPAVTT RGFGEAEVRD LASWIADVLD SKGDEKVIAD VKAKVEAVCA KFPVYEN

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR543861 Genomic DNA. Translation: CAG69047.1.
RefSeqYP_046869.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6FA66.
SMRQ6FA66. Positions 5-415.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FA66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2880606.
GenomeReviewsGene locus ACIAD2255 in contig CR543861_GR.
KEGGaci:ACIAD2255.
NMPDRfig|62977.3.peg.2156.
PATRIC20742164. VBIAciSp98416_2025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAFSASYEM.
PhylomeDBQ6FA66.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycASP62977:ACIAD2255-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_ACIAD
AccessionPrimary (citable) accession number: Q6FA66
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 55 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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