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Reviewed, UniProtKB/Swiss-Prot B0VBB3 (GLYA_ACIBY)

Last modified November 3, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine hydroxymethyltransferase
      Short name=Serine methylase
      Short name=SHMT
    EC=2.1.2.1
Gene names
Name: glyA
Ordered Locus Names: ABAYE1171
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Interconversion of serine and glycine By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_00051

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine metabolic process

Inferred from electronic annotation. Source: InterPro

glycine metabolic process

Inferred from electronic annotation. Source: InterPro

one-carbon metabolic process

Inferred from electronic annotation. Source: HAMAP

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Serine hydroxymethyltransferase HAMAP MF_00051
PRO_1000091509

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VBB3-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C6D7ACE5AEFF75B8

FASTA41744,995
        10         20         30         40         50         60 
MFANISISEF DPELAQAIAS EDERQEAHIE LIASENYCSP AVMEAQGSKL TNKYAEGYPG 

        70         80         90        100        110        120 
KRYYGGCEFV DVIEQMAIDR AKELFGADYA NVQPHAGSQA NSAVYLALLN PGDTVLGMSL 

       130        140        150        160        170        180 
AHGGHLTHGA KVSFSGKTYN AVQYGLNAET GEIDYEEVER LALEHKPRMI VAGFSAYSRV 

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

       250        260        270        280        290        300 
AKANEEIEKK LQSAVFPGNQ GGPLMHAIAA KAICFKEAMS DDFKAYQQQV VKNAQAMAEV 

       310        320        330        340        350        360 
FIARGYDVVS GGTDNHLFLL SLIKQDVTGK DADAWLGAAH ITVNKNSVPN DPRSPFVTSG 

       370        380        390        400        410 
IRIGTPAVTT RGFGEAEVRE LAGWIADVID SKGDEKVIAD VKAKVEAVCA KFPVYAK 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CU459141 Genomic DNA. Translation: CAM86097.1.
RefSeqYP_001713100.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6001022.
GenomeReviewsGene locus ABAYE1171 in contig CU459141_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYNFVSYS.

Family and domain databases

HAMAPMF_00051.
[Tree]
InterProIPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11680. Gly_HO-Metrfase. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_ACIBY
AccessionPrimary (citable) accession number: B0VBB3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents