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B0VBB3 (GLYA_ACIBY) 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:ABAYE1171
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

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_1000091509

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
B0VBB3 [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].
Strain: AYE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU459141 Genomic DNA. Translation: CAM86097.1.
RefSeqYP_001713100.1. NC_010410.1.

3D structure databases

ProteinModelPortalB0VBB3.
SMRB0VBB3. Positions 5-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0VBB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6001022.
GenomeReviewsGene locus ABAYE1171 in contig CU459141_GR.
PATRIC20725763. VBIAciBau69881_1204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAFSASYEM.
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.
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_ACIBY
AccessionPrimary (citable) accession number: B0VBB3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 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

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