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Q87RR2 (GLYA1_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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 1

Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Ordered Locus Names:VP0715
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length416 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 – 416416Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 1
PRO_0000113692

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 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
Q87RR2 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: D8B078D662D62BA2

FASTA41645,505
        10         20         30         40         50         60 
MLKRDMNIAD YDAELFAAIQ EETLRQEEHI ELIASENYTS PRVMEAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEY VDKAEQLAID RACKLFGCEY ANVQPHSGSQ ANSAVYMALL NPGDTVLGMS 

       130        140        150        160        170        180 
LAHGGHLTHG SPVNFSGKHY NVIPYGIDEA GQINYDEMEQ LALEHKPKMI IGGFSAYSQI 

       190        200        210        220        230        240 
VDWKRMREIA DKVDAYLFVD MAHVAGLIAA GEYPTPVPHA HVVTTTTHKT LAGPRGGLIL 

       250        260        270        280        290        300 
SNAGEDMYKK LNSAVFPGGQ GGPLMHVIAG KAVAFKEAME PEFKAYQARV VKNAKAMVGQ 

       310        320        330        340        350        360 
FQERGYKIVS NGTENHLFLV DLIDKDITGK DADAALGAAN ITVNKNSVPN DPRSPFVTSG 

       370        380        390        400        410 
IRVGTPAITR RGFTEEDAKD LANWMCDVLD NIGNEEVIEA TKQKVLEICK RLPVYA 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC58978.1.
RefSeqNP_797094.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87RR2.
SMRQ87RR2. Positions 1-416.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1188190.
GenomeReviewsGene locus VP0715 in contig BA000031_GR.
KEGGvpa:VP0715.
NMPDRfig|223926.1.peg.715.
PATRIC20139634. VBIVibPar50997_0684.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAKAICAKF.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycVPAR223926:VP0715-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 nameGLYA1_VIBPA
AccessionPrimary (citable) accession number: Q87RR2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: January 25, 2012
This is version 61 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