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Q64U78 (GLYA_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:BF2204
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length426 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 – 426426Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113528

Regions

Region117 – 1193Substrate binding By similarity

Sites

Binding site271Pyridoxal phosphate By similarity
Binding site471Pyridoxal phosphate By similarity
Binding site491Substrate By similarity
Binding site561Substrate binding By similarity
Binding site571Pyridoxal phosphate By similarity
Binding site1131Substrate By similarity
Binding site1681Pyridoxal phosphate By similarity
Binding site1961Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2691Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3711Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2221N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64U78 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: C2F6337612D0FB4C

FASTA42646,858
        10         20         30         40         50         60 
MKRDDLIFDI IEKEHQRQLK GIELIASENF VSDQVMEAMG SCLTNKYAEG YPGKRYYGGC 

        70         80         90        100        110        120 
EVVDQSEQIA IDRLKEIFGA EWANVQPHSG AQANAAVFLA VLNPGDKFMG LNLAHGGHLS 

       130        140        150        160        170        180 
HGSLVNTSGI IYTPCEYNLK QETGRVDYDQ MEEVALREKP KMIIGGGSAY SREWDYKRMR 

       190        200        210        220        230        240 
EIADKVGAIL MIDMAHPAGL IAAGLLDNPV KYAHIVTSTT HKTLRGPRGG VIMMGKDFPN 

       250        260        270        280        290        300 
PWGKKTPKGE IKMMSQLLDS AVFPGIQGGP LEHVIAAKAV AFGECLQPEY KEYQKQVQKN 

       310        320        330        340        350        360 
AAVLAQALID RGFTIVSGGT DNHSMLVDLR SKYPTLTGKV AEKALVSADI TVNKNMVPFD 

       370        380        390        400        410        420 
SRSAFQTSGI RLGTPAITTR GAKEDLMLEI AEMIETVLSN VENEEVIAQV RARVNKTMEK 


YPIFAY

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References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006841 Genomic DNA. Translation: BAD48951.1.
RefSeqYP_099485.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64U78.
SMRQ64U78. Positions 2-419.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3084132.
GenomeReviewsGene locus BF2204 in contig AP006841_GR.
KEGGbfr:BF2204.
PATRIC21050060. VBIBacFra17906_2142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAAHMTINK.
PhylomeDBQ64U78.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycBFRA295405:BF2204-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_BACFR
AccessionPrimary (citable) accession number: Q64U78
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 53 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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