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A6L5K3 (GLYA_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:BVU_3341
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

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_1000006222

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
A6L5K3 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 007F3EF0206192ED

FASTA42646,827
        10         20         30         40         50         60 
MKRDDLIFDI IEKEHQRQLK GIELIASENF VSDQVMQAMG SCLTNKYAEG YPGKRYYGGC 

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

       130        140        150        160        170        180 
HGSLVNTSGI IYTPCEYNLN KETGRVDYDQ MEEIALREKP 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 KEYQTQVKKN 

       310        320        330        340        350        360 
AAVLAQALID RGFTIVSGGT DNHSMLVDLR TKYPDLTGKV AEKALVAADI TVNKNMVPFD 

       370        380        390        400        410        420 
SRSAFQTSGI RLGTPAITTR GAKEDLMLEI AEMIETVLSN VDNEEVIAQV RARVNETMKK 


YPIFAY 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR40967.1.
RefSeqYP_001300589.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L5K3.
SMRA6L5K3. Positions 2-418.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6L5K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5304302.
GenomeReviewsGene locus BVU_3341 in contig CP000139_GR.
KEGGbvu:BVU_3341.
NMPDRfig|435590.6.peg.3115.
PATRIC21071710. VBIBacVul85104_3436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAAHMTINK.
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.
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_BACV8
AccessionPrimary (citable) accession number: A6L5K3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: January 25, 2012
This is version 37 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