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Q28N04 (GLYA_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:Jann_2991
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length439 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 – 439439Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000369930

Regions

Region140 – 1423Substrate binding By similarity

Sites

Binding site501Pyridoxal phosphate By similarity
Binding site701Pyridoxal phosphate By similarity
Binding site721Substrate By similarity
Binding site791Substrate binding By similarity
Binding site801Pyridoxal phosphate By similarity
Binding site1141Pyridoxal phosphate By similarity
Binding site1361Substrate By similarity
Binding site1911Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2771Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3771Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28N04 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 5DC2C4414FE010A8

FASTA43947,045
        10         20         30         40         50         60 
MNAPHRDETT ASHRDDGFFT ESLESRDPEI FAASQKELGR QRDEIELIAS ENIVSAAVME 

        70         80         90        100        110        120 
AQGGVMTNKY AEGYPGRRYY GGCQYVDIAE ELAIDRAKQL FGCDFANVQP NSGSQANQGV 

       130        140        150        160        170        180 
FTALLQPGDT ILGMSLDAGG HLTHGARPNQ SGKWFNAVQY GVREGDLEID YDQIAALAAE 

       190        200        210        220        230        240 
HKPKMIIAGG SAIPRIIDFA RMREIADTIG AYLLVDMAHF AGMVASGHYP SPFPHAHVAT 

       250        260        270        280        290        300 
TTTHKTLRGP RGGMIVTNDE AIAKKVNSAI FPGIQGGPLM HVIAGKAVAF GEALRPEFRD 

       310        320        330        340        350        360 
YQTQVIANAQ ALAAQLIKGG LDIVTGGTDT HLMLVDLRAK GVKGNATEKA LGRAHITCNK 

       370        380        390        400        410        420 
NGIPFDTEKP MVTSGLRLGS PAGTTRGFGE AEFRQIADWI VEVVDGLAAN GEDANDAVEA 

       430 
KVRGEVQALC DRFPIYPNL 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD55908.1.
RefSeqYP_510933.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28N04.
SMRQ28N04. Positions 21-431.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28N04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3935461.
GenomeReviewsGene locus Jann_2991 in contig CP000264_GR.
KEGGjan:Jann_2991.
PATRIC22149842. VBIJanSp43325_3172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMADYDQIAA.
PhylomeDBQ28N04.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycJSP290400:JANN_2991-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_JANSC
AccessionPrimary (citable) accession number: Q28N04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 48 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