Skip Header

Contribute Send feedback
Read comments (?) or add your own

O53441 (GLYA1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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 1
Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Synonyms:glyA
Ordered Locus Names:Rv1093, MT1125
ORF Names:MTV017.46
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm 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 1
PRO_0000113618

Regions

Region122 – 1243Substrate binding By similarity

Sites

Binding site321Pyridoxal phosphate By similarity
Binding site521Pyridoxal phosphate By similarity
Binding site541Substrate By similarity
Binding site611Substrate binding By similarity
Binding site621Pyridoxal phosphate By similarity
Binding site1181Substrate By similarity
Binding site1731Pyridoxal phosphate By similarity
Binding site2011Pyridoxal phosphate By similarity
Binding site2261Pyridoxal phosphate By similarity
Binding site2331Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict361V → A in AAK45383. Ref.2

Secondary structure

1 ......................................................................... 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O53441 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: B17AFE1115D9AFFB

FASTA42645,029
        10         20         30         40         50         60 
MSAPLAEVDP DIAELLAKEL GRQRDTLEMI ASENFVPRAV LQAQGSVLTN KYAEGLPGRR 

        70         80         90        100        110        120 
YYGGCEHVDV VENLARDRAK ALFGAEFANV QPHSGAQANA AVLHALMSPG ERLLGLDLAN 

       130        140        150        160        170        180 
GGHLTHGMRL NFSGKLYENG FYGVDPATHL IDMDAVRATA LEFRPKVIIA GWSAYPRVLD 

       190        200        210        220        230        240 
FAAFRSIADE VGAKLLVDMA HFAGLVAAGL HPSPVPHADV VSTTVHKTLG GGRSGLIVGK 

       250        260        270        280        290        300 
QQYAKAINSA VFPGQQGGPL MHVIAGKAVA LKIAATPEFA DRQRRTLSGA RIIADRLMAP 

       310        320        330        340        350        360 
DVAKAGVSVV SGGTDVHLVL VDLRDSPLDG QAAEDLLHEV GITVNRNAVP NDPRPPMVTS 

       370        380        390        400        410        420 
GLRIGTPALA TRGFGDTEFT EVADIIATAL ATGSSVDVSA LKDRATRLAR AFPLYDGLEE 


WSLVGR

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Crystal structure of serine hydroxymethyltransferase from Mycobacterium tuberculosis."
Seattle structural genomics center for infectious disease (SSGCID)
Submitted (APR-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842575 Genomic DNA. Translation: CAE55360.1.
AE000516 Genomic DNA. Translation: AAK45383.1.
PIRC70896.
RefSeqNP_335569.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LXBmodel-A1-426[»]
3H7FX-ray1.50A/B1-426[»]
ProteinModelPortalO53441.
SMRO53441. Positions 9-414.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001613; EBMYCP00000001613; EBMYCG00000001613.
EBMYCT00000071670; EBMYCP00000069729; EBMYCG00000071665.
GeneID924979.
GenomeReviewsGene locus MT1125 in contig AE000516_GR.
Gene locus Rv1093 in contig AL123456_GR.
KEGGmtc:MT1125.
mtu:Rv1093.
PATRIC18124236. VBIMycTub22151_1238.
TIGRMT1125.

Organism-specific databases

TubercuListRv1093.

Phylogenomic databases

GeneTreeEBGT00050000015531.
HOGENOMHBG301263.
OMADYARIKK.
PhylomeDBO53441.
ProtClustDBPRK00011.

Enzyme and pathway databases

BRENDA2.1.2.1. 3445.

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_MYCTU
AccessionPrimary (citable) accession number: O53441
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 91 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents