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Q5QXT4 (GLYA_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:IL1872
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length418 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 – 418418Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113589

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 site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3641Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QXT4 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 5D55838E40D463DD

FASTA41845,536
        10         20         30         40         50         60 
MLKSEMNIAD FDADLWQAMQ DEVERQEQHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
HKRYYGGCEF VDKVEDLAIE RAKELFGAKY ANVQPHSGSQ ANTAAFMAMM EAGDTFLGMS 

       130        140        150        160        170        180 
LAHGGHLTHG SGVNFSGKLY NAVSYGLDES TGEIDYAEVE KLAQEHKPKV IVAGFSAYSG 

       190        200        210        220        230        240 
IVDWAKFREI ADKVDAYLMV DMAHVAGLVA AGVYPNPVPY AHVVTTTTHK TLAGPRGGLI 

       250        260        270        280        290        300 
ISGSDDEKLH KKLNSAVFPG NQGGPLCHVI AGKAVAFQEA LQPEFKDYQK QVLVNANAMV 

       310        320        330        340        350        360 
KTMQARGYKI VSNGTQNHLF LVDLIDKDIT GKDADAALGN AFITVNKNAV PNDPRSPFVT 

       370        380        390        400        410 
SGLRLGTPAI TRRGFKEAEA EQVANWICDV LDDIADESKI NQVREQVKAL CAKFPVYG

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017340 Genomic DNA. Translation: AAV82704.1.
RefSeqYP_156253.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXT4.
SMRQ5QXT4. Positions 1-418.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3172588.
GenomeReviewsGene locus IL1872 in contig AE017340_GR.
KEGGilo:IL1872.
NMPDRfig|283942.3.peg.1824.
PATRIC22141864. VBIIdiLoi21852_1881.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAGTSNHLM.

Enzyme and pathway databases

BioCycILOI283942:IL1872-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_IDILO
AccessionPrimary (citable) accession number: Q5QXT4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 51 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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