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Q2RFW7 (GLYA_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:Moth_2390
OrganismMoorella thermoacetica (strain ATCC 39073)
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Moorella group › Moorella

Protein attributes

Sequence length416 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 – 416416Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000234986

Regions

Region123 – 1253Substrate binding By similarity

Sites

Binding site331Pyridoxal phosphate By similarity
Binding site531Pyridoxal phosphate By similarity
Binding site551Substrate By similarity
Binding site621Substrate binding By similarity
Binding site631Pyridoxal phosphate By similarity
Binding site971Pyridoxal phosphate By similarity
Binding site1191Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2591Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3591Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RFW7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 82E486F995F17984

FASTA41645,196
        10         20         30         40         50         60 
MNLETVAKVD PEIVAAVRGE LQRQRTHLEL IASENFVSQA VMEAYSCVLT NKYAEGYPGK 

        70         80         90        100        110        120 
RYYGGCEWAD VVENLARERA KALFGAEHAN VQPHSGSQAN TAVYLAVLNP GDKALGMNLA 

       130        140        150        160        170        180 
HGGHLTHGSP VSLSGKYYNF CFYGVDAKTG RIDYDAVARI AREERPRLIV AGASAYPRVI 

       190        200        210        220        230        240 
DFARFREIAD EVGALLMVDM AHIAGLVAAG IHPNPVPYAH FVTTTTHKTM RGPRGGIILT 

       250        260        270        280        290        300 
TREYARDIDK AVFPGVQGGP LMHVIAAKAV ALKEAMLPEF KRYQEQIVTN ARTLADALMG 

       310        320        330        340        350        360 
YGFNLVSGGT DNHLMLVDLR NKNITGREAE DILASVQITV NKNAIPFDPQ KPSVTSGIRL 

       370        380        390        400        410 
GTAALTSRGM DADAMVQVAR AIDLALSYGP DEKKLEEARG IVAELCRAFP LYQELD

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed: 18631365] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000232 Genomic DNA. Translation: ABC20672.1.
RefSeqYP_431215.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RFW7.
SMRQ2RFW7. Positions 3-405.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2RFW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3832029.
GenomeReviewsGene locus Moth_2390 in contig CP000232_GR.
KEGGmta:Moth_2390.
NMPDRfig|264732.9.peg.2422.
PATRIC22642278. VBIMooThe6753_2603.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMADYLIDMD.
PhylomeDBQ2RFW7.

Enzyme and pathway databases

BioCycMTHE264732:MOTH_2390-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_MOOTA
AccessionPrimary (citable) accession number: Q2RFW7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 47 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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