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Q2LQM6 (GLYA_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:SYNAS_01860
ORF Names:SYN_02367
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Syntrophobacterales › Syntrophaceae › Syntrophus

Protein attributes

Sequence length417 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 – 417417Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000235040

Regions

Region121 – 1233Substrate binding By similarity

Sites

Binding site311Pyridoxal phosphate By similarity
Binding site511Pyridoxal phosphate By similarity
Binding site531Substrate By similarity
Binding site601Substrate binding By similarity
Binding site611Pyridoxal phosphate By similarity
Binding site1171Substrate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site2001Pyridoxal phosphate By similarity
Binding site2251Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3571Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LQM6 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: D77AD03FB2C78C50

FASTA41745,326
        10         20         30         40         50         60 
MSALMKTDPE IAEAIRLETR RQAGKLELIA SENFVSEAVL EAQGCIMTNK YAEGYPGKRY 

        70         80         90        100        110        120 
YGGCEYVDIA ENLAIERCKA LFGADYVNVQ PHSGTQANMA VYFSALSVGD TILGMNLAHG 

       130        140        150        160        170        180 
GHLSHGSPAN FSGKFYNVVP YGVDRETETI DYNQVEDLAL QHKPRMIVVG ASAYPRTIDF 

       190        200        210        220        230        240 
EKFRAIADKV GALVMADIAH IAGLVATGLH PSPVPVCEYV TSTTHKTLRG PRGGLVMCQA 

       250        260        270        280        290        300 
SYQKTLSSRV FPGVQGGPLM HIIAAKAVAF KEALTDEFKD YQSQIVKNAQ ALAKELIGRG 

       310        320        330        340        350        360 
YRLVSGGTDN HLLLMDLTDK GLTGKEAQES LDSAGITVNK NGIPFDTRGP MVTSGIRIGT 

       370        380        390        400        410 
PALTSRGMKE EEMRTIARLI AEVLEHRDNE KHLMAVKEEV GRLCQNFPLY AERIASA

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References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000252 Genomic DNA. Translation: ABC76065.1.
RefSeqYP_460233.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LQM6.
SMRQ2LQM6. Positions 1-403.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2LQM6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3884485.
GenomeReviewsGene locus SYNAS_01860 in contig CP000252_GR.
KEGGsat:SYN_02367.
NMPDRfig|56780.10.peg.184.
PATRIC23860747. VBISynAci70500_0202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGTSNHLM.
PhylomeDBQ2LQM6.

Enzyme and pathway databases

BioCycSACI56780:SYN_02367-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_SYNAS
AccessionPrimary (citable) accession number: Q2LQM6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: February 21, 2006
Last modified: January 25, 2012
This is version 43 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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