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Q30R29 (GLYA1_SULDN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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 1
Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Ordered Locus Names:Suden_1274
OrganismSulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira denitrificans (strain ATCC 33889 / DSM 1251)) [Complete proteome] [HAMAP]
Taxonomic identifier326298 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Sulfurimonas

Protein attributes

Sequence length415 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 – 415415Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 1
PRO_0000235045

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 site951Pyridoxal phosphate By similarity
Binding site1171Substrate By similarity
Binding site1711Pyridoxal phosphate By similarity
Binding site1991Pyridoxal phosphate By similarity
Binding site2241Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2571Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3571Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2251N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q30R29 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: F6EE20DFE26ED2C8

FASTA41545,183
        10         20         30         40         50         60 
MSFLKEFDKD IFDLCEKELE RQSNHLEMIA SENFTLPAVM EAMGSVFTNK YAEGYPAKRY 

        70         80         90        100        110        120 
YGGCEYADGV EQLAIDRACK LFGCNYANVQ PHSGSQANAA VYAALLKAGD KLLGMDLSHG 

       130        140        150        160        170        180 
GHLTHGSKPS FSGQNYSSFT YGVELDGRMN YDKILEIAKA VQPKIIVCGA SAYAREIDFK 

       190        200        210        220        230        240 
KFREIADAVG AIMFADIAHV AGLVVAGEHM SPFPHAHVVT TTTHKTLAGP RGGMIMTNDE 

       250        260        270        280        290        300 
DIAKKINSAI FPGIQGGPLV HVIAAKAVGF KYNLSAEWKD YAVQVKANAK ILGEVLVKRG 

       310        320        330        340        350        360 
YDLVSGGTDN HLVLLSFLNR DFSGKDADIA LGNAGITVNK NTVPGETRSP FVTSGIRIGS 

       370        380        390        400        410 
PALTSRGMKE REFEFIANKI ADVLDDINNT KLQESVKKEL KELAQKFVIY NQSTY

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000153 Genomic DNA. Translation: ABB44552.1.
RefSeqYP_393787.1. NC_007575.1.

3D structure databases

ProteinModelPortalQ30R29.
SMRQ30R29. Positions 4-411.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ30R29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3763597.
GenomeReviewsGene locus Suden_1274 in contig CP000153_GR.
KEGGtdn:Suden_1274.
NMPDRfig|326298.3.peg.498.
PATRIC23771176. VBISulDen68967_1323.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAKEREFEF.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycTDEN326298:TMDEN_1274-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 nameGLYA1_SULDN
AccessionPrimary (citable) accession number: Q30R29
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: December 6, 2005
Last modified: January 25, 2012
This is version 50 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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