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Q0K7W0 (GLYA_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:H16_A2834
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

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
PRO_1000006302

Regions

Region126 – 1283Substrate binding By similarity

Sites

Binding site361Pyridoxal phosphate By similarity
Binding site561Pyridoxal phosphate By similarity
Binding site581Substrate By similarity
Binding site651Substrate binding By similarity
Binding site661Pyridoxal phosphate By similarity
Binding site1001Pyridoxal phosphate By similarity
Binding site1221Substrate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3611Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0K7W0 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 1B7C43C63D55475D

FASTA41545,112
        10         20         30         40         50         60 
MFERSRFTID QIDPEVFAAI QQENQRQEDH IELIASENYT SPAVMAAQGS QLTNKYAEGY 

        70         80         90        100        110        120 
PGKRYYGGCE YVDVVEQLAI DRVKQLFGAE AANVQPNSGS QANQGVYFAV LKPGDTIMGM 

       130        140        150        160        170        180 
SLAEGGHLTH GMALNMSGKW FNVVSYGLNA QEDIDYDALE KLAQEKKPKL IIAGASAFAL 

       190        200        210        220        230        240 
RIDFERISKV AKSIGAYFMV DMAHYAGLIA AGVYPNPVPH ADFVTTTTHK SLRGPRGGVI 

       250        260        270        280        290        300 
LMKAEHEKAI NSAIFPGIQG GPLMHVIAGK AVAFKEALTP EFKEYQQQVV KNAAVLAETL 

       310        320        330        340        350        360 
IARGLRIVSG RTESHVMLVD LRAKNITGKE AERILGEAHI TVNKNAIPND PEKPFVTSGI 

       370        380        390        400        410 
RLGSPAMTTR GFKEEEARIV GNLIADVLDN PHDAANIASV REQAAALTKR FPVYG 

« Hide

References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM260479 Genomic DNA. Translation: CAJ93911.1.
RefSeqYP_727279.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K7W0.
SMRQ0K7W0. Positions 4-415.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0K7W0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4248400.
GenomeReviewsGene locus H16_A2834 in contig AM260479_GR.
KEGGreh:H16_A2834.
PATRIC35235207. VBIRalEut6770_3234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMARIDFERI.
PhylomeDBQ0K7W0.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycREUT381666:H16_A2834-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_CUPNH
AccessionPrimary (citable) accession number: Q0K7W0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: January 25, 2012
This is version 40 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