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Q9ZMP7 (GLYA_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. 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:jhp_0171
OrganismHelicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

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_0000113587

Regions

Region122 – 1243Substrate binding By similarity

Sites

Binding site321Pyridoxal phosphate By similarity
Binding site521Pyridoxal phosphate By similarity
Binding site541Substrate By similarity
Binding site611Substrate binding By similarity
Binding site621Pyridoxal phosphate By similarity
Binding site961Pyridoxal phosphate By similarity
Binding site1181Substrate By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site2001Pyridoxal phosphate By similarity
Binding site2251Pyridoxal phosphate By similarity
Binding site2321Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3581Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZMP7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 58D9DC2E9E8A7D9C

FASTA41645,706
        10         20         30         40         50         60 
MAYFLEQTDS EIFEFIVEEF KRQNEHLEMI ASENYTFPSV MEAMGSILTN KYAEGYPNKR 

        70         80         90        100        110        120 
YYGGCEVVDK IESLAIERAK KLFNCQFANV QAHSGSQANN AVYHALLKLY DKILGMDLSC 

       130        140        150        160        170        180 
GGHLTHGAKV SLTGKHYQSF SYGVGLDGYI DYEEALKIAQ SVKPQIIVCG FSAYPREIDF 

       190        200        210        220        230        240 
KKFREIADAV GALLLGDIAH VAGLVVANEH AHPFPHCHVV SSTTHKTLRG PRGGLILTND 

       250        260        270        280        290        300 
EEIAAKIDKA IFPGTQGGPL MHVIAAKAVG FKENLKPEFK AYAKLVKSNM QVLAKTLKEK 

       310        320        330        340        350        360 
NHKLVSGGTS NHLLLMDFLD KPYSGKDADI ALGNAGITVN KNTIPGETRN PFVTSGIRIG 

       370        380        390        400        410 
SAALSARGMG AKEFEIIGNK ISDILNDINN VSLQLHVKEE LKTMANQFPV YHQPIF 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD05752.1.
PIRG71965.
RefSeqNP_222892.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZMP7.
SMRQ9ZMP7. Positions 7-410.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9ZMP7. 1 interaction.
STRINGQ9ZMP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID889253.
GenomeReviewsGene locus jhp_0171 in contig AE001439_GR.
KEGGhpj:jhp0171.
NMPDRfig|85963.1.peg.170.
PATRIC20604964. VBIHelPyl98156_0194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMARGMGAKE.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycHPYL85963:JHP0171-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_HELPJ
AccessionPrimary (citable) accession number: Q9ZMP7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 79 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