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Q2SFI7 (GLYA1_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:HCH_03860
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length426 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 – 426426Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 1
PRO_0000234981

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2SFI7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 95FE448D89509CB5

FASTA42646,213
        10         20         30         40         50         60 
MFTEDMRIAD YDPELSAAIN AEKRRQEEHI ELIASENYVS PRVMEAQGGV LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDVAEQLAID RAKQLFGADY ANVQPHSGSQ ANAGVYLALA KPGDTILGMS 

       130        140        150        160        170        180 
LDHGGHLTHG AKPNFSGKIF NAVQYGLNPE TGEIDYDQVE RLAKEHKPKL VIAGFSAYSR 

       190        200        210        220        230        240 
VVDWQRFRDI ADSVGAYLIV DMAHVAGLVA AGLYPSPVQI ADVTTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LAKSNPEIEK KLQSLIFPGI QGGPLMHVIA AKAVAFKEAL EPAFRDYQQQ VVNNARAMAD 

       310        320        330        340        350        360 
AVKARGYKVV SGGTDNHLFL IDLIDKGVTG KDADAALGRA YITVNKNTVP NDPQSPFVTS 

       370        380        390        400        410        420 
GLRIGTPGVT TRGFKEKEVV ELANWICDVL DNMGDESVVE KVREKVLSIC RDFPVYRANA 


KSGAAL 

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References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000155 Genomic DNA. Translation: ABC30587.1.
RefSeqYP_435012.1. NC_007645.1.

3D structure databases

ProteinModelPortalQ2SFI7.
SMRQ2SFI7. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SFI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3838963.
GenomeReviewsGene locus HCH_03860 in contig CP000155_GR.
KEGGhch:HCH_03860.
NMPDRfig|349521.5.peg.3380.
PATRIC22088254. VBIHahChe29232_3500.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAFSASYEM.
PhylomeDBQ2SFI7.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycHCHE349521:HCH_03860-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_HAHCH
AccessionPrimary (citable) accession number: Q2SFI7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 44 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