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Q3IZN2 (GLYA_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:RHOS4_24340
ORF Names:RSP_0823
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length431 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 – 431431Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000235014

Regions

Region132 – 1343Substrate binding By similarity

Sites

Binding site421Pyridoxal phosphate By similarity
Binding site621Pyridoxal phosphate By similarity
Binding site641Substrate By similarity
Binding site711Substrate binding By similarity
Binding site721Pyridoxal phosphate By similarity
Binding site1061Pyridoxal phosphate By similarity
Binding site1281Substrate By similarity
Binding site1831Pyridoxal phosphate By similarity
Binding site2111Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2431Pyridoxal phosphate By similarity
Binding site2691Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3691Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2371N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IZN2 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 9BD0B30E66F97FC0

FASTA43145,734
        10         20         30         40         50         60 
MNAPHRDDGF FTESLSSRDP ELFASITGEL GRQRDEIELI ASENIVSRAV MEAQGSVMTN 

        70         80         90        100        110        120 
KYAEGYAGKR YYGGCDYVDV AETLAIERAK QLFGCAYVNV QPNSGSQANQ GVFQALIKPG 

       130        140        150        160        170        180 
DTILGMELAS GGHLTHGAAP NQSGKWFNAI QYGVRQQDQL IDYDQVAALA REHKPKLIIA 

       190        200        210        220        230        240 
GGSAIPRQID FARFRAIADE VGALLMVDMA HFAGLVAGGA HPSPFPHADV ATTTTHKTLR 

       250        260        270        280        290        300 
GPRGGMILTN SEEIAKKVNS AIFPGIQGGP LMHVIAAKAV AFGEALRPEF KAYAAQVVKN 

       310        320        330        340        350        360 
AQALADELMK GGLDIVTGGT DTHLMLVDLR PKGVKGNATE KALGRAHITC NKNGIPFDPE 

       370        380        390        400        410        420 
KPTVTSGVRL GTPAGTTRGF GEAEFREIGR LIVEVVDGLA ANGEEGNAAV EEAVKAKVAA 

       430 
LCARFPLYPT L 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA80002.1.
RefSeqYP_353903.1. NC_007493.1.

3D structure databases

ProteinModelPortalQ3IZN2.
SMRQ3IZN2. Positions 15-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IZN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3718402.
GenomeReviewsGene locus RHOS4_24340 in contig CP000143_GR.
KEGGrsp:RSP_0823.
NMPDRfig|272943.3.peg.2455.
PATRIC23154829. VBIRhoSph57909_2784.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAIFNAGYA.
PhylomeDBQ3IZN2.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycRSPH272943:RSP_0823-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_RHOS4
AccessionPrimary (citable) accession number: Q3IZN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 47 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