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A4SFY3 (GLYA_PROVI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Cvib_1381
OrganismProsthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides (strain DSM 265)) [Complete proteome] [HAMAP]
Taxonomic identifier290318 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length441 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 – 441441Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000074904

Regions

Region123 – 1253Substrate binding By similarity

Sites

Binding site331Pyridoxal phosphate By similarity
Binding site531Pyridoxal phosphate By similarity
Binding site551Substrate By similarity
Binding site621Substrate binding By similarity
Binding site631Pyridoxal phosphate By similarity
Binding site971Pyridoxal phosphate By similarity
Binding site1191Substrate By similarity
Binding site1741Pyridoxal phosphate By similarity
Binding site2021Pyridoxal phosphate By similarity
Binding site2271Pyridoxal phosphate By similarity
Binding site2341Pyridoxal phosphate By similarity
Binding site2781Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3781Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SFY3 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 584942D51894EC15

FASTA44148,029
        10         20         30         40         50         60 
MDTDILKMQD REVFEAIALE TGRQMETLEL IASENFTSRA VMQACGSVMT NKYAEGYPGK 

        70         80         90        100        110        120 
RYYGGCEFVD IAENLARDRA KKLFGCEYVN VQPHSGSSAN MAVLFSVLKP GDCIMGLDLS 

       130        140        150        160        170        180 
HGGHLTHGSS VNFSGQMYKA HAYGVDGETG IIDMNQVEKM ALEVRPRLII CGASAYSQGF 

       190        200        210        220        230        240 
DFKAFREIAD KVGAFLMADI AHPAGLIVSG LLSDPMPHCH FVTTTTHKTL RGPRGGMIMM 

       250        260        270        280        290        300 
GKDFENPMGI TIKTKNGQRV KMMSEVMDAE VMPGIQGGPL MHIIAGKAVA FGEALRPEFR 

       310        320        330        340        350        360 
QYAMQVRSNA AAMSERFLSL GYNIVSGGTK NHLMLLDLRN KDITGKVVEN TLHEAGITVN 

       370        380        390        400        410        420 
KNMVPFDDKS PFVTSGIRIG TAAMTTRGMN EDDSRLIAEL IDRVILSAAS PESSSVCRSV 

       430        440 
KEEIRSLCLR NPLEGYGVTP S 

« Hide

References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37392.1.
RefSeqYP_001130894.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SFY3.
SMRA4SFY3. Positions 4-428.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SFY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4970188.
GenomeReviewsGene locus Cvib_1381 in contig CP000607_GR.
KEGGpvi:Cvib_1381.
PATRIC21397262. VBIChlPha132153_1457.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGMILAKE.
PhylomeDBA4SFY3.
ProtClustDBPRK00011.

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_PROVI
AccessionPrimary (citable) accession number: A4SFY3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 37 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