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B4S5Y9 (GLYA_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Paes_0584
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Prosthecochloris

Protein attributes

Sequence length440 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 – 440440Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000091568

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
B4S5Y9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 951D1E7A342A2612

FASTA44047,415
        10         20         30         40         50         60 
MSIEILQKQD KEIFDAISNE VLRQTETLEL IASENFASKA VMEACGSVMT NKYAEGYPGK 

        70         80         90        100        110        120 
RYYGGCEFVD VAEDLARERA KKLFGCQYVN VQPHSGSSAN MGVLFSVLKP GDTIMGLDLS 

       130        140        150        160        170        180 
HGGHLTHGSS VNFSGQLFDA HSYGVDRETG LIDMDRVEDM ALSVRPRLII CGASAYSQGF 

       190        200        210        220        230        240 
DFKAFRQIAD KVGAFLMADI AHPAGLIAAG LLNDPMPHCH FVTTTTHKTL RGPRGGMIMM 

       250        260        270        280        290        300 
GEDFENPMGI TIKTKAGRRT KMMSEVIDAE IMPGIQGGPL MHIIAAKAVA FGEALQPEFK 

       310        320        330        340        350        360 
EYAVQVRANA AAMAQKFISL DYNIVSGGTK NHLMLIDLRN KNVTGKVAEN LLHEAGITVN 

       370        380        390        400        410        420 
KNMVPFDDKS PFVTSGIRIG TPAMTTRGMT ESHAEAIVSL IDRVIGAAGS PDAGTVCGEV 

       430        440 
RSEIKAMCGT LPLNDFSPTL

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001108 Genomic DNA. Translation: ACF45640.1.
RefSeqYP_002015287.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S5Y9.
SMRB4S5Y9. Positions 4-428.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4S5Y9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6459962.
GenomeReviewsGene locus Paes_0584 in contig CP001108_GR.
KEGGpaa:Paes_0584.
PATRIC23040832. VBIProAes37017_0611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMADFENPLG.
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_PROA2
AccessionPrimary (citable) accession number: B4S5Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 27 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

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