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Q481S6 (GLYA2_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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 2

Short name=SHMT 2
Short name=Serine methylase 2
EC=2.1.2.1
Gene names
Name:glyA2
Ordered Locus Names:CPS_2477
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length417 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 – 417417Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000234968

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
Q481S6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 492CADB4737489D5

FASTA41745,458
        10         20         30         40         50         60 
MFYKNDQIAG FDDSIWQAME QEDKRQQDHV ELIASENYTS ARVMQAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEH VDVIEQLAID RAKELFGADY ANVQPHSGSQ ANAAVFMALL KPGETVLGMS 

       130        140        150        160        170        180 
LAHGGHLTHG SKVSFSGKIY NAVQYGLNEA TGEIDYEEVE RLAKEHQPKM IIAGFSAYSR 

       190        200        210        220        230        240 
VVDWQRFRDI ADSIGAWLFV DMAHVAGLVA AGLYPNPVPI ADVVTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LAKQNDELAK KLNSAVFPAG QGGPLMHVIA AKAICFKEAL GEGYVEYQQQ VIDNAREMAK 

       310        320        330        340        350        360 
TFQTRGYNVV SGGTDNHLFL LDLIDKGITG KDADAALGRA NITVNKNSVP NDPQSPFVTS 

       370        380        390        400        410 
GLRIGTPAIT SRGFGLEEAA ALTGWICDVL DDISNEQVID DVRSKVLDLC EKNPVYR 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ25763.1.
RefSeqYP_269193.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ481S6.
SMRQ481S6. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ481S6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3520009.
GenomeReviewsGene locus CPS_2477 in contig CP000083_GR.
KEGGcps:CPS_2477.
NMPDRfig|167879.3.peg.2411.
PATRIC21468023. VBIColPsy94388_2245.
TIGRCPS_2477.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycCPSY167879:CPS_2477-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 nameGLYA2_COLP3
AccessionPrimary (citable) accession number: Q481S6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 43 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