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Q31CS4 (GLYA_PROM9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:PMT9312_0260
OrganismProchlorococcus marinus (strain MIT 9312) [Complete proteome] [HAMAP]
Taxonomic identifier74546 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length423 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 – 423423Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000234998

Regions

Region124 – 1263Substrate binding By similarity

Sites

Binding site341Pyridoxal phosphate By similarity
Binding site541Pyridoxal phosphate By similarity
Binding site561Substrate By similarity
Binding site631Substrate binding By similarity
Binding site641Pyridoxal phosphate By similarity
Binding site1201Substrate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3611Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31CS4 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: AAF63E243EE55A8E

FASTA42346,016
        10         20         30         40         50         60 
MNILQNLKKS DPVISNFINS EKNRQETHLE LIASENFASI AVMQAQGSVL TNKYAEGLPQ 

        70         80         90        100        110        120 
KRYYGGCEFV DEIEELAIQR AKKLFNANWA NVQPHSGAQA NAAVFLSLLQ PGDTIMGMDL 

       130        140        150        160        170        180 
SHGGHLTHGS PVNMSGKWFN AVHYGVNKET SELNFDEIRE IALETKPKLI ICGYSAYPRT 

       190        200        210        220        230        240 
IDFESFRNIA DEVGAFLMAD IAHIAGLVAS KLHPNPLPYC DVVTTTTHKT LRGPRGGLIL 

       250        260        270        280        290        300 
CKDGEFGKKF DKSVFPGTQG GPLEHIIAAK AVAFGEALQP DFVNYSQQVI KNAKVLASTL 

       310        320        330        340        350        360 
ISRGIDIVSG GTDNHIVLLD LRSINMTGKI ADLLVSAVNI TANKNTVPFD PESPFVTSGL 

       370        380        390        400        410        420 
RLGTAALTTR GFNETAFAEV GEIIADRLLN PNDSVIESQC KDKVLALCNR FPLYEGKLEA 


SIK

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References

[1]"Complete sequence of Prochlorococcus marinus str. MIT 9312."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9312.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000111 Genomic DNA. Translation: ABB49321.1.
RefSeqYP_396757.1. NC_007577.1.

3D structure databases

ProteinModelPortalQ31CS4.
SMRQ31CS4. Positions 4-409.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ31CS4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3765046.
GenomeReviewsGene locus PMT9312_0260 in contig CP000111_GR.
KEGGpmi:PMT9312_0260.
PATRIC23004142. VBIProMar70153_0265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAIFNAGYA.
PhylomeDBQ31CS4.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycPMAR74546:PMT9312_0260-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_PROM9
AccessionPrimary (citable) accession number: Q31CS4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: December 6, 2005
Last modified: January 25, 2012
This is version 46 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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