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O59347 (GLYA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. 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:PH1654
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length427 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.

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 – 427427Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113722

Regions

Region120 – 1223Substrate binding By similarity

Sites

Binding site301Pyridoxal phosphate By similarity
Binding site501Pyridoxal phosphate By similarity
Binding site521Substrate By similarity
Binding site591Substrate binding By similarity
Binding site601Pyridoxal phosphate By similarity
Binding site1711Pyridoxal phosphate By similarity
Binding site1991Pyridoxal phosphate By similarity
Binding site2251Pyridoxal phosphate By similarity
Binding site3651Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O59347 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 88BC027E2A086CF7

FASTA42747,982
        10         20         30         40         50         60 
MTYREYRDKV LHFIEEHEKW RSHTINLIAS ENITSPSVNR AVASGFMHKY AEGWPKQRYY 

        70         80         90        100        110        120 
QGCKYVDEVE LIGVELFTKL FKSDYADLRP VSGTNANQAV FFGLGQPGDK VIVLHTSHGG 

       130        140        150        160        170        180 
HISHMPFGAA GMRGLEVHTW PFDFESFNID VDKAEKMIRE LEPKIVVFGG SLFPFPHPVK 

       190        200        210        220        230        240 
ELAPVAKEVG AFVVYDAAHV LGLIAGGEFQ DPLREGADIM TASTHKTFPG PQGGVILYKK 

       250        260        270        280        290        300 
FADDETIAKL QWAIFPGVVS NHHLHHMAGK VITAAEMLEY GEAYAKQIVK NAKALAEALA 

       310        320        330        340        350        360 
EEGFKVIGED QGYTKSHQVI VDVSDLHPAG GGWAAPLLEE AGIILNKNLL PWDPLEKVNE 

       370        380        390        400        410        420 
PSGLRIGVQE MTRVGMMEDE MKEIAHFMKR VLIDKEDPKK VRKDVYYFRL EYQKVYYSFD 


YGLPMKE

« Hide

References

[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA30766.1.
PIRF71045.
RefSeqNP_143503.1. NC_000961.1.

3D structure databases

ProteinModelPortalO59347.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000001995; EBPYRP00000001995; EBPYRG00000001995.
GeneID1442502.
GenomeReviewsGene locus PH1654 in contig BA000001_GR.
KEGGpho:PH1654.
NMPDRfig|70601.1.peg.1616.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022355.
HOGENOMHBG301263.
OMARGMGAKE.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycPHOR70601:PH1654-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_PYRHO
AccessionPrimary (citable) accession number: O59347
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 83 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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