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Q9HI38 (GLYA_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. 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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Names and origin

Protein namesRecommended name:
Serine hydroxymethyltransferase
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.-
Gene names
Name:glyA
Ordered Locus Names:Ta1509
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma ›

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with a modified folate serving as the one-carbon carrier. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism By similarity. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the SHMT family.

Sequence caution

The sequence CAC12627.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_0000113727

Regions

Region119 – 1213Substrate binding By similarity

Sites

Binding site291Pyridoxal phosphate By similarity
Binding site491Pyridoxal phosphate By similarity
Binding site511Substrate By similarity
Binding site581Substrate By similarity
Binding site591Pyridoxal phosphate By similarity
Binding site931Pyridoxal phosphate By similarity
Binding site1151Substrate; via carbonyl oxygen By similarity
Binding site1701Pyridoxal phosphate By similarity
Binding site1981Pyridoxal phosphate By similarity
Binding site2241Pyridoxal phosphate By similarity
Binding site3601Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2251N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HI38 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 2FF2525003EB5DB5

FASTA42646,975
        10         20         30         40         50         60 
MSYEDAEYIR EMAMKHSEMF GEGIALIASE NVMSPLAKEV MISDLESRYA EGLPHHRYYQ 

        70         80         90        100        110        120 
GNYYVDLIED RTNELLSKLF RTSQTDPRPI SGTNANSAAI YALAGPGDLV ATPSLSGGGH 

       130        140        150        160        170        180 
ISAAEFGILG MRSVRTINYP YDMDTMTIDP DQASKMIIKE KPKVCLFGQS VFMFPAPLKE 

       190        200        210        220        230        240 
MAEAFHEVGC KVWYDGAHVL GLIAGGRFQD PLREGADIVT GSTHKTFPGP QHGVILGNTD 

       250        260        270        280        290        300 
DETWKAVRRA VFPGVLSNHH LNAMAALGIT AAEELEFGKR YADDIISNAK VLAEELYANG 

       310        320        330        340        350        360 
FNVLAEKRGF TESHTMAVDV SKNGGGKYVA ETLEKCGIIL NKNLLPWDDN KKSQNPSGIR 

       370        380        390        400        410        420 
IGVQEATRVG MGKSEMKEIA SLITRAIIRH EDPEKIKAEV KQLKSGFREV KYCYGKMDGY 


SYIKLI

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References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445067 Genomic DNA. Translation: CAC12627.1. Different initiation.
RefSeqNP_394959.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HI38.
ModBaseSearch...

Protein-protein interaction databases

STRING273075.Ta1509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12627; CAC12627; CAC12627.
GeneID1456954.
KEGGtac:Ta1509.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239403.
KOK00600.
OMAIAKLQWA.
ProtClustDBPRK00011.

Enzyme and pathway databases

UniPathwayUPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 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_THEAC
AccessionPrimary (citable) accession number: Q9HI38
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 27, 2002
Last modified: May 1, 2013
This is version 83 of the entry and version 2 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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