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B8GG35 (GLYA_METPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 24. 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:Mpal_0745
OrganismMethanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c) [Complete proteome] [HAMAP]
Taxonomic identifier521011 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesGenera incertae sedisMethanosphaerula

Protein attributes

Sequence length415 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 – 415415Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000202267

Regions

Region122 – 1243Substrate binding By similarity

Sites

Binding site311Pyridoxal phosphate By similarity
Binding site511Pyridoxal phosphate By similarity
Binding site531Substrate By similarity
Binding site601Substrate binding By similarity
Binding site611Pyridoxal phosphate By similarity
Binding site1181Substrate By similarity
Binding site1731Pyridoxal phosphate By similarity
Binding site2011Pyridoxal phosphate By similarity
Binding site2261Pyridoxal phosphate By similarity
Binding site2331Pyridoxal phosphate By similarity
Binding site2581Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3581Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B8GG35 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 9BA1ACB87FC99254

FASTA41544,991
        10         20         30         40         50         60 
MSYLATADPE IAELIECERL RQVNGLELIA SENLVSKAVL EAMGSILTNK YAEGYPGKRY 

        70         80         90        100        110        120 
YGGCEFHDRI ENLARDRLKQ LFNAEHANVQ PHSGTQANMA VYFSVMECGK DRMMSMSLTQ 

       130        140        150        160        170        180 
GGHLSHGSPV SFSGKMYEVS QYGVDLKTEL IDYGAVEEMA KKVKPKVIVC GASAYPREID 

       190        200        210        220        230        240 
FKAFQEIADS VGAYCMADIA HIAGLCATGV HPSPVNVVNF TTSTTHKTLR GPRGGVIMCN 

       250        260        270        280        290        300 
EEYGAMIDKA IFPGMQGGPL MHTIAGKAVC FKEALQPSFK QYSRQVVKNA QALAETLGEA 

       310        320        330        340        350        360 
GLRLVSGGTD NHLILIDLSN RGLTGLEAEV ALGKAGITVN KNTIPNENRS PFVTSGLRIG 

       370        380        390        400        410 
TPAVTSRGMK EDEMHQIGEY IIRVLKDIQD EATISAVKNE VTALASRYSL YPPSL 

« Hide

References

[1]"Complete sequence of Candidatus Methanosphaerula E1-9c."
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., Kiss H., Lu M., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.O., Zinder S.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1556 / DSM 19958 / E1-9c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001338 Genomic DNA. Translation: ACL16109.1.
RefSeqYP_002465832.1. NC_011832.1.

3D structure databases

ProteinModelPortalB8GG35.
ModBaseSearch...

Protein-protein interaction databases

STRINGB8GG35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7270480.
GenomeReviewsGene locus Mpal_0745 in contig CP001338_GR.
KEGGmpl:Mpal_0745.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMAFPMYADR.
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.
[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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_METPE
AccessionPrimary (citable) accession number: B8GG35
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: March 3, 2009
Last modified: January 25, 2012
This is version 24 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