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A0M3N2 (GLYA_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:GFO_2262
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length424 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 – 424424Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006257

Regions

Region117 – 1193Substrate binding By similarity

Sites

Binding site271Pyridoxal phosphate By similarity
Binding site471Pyridoxal phosphate By similarity
Binding site491Substrate By similarity
Binding site561Substrate binding By similarity
Binding site571Pyridoxal phosphate By similarity
Binding site911Pyridoxal phosphate By similarity
Binding site1131Substrate By similarity
Binding site1681Pyridoxal phosphate By similarity
Binding site1961Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2691Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3691Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2221N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M3N2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 25A334F39BBE7CBB

FASTA42446,404
        10         20         30         40         50         60 
MQRDTQVFDL IAKEKERQLN GLELIASENF VSEAVLEAAG SVLTNKYAEG YPGKRYYGGC 

        70         80         90        100        110        120 
EVVDQVEQLA IDRLKELFNA EYANVQPHSG SQANTAVFHT VMKPGDKFLG FDLSHGGHLT 

       130        140        150        160        170        180 
HGSPVNFSGK LYNPVFYGVD KETGLIDYDA VAEIAEKEKP KMIIAGASAY SREIDYKRFR 

       190        200        210        220        230        240 
EIADSVGAIL VADMAHPAGL IAKGLISDPL PHCHIVTSTT HKTLRGPRGG IILMGKDFEN 

       250        260        270        280        290        300 
PFGEKLKNGN LKKMSTMLNS GIFPGNQGGP LEHIIAAKAI AFGEALTDEF LHYTVQVKKN 

       310        320        330        340        350        360 
AEKLAQAFVE KDYKVISGGT DNHMMLIDLR NKNVSGKEAE EALSKADITV NKNMVPFDDK 

       370        380        390        400        410        420 
SPFVTSGIRI GTPAVTTRGL QENDMNKIVD LIDRVITNIE NDTELEAVKK EVNSMMSGRP 


LFVA 

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References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL67227.1.
RefSeqYP_862294.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M3N2.
SMRA0M3N2. Positions 2-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M3N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4650520.
GenomeReviewsGene locus GFO_2262 in contig CU207366_GR.
KEGGgfo:GFO_2262.
NMPDRfig|411154.5.peg.2146.
PATRIC22073297. VBIGraFor5527_2186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAGTSNHLM.
PhylomeDBA0M3N2.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycGFOR411154:GFO_2262-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_GRAFK
AccessionPrimary (citable) accession number: A0M3N2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 40 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