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A5G0E0 (GLYA_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Acry_2123
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

Protein attributes

Sequence length432 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 – 432432Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006210

Regions

Region135 – 1373Substrate binding By similarity

Sites

Binding site451Pyridoxal phosphate By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site671Substrate By similarity
Binding site741Substrate binding By similarity
Binding site751Pyridoxal phosphate By similarity
Binding site1311Substrate By similarity
Binding site1861Pyridoxal phosphate By similarity
Binding site2141Pyridoxal phosphate By similarity
Binding site2391Pyridoxal phosphate By similarity
Binding site2461Pyridoxal phosphate By similarity
Binding site2721Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2401N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5G0E0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6A5A603C1F5B387D

FASTA43245,773
        10         20         30         40         50         60 
MNQQSPIANI SRFFNAPLAE TDPDLAAAIG RELGRQQDGI ELIASENIVS RAVLEAQGSV 

        70         80         90        100        110        120 
LTNKYAEGYP GKRYYGGCAA VDIAEELAIA RAKELFGCAF ANVQPHSGAQ ANQAVFLALL 

       130        140        150        160        170        180 
NAGDTILGMS LAAGGHLTHG AAPNLSGKWF DAVQYGVKRE DGTLDYEELE RLARERKPKL 

       190        200        210        220        230        240 
IIAGGSAYPR FIDFARIRKV ADEVGAYFMV DMAHFAGLVA AGIFPSPVPH AHVVTTTTHK 

       250        260        270        280        290        300 
TLRGPRGGMI LSNDLDLGKK INSAVFPGLQ GGPLMHVIAA KAVAFGEALR PEFRAYQKAL 

       310        320        330        340        350        360 
AENAKVLAET LVEGGLDIVT GGTDCHLMLV DLRPKNVTGK AAEASLERAH MTANKNAIPF 

       370        380        390        400        410        420 
DPAKPAVTSG IRLGTPAATT RGFGPDEFRM VGRFIVEVLD GLSASNDGDN AAVEAAVGAK 

       430 
VLELCARFPI YR

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000697 Genomic DNA. Translation: ABQ31322.1.
RefSeqYP_001235241.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5G0E0.
SMRA5G0E0. Positions 20-430.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5G0E0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5162416.
GenomeReviewsGene locus Acry_2123 in contig CP000697_GR.
KEGGacr:Acry_2123.
PATRIC20649318. VBIAciCry6074_2630.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAMILTNHE.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycACRY349163:ACRY_2123-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_ACICJ
AccessionPrimary (citable) accession number: A5G0E0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 34 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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