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Q2RTB8 (GLYA2_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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 2
Short name=SHMT 2
Short name=Serine methylase 2
EC=2.1.2.1
Gene names
Name:glyA2
Ordered Locus Names:Rru_A1827
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255)
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length430 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 – 430430Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000235016

Regions

Region132 – 1343Substrate binding By similarity

Sites

Binding site421Pyridoxal phosphate By similarity
Binding site621Pyridoxal phosphate By similarity
Binding site641Substrate By similarity
Binding site711Substrate binding By similarity
Binding site721Pyridoxal phosphate By similarity
Binding site1281Substrate By similarity
Binding site1831Pyridoxal phosphate By similarity
Binding site2111Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2431Pyridoxal phosphate By similarity
Binding site2691Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3691Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2371N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RTB8 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: CC5FC9DCF64D91A1

FASTA43045,352
        10         20         30         40         50         60 
MTAYTPWTGF FSASVAQADP ELDRVLRAEL SRQQDQIELI ASENIVSRAV LEAAGSVLTN 

        70         80         90        100        110        120 
KYAEGYPGKR YYGGCEEVDV AEELAIERAK ALFGCSYVNV QPHSGAQANG AVMMALVKPG 

       130        140        150        160        170        180 
DTIMGMSLAA GGHLTHGAPP AQSGKWFNAV QYGVRLQDAS IDFDEVATLA ETHKPKLIIA 

       190        200        210        220        230        240 
GGSAYPRIID FAKFREIADR VGALFMVDMA HFAGLVAAGL HPSPLPYADI VTTTTHKTLR 

       250        260        270        280        290        300 
GPRGGMVLSN NPDIGKKINS AVFPGLQGGP LMHIIAAKAV AFGEALRPEF KVYAQAVIDN 

       310        320        330        340        350        360 
AKALTDALAA GGLNIVSGGT DTHLALVDLR PKALTGNIVE KSLERANITT NKNGIPFDPE 

       370        380        390        400        410        420 
KPAITSGIRV GTPAGTTRGF GTAEFTEIGK LIVEVLDGLA ANGEDNSQAE AAVREKVAVL 

       430 
CRRFPIYGGL

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / NCIB 8255.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000230 Genomic DNA. Translation: ABC22627.1.
RefSeqYP_426914.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RTB8.
SMRQ2RTB8. Positions 17-420.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2RTB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3835251.
GenomeReviewsGene locus Rru_A1827 in contig CP000230_GR.
KEGGrru:Rru_A1827.
NMPDRfig|1085.1.peg.2402.
PATRIC23327316. VBIRhoRub82919_1905.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMADYDQIAA.
PhylomeDBQ2RTB8.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycRRUB269796:RRU_A1827-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 nameGLYA2_RHORT
AccessionPrimary (citable) accession number: Q2RTB8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 46 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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