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UniProtKB/Swiss-Prot entry P27248

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GCST_ECOLI
Primary accession number P27248
Secondary accession number Q2M9T6
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name Aminomethyltransferase
Synonyms EC 2.1.2.10
Glycine cleavage system T protein
Gene name
Name: gcvT
OrderedLocusNames: b2905, JW2873
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8219277 [NCBI, ExPASy, EBI, Israel, Japan]
Stauffer L.T., Ghrist A., Stauffer G.V.;
"The Escherichia coli gcvT gene encoding the T-protein of the glycine cleavage enzyme system.";
DNA Seq. 3:339-346(1993).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8375392 [NCBI, ExPASy, EBI, Israel, Japan]
Okamura-Ikeda K., Ohmura Y., Fujiwara K., Motokawa Y.;
"Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system.";
Eur. J. Biochem. 216:539-548(1993).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
 PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
Comments
  • FUNCTION: The glycine cleavage system catalyzes the degradation of glycine.
  • CATALYTIC ACTIVITY: [Protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3.
  • SUBUNIT: The glycine cleavage system is composed of four proteins: P, T, L and H.
  • SIMILARITY: Belongs to the gcvT family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M97263; AAC36843.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X73958; CAA52144.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28377; AAA69073.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75943.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76970.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A56689; A56689.
RefSeq AP_003464.1; -.
NP_417381.1; -.
3D structure databases
PDB
1VLO; X-ray; 1.70 A; A=1-364.[ExPASy / RCSB / EBI]
PDBsum 1VLO; -.
ModBase P27248.
Enzyme and pathway databases
BioCyc EcoCyc:GCVT-MON; -.
MetaCyc:GCVT-MON; -.
Organism-specific databases
EchoBASE EB1412; -.
EcoGene EG11442; gcvT.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004047; Molecular function: aminomethyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0008483; Molecular function: transaminase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0019464; Biological process: glycine decarboxylation via glycine cleavage system (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00259; -; 1.
PBIL [Tree]
InterPro IPR013977; GCV_T_C.
IPR006222; GCV_T_N.
IPR006223; GcvT.
Graphical view of domain structure.
Pfam PF01571; GCV_T; 1.
PF08669; GCV_T_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF006487; GcvT; 1.
TIGRFAMs TIGR00528; gcvT; 1.
BLOCKS P27248.
ProtoNet P27248.
Genome annotation databases
GeneID 947390; -.
GenomeReviews U00096_GR; b2905.
AP009048_GR; JW2873.
KEGG ecj:JW2873; -.
eco:b2905; -.
Phylogenomic databases
HOGENOM P27248; -.
Genome annotation databases
CMR P27248; b2905.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminotransferase; Complete proteome; Direct protein sequencing; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   364  363     Aminomethyltransferase. PRO_0000122554
HELIX   8    13  6      
STRAND   17    21  5      
STRAND   24    31  8      
HELIX   33    42  10      
STRAND   45    48  4      
STRAND   52    59  8      
HELIX   62    69  8      
STRAND   70    72  3      
HELIX   74    76  3      
STRAND   82    89  8      
STRAND   95   105  11      
STRAND   108   113  6      
HELIX   115   117  3      
HELIX   118   129  12      
HELIX   130   132  3      
STRAND   135   138  4      
STRAND   142   149  8      
HELIX   152   157  6      
HELIX   162   168  7      
STRAND   173   179  7      
STRAND   182   185  4      
STRAND   189   192  4      
STRAND   194   200  7      
HELIX   201   213  13      
HELIX   221   230  10      
TURN   236   238  3      
HELIX   246   248  3      
HELIX   252   254  3      
HELIX   267   276  10      
STRAND   280   286  7      
STRAND   288   290  3      
STRAND   297   301  5      
STRAND   307   318  12      
TURN   319   322  4      
STRAND   323   330  8      
STRAND   336   342  7      
STRAND   345   352  8      
Sequence information
Length: 364 AA [This is the length of the unprocessed precursor] Molecular weight: 40147 Da [This is the MW of the unprocessed precursor] CRC64: 1F58C5A244F82242 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAQQTPLYEQ HTLCGARMVD FHGWMMPLHY GSQIDEHHAV RTDAGMFDVS HMTIVDLRGS 

        70         80         90        100        110        120 
RTREFLRYLL ANDVAKLTKS GKALYSGMLN ASGGVIDDLI VYYFTEDFFR LVVNSATREK 

       130        140        150        160        170        180 
DLSWITQHAE PFGIEITVRD DLSMIAVQGP NAQAKAATLF NDAQRQAVEG MKPFFGVQAG 

       190        200        210        220        230        240 
DLFIATTGYT GEAGYEIALP NEKAADFWRA LVEAGVKPCG LGARDTLRLE AGMNLYGQEM 

       250        260        270        280        290        300 
DETISPLAAN MGWTIAWEPA DRDFIGREAL EVQREHGTEK LVGLVMTEKG VLRNELPVRF 

       310        320        330        340        350        360 
TDAQGNQHEG IITSGTFSPT LGYSIALARV PEGIGETAIV QIRNREMPVK VTKPVFVRNG 


KAVA
P27248 in FASTA format

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