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UniProtKB/Swiss-Prot entry Q3AET5


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

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Entry information
Entry name GCSPA_CARHZ
Primary accession number Q3AET5
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 20)
Name and origin of the protein
Protein name Probable glycine dehydrogenase [decarboxylating] subunit 1
Synonyms EC 1.4.4.2
Glycine decarboxylase subunit 1
Glycine cleavage system P-protein subunit 1
Gene name
Name: gcvPA
OrderedLocusNames: CHY_0491
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(2005).
Comments
  • FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).
  • CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2.
  • SUBUNIT: The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is an heterodimer of two subunits (By similarity).
  • SIMILARITY: Belongs to the gcvP family. N-terminal subunit subfamily.
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
CP000141; ABB15168.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_359349.1; -.
3D structure databases
ModBase Q3AET5.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_0491-MON; -.
Ontologies
GO
GO:0004375; Molecular function: glycine dehydrogenase (decarboxylating) activity (inferred from electronic annotation from InterPro).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0019464; Biological process: glycine decarboxylation via glycine cleavage system (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00712; -; 1.
PBIL [Tree]
InterPro IPR003437; GDC-P.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11773; GDC-P; 1.
Pfam PF02347; GDC-P; 1.
Pfam graphical view of domain structure.
ProtoNet Q3AET5.
Genome annotation databases
GeneID 3727270; -.
GenomeReviews CP000141_GR; CHY_0491.
KEGG chy:CHY_0491; -.
NMPDR fig|246194.3.peg.976; -.
TIGR CHY_0491; -.
Phylogenomic databases
HOGENOM Q3AET5; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   444  444     Probable glycine dehydrogenase [decarboxylating] subunit 1. PRO_1000045640
Sequence information
Length: 444 AA [This is the length of the unprocessed precursor] Molecular weight: 48908 Da [This is the MW of the unprocessed precursor] CRC64: A9A0197BAEEB89D9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKYTPHTPDE VREMLSSLGL SSIEELFSDI PEEVKLKRPL NLPSGMSELE VKKHLANLAA 

        70         80         90        100        110        120 
KNGSADKYTV FLGAGVYDHY VPAVVNHILL RSEFYTAYTP YQAEMSQGVL QSIFEYQTMI 

       130        140        150        160        170        180 
CELTGLDITN ASMYDGGSAL AEAALMAVSQ TRRDKVLVLA TVHPEYRSVV KTYTWGPEIE 

       190        200        210        220        230        240 
VVEVPYKSGT VDLEKLEELI DDKTAAVLVQ HPNFFGQLEP VEEISRLIHA QKGLLVVAVD 

       250        260        270        280        290        300 
PISLGILKPP AEYGADIAVG DGQALGNGLA FGGPHLGFFA ARKDLARRMP GRLVGLTTDK 

       310        320        330        340        350        360 
EGNRGFVLTL QAREQHIRRE KATSNICSNQ ALNALAATVY LATVGKKGLK EIALQSLQKA 

       370        380        390        400        410        420 
HYAFERLIGE GYEPLFSGPF FKEFVVKVKN EEEITQKLLK HHILAGPGIS RFYPELAPAL 

       430        440 
MIAVTEKRTR EEIDNLVEVL GGDR 

Q3AET5 in FASTA format

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