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UniProtKB/Swiss-Prot entry Q8CXE0


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

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Entry information
Entry name GCSPA_OCEIH
Primary accession number Q8CXE0
Secondary accession numbers None
Integrated into Swiss-Prot on October 3, 2003
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 30)
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: OB1903
From
Oceanobacillus iheyensis [TaxID: 182710] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
DOI=10.1093/nar/gkf526; PubMed=12235376 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Uchiyama I.;
"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments.";
Nucleic Acids Res. 30:3927-3935(2002).
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
BA000028; BAC13859.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_692824.1; -.
3D structure databases
ModBase Q8CXE0.
Enzyme and pathway databases
BioCyc OIHE221109:OB1903-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.
Genome annotation databases
GeneID 1018395; -.
GenomeReviews BA000028_GR; OB1903.
KEGG oih:OB1903; -.
NMPDR fig|221109.1.peg.1903; -.
Phylogenomic databases
HOGENOM Q8CXE0; -.
Genome annotation databases
CMR Q8CXE0; OB1903.
Other
ProtoNet Q8CXE0.
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   449  449     Probable glycine dehydrogenase [decarboxylating] subunit 1. PRO_0000166969
Sequence information
Length: 449 AA [This is the length of the unprocessed precursor] Molecular weight: 49746 Da [This is the MW of the unprocessed precursor] CRC64: 75554C029B2B1750 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEFRYLPMTN QDKQEMLDAI GIKSTEELFS DIPEHVRFKG EMNLKAPISE YELTKELTEL 

        70         80         90        100        110        120 
ASRNIHTKEY TSFLGAGVYD HYIPSVVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT 

       130        140        150        160        170        180 
MISELTGLPV ANSSMYDGGT ALAEAVNLSA AHTKRKKVLV SKAVHPEYRA VIDSYTRGQS 

       190        200        210        220        230        240 
IDIVEIDTVN GVTDLAQLDQ AIDETIAGVV VQYPNFFGQL EPMKKIEQLL ENHQKTMLIV 

       250        260        270        280        290        300 
SSNPLALGYL TPPGEFGADI VTGDTQVFGI PAQFGGPHCG YFATSKKLMR KVPGRLVGET 

       310        320        330        340        350        360 
VDEEGTRGYV LTLQAREQHI RRDKATSNIC SNQALNALAS SVAMSSIGKH GLRKLASVNM 

       370        380        390        400        410        420 
QKARYARKKL LEAGVELAFD GSFFNEFVIK VPGSVSKINK QLLDKGIIAG YDLAKDDKSL 

       430        440 
EGYMLIAVTE VRTKQEIDQF VKELGDIHV 

Q8CXE0 in FASTA format

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