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UniProtKB/Swiss-Prot entry Q6MEJ2

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

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Entry information
Entry name GCSPA_PARUW
Primary accession number Q6MEJ2
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on July 5, 2004 (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: pc0283
From
Protochlamydia amoebophila (strain UWE25) [TaxID: 264201] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae; Candidatus Protochlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1096330; PubMed=15073324 [NCBI, ExPASy, EBI, Israel, Japan]
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.;
"Illuminating the evolutionary history of chlamydiae.";
Science 304:728-730(2004).
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
BX908798; CAF23007.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_007282.1; -.
3D structure databases
ModBase Q6MEJ2.
Enzyme and pathway databases
BioCyc CPRO264201:PC0283-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 Q6MEJ2.
Genome annotation databases
GeneID 2780941; -.
GenomeReviews BX908798_GR; pc0283.
KEGG pcu:pc0283; -.
NMPDR fig|264201.1.peg.283; -.
Phylogenomic databases
HOGENOM Q6MEJ2; -.
Genome annotation databases
CMR Q6MEJ2; pc0283.
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   446  446     Probable glycine dehydrogenase [decarboxylating] subunit 1. PRO_1000045673
Sequence information
Length: 446 AA [This is the length of the unprocessed precursor] Molecular weight: 49350 Da [This is the MW of the unprocessed precursor] CRC64: 2C14E46369B97FDD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDFISNKTPQ IEAMLTEIGI QNVEELFKSI PSSLILQAPS VDDGLSEYEG IQLIESLAVR 

        70         80         90        100        110        120 
NTFPNLVSYL GAGAYEHHIP ALVGAVCSKS EFLTAYTPYQ AEASQGMLQI IFEFQSAICA 

       130        140        150        160        170        180 
LTGMDVANAS VYDGASACAE AILMSLRHHK TRRQILLSDS LHPHYKKVIE QYLKSQDCEL 

       190        200        210        220        230        240 
ITVPFLQEGT LDASFLKMYL NDQTAAILLQ SPNFFGCIED VQPITEMAKS QGALTILCAN 

       250        260        270        280        290        300 
PISYGLLSSA KELGVDIAVG DCQPFGLSLS FGGPYAGYMA CKQELMRQLP GRIVGETLDV 

       310        320        330        340        350        360 
QGSRGFVLTL QAREQHIRRE KATSNICTNQ ALAALASLVA MLWYGKEGVK ELALTNYQRA 

       370        380        390        400        410        420 
NYLKFHLGKI STINVWNQGA SFNEFVVDFK QDSNQVLEFF RLNGIEPGIE LKRYYPSLKT 

       430        440 
CLLIAVTETK NQIQLDQFIK VCKELF
Q6MEJ2 in FASTA format

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