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UniProtKB/Swiss-Prot entry Q2IQD6

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

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Entry information
Entry name GCSPA_ANADE
Primary accession number Q2IQD6
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on March 7, 2006 (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: Adeh_1243
From
Anaeromyxobacter dehalogenans (strain 2CP-C) [TaxID: 290397] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000251; ABC81017.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_464454.1; -.
3D structure databases
ModBase Q2IQD6.
Enzyme and pathway databases
BioCyc ADEH290397:ADEH_1243-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 Q2IQD6.
Genome annotation databases
GeneID 3888812; -.
GenomeReviews CP000251_GR; Adeh_1243.
KEGG ade:Adeh_1243; -.
Phylogenomic databases
HOGENOM Q2IQD6; -.
Genome annotation databases
CMR Q2IQD6; Adeh_1243.
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   445  445     Probable glycine dehydrogenase [decarboxylating] subunit 1. PRO_1000045635
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 47431 Da [This is the MW of the unprocessed precursor] CRC64: DCA9DE4E6FB9FC7B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRYHPHTPDD VRAMLDVVGA ERVDDLFRSI PQALRLDRPL DLPPAADEIA LFSELRRLAA 

        70         80         90        100        110        120 
RNETAHPPFV GAGCYPHHVP PVVDQLLLRG EFFTAYTPYQ PEISQGTLQA LFEWQTFVCL 

       130        140        150        160        170        180 
LTGMDVSNAS MYDGATATAE AALMAGRITG RDKVVVSAAL HPEYRKVLAT YLRSTGDEIV 

       190        200        210        220        230        240 
TVPFGADGRT DLAALQQAVD GRTACVILGY PNFLGVVDAL PEAAAIARKA GALTVSATAE 

       250        260        270        280        290        300 
AVSLGLLQAP GALGADVAVG TFQSFGNPMS FGGPAPGFFA TREKHVRQMP GRVAGATVDK 

       310        320        330        340        350        360 
QGRRGFVLTL STREQHIRRE KATSNICTNS GLCALASTVH LSLLGKRGLA ELARLNHGRA 

       370        380        390        400        410        420 
RMLRDAMERA GCRPVFSGPF FNEQVFDVGD AEAVVAKLAK RGIVAGAPLA RWFPDAPSAK 

       430        440 
GALLCAATEL HGPELIQLFA GAVRS
Q2IQD6 in FASTA format

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