NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571.";
Submitted (APR-2007) 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

AP009384; BAF90246.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001527164.1; -.

3D structure databases

ModBase

A8HT29.

Ontologies

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.
Graphical view of domain structure.

PANTHER

PTHR11773; GDC-P; 1.

Pfam

PF02347; GDC-P; 1.
Pfam graphical view of domain structure.

Genome annotation databases

GeneID

5691343; -.

GenomeReviews

AP009384_GR; AZC_4248.

KEGG

azc:AZC_4248; -.

CMR

A8HT29; AZC_4248.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 447`	`447`		`Probable glycine dehydrogenase [decarboxylating] subunit 1.`	`PRO_1000072767`

Sequence information

Length: 447 AA [This is the length of the unprocessed precursor]

Molecular weight: 47277 Da [This is the MW of the unprocessed precursor]

CRC64: D776DEC3602BF231 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRYLPLTPED RTEMLARIGA PSVDALFADI PAAKLDPALA DLPAHKTELS VERTLGALSA 

        70         80         90        100        110        120 
QNVPAGSVPF FVGAGAYRHH VPATVDHLIQ RSEFLTSYTP YQPEIAQGTL QYLFEFQTQV 

       130        140        150        160        170        180 
GELTGMEVAN ASMYDGSTAA AEAVLMAHRV TKRRKAVVAG NVHPHYRETI ATLSLYADDA 

       190        200        210        220        230        240 
VVALSPVPQG GEDILSAIDG ETSCVVVQSP DVFGNIVDLK PIAEKAHAAG ALLIAVFTEV 

       250        260        270        280        290        300 
VSLGLIEPPG AQGADIVVGE GQSIGNPLTF GGPYVGLFAT RQKYVRQMPG RLAGETVDAS 

       310        320        330        340        350        360 
GKRGFVLTLS TREQHIRREK ATSNICTNSG LCALAFTIHL TLLGETGLRK LARLNHANAC 

       370        380        390        400        410        420 
KLADKLAAVP GVQVLNSAFF NEFTLRVPGK AVDVIEKLAA KGVLGGVPYA RLAPKAGLDD 

       430        440 
LILVAATEIN TDEDRAAYAA ALKEVLA

A8HT29 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools