NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Richardson P.;
"Complete sequence of chromosome of Francisella philomiragia subsp. philomiragia ATCC 25017.";
Submitted (DEC-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

CP000937; ABZ86555.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001677056.1; -.

3D structure databases

ModBase

B0TZJ6.

Ontologies

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

5907508; -.

GenomeReviews

CP000937_GR; Fphi_0338.

KEGG

fph:Fphi_0338; -.

CMR

B0TZJ6; Fphi_0338.

Other

ProtoNet

B0TZJ6.

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`	`1 455`	`455`		`Probable glycine dehydrogenase [decarboxylating] subunit 1.`	`PRO_1000083221`

Sequence information

Length: 455 AA [This is the length of the unprocessed precursor]

Molecular weight: 49664 Da [This is the MW of the unprocessed precursor]

CRC64: DE1E0C9E5C1DD1FD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFIPHKPEQ IEKMLGTIGA SSIDQLFDEI PAHLRADTLK IKDGINEIQL ANQMRKRANR 

        70         80         90        100        110        120 
NHHNTNFIGA GAYSHHIPAA IWDIVARGEF YTAYTPYQAE ASQGGLQVIY EFQTMMAGLT 

       130        140        150        160        170        180 
GMDASNASMY DGATALAESV LMAIRSNKKA KSQKILIAEA LHPTYLRVLE TITKHQGIEF 

       190        200        210        220        230        240 
DIVNLDSKNG KTDITKLEDF ANTDYAAVVI QSPNFLGQLA DVDGITNWAH KHGALVIAVT 

       250        260        270        280        290        300 
NPMSLAILKS PAEWGENGAD IVCGEGQPMG VPLASGGPYF GFMTCKMAHV RQMPGRIVGR 

       310        320        330        340        350        360 
TVDLDGNEGF CLTLQAREQH IRRAKATSNI CTNQGLMVTA ATIYMSLLGA KGLERVASIS 

       370        380        390        400        410        420 
HENTTKLANE LSKLDGVNAR FNNVSFNEVV IDLPVNAEIF VTEMEKEGID AGYFLGEYHS 

       430        440        450 
DLDNSIMVCA TEIHTSEDIK EYIEATKKVL ARIGG

B0TZJ6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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