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.
COFACTOR: Pyridoxal phosphate (By similarity).
SUBUNIT: The glycine cleavage system is composed of four proteins: P, T, L and H (By similarity).
SIMILARITY: Belongs to the gcvP family.

Copyright

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Cross-references

Sequence databases

EMBL

AE015451; AAN66613.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_743149.1; -.

3D structure databases

ModBase

Q88P65.

Enzyme and pathway databases

BioCyc

PPUT160488:PP_0988-MON; -.

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_00711; -; 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; 2.

PANTHER

PTHR11773; GDC-P; 1.

Pfam

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

TIGR00461; gcvP; 1.

Genome annotation databases

GeneID

1044914; -.

GenomeReviews

AE015451_GR; PP_0988.

KEGG

ppu:PP_0988; -.

NMPDR

fig|160488.1.peg.979; -.

TIGR

PP_0988; -.

Phylogenomic databases

HOGENOM

Q88P65; -.

Other

UniRef

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

Keywords

Complete proteome; Oxidoreductase; Pyridoxal phosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 951`	`951`	`Glycine dehydrogenase [decarboxylating] 1.`	`PRO_0000166927`
`BINDING`	`703 703`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 951 AA [This is the length of the unprocessed precursor]

Molecular weight: 101992 Da [This is the MW of the unprocessed precursor]

CRC64: EDDBDB715CDE148E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTINLGTANE FIARHIGPRA ADEQAMLTAL GFDSLDAMTA AVIPDSIKGT SVLGSHDGQS 

        70         80         90        100        110        120 
EADALAALKA IAGKNQLFKS YIGQGYYNTH TPAPILRNLL ENPAWYTAYT PYQPEISQGR 

       130        140        150        160        170        180 
LEALLNFQTL ISDLTGLPIA NASLLDEATA AAEAMTFCKR LSKNKSSHAF FASVHCHPQT 

       190        200        210        220        230        240 
LDVLRTRAEP LGIEVVVGDE RELGDVSAFF GALLQYPASN GEVFDYREVV QRFHAANALV 

       250        260        270        280        290        300 
AVAADLLALT LLTPPGEFDA DVAIGSAQRF GVPLGFGGPH AAYFATRDAF KRDMPGRLVG 

       310        320        330        340        350        360 
VSIDRFGKTA LRLAMQTREQ HIRREKATSN ICTAQVLLAN IASMFAVYHG PAGLKRIAER 

       370        380        390        400        410        420 
THALTAILAA GLKALGVQVV GASAFDTLTL ATGTATASLH DKARAQGINL RQIDAAHVGL 

       430        440        450        460        470        480 
SLDETSTQAD VESLWQLLGG EQAQPDFTAL AASTGSLLPA ALLRQSAILE HPVFNRYHSE 

       490        500        510        520        530        540 
TELMRYLRRL ADKDLALDRS MIPLGSCTMK LNAASEMIPV TWAEFGNLHP FAPAEQSQGY 

       550        560        570        580        590        600 
LQMTTELEAM LCAATGYDAV SLQPNAGSQG EYAGLLAIRA YHRSRGEGHR DICLIPSSAH 

       610        620        630        640        650        660 
GTNPATAHMA GMRVVVTACD ARGNVDVEDL RAKAIEHRER LAAIMITYPS THGVFEEAIG 

       670        680        690        700        710        720 
EICAIIHDNG GQVYIDGANM NAMVGLCAPG KFGGDVSHLN LHKTFCIPHG GGGPGVGPIG 

       730        740        750        760        770        780 
VKSHLAPFLP GHAQLENTQG AVCAAPFGSA SILPITWMYI RMMGGAGLKR ASQMAILNAN 

       790        800        810        820        830        840 
YIARRLEEHY PVLYTGGNGL VAHECILDLR PLKDTSGISV DDVAKRLIDF GFHAPTMSFP 

       850        860        870        880        890        900 
VAGTLMIEPT ESESKEELDR FCNAMIQIRE EIRAVEDGSL DKDDNPLKNA PHTAAELVGE 

       910        920        930        940        950 
WTHGYSREQA VYPLASLVEG KYWPPVGRVD NVFGDRNLVC ACPSIESYQD A

Q88P65 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