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P26969 (GCSP_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine dehydrogenase (decarboxylating), mitochondrial

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P protein
Glycine decarboxylase
Glycine dehydrogenase (aminomethyl-transferring)
Gene names
Name:GDCSP
Synonyms:GDCP
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length1057 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. HAMAP-Rule MF_00711

Catalytic activity

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2. HAMAP-Rule MF_00711

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. The glycine cleavage system is composed of four proteins: P, T, L and H.

Subcellular location

Mitochondrion HAMAP-Rule MF_00711.

Tissue specificity

Highly expressed in leaves. Detected in roots and embryos. Ref.1

Induction

Induced more than 4-fold after exposure to light for 6 hours. Ref.1

Sequence similarities

Belongs to the GcvP family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglycine catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentglycine cleavage complex

Inferred from direct assay PubMed 3143355. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglycine dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8686Mitochondrion Ref.1
Chain87 – 1057971Glycine dehydrogenase (decarboxylating), mitochondrial HAMAP-Rule MF_00711
PRO_0000010749

Amino acid modifications

Modified residue7921N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict9061I → Y in CAA38252. Ref.2
Sequence conflict9191P → A in CAA38252. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26969 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 2F2EA58E9A2AC447

FASTA1,057114,686
        10         20         30         40         50         60 
MERARRLANR ATLKRLLSEA KQNRKTESTS TTTTTPLPFS LSGSSSRYVS SVSNSILRGR 

        70         80         90        100        110        120 
GSKPDNNVSR RVGGFLGVGY PSQSRSISVE ALKPSDTFPR RHNSATPDEQ TKMAESVGFD 

       130        140        150        160        170        180 
TLDSLVDATV PKSIRLKEMK FNKFDGGLTE GQMIEHMKDL ASKNKVFKSF IGMGYYNTHV 

       190        200        210        220        230        240 
PPVILRNIME NPAWYTQYTP YQAEISQGRL ESLLNFQTMI TDLTGLPMSN ASLLDEGTAA 

       250        260        270        280        290        300 
AEAMSMCNNI QKGKKKTFII ASNCHPQTID ICQTRADGFE LKVVVKDLKD IDYKSGDVCG 

       310        320        330        340        350        360 
VLVQYPGTEG EVLDYGEFIK KAHANEVKVV MASDLLALTV LKPPGEFGAD IVVGSAQRFG 

       370        380        390        400        410        420 
VPMGYGGPHA AFLATSQEYK RMMPGRIIGV SVDSSGKQAL RMAMQTREQH IRRDKATSNI 

       430        440        450        460        470        480 
CTAQALLANM AAMYAVYHGP EGLKAIAQRV HGLAGVFALG LKKLGLEVQD LGFFDTVKVK 

       490        500        510        520        530        540 
TSNAKAIADA AIKSEINLRV VDGNTITAAF DETTTLEDVD KLFKVFAGGK PVSFTAASLA 

       550        560        570        580        590        600 
PEFQNAIPSG LVRESPYLTH PIFNTYQTEH ELLRYIHRLQ SKDLSLCHSM IPLGSCTMKL 

       610        620        630        640        650        660 
NATTEMMPVT WPSFTDLHPF APTEQAQGYQ EMFNNLGDLL CTITGFDSFS LQPNAGAAGE 

       670        680        690        700        710        720 
YAGLMVIRAY HLSRGDHHRN VCIIPASAHG TNPASAAMVG MKIVTIGTDA KGNINIEELK 

       730        740        750        760        770        780 
KAAEKHKDNL SAFMVTYPST HGVYEEGIDD ICKIIHDNGG QVYMDGANMN AQVGLTSPGW 

       790        800        810        820        830        840 
IGADVCHLNL HKTFCIPHGG GGPGMGPIGV KKHLAPFLPS HPVVPTGGIP APENPQPLGS 

       850        860        870        880        890        900 
ISAAPWGSAL ILPISYTYIA MMGSQGLTDA SKIAILNANY MAKRLESYYP VLFRGVNGTV 

       910        920        930        940        950        960 
AHEFIIDLRG FKNTAGIEPE DVAKRLMDYG FHGPTMSWPV AGTLMIEPTE SESKAELDRF 

       970        980        990       1000       1010       1020 
CDALISIRKE IAEVEKGNAD VHNNVLKGAP HPPSLLMADA WTKPYSREYA AFPAAWLRGA 

      1030       1040       1050 
KFWPTTGRVD NVYGDRNLVC TLLPASQAVE EQAAATA 

« Hide

References

[1]"Cloning and characterization of the P subunit of glycine decarboxylase from pea (Pisum sativum)."
Turner S.R., Irland R., Rawsthorne S.
J. Biol. Chem. 267:5355-5360(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 87-94, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Birte.
Tissue: Leaf.
[2]Shah K.S., Kim Y., Oliver D.J.
Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 905-1057.
Strain: cv. Alaska.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59773 mRNA. Translation: CAA42443.1.
X54377 mRNA. Translation: CAA38252.1.
PIRA42109.

3D structure databases

ProteinModelPortalP26969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP26969. 1 interaction.

Proteomic databases

PRIDEP26969.
ProMEXP26969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.640.10. 2 hits.
HAMAPMF_00711. GcvP.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMSSF53383. SSF53383. 3 hits.
TIGRFAMsTIGR00461. gcvP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSP_PEA
AccessionPrimary (citable) accession number: P26969
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families