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P49361 (GCSPA_FLAPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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) A, mitochondrial

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P protein A
Glycine decarboxylase A
Glycine dehydrogenase (aminomethyl-transferring) A
Gene names
Name:GDCSPA
OrganismFlaveria pringlei
Taxonomic identifier4226 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity. The glycine cleavage system is composed of four proteins: P, T, L and H. HAMAP-Rule MF_00711

Subcellular location

Mitochondrion HAMAP-Rule MF_00711.

Tissue specificity

Expressed in leaves, stems and roots. Ref.3

Sequence similarities

Belongs to the GcvP family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

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 – 6666Mitochondrion Potential
Chain67 – 1037971Glycine dehydrogenase (decarboxylating) A, mitochondrial HAMAP-Rule MF_00711
PRO_0000010746

Amino acid modifications

Modified residue7731N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict21E → D in CAA81076. Ref.2
Sequence conflict4951T → I in CAA81076. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P49361 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: ED248FA227F9E0F3

FASTA1,037113,032
        10         20         30         40         50         60 
MERARRLANK AILGRLVSQT KHNPSISSPA LCSPSRYVSS LSPYVCSGTN VRSDRNLNGF 

        70         80         90        100        110        120 
GSQVRTISVE ALKPSDTFPR RHNSATPEEQ TKMAEFVGFP NLDSLIDATV PKSIRLDSMK 

       130        140        150        160        170        180 
YSKFDEGLTE SQMIAHMQDL ASKNKIFKSF IGMGYYNTSV PTVILRNIME NPGWYTQYTP 

       190        200        210        220        230        240 
YQAEIAQGRL ESLLNFQTMV TDLTGLPMSN ASLLDEGTAA AEAMAMCNNI QKGKKKTFII 

       250        260        270        280        290        300 
ASNCHPQTID ICKTRADGFD LKVVTSDLKD FDYSSGDVCG VLVQYPGTEG ELLDYSEFIK 

       310        320        330        340        350        360 
NAHANGVKVV MASDLLALTI LKPPGELGAD IVVGSAQRFG VPMGYGGPHA AFLATSQEYK 

       370        380        390        400        410        420 
RMMPGRIIGV SVDSSGKPAL RMAMQTREQH IRRDKATSNI CTAQALLANM AAMFGVYHGP 

       430        440        450        460        470        480 
EGLKTIAKRV HGLAGTFAAG LKKLGTVQVQ DLPFFDTVKV TCVDSKAIAE EAYKHKMNLR 

       490        500        510        520        530        540 
IVDKNTITVA FDETTTIEDV DTLFKVFALG KPVTFTAASI APEVQDAIPS GLVRETPYLT 

       550        560        570        580        590        600 
HPIFNMYHTE HELLRYISKL QSKDLSLCHS MIPLGSCTMK LNATTEMMPV TWPAFADIHP 

       610        620        630        640        650        660 
FAPTEQAQGY QEMFKNLGDL LCTITGFDSF SLQPNAGAAG EYAGLMVIRA YHMARGDHHR 

       670        680        690        700        710        720 
NVCIIPVSAH GTNPASAAMC GMKIITVGTD SKGNINIEEL RKAAEANKEN LSALMVTYPS 

       730        740        750        760        770        780 
THGVYEEGID EICKIIHDNG GQVYMDGANM NAQVGLTSPG WIGADVCHLN LHKTFCIPHG 

       790        800        810        820        830        840 
GGGPGMGPIG VKKHLAPYLP SHPVVATGGI PAPEQSQPLG TIAAAPWGSA LILPISYTYI 

       850        860        870        880        890        900 
AMMGSQGITN ASKIAILNAN YMAKRLENHY PILFRGVNGT VAHEFIVDLR PLKTTAGIEP 

       910        920        930        940        950        960 
EDVAKRLIDY GFHGPTMSWP VPGTLMIEPT ESESKAELDR FCDALISIRQ EIAEIEKGNV 

       970        980        990       1000       1010       1020 
DLNNNVIKGA PHPPQLLMAD KWTKPYSREY AAYPAPWLRA AKFWPTTCRV DNVYGDRNLI 

      1030 
CTLQPPQEYE EKAEATA 

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References

[1]"The gdcsPA gene from Flaveria pringlei (Asteraceae)."
Bauwe H., Kopriva S.
Plant Physiol. 107:655-655(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leaf.
[2]"P-protein of glycine decarboxylase from Flaveria pringlei."
Kopriva S., Bauwe H.
Plant Physiol. 104:1077-1078(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[3]"Structure and expression analysis of the gdcsPA and gdcsPB genes encoding two P-isoproteins of the glycine-cleavage system from Flaveria pringlei."
Bauwe H., Chu C.-C., Kopriva S., Nan Q.
Eur. J. Biochem. 234:116-124(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36879 Genomic DNA. Translation: CAA85353.1.
Z25857 mRNA. Translation: CAA81076.1.
PIRS63535.

3D structure databases

ProteinModelPortalP49361.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP49361.

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 nameGCSPA_FLAPR
AccessionPrimary (citable) accession number: P49361
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 77 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