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P26969

- GCSP_PEA

UniProt

P26969 - GCSP_PEA

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Protein

Glycine dehydrogenase (decarboxylating), mitochondrial

Gene

GDCSP

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Cofactori

GO - Molecular functioni

  1. glycine dehydrogenase (decarboxylating) activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glycine catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GDCSP
Synonyms:GDCP
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. glycine cleavage complex Source: UniProtKB
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8686Mitochondrion1 PublicationAdd
BLAST
Chaini87 – 1057971Glycine dehydrogenase (decarboxylating), mitochondrialPRO_0000010749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei792 – 7921N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiP26969.

Expressioni

Tissue specificityi

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

Inductioni

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP26969. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP26969.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26969-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERARRLANR ATLKRLLSEA KQNRKTESTS TTTTTPLPFS LSGSSSRYVS
60 70 80 90 100
SVSNSILRGR GSKPDNNVSR RVGGFLGVGY PSQSRSISVE ALKPSDTFPR
110 120 130 140 150
RHNSATPDEQ TKMAESVGFD TLDSLVDATV PKSIRLKEMK FNKFDGGLTE
160 170 180 190 200
GQMIEHMKDL ASKNKVFKSF IGMGYYNTHV PPVILRNIME NPAWYTQYTP
210 220 230 240 250
YQAEISQGRL ESLLNFQTMI TDLTGLPMSN ASLLDEGTAA AEAMSMCNNI
260 270 280 290 300
QKGKKKTFII ASNCHPQTID ICQTRADGFE LKVVVKDLKD IDYKSGDVCG
310 320 330 340 350
VLVQYPGTEG EVLDYGEFIK KAHANEVKVV MASDLLALTV LKPPGEFGAD
360 370 380 390 400
IVVGSAQRFG VPMGYGGPHA AFLATSQEYK RMMPGRIIGV SVDSSGKQAL
410 420 430 440 450
RMAMQTREQH IRRDKATSNI CTAQALLANM AAMYAVYHGP EGLKAIAQRV
460 470 480 490 500
HGLAGVFALG LKKLGLEVQD LGFFDTVKVK TSNAKAIADA AIKSEINLRV
510 520 530 540 550
VDGNTITAAF DETTTLEDVD KLFKVFAGGK PVSFTAASLA PEFQNAIPSG
560 570 580 590 600
LVRESPYLTH PIFNTYQTEH ELLRYIHRLQ SKDLSLCHSM IPLGSCTMKL
610 620 630 640 650
NATTEMMPVT WPSFTDLHPF APTEQAQGYQ EMFNNLGDLL CTITGFDSFS
660 670 680 690 700
LQPNAGAAGE YAGLMVIRAY HLSRGDHHRN VCIIPASAHG TNPASAAMVG
710 720 730 740 750
MKIVTIGTDA KGNINIEELK KAAEKHKDNL SAFMVTYPST HGVYEEGIDD
760 770 780 790 800
ICKIIHDNGG QVYMDGANMN AQVGLTSPGW IGADVCHLNL HKTFCIPHGG
810 820 830 840 850
GGPGMGPIGV KKHLAPFLPS HPVVPTGGIP APENPQPLGS ISAAPWGSAL
860 870 880 890 900
ILPISYTYIA MMGSQGLTDA SKIAILNANY MAKRLESYYP VLFRGVNGTV
910 920 930 940 950
AHEFIIDLRG FKNTAGIEPE DVAKRLMDYG FHGPTMSWPV AGTLMIEPTE
960 970 980 990 1000
SESKAELDRF CDALISIRKE IAEVEKGNAD VHNNVLKGAP HPPSLLMADA
1010 1020 1030 1040 1050
WTKPYSREYA AFPAAWLRGA KFWPTTGRVD NVYGDRNLVC TLLPASQAVE

EQAAATA
Length:1,057
Mass (Da):114,686
Last modified:August 1, 1992 - v1
Checksum:i2F2EA58E9A2AC447
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti906 – 9061I → Y in CAA38252. 1 PublicationCurated
Sequence conflicti919 – 9191P → A in CAA38252. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59773 mRNA. Translation: CAA42443.1.
X54377 mRNA. Translation: CAA38252.1.
PIRiA42109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59773 mRNA. Translation: CAA42443.1 .
X54377 mRNA. Translation: CAA38252.1 .
PIRi A42109.

3D structure databases

ProteinModelPortali P26969.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P26969. 1 interaction.

Proteomic databases

PRIDEi P26969.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.640.10. 2 hits.
HAMAPi MF_00711. GcvP.
InterProi IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view ]
PANTHERi PTHR11773. PTHR11773. 1 hit.
Pfami PF02347. GDC-P. 2 hits.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 3 hits.
TIGRFAMsi TIGR00461. gcvP. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGCSP_PEA
AccessioniPrimary (citable) accession number: P26969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 26, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3