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Protein

Glycine cleavage system H protein, mitochondrial

Gene

GDCSH

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

Functioni

The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SABIO-RKP16048.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H protein, mitochondrial
Gene namesi
Name:GDCSH
Synonyms:GCDH
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  • glycine cleavage complex Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionAdd
BLAST
Chaini35 – 165131Glycine cleavage system H protein, mitochondrialPRO_0000010738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei97 – 971N6-lipoyllysinePROSITE-ProRule annotation1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP16048. 1 interaction.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 537Combined sources
Beta strandi56 – 616Combined sources
Helixi63 – 697Combined sources
Beta strandi71 – 766Combined sources
Beta strandi88 – 9710Combined sources
Beta strandi99 – 1068Combined sources
Beta strandi108 – 1136Combined sources
Helixi116 – 1194Combined sources
Helixi123 – 1264Combined sources
Turni128 – 1325Combined sources
Beta strandi135 – 1417Combined sources
Helixi142 – 1476Combined sources
Helixi151 – 16313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXMX-ray2.60A/B35-165[»]
1HPCX-ray2.00A/B35-165[»]
1HTPX-ray2.20A35-165[»]
ProteinModelPortaliP16048.
SMRiP16048. Positions 35-165.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16048.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13883Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GcvH family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Family and domain databases

HAMAPiMF_00272. GcvH.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR11715. PTHR11715. 1 hit.
PfamiPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR00527. gcvH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16048-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRMWASST ANALKLSSSS RLHLSPTFSI SRCFSNVLDG LKYAPSHEWV
60 70 80 90 100
KHEGSVATIG ITDHAQDHLG EVVFVELPEP GVSVTKGKGF GAVESVKATS
110 120 130 140 150
DVNSPISGEV IEVNTGLTGK PGLINSSPYE DGWMIKIKPT SPDELESLLG
160
AKEYTKFCEE EDAAH
Length:165
Mass (Da):17,688
Last modified:April 1, 1990 - v1
Checksum:i095CBA89F4B565A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05164 mRNA. Translation: AAA33668.1.
X53656 mRNA. Translation: CAA37704.1.
X64726 Genomic DNA. Translation: CAA45978.1.
PIRiS29122. GCPMH.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05164 mRNA. Translation: AAA33668.1.
X53656 mRNA. Translation: CAA37704.1.
X64726 Genomic DNA. Translation: CAA45978.1.
PIRiS29122. GCPMH.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXMX-ray2.60A/B35-165[»]
1HPCX-ray2.00A/B35-165[»]
1HTPX-ray2.20A35-165[»]
ProteinModelPortaliP16048.
SMRiP16048. Positions 35-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16048. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP16048.

Miscellaneous databases

EvolutionaryTraceiP16048.

Family and domain databases

HAMAPiMF_00272. GcvH.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR11715. PTHR11715. 1 hit.
PfamiPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR00527. gcvH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning, transcriptional characterization, and sequencing of cDNA encoding the H-protein of the mitochondrial glycine decarboxylase complex in peas."
    Kim Y., Oliver D.J.
    J. Biol. Chem. 265:848-853(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "cDNA cloning, primary structure and gene expression for H-protein, a component of the glycine-cleavage system (glycine decarboxylase) of pea (Pisum sativum) leaf mitochondria."
    Macherel D., Lebrun M., Gagnon J., Neuburger M., Douce R.
    Biochem. J. 268:783-789(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], LIPOYLATION AT LYS-97.
    Tissue: Leaf.
  3. "Cloning of the gene (gdcH) encoding H-protein, a component of the glycine decarboxylase complex of pea (Pisum sativum L.)."
    Macherel D., Bourguignon J., Douce R.
    Biochem. J. 286:627-630(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves."
    Pares S., Cohen-Addad C., Sieker L., Neuburger M., Douce R.
    Proc. Natl. Acad. Sci. U.S.A. 91:4850-4853(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-165.

Entry informationi

Entry nameiGCSH_PEA
AccessioniPrimary (citable) accession number: P16048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 13, 2016
This is version 107 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.