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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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionAdd BLAST34
ChainiPRO_000001073835 – 165Glycine cleavage system H protein, mitochondrialAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei97N6-lipoyllysinePROSITE-ProRule annotation1 Publication1

Proteomic databases

PRIDEiP16048.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP16048. 1 interactor.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 53Combined sources7
Beta strandi56 – 61Combined sources6
Helixi63 – 69Combined sources7
Beta strandi71 – 76Combined sources6
Beta strandi88 – 97Combined sources10
Beta strandi99 – 106Combined sources8
Beta strandi108 – 113Combined sources6
Helixi116 – 119Combined sources4
Helixi123 – 126Combined sources4
Turni128 – 132Combined sources5
Beta strandi135 – 141Combined sources7
Helixi142 – 147Combined sources6
Helixi151 – 163Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP16048.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 138Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST83

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

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXMX-ray2.60A/B35-165[»]
1HPCX-ray2.00A/B35-165[»]
1HTPX-ray2.20A35-165[»]
ProteinModelPortaliP16048.
SMRiP16048.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP16048. 1 interactor.

Proteomic databases

PRIDEiP16048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP16048.

Miscellaneous databases

EvolutionaryTraceiP16048.

Family and domain databases

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
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...

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: November 30, 2016
This is version 111 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.