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15  structures 2019  species 3  interactions 4341  sequences 23  architectures

Family: GCV_T_C (PF08669)

Summary: Glycine cleavage T-protein C-terminal barrel domain

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This is the Wikipedia entry entitled "Glycine cleavage system". More...

Glycine cleavage system Edit Wikipedia article

Glycine cleavage in the photorespiratory pathway.
Glycine cleavage H-protein
PDB 1hpc EBI.jpg
refined structures at 2 angstroms and 2.2 angstroms of the two forms of the h-protein, a lipoamide-containing protein of the glycine decarboxylase
Identifiers
Symbol GCV_H
Pfam PF01597
Pfam clan CL0105
InterPro IPR002930
SCOP 1htp
SUPERFAMILY 1htp
Glycine cleavage T-protein, Aminomethyltransferase folate-binding domain
PDB 1v5v EBI.jpg
crystal structure of a component of glycine cleavage system: t-protein from pyrococcus horikoshii ot3 at 1.5 a resolution
Identifiers
Symbol GCV_T
Pfam PF01571
Pfam clan CL0289
InterPro IPR006222
SCOP 1pj5
SUPERFAMILY 1pj5
Glycine cleavage T-protein C-terminal barrel domain
PDB 1wor EBI.jpg
crystal structure of t-protein of the glycine cleavage system
Identifiers
Symbol GCV_T_C
Pfam PF08669
InterPro IPR013977
SCOP 1pj5
SUPERFAMILY 1pj5

The glycine cleavage system is also known as the glycine decarboxylase complex or GCS. The system is a series of enzymes that are triggered in response to high concentrations of the amino acid glycine.[1] The glycine cleavage system is composed of four proteins: the T-protein, P-protein, L-protein, and H-protein. They do not form a stable complex,[2] so it is more appropriate to call it a "system" instead of a "complex"

Contents

[edit] Components

Name EC number Function
T-protein (GCST or AMT) EC 2.1.2.10 aminomethyltransferase
P-protein (GLDC) EC 1.4.4.2 glycine dehydrogenase (decarboxylating) or just glycine dehydrogenase.
L-protein (GCSL or DLD) EC 1.8.1.4 known by many names, but most commonly dihydrolipoyl dehydrogenase
H-protein (GCSH) is modified with lipoic acid and interacts with all other components in a cycle of reductive methylamination (catalysed by the P-protein), methylamine transfer (catalysed by the T-protein) and electron transfer (catalysed by the L-protein).[2]

[edit] Function

In plants the glycine cleavage system is coupled to serine hydroxymethyltransferase to give an overall reaction of:

2 glycine + NAD+ + H2O → serine + CO2 + NH3 + NADH + H+

This reaction, and by extension the glycine cleavage system, is required for photorespiration in C3 plants. Together the proteins involved in these reactions comprise about half the proteins in mitochondria from spinach and pea leaves.[2]

[edit] See also

[edit] References

  1. ^ Kikuchi G (June 1973). "The glycine cleavage system: composition, reaction mechanism, and physiological significance". Mol. Cell. Biochem. 1 (2): 169–87. doi:10.1007/BF01659328. PMID 4585091. 
  2. ^ a b c Douce R, Bourguignon J, Neuburger M, Rébeillé F (April 2001). "The glycine decarboxylase system: a fascinating complex". Trends Plant Sci. 6 (4): 167–76. doi:10.1016/S1360-1385(01)01892-1. PMID 11286922. 


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Glycine cleavage T-protein C-terminal barrel domain

This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.

Literature references

  1. McNeil JB, Zhang F, Taylor BV, Sinclair DA, Pearlman RE, Bognar AL; , Gene 1997;186:13-20.: Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae. PUBMED:9047339



External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013977

This entry shows glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyses the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.

Domain organisation

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Alignments

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The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_933 (release 4.0)
Previous IDs: none
Type: Domain
Author: Bashton M, Bateman A
Number in seed: 192
Number in full: 4341
Average length of the domain: 94.60 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 19.16 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 15929002 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.0 21.0
Noise cut-off 20.9 20.9
Model length: 95
Family (HMM) version: 6
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Interactions

There are 3 interactions for this family. More...

DAO SoxD GCV_T

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GCV_T_C domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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