Glycine cleavage system H protein, mitochondrial precursor

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P20821 (GCSH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycine cleavage system H protein, mitochondrial

Gene names

Name:

GCSH

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Cofactor	Binds 1 lipoyl cofactor covalently.
Subunit structure	The glycine cleavage system is composed of four proteins: P, T, L and H.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the GcvH family. Contains 1 lipoyl-binding domain.
Caution	Was originally (Ref.3 and Ref.4) thought to be a ferredoxin.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Lipoyl Transit peptide
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycine decarboxylation via glycine cleavage system Inferred from electronic annotation. Source: InterPro
Cellular_component	glycine cleavage complex Inferred from electronic annotation. Source: InterPro mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 48

Mitochondrion Ref.1 Ref.3 Ref.4

Chain

49 – 173

125

Glycine cleavage system H protein, mitochondrial

PRO_0000010722

Amino acid modifications

Modified residue

107

N6-lipoyllysine

Experimental info

Sequence conflict

S → G AA sequence Ref.4

Secondary structure

173

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P20821 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 6FBF64293B465D22
Show »

FASTA

173

18,791

        10         20         30         40         50         60 
MALRAVRSVR AAVGGLRAIS APSAPCLPRP WGLRAGAVRE LRTGPALLSV RKFTEKHEWV 

        70         80         90        100        110        120 
TTENGVGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQEEF GALESVKAAS ELYSPLSGEV 

       130        140        150        160        170 
TEINKALAEN PGLVNKSCYE DGWLIKMTFS NPSELDELMS EEAYEKYIKS IEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence, in vitro synthesis, and intramitochondrial lipoylation of H-protein of the glycine cleavage system." Fujiwara K., Okamura-Ikeda K., Motokawa Y. J. Biol. Chem. 265:17463-17467(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-78 AND 97-115. Tissue: Liver.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal pons.
[3]	"Purification and biochemical characterization of hepatic ferredoxin (hepatoredoxin) from bovine liver mitochondria." Waki N., Hiwatashi A., Ichikawa Y. FEBS Lett. 195:87-91(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-65. Tissue: Liver.
[4]	"Characterization and N-terminal amino acid sequence of multiple ferredoxins in kidney and adrenal mitochondria." Driscoll W.J., Omdahl J.L. Eur. J. Biochem. 185:181-187(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-63.
[5]	"High-resolution X-ray crystal structure of bovine H-protein at 0.88 A resolution." Higashiura A., Kurakane T., Matsuda M., Suzuki M., Inaka K., Sato M., Kobayashi T., Tanaka T., Tanaka H., Fujiwara K., Nakagawa A. Acta Crystallogr. D 66:698-708(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS) OF 49-173.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M58361 mRNA. Translation: AAA62710.1.
BC120070 mRNA. Translation: AAI20071.1.

IPI

IPI00690944.

PIR

GCBOH. A39214.

RefSeq

NP_777269.1. NM_174844.1.

UniGene

Bt.4195.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KLR	X-ray	0.88	A	49-173	[»]

ProteinModelPortal

P20821.

SMR

P20821. Positions 49-173.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000008936.

Proteomic databases

PaxDb

P20821.

PRIDE

P20821.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.

GeneID

317723.

KEGG

bta:317723.

Organism-specific databases

CTD

2653.

Phylogenomic databases

eggNOG

COG0509.

GeneTree

ENSGT00390000011666.

HOGENOM

HOG000239392.

HOVERGEN

HBG001129.

InParanoid

P20821.

K02437.

OMA

TPKELRY.

OrthoDB

EOG43N7DX.

Family and domain databases

InterPro

IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]

PANTHER

PTHR11715. PTHR11715. 1 hit.

Pfam

PF01597. GCV_H. 1 hit.
[Graphical view]

SUPFAM

SSF51230. Hybrid_motif. 1 hit.

TIGRFAMs

TIGR00527. gcvH. 1 hit.

PROSITE

PS00189. LIPOYL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P20821.

NextBio

20807157.

Entry information

Entry name

GCSH_BOVIN

Accession

Primary (citable) accession number: P20821
Secondary accession number(s): Q0P5G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents