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Protein

Glycine cleavage system H protein, mitochondrial

Gene

GCSH

Organism
Bos taurus (Bovine)
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 (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-6783984. Glycine degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H protein, mitochondrial
Alternative name(s):
Lipoic acid-containing protein
Gene namesi
Name:GCSH
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848Mitochondrion3 PublicationsAdd
BLAST
Chaini49 – 173125Glycine cleavage system H protein, mitochondrialPRO_0000010722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071N6-lipoyllysinePROSITE-ProRule annotation1 Publication

Proteomic databases

PaxDbiP20821.
PRIDEiP20821.

Interactioni

Subunit structurei

Interacts with GLDC (By similarity). The glycine cleavage system is composed of four proteins: P (GLDC), T (GCST), L (DLD) and H (GCSH).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008936.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 637Combined sources
Beta strandi66 – 716Combined sources
Helixi73 – 797Combined sources
Beta strandi81 – 866Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi115 – 1239Combined sources
Helixi125 – 1273Combined sources
Helixi133 – 1364Combined sources
Turni138 – 1425Combined sources
Beta strandi145 – 1506Combined sources
Helixi152 – 1576Combined sources
Beta strandi158 – 1603Combined sources
Helixi161 – 17212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KLRX-ray0.88A49-173[»]
3WDNX-ray0.86A49-173[»]
ProteinModelPortaliP20821.
SMRiP20821. Positions 49-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 14883Lipoyl-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

Phylogenomic databases

eggNOGiKOG3373. Eukaryota.
COG0509. LUCA.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiP20821.
KOiK02437.
OMAiHEWVELV.
OrthoDBiEOG7RNK1M.
TreeFamiTF300258.

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.

P20821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAVRSVR AAVGGLRAIS APSAPCLPRP WGLRAGAVRE LRTGPALLSV
60 70 80 90 100
RKFTEKHEWV TTENGVGTVG ISNFAQEALG DVVYCSLPEV GTKLNKQEEF
110 120 130 140 150
GALESVKAAS ELYSPLSGEV TEINKALAEN PGLVNKSCYE DGWLIKMTFS
160 170
NPSELDELMS EEAYEKYIKS IEE
Length:173
Mass (Da):18,791
Last modified:February 1, 1991 - v1
Checksum:i6FBF64293B465D22
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491S → G AA sequence (PubMed:2553401).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58361 mRNA. Translation: AAA62710.1.
BC120070 mRNA. Translation: AAI20071.1.
PIRiA39214. GCBOH.
RefSeqiNP_777269.1. NM_174844.1.
XP_005218441.1. XM_005218384.2.
UniGeneiBt.4195.

Genome annotation databases

EnsembliENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.
GeneIDi317723.
KEGGibta:317723.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58361 mRNA. Translation: AAA62710.1.
BC120070 mRNA. Translation: AAI20071.1.
PIRiA39214. GCBOH.
RefSeqiNP_777269.1. NM_174844.1.
XP_005218441.1. XM_005218384.2.
UniGeneiBt.4195.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KLRX-ray0.88A49-173[»]
3WDNX-ray0.86A49-173[»]
ProteinModelPortaliP20821.
SMRiP20821. Positions 49-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008936.

Proteomic databases

PaxDbiP20821.
PRIDEiP20821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008936; ENSBTAP00000008936; ENSBTAG00000006795.
GeneIDi317723.
KEGGibta:317723.

Organism-specific databases

CTDi2653.

Phylogenomic databases

eggNOGiKOG3373. Eukaryota.
COG0509. LUCA.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
HOVERGENiHBG001129.
InParanoidiP20821.
KOiK02437.
OMAiHEWVELV.
OrthoDBiEOG7RNK1M.
TreeFamiTF300258.

Enzyme and pathway databases

ReactomeiR-BTA-389661. Glyoxylate metabolism and glycine degradation.
R-BTA-6783984. Glycine degradation.

Miscellaneous databases

EvolutionaryTraceiP20821.

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

« Hide 'large scale' publications
  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, LIPOYLATION AT LYS-107.
    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. Cited for: X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS) OF 49-173.

Entry informationi

Entry nameiGCSH_BOVIN
AccessioniPrimary (citable) accession number: P20821
Secondary accession number(s): Q0P5G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:3080335 and PubMed:2553401) thought to be a ferredoxin.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.