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Protein

Glycine cleavage system H protein, mitochondrial

Gene

GCV3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).By similarity

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

GO - Biological processi

  • glycine catabolic process Source: SGD
  • glycine decarboxylation via glycine cleavage system Source: InterPro
  • one-carbon metabolic process Source: SGD
  • oxidation-reduction process Source: GOC
  • protein lipoylation Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-28852-MONOMER.
YEAST:GCVH-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H protein, mitochondrial
Alternative name(s):
Glycine decarboxylase complex subunit H
Gene namesi
Name:GCV3
Ordered Locus Names:YAL044C
ORF Names:FUN40
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome I

Organism-specific databases

CYGDiYAL044c.
EuPathDBiFungiDB:YAL044C.
SGDiS000000042. GCV3.

Subcellular locationi

GO - Cellular componenti

  • glycine cleavage complex Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747MitochondrionSequence AnalysisAdd
BLAST
Chaini48 – 170123Glycine cleavage system H protein, mitochondrialPRO_0000010739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

MaxQBiP39726.
PaxDbiP39726.
PeptideAtlasiP39726.

Expressioni

Inductioni

Induced by glycine and repressed by the C1 metabolic end products.1 Publication

Interactioni

Subunit structurei

Component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-7486,EBI-7486

Protein-protein interaction databases

BioGridi31783. 45 interactions.
IntActiP39726. 1 interaction.
MINTiMINT-669758.
STRINGi4932.YAL044C.

Structurei

3D structure databases

ProteinModelPortaliP39726.
SMRiP39726. Positions 42-143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 14383Lipoyl-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

eggNOGiCOG0509.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
InParanoidiP39726.
KOiK02437.
OMAiMDESAYK.
OrthoDBiEOG7SR4ZT.

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.

P39726-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTTRLWTT RMPTVSKLFL RNSSGNALNK NKLPFLYSSQ GPQAVRYTSQ
60 70 80 90 100
HEWIAVHQDK TAFVGITKYA TDALGDATYV ELPEVGTEIA QGESLGSIES
110 120 130 140 150
VKSASEIYQP ADGTVEEINT NLEENPGVVN EDPMGDGWLV KMKLGEGVNV
160 170
EQVEGLMSLE QYEKTLVHDD
Length:170
Mass (Da):18,793
Last modified:November 2, 2010 - v3
Checksum:i6DC35B6CCC71A6D6
GO

Sequence cautioni

The sequence AAC04987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141T → A in AAC04987 (PubMed:7731988).Curated
Sequence conflicti73 – 731A → S in AAC04987 (PubMed:7731988).Curated
Sequence conflicti90 – 901A → S in AAC04987 (PubMed:7731988).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12980 Genomic DNA. Translation: AAC04987.1. Different initiation.
BK006935 Genomic DNA. Translation: DAA06942.1.
PIRiS51975.
RefSeqiNP_009355.3. NM_001178189.1.

Genome annotation databases

EnsemblFungiiYAL044C; YAL044C; YAL044C.
GeneIDi851254.
KEGGisce:YAL044C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12980 Genomic DNA. Translation: AAC04987.1. Different initiation.
BK006935 Genomic DNA. Translation: DAA06942.1.
PIRiS51975.
RefSeqiNP_009355.3. NM_001178189.1.

3D structure databases

ProteinModelPortaliP39726.
SMRiP39726. Positions 42-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31783. 45 interactions.
IntActiP39726. 1 interaction.
MINTiMINT-669758.
STRINGi4932.YAL044C.

Proteomic databases

MaxQBiP39726.
PaxDbiP39726.
PeptideAtlasiP39726.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL044C; YAL044C; YAL044C.
GeneIDi851254.
KEGGisce:YAL044C.

Organism-specific databases

CYGDiYAL044c.
EuPathDBiFungiDB:YAL044C.
SGDiS000000042. GCV3.

Phylogenomic databases

eggNOGiCOG0509.
GeneTreeiENSGT00390000011666.
HOGENOMiHOG000239392.
InParanoidiP39726.
KOiK02437.
OMAiMDESAYK.
OrthoDBiEOG7SR4ZT.

Enzyme and pathway databases

BioCyciYEAST:G3O-28852-MONOMER.
YEAST:GCVH-MONOMER.

Miscellaneous databases

NextBioi968204.
PROiP39726.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 14; 73 AND 90.
    Strain: ATCC 204508 / S288c.
  3. "Molecular characterization of GCV3, the Saccharomyces cerevisiae gene coding for the glycine cleavage system hydrogen carrier protein."
    Nagarajan L., Storms R.K.
    J. Biol. Chem. 272:4444-4450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  4. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGCSH_YEAST
AccessioniPrimary (citable) accession number: P39726
Secondary accession number(s): D6VPH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 2, 2010
Last modified: June 24, 2015
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3510 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

External Data

Dasty 3

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 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.