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YEAST:ACON
Contents
Species (Taxon ID) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292) | |
Gene Name(s) | ACO1 (synonyms: GLU1) | |
Protein Name(s) | Aconitate hydratase, mitochondrial
Aconitase Citrate hydro-lyase | |
External Links | ||
UniProt | P19414 | |
EMBL | M33131 U17243 BK006945 | |
PIR | S50387 | |
RefSeq | NP_013407.1 | |
ProteinModelPortal | P19414 | |
SMR | P19414 | |
BioGrid | 31569 | |
DIP | DIP-4679N | |
IntAct | P19414 | |
MINT | MINT-557728 | |
STRING | 4932.YLR304C | |
MaxQB | P19414 | |
PaxDb | P19414 | |
PeptideAtlas | P19414 | |
PRIDE | P19414 | |
EnsemblFungi | [example_ID YLR304C] | |
GeneID | 851013 | |
KEGG | sce:YLR304C | |
CYGD | YLR304c | |
SGD | S000004295 | |
eggNOG | COG1048 | |
GeneTree | ENSGT00760000119830 | |
HOGENOM | HOG000224293 | |
InParanoid | P19414 | |
KO | K01681 | |
OMA | AVEANKW | |
OrthoDB | EOG7X6M7Q | |
BioCyc | MetaCyc:YLR304C-MONOMER YEAST:YLR304C-MONOMER | |
Reactome | REACT_189012 REACT_245486 | |
UniPathway | UPA00223 | |
NextBio | 967571 | |
PRO | PR:P19414 | |
Proteomes | UP000002311 | |
Genevestigator | P19414 | |
GO | GO:0005829 GO:0005758 GO:0005759 GO:0042645 GO:0051539 GO:0003994 GO:0003690 GO:0046872 GO:0003697 GO:0000002 GO:0006099 | |
Gene3D | 3.20.19.10 3.30.499.10 3.40.1060.10 | |
InterPro | IPR015931 IPR015937 IPR001030 IPR015928 IPR015932 IPR018136 IPR006248 IPR000573 | |
PANTHER | PTHR11670 | |
Pfam | PF00330 PF00694 | |
PRINTS | PR00415 | |
SUPFAM | SSF52016 SSF53732 | |
TIGRFAMs | TIGR01340 | |
PROSITE | PS00450 PS01244 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0042645 |
mitochondrial nucleoid |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005759 |
mitochondrial matrix |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0003994 |
aconitate hydratase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003994 |
aconitate hydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003697 |
single-stranded DNA binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003690 |
double-stranded DNA binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0000002 |
mitochondrial genome maintenance |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG12316 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0010100 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG12316 |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005739 |
mitochondrion |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0010100 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0003994 |
aconitate hydratase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG12316 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0003994 |
aconitate hydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003994 |
aconitate hydratase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
Reactome:R-SCE-1252255 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005758 |
mitochondrial intermembrane space |
Reactome:R-SCE-1252255 |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006099 |
tricarboxylic acid cycle |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0816 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0051539 |
4 iron, 4 sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051536 |
iron-sulfur cluster binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
- ↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
- ↑ Kaufman, BA et al. (2000) In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Proc. Natl. Acad. Sci. U.S.A. 97 7772-7 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Gangloff, SP et al. (1990) Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol. 10 3551-61 PubMed GONUTS page
- ↑ Regev-Rudzki, N et al. (2005) Yeast aconitase in two locations and two metabolic pathways: seeing small amounts is believing. Mol. Biol. Cell 16 4163-71 PubMed GONUTS page
- ↑ 6.0 6.1 Chen, XJ et al. (2005) Aconitase couples metabolic regulation to mitochondrial DNA maintenance. Science 307 714-7 PubMed GONUTS page
- ↑ 7.0 7.1 Chen, XJ et al. (2007) Yeast aconitase binds and provides metabolically coupled protection to mitochondrial DNA. Proc. Natl. Acad. Sci. U.S.A. 104 13738-43 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 8.3 8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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