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ECOLI:FABH
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | fabH | |
Protein Name(s) | 3-oxoacyl-[acyl-carrier-protein] synthase 3
3-oxoacyl-[acyl-carrier-protein] synthase III Beta-ketoacyl-ACP synthase III KAS III EcFabH | |
External Links | ||
UniProt | P0A6R0 | |
EMBL | M77744 M96793 U00096 AP009048 M87040 Z11565 | |
PIR | A42431 | |
RefSeq | NP_415609.1 YP_489359.1 | |
PDB | 1EBL 1HN9 1HND 1HNH 1HNJ 1HNK 1MZS 2EFT 2GYO 3IL9 | |
PDBsum | 1EBL 1HN9 1HND 1HNH 1HNJ 1HNK 1MZS 2EFT 2GYO 3IL9 | |
ProteinModelPortal | P0A6R0 | |
SMR | P0A6R0 | |
DIP | DIP-48255N | |
IntAct | P0A6R0 | |
MINT | MINT-1263292 | |
STRING | 511145.b1091 | |
BindingDB | P0A6R0 | |
ChEMBL | CHEMBL4914 | |
DrugBank | DB01034 | |
PaxDb | P0A6R0 | |
PRIDE | P0A6R0 | |
EnsemblBacteria | AAC74175 BAA35899 | |
GeneID | 12932037 946003 | |
KEGG | ecj:Y75_p1061 eco:b1091 | |
PATRIC | 32117423 | |
EchoBASE | EB0273 | |
EcoGene | EG10277 | |
eggNOG | COG0332 | |
HOGENOM | HOG000246674 | |
InParanoid | P0A6R0 | |
KO | K00648 | |
OMA | AHIVEET | |
OrthoDB | EOG6J74XN | |
PhylomeDB | P0A6R0 | |
BioCyc | EcoCyc:FABH-MONOMER ECOL316407:JW1077-MONOMER MetaCyc:FABH-MONOMER | |
BRENDA | 2.3.1.180 | |
UniPathway | UPA00094 | |
EvolutionaryTrace | P0A6R0 | |
PRO | PR:P0A6R0 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P0A6R0 | |
GO | GO:0005737 GO:0004315 GO:0033818 GO:0006633 GO:0006631 | |
Gene3D | 3.40.47.10 | |
HAMAP | MF_01815 | |
InterPro | IPR013751 IPR013747 IPR004655 IPR016039 IPR016038 | |
Pfam | PF08545 PF08541 | |
SUPFAM | SSF53901 | |
TIGRFAMs | TIGR00747 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
Contributes to |
GO:0004315 |
3-oxoacyl-(acyl-carrier-protein) synthase activity |
ECO:0000314 |
F |
FabH catalyzes the condensation of acetyl-CoA and initiation of fatty acid synthesis. Table 2 shows the level of FabH correlates with the membrane fatty acid composition. Chromatography was used to analyze the fatty acid methyl esters. |
complete | ||||
involved_in |
GO:0006631 |
fatty acid metabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0033818 |
beta-ketoacyl-acyl-carrier-protein synthase III activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
GO:0006631 |
fatty acid metabolic process |
ECO:0000315 |
P |
Table 2: The level of FabH expression is correlated to the overall fatty acid membrane composition. |
complete | |||||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004315 |
3-oxoacyl-[acyl-carrier-protein] synthase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006633 |
fatty acid biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0033818 |
beta-ketoacyl-acyl-carrier-protein synthase III activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0033818 |
beta-ketoacyl-acyl-carrier-protein synthase III activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000085060 |
F |
Seeded From UniProt |
complete | ||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000085060 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006633 |
fatty acid biosynthetic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000085060 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016740 |
transferase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006631 |
fatty acid metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016746 |
transferase activity, transferring acyl groups |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003824 |
catalytic activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006633 |
fatty acid biosynthetic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0275 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0008152 |
metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006629 |
lipid metabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Tsay, JT et al. (1992) Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267 6807-14 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page