Domains within Drosophila melanogaster protein Q7KN85_DROME (Q7KN85)

ATP-citrate synthase

Alternative representations: 1 /

Protein length1112 aa
Source databaseUniProt
Identifiers Q7KN85_DROME, Q7KN85, FBPP0289823, FBPP0289824, A1ZA78, B7YZH5
Source gene FBgn0020236
Alternative splicing A0A0B4LFH8_DROME, Q7KN85_DROME, E2QCF1_DROME

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

Q7KN85_DROME is shown as ATPCL in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for ATPCL

Protein Q7KN85_DROME is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00720Other carbon fixation pathways iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K01648ACLYATP citrate (pro-S)-lyase [EC:2.3.3.8] iPath3
K01903sucCsuccinyl-CoA synthetase beta subunit [EC:6.2.1.5] iPath3
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 40 PTMs annotated in this protein:

PTMCount
Ubiquitination18
Phosphorylation14
Acetylation7
Nitrosylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein ATPCL.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 7227.FBpp0289824 in eggNOG.

OGTaxonomic classDescription
FUUSDmelanogaster group (species group)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
LCOG0045All organisms (root)succinyl-CoA synthetase beta subunit [EC:6.2.1.5],ATP citrate (pro-S)-lyase [EC:2.3.3.8],succinyl-CoA synthetase beta subunit [EC:6.2.1.4 6.2.1.5]
EIY7NEndopterygota (cohort)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
FDXG6melanogaster subgroup (species subgroup)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
KOG1254Eukaryota (superkingdom)ATP citrate (pro-S)-lyase [EC:2.3.3.8],anthranilate phosphoribosyltransferase [EC:2.4.2.18],large subunit ribosomal protein L30
HSZX5Metazoa (kingdom)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
HIM57Arthropoda (phylum)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
85H6THexapoda (subphylum)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
AGM29Neoptera (infraclass)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
ANM1YDiptera (order)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
7P2FKOpisthokonta (clade)ATP citrate (pro-S)-lyase [EC:2.3.3.8],large subunit ribosomal protein L30,kelch-like protein 11
H5SXWBilateria (clade)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
EH051Drosophila (genus)ATP citrate (pro-S)-lyase [EC:2.3.3.8]
50P26Sophophora (subgenus)ATP citrate (pro-S)-lyase [EC:2.3.3.8]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: