citrate lyase subunit alpha is the citrate:acetyl-ACP transferase subunit of citrate lyase that catalyzes the conversion of citrate to acetate and oxaloacetate; also catalyzes the transfer of thioacyl carrier protein from its acetyl thioester to citrate
citrate lyase, alpha subunit; This is a model of the alpha subunit of the holoenzyme citrate ...
23-512
0e+00
citrate lyase, alpha subunit; This is a model of the alpha subunit of the holoenzyme citrate lyase (EC 4.1.3.6) composed of alpha (EC 2.8.3.10), beta (EC 4.1.3.34), and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The alpha subunit catalyzes the reaction Acetyl-CoA + citrate = acetate + (3S)-citryl-CoA. The seed contains an experimentally characterized member from Lactococcus lactis subsp. lactis. The model covers both Gram positive and Gram negative bacteria. It is quite robust with queries scoring either quite well or quite poorly against the model. There are currently no hits in between the noise cutoff and trusted cutoff. [Energy metabolism, Fermentation]
Pssm-ID: 130646 Cd Length: 492 Bit Score: 742.43 E-value: 0e+00
Citrate lyase, alpha subunit (CitF); In citrate-utilizing prokaryotes, citrate lyase EC:4.1.3.6 cleaves intracellular citrate into acetate and oxaloacetate, and is organized as a functional complex consisting of alpha, beta, and gamma subunits. The gamma subunit serves as an acyl carrier protein (ACP), and has a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group. The citrate lyase is active only if this prosthetic group is acetylated; this acetylation is catalyzed by an acetate:SH-citrate lyase ligase. The alpha subunit substitutes citryl for the acetyl group to form citryl-S-ACP. The beta subunit completes the reaction by cleaving the citryl to yield oxaloacetate and (regenerated) acetyl-S-ACP. This family represents the alpha subunit EC:2.8.3.10.
Pssm-ID: 427798 [Multi-domain] Cd Length: 466 Bit Score: 674.23 E-value: 0e+00
citrate lyase, alpha subunit; This is a model of the alpha subunit of the holoenzyme citrate ...
23-512
0e+00
citrate lyase, alpha subunit; This is a model of the alpha subunit of the holoenzyme citrate lyase (EC 4.1.3.6) composed of alpha (EC 2.8.3.10), beta (EC 4.1.3.34), and acyl carrier protein subunits in a stoichiometric relationship of 6:6:6. Citrate lyase is an enzyme which converts citrate to oxaloacetate. In bacteria, this reaction is involved in citrate fermentation. The alpha subunit catalyzes the reaction Acetyl-CoA + citrate = acetate + (3S)-citryl-CoA. The seed contains an experimentally characterized member from Lactococcus lactis subsp. lactis. The model covers both Gram positive and Gram negative bacteria. It is quite robust with queries scoring either quite well or quite poorly against the model. There are currently no hits in between the noise cutoff and trusted cutoff. [Energy metabolism, Fermentation]
Pssm-ID: 130646 Cd Length: 492 Bit Score: 742.43 E-value: 0e+00
Citrate lyase, alpha subunit (CitF); In citrate-utilizing prokaryotes, citrate lyase EC:4.1.3.6 cleaves intracellular citrate into acetate and oxaloacetate, and is organized as a functional complex consisting of alpha, beta, and gamma subunits. The gamma subunit serves as an acyl carrier protein (ACP), and has a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group. The citrate lyase is active only if this prosthetic group is acetylated; this acetylation is catalyzed by an acetate:SH-citrate lyase ligase. The alpha subunit substitutes citryl for the acetyl group to form citryl-S-ACP. The beta subunit completes the reaction by cleaving the citryl to yield oxaloacetate and (regenerated) acetyl-S-ACP. This family represents the alpha subunit EC:2.8.3.10.
Pssm-ID: 427798 [Multi-domain] Cd Length: 466 Bit Score: 674.23 E-value: 0e+00
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
368-446
3.56e-07
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.
Pssm-ID: 433126 [Multi-domain] Cd Length: 154 Bit Score: 49.74 E-value: 3.56e-07
Flp pilus assembly protein RcpC/CpaB; RcpC is a family of Gram-negative proteins expressed ...
423-495
3.73e-03
Flp pilus assembly protein RcpC/CpaB; RcpC is a family of Gram-negative proteins expressed from the tight-adherence tad locus. RcpC is an auxillary protein that sits in the inner membrane and interacts with TadB and TadZ, an AAA ATPase. A recent study has identified two tandem beta-clip domains in RcpC95. beta-Clip domains are known to interact with carbohydrate moieties in other systems, such as SAF.
Pssm-ID: 435686 Cd Length: 115 Bit Score: 37.18 E-value: 3.73e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
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if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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