| NZ_AP022567.1|WP_036437746.1|525537_526329_+|FadR-family-transcriptional-regulator |
gnl|CDD|225097 |
COG2186, FadR, Transcriptional regulators [Transcription].
|
8.35758e-46 |
| NZ_AP022567.1|WP_036437720.1|508295_508934_-|class-I-SAM-dependent-methyltransferase |
gnl|CDD|372616 |
pfam13489, Methyltransf_23, Methyltransferase domain. This family appears to be a methyltransferase domain.
|
3.28794e-15 |
| NZ_AP022567.1|WP_036438634.1|518371_518884_-|gamma-carbonic-anhydrase-family-protein |
gnl|CDD|100051 |
cd04645, LbH_gamma_CA_like, Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.
|
2.46722e-80 |
| NZ_AP022567.1|WP_036437750.1|526704_528441_-|DUF3556-domain-containing-protein |
gnl|CDD|371888 |
pfam12077, DUF3556, Transmembrane protein of unknown function (DUF3556). This family of transmembrane proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 576 to 592 amino acids in length.
|
0 |
| NZ_AP022567.1|WP_036437730.1|514821_515913_-|CoA-transferase |
gnl|CDD|224717 |
COG1804, CaiB, Predicted acyl-CoA transferases/carnitine dehydratase [Energy production and conversion].
|
4.9755e-114 |
| NZ_AP022567.1|WP_036437744.1|524163_525312_-|thiolase-family-protein |
gnl|CDD|238383 |
cd00751, thiolase, Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
|
1.12898e-178 |
| NZ_AP022567.1|WP_036437724.1|509611_511927_-|MMPL-family-transporter |
gnl|CDD|225272 |
COG2409, COG2409, Predicted drug exporters of the RND superfamily [General function prediction only].
|
4.87159e-114 |
| NZ_AP022567.1|WP_036437742.1|523378_524167_-|crotonase/enoyl-CoA-hydratase-family-protein |
gnl|CDD|181325 |
PRK08252, PRK08252, crotonase/enoyl-CoA hydratase family protein.
|
9.82007e-94 |
| NZ_AP022567.1|WP_036437722.1|508926_509610_-|TetR/AcrR-family-transcriptional-regulator |
gnl|CDD|224228 |
COG1309, AcrR, Transcriptional regulator [Transcription].
|
3.94927e-15 |
| NZ_AP022567.1|WP_036438636.1|521435_522161_+|fasciclin-domain-containing-protein |
gnl|CDD|367095 |
pfam02469, Fasciclin, Fasciclin domain. This extracellular domain is found repeated four times in grasshopper fasciclin I as well as in proteins from mammals, sea urchins, plants, yeast and bacteria.
|
3.5983e-23 |
| NZ_AP022567.1|WP_051579039.1|519925_521278_+|MFS-transporter |
gnl|CDD|340913 |
cd17355, MFS_YcxA_like, MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters. This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
|
3.12273e-102 |
| NZ_AP022567.1|WP_036437732.1|516023_516851_+|enoyl-CoA-hydratase |
gnl|CDD|235852 |
PRK06688, PRK06688, enoyl-CoA hydratase; Provisional.
|
1.09722e-111 |
| NZ_AP022567.1|WP_036437740.1|522229_523372_-|acyl-CoA-dehydrogenase-family-protein |
gnl|CDD|173849 |
cd01160, LCAD, Long chain acyl-CoA dehydrogenase. LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
|
2.72163e-164 |
| NZ_AP022567.1|WP_036437736.1|518917_519874_-|helix-turn-helix-domain-containing-protein |
gnl|CDD|181818 |
PRK09393, ftrA, transcriptional activator FtrA; Provisional.
|
1.38144e-106 |
| NZ_AP022567.1|WP_036438632.1|512100_512637_+|DoxX-family-protein |
gnl|CDD|225168 |
COG2259, COG2259, Predicted membrane protein [Function unknown].
|
1.11091e-10 |
| NZ_AP022567.1|WP_036437733.1|516923_518210_+|tetracycline-efflux-MFS-transporter-Tet(V) |
gnl|CDD|162098 |
TIGR00900, multidrug_transporter, H+ Antiporter protein. [Transport and binding proteins, Cations and iron carrying compounds].
|
2.23985e-90 |
| NZ_AP022567.1|WP_036438629.1|507572_508286_+|NAD-dependent-deacylase |
gnl|CDD|234777 |
PRK00481, PRK00481, NAD-dependent deacetylase; Provisional.
|
1.66068e-117 |
| NZ_AP022567.1|WP_036437726.1|512963_513974_-|nitronate-monooxygenase |
gnl|CDD|240081 |
cd04730, NPD_like, 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
|
4.45265e-88 |
| NZ_AP022567.1|WP_036437728.1|514014_514767_-|3-hydroxyacyl-CoA-dehydrogenase |
gnl|CDD|187629 |
cd05371, HSD10-like_SDR_c, 17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs. HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
|
1.65104e-132 |
