| NZ_CP017477.1|WP_065317666.1|1988138_1988468_-|MerR-family-transcriptional-regulator |
gnl|CDD|133393 |
cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.
|
5.62604e-32 |
| NZ_CP017477.1|WP_065317679.1|1973490_1974090_+|nucleotidyltransferase-family-protein |
gnl|CDD|133025 |
cd04182, GT_2_like_f, GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
|
4.42164e-62 |
| NZ_CP017477.1|WP_065317677.1|1977806_1978184_+|DUF423-domain-containing-protein |
gnl|CDD|225238 |
COG2363, COG2363, Uncharacterized small membrane protein [Function unknown].
|
3.98628e-24 |
| NZ_CP017477.1|WP_065317665.1|1988729_1989692_-|M23-family-metallopeptidase |
gnl|CDD|366703 |
pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
|
3.99266e-44 |
| NZ_CP017477.1|WP_065317678.1|1974104_1977803_+|phosphoesterase |
gnl|CDD|277324 |
cd07378, MPP_ACP5, Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain. Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
|
2.3348e-12 |
| NZ_CP017477.1|WP_065317670.1|1983212_1984433_-|acyl-CoA-dehydrogenase |
gnl|CDD|173844 |
cd01155, ACAD_FadE2, Acyl-CoA dehydrogenases similar to fadE2. FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD 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. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
|
0 |
| NZ_CP017477.1|WP_065317681.1|1970157_1972308_+|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit |
gnl|CDD|224446 |
COG1529, CoxL, Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL homologs [Energy production and conversion].
|
1.0335e-56 |
| NZ_CP017477.1|WP_065317680.1|1972312_1973338_+|XdhC-family-protein |
gnl|CDD|379212 |
pfam13478, XdhC_C, XdhC Rossmann domain. This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.
|
1.25478e-43 |
| NZ_CP017477.1|WP_065317685.1|1967138_1967657_+|peptide-methionine-sulfoxide-reductase |
gnl|CDD|237597 |
PRK14054, PRK14054, peptide-methionine (S)-S-oxide reductase.
|
1.44738e-35 |
| NZ_CP017477.1|WP_065317668.1|1985376_1986150_-|glucose-1-dehydrogenase |
gnl|CDD|180802 |
PRK07035, PRK07035, SDR family oxidoreductase.
|
5.03184e-93 |
| NZ_CP017477.1|WP_139058907.1|1984451_1985177_-|VIT-family-protein |
gnl|CDD|153123 |
cd02432, Nodulin-21_like_1, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_1: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter. .
|
9.45424e-104 |
| NZ_CP017477.1|WP_065317672.1|1981242_1981995_-|glucose-1-dehydrogenase |
gnl|CDD|235506 |
PRK05565, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.
|
5.41221e-84 |
| NZ_CP017477.1|WP_065317682.1|1969680_1970154_+|(2Fe-2S)-binding-protein |
gnl|CDD|224991 |
COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].
|
3.63255e-66 |
| NZ_CP017477.1|WP_065317674.1|1980075_1980513_-|TPM-domain-containing-protein |
gnl|CDD|377378 |
pfam04536, TPM_phosphatase, TPM domain. This family was first named TPM domain after its founding proteins: TLP18.3, Psb32 and MOLO-1. In Arabidopsis, this domain is called the thylakoid acid phosphatase -TAP - domain and has a Rossmann-like fold. In plants, the family resides in the thylakoid lumen attached to the outer membrane of the chloroplast/plastid. It is active in the photosystem II.
|
1.92237e-26 |
| NZ_CP017477.1|WP_065317684.1|1967669_1968890_+|OsmC-family-protein |
gnl|CDD|224679 |
COG1765, COG1765, Predicted redox protein, regulator of disulfide bond formation [Posttranslational modification, protein turnover, chaperones].
|
4.62449e-21 |
| NZ_CP017477.1|WP_065317667.1|1986149_1987964_-|acyl-CoA-dehydrogenase |
gnl|CDD|173842 |
cd01153, ACAD_fadE5, Putative acyl-CoA dehydrogenases similar to fadE5. Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD 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. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
|
1.47644e-129 |
| NZ_CP017477.1|WP_065317671.1|1982157_1983216_-|phosphotransferase-family-protein |
gnl|CDD|270703 |
cd05154, ACAD10_11_N-like, N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins. This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
|
2.77398e-87 |
| NZ_CP017477.1|WP_065317673.1|1980513_1981128_-|LemA-family-protein |
gnl|CDD|377192 |
pfam04011, LemA, LemA family. The members of this family are related to the LemA protein. LemA contains an amino terminal predicted transmembrane helix. It has been predicted that the small amino terminus is extracellular. The exact molecular function of this protein is uncertain.
|
4.12574e-69 |
