| NZ_CP013342.1|WP_062900842.1|793783_794536_-|ABC-transporter-permease |
gnl|CDD|223673 |
COG0600, TauC, ABC-type nitrate/sulfonate/bicarbonate transport system, permease component [Inorganic ion transport and metabolism].
|
2.80087e-59 |
| NZ_CP013342.1|WP_062900854.1|804625_804922_-|DUF2282-domain-containing-protein |
gnl|CDD|370796 |
pfam10048, DUF2282, Predicted integral membrane protein (DUF2282). Members of this family of hypothetical bacterial proteins and putative signal peptide proteins have no known function.
|
8.01287e-22 |
| NZ_CP013342.1|WP_003052658.1|798995_799433_+|VOC-family-protein |
gnl|CDD|319898 |
cd06587, VOC, vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.
|
2.32277e-10 |
| NZ_CP013342.1|WP_062900850.1|801401_802052_-|DUF1109-domain-containing-protein |
gnl|CDD|377671 |
pfam06532, DUF1109, Protein of unknown function (DUF1109). This family consists of several hypothetical bacterial proteins of unknown function.
|
4.73178e-31 |
| NZ_CP013342.1|WP_062900843.1|794532_795090_-|glyoxalase |
gnl|CDD|319931 |
cd08343, ED_TypeI_classII_C, C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain. This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.
|
1.4206e-27 |
| NZ_CP013342.1|WP_062900857.1|807055_808885_+|DEAD/DEAH-box-helicase |
gnl|CDD|223587 |
COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].
|
4.26611e-118 |
| NZ_CP013342.1|WP_062900851.1|802571_803030_-|DoxX-family-protein |
gnl|CDD|225168 |
COG2259, COG2259, Predicted membrane protein [Function unknown].
|
2.58431e-09 |
| NZ_CP013342.1|WP_082819811.1|796135_797170_-|FAA-hydrolase-family-protein |
gnl|CDD|223257 |
COG0179, MhpD, 2-keto-4-pentenoate hydratase/2-oxohepta-3-ene-1,7-dioic acid hydratase (catechol pathway) [Secondary metabolites biosynthesis, transport, and catabolism].
|
2.42323e-84 |
| NZ_CP013342.1|WP_082819812.1|805111_805549_+|GreA/GreB-family-elongation-factor |
gnl|CDD|180535 |
PRK06342, PRK06342, transcription elongation factor GreA.
|
6.52359e-19 |
| NZ_CP013342.1|WP_062900846.1|798178_798982_+|aspartate-dehydrogenase |
gnl|CDD|237341 |
PRK13302, PRK13302, aspartate dehydrogenase.
|
9.4141e-94 |
| NZ_CP013342.1|WP_062900844.1|795086_796139_-|nitrate-ABC-transporter-permease |
gnl|CDD|378117 |
pfam09084, NMT1, NMT1/THI5 like. This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.
|
1.24034e-33 |
| NZ_CP013342.1|WP_082820028.1|803740_804574_-|DUF692-domain-containing-protein |
gnl|CDD|377459 |
pfam05114, DUF692, Protein of unknown function (DUF692). This family consists of several uncharacterized bacterial proteins.
|
1.03467e-121 |
| NZ_CP013342.1|WP_062900847.1|799486_799798_-|hypothetical-protein |
gnl|CDD|379149 |
pfam13376, OmdA, Bacteriocin-protection, YdeI or OmpD-Associated. This is a family of archaeal and bacterial proteins predicted to be periplasmic. YdeI is important for resistance to polymyxin B in broth and for bacterial survival in mice upon oral, but not intraperitoneal inoculation, suggesting a role for YdeI in the gastrointestinal tract of mice. Production of the ydeI gene is regulated by the Rcs (regulator of capsule synthesis) phospho-relay system pathway independently of RcsA, and additionally transcription of the protein is regulated by the stationary-phase sigma factor, RpoS (sigma-S). YdeI confers protection against cationic AMPs (Antimicrobial peptides) or bacteriocins in conjunction with the general porin Omp, thus justifying its name of OmdA, for OmpD-Associated protein.
|
1.61772e-16 |
| NZ_CP013342.1|WP_003052645.1|802053_802575_-|sigma-70-family-RNA-polymerase-sigma-factor |
gnl|CDD|237132 |
PRK12539, PRK12539, RNA polymerase sigma factor SigF.
|
2.88248e-38 |
| NZ_CP013342.1|WP_062902989.1|797166_797994_-|sulfite-exporter-TauE/SafE-family-protein |
gnl|CDD|376667 |
pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.
|
6.09102e-25 |
| NZ_CP013342.1|WP_062900852.1|803031_803748_-|DUF2063-domain-containing-protein |
gnl|CDD|378264 |
pfam09836, DUF2063, Putative DNA-binding domain. This family represents the N-terminal part of a Neisseria protein, UniProtKB:Q5F5I0, Structure 3dee. It runs from residues 31-117 as a helical bundle with 4 main helices. \From genomic context and the fold of the C-terminal part, it is suggested that this protein is involved in transcriptional regulation.
|
2.0205e-07 |
| NZ_CP013342.1|WP_062900848.1|799830_800541_-|DUF2807-domain-containing-protein |
gnl|CDD|371327 |
pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).
|
2.46177e-31 |
| NZ_CP013342.1|WP_062900856.1|805734_806907_+|NAD(P)/FAD-dependent-oxidoreductase |
gnl|CDD|367519 |
pfam03486, HI0933_like, HI0933-like protein.
|
2.13304e-167 |
| NZ_CP013342.1|WP_082819810.1|793037_793799_-|ABC-transporter-ATP-binding-protein |
gnl|CDD|224041 |
COG1116, TauB, ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism].
|
6.2731e-112 |
