| CP030849.1|QBC33734.1|978029_979004_+|agmatinase |
gnl|CDD|212538 |
cd11592, Agmatinase_PAH, Agmatinase-like family includes proclavaminic acid amidinohydrolase. This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.
|
1.50558e-160 |
| CP030849.1|QBC30776.1|981428_983288_-|amidohydrolase |
gnl|CDD|224490 |
COG1574, COG1574, Predicted metal-dependent hydrolase with the TIM-barrel fold [General function prediction only].
|
0 |
| CP030849.1|QBC33735.1|991554_992394_-|peptidase |
gnl|CDD|236952 |
PRK11669, pbpG, D-alanyl-D-alanine endopeptidase; Provisional.
|
7.36947e-69 |
| CP030849.1|QBC30775.1|981120_981402_-|DUF1427-family-protein |
gnl|CDD|369277 |
pfam07235, DUF1427, Protein of unknown function (DUF1427). This family consists of several bacterial proteins of around 100 residues in length. The function of this family is unknown.
|
7.93463e-39 |
| CP030849.1|QBC30780.1|995350_996085_-|SURF1-family-protein |
gnl|CDD|225883 |
COG3346, COG3346, Uncharacterized conserved protein [Function unknown].
|
1.13469e-75 |
| CP030849.1|QBC30783.1|997273_999265_-|cytochrome-o-ubiquinol-oxidase-subunit-I |
gnl|CDD|131890 |
TIGR02843, Cytochrome_bo3_ubiquinol_oxidase_subunit_1, cytochrome o ubiquinol oxidase, subunit I. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport].
|
0 |
| CP030849.1|QBC30785.1|1000471_1001860_+|MFS-transporter |
gnl|CDD|340927 |
cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) 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.
|
1.09644e-90 |
| CP030849.1|QBC30781.1|996208_996616_-|cytochrome-o-ubiquinol-oxidase-subunit-IV |
gnl|CDD|225667 |
COG3125, CyoD, Heme/copper-type cytochrome/quinol oxidase, subunit 4 [Energy production and conversion].
|
1.24562e-36 |
| CP030849.1|QBC30787.1|1002958_1003990_+|dipeptide-ABC-transporter-ATP-binding-protein-DppD |
gnl|CDD|223521 |
COG0444, DppD, ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism / Inorganic ion transport and metabolism].
|
2.56802e-174 |
| CP030849.1|QBC30784.1|999330_1000365_-|ubiquinol-oxidase-subunit-II |
gnl|CDD|213620 |
TIGR01433, precursor_Cytochrome_o_subunit_2_Oxidase, cytochrome o ubiquinol oxidase subunit II. This enzyme catalyzes the oxidation of ubiquinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. Subunit II is responsible for binding and oxidation of the ubiquinone substrate. This sequence is closely related to QoxA, which oxidizes quinol in gram positive bacteria but which is in complex with subunits which utilize cytochromes a in the reduction of molecular oxygen. Slightly more distantly related is subunit II of cytochrome c oxidase which uses cyt. c as the oxidant. [Energy metabolism, Electron transport].
|
1.14522e-128 |
| CP030849.1|QBC30782.1|996612_997281_-|cytochrome-o-ubiquinol-oxidase-subunit-III |
gnl|CDD|131889 |
TIGR02842, Cytochrome_bo3_ubiquinol_oxidase_subunit_3, cytochrome o ubiquinol oxidase, subunit III. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport].
|
3.66263e-101 |
| CP030849.1|QBC30779.1|993145_994873_-|gamma-glutamyltransferase |
gnl|CDD|223482 |
COG0405, Ggt, Gamma-glutamyltransferase [Amino acid transport and metabolism].
|
0 |
| CP030849.1|QBC30772.1|976914_977820_-|LysR-family-transcriptional-regulator |
gnl|CDD|223656 |
COG0583, LysR, Transcriptional regulator [Transcription].
|
5.42613e-41 |
| CP030849.1|QBC30773.1|979083_980118_+|taurine-ABC-transporter-substrate-binding-protein |
gnl|CDD|226904 |
COG4521, TauA, ABC-type taurine transport system, periplasmic component [Inorganic ion transport and metabolism].
|
3.06127e-100 |
| CP030849.1|QBC30777.1|983301_983988_-|hydrolase |
gnl|CDD|238494 |
cd01012, YcaC_related, YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.
|
1.73474e-70 |
| CP030849.1|QBC30771.1|974973_975825_-|hypothetical-protein |
gnl|CDD|275082 |
TIGR04255, hypothetical_protein, TIGR04255 family protein. Members of this uncharacterized protein family are found broadly but sporadically among bacteria and archaea, including members of the genera Mycobacterium, Nostoc, Acinetobacter, Planctomyces, Geobacter, Streptomyces, Methanospirillum, etc. The function is unknown.
|
2.11033e-31 |
| CP030849.1|QBC30786.1|1001942_1002812_-|LysR-family-transcriptional-regulator |
gnl|CDD|176118 |
cd08427, PBP2_LTTR_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.
|
4.82654e-43 |
| CP030849.1|QBC30778.1|984240_984921_+|DNA-binding-response-regulator |
gnl|CDD|226932 |
COG4566, TtrR, Response regulator [Signal transduction mechanisms].
|
4.60243e-62 |
