| NZ_CP025116.1|WP_101013083.1|1310653_1315006_-|DNA-polymerase-III-subunit-alpha |
gnl|CDD|235554 |
PRK05673, dnaE, DNA polymerase III subunit alpha; Validated.
|
0 |
| NZ_CP025116.1|WP_101013065.1|1301083_1301557_+|GNAT-family-N-acetyltransferase |
gnl|CDD|366181 |
pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
|
1.29264e-15 |
| NZ_CP025116.1|WP_101013085.1|1316526_1319130_-|ribonucleoside-diphosphate-reductase-subunit-alpha |
gnl|CDD|178056 |
PLN02437, PLN02437, ribonucleoside--diphosphate reductase large subunit.
|
0 |
| NZ_CP025116.1|WP_101013074.1|1306341_1306716_-|TM2-domain-containing-protein |
gnl|CDD|377473 |
pfam05154, TM2, TM2 domain. This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts.
|
1.10132e-13 |
| NZ_CP025116.1|WP_101013076.1|1306751_1307150_-|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.
|
0.00012753 |
| NZ_CP025116.1|WP_101013086.1|1319277_1320270_-|ribonucleoside-diphosphate-reductase |
gnl|CDD|215272 |
PLN02492, PLN02492, ribonucleoside-diphosphate reductase.
|
0 |
| NZ_CP025116.1|WP_157810889.1|1305777_1306212_-|hypothetical-protein |
gnl|CDD|319973 |
cd16345, LMWP_ArsC, Arsenate reductase of the LMWP family. Arsenate reductase plays an important role in the reduction of intracellular arsenate to arsenite, an important step in arsenic detoxification. The reduction involves three different thiolate nucleophiles. In arsenate reductases of the LMWP family, reduction can be coupled with thioredoxin (Trx)/thioredoxin reductase (TrxR) or glutathione (GSH)/glutaredoxin (Grx).
|
3.19871e-17 |
| NZ_CP025116.1|WP_101013082.1|1309095_1310445_-|magnesium-transporter |
gnl|CDD|225148 |
COG2239, MgtE, Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism].
|
1.73494e-118 |
| NZ_CP025116.1|WP_101013089.1|1322311_1322866_+|ribosome-recycling-factor |
gnl|CDD|178850 |
PRK00083, frr, ribosome recycling factor; Reviewed.
|
6.09908e-92 |
| NZ_CP025116.1|WP_101013067.1|1301557_1302844_+|aspartate-kinase |
gnl|CDD|239776 |
cd04243, AAK_AK-HSDH-like, AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine.
|
2.07901e-96 |
| NZ_CP025116.1|WP_101013084.1|1315639_1316086_-|PA2169-family-four-helix-bundle-protein |
gnl|CDD|378201 |
pfam09537, DUF2383, Domain of unknown function (DUF2383). Members of this protein family are found mostly in the Proteobacteria, although one member is found in the the marine planctomycete Pirellula sp. strain 1. The function is unknown.
|
3.70709e-39 |
| NZ_CP025116.1|WP_157810888.1|1304739_1305774_+|hypothetical-protein |
gnl|CDD|372685 |
pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.
|
9.03252e-15 |
| NZ_CP025116.1|WP_101013078.1|1307143_1308088_-|hydroxyacid-dehydrogenase |
gnl|CDD|240656 |
cd12179, 2-Hacid_dh_14, Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
|
0 |
| NZ_CP025116.1|WP_101013063.1|1299959_1300970_-|class-1-fructose-bisphosphatase |
gnl|CDD|236458 |
PRK09293, PRK09293, class 1 fructose-bisphosphatase.
|
0 |
| NZ_CP025116.1|WP_101013087.1|1320633_1321197_-|DUF3109-family-protein |
gnl|CDD|378636 |
pfam11307, DUF3109, Protein of unknown function (DUF3109). This bacterial family of proteins has no known function.
|
8.27413e-111 |
| NZ_CP025116.1|WP_101013060.1|1299394_1299820_+|TerB-family-tellurite-resistance-protein |
gnl|CDD|143581 |
cd07177, terB_like, tellurium resistance terB-like protein. This family consists of tellurium resistance terB proteins, N-terminal domain of heat shock DnaJ-like proteins, N-terminal domain of Mo-dependent nitrogenase-like proteins, C-terminal domain of ABC transporter ATP-binding proteins, C-terminal domain of serine/threonine protein kinase, and many hypothetical bacterial proteins. The function of this family is unknown.
|
7.94523e-05 |
| NZ_CP025116.1|WP_101013069.1|1302892_1304722_+|lysophospholipid-acyltransferase-family-protein |
gnl|CDD|153248 |
cd07986, LPLAT_ACT14924-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.
|
4.89546e-71 |
| NZ_CP025116.1|WP_101013088.1|1321560_1322268_+|UMP-kinase |
gnl|CDD|239787 |
cd04254, AAK_UMPK-PyrH-Ec, UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK).
|
4.53608e-150 |
