mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase [Pseudomonas protegens]
Protein Classification
mannose-6-phosphate isomerase type 2 family protein( domain architecture ID 11492682)
mannose-6-phosphate isomerase type 2 family protein is involved in nucleotide-sugar biosynthesis, similar to bifunctional mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| GMP_PMI | TIGR01479 | mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
1-468 | 0e+00 | |||||||
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] : Pssm-ID: 273648 [Multi-domain] Cd Length: 468 Bit Score: 808.86 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| GMP_PMI | TIGR01479 | mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
1-468 | 0e+00 | |||||||
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 273648 [Multi-domain] Cd Length: 468 Bit Score: 808.86 E-value: 0e+00
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| cpsB | PRK15460 | mannose-1-phosphate guanyltransferase; Provisional |
1-468 | 0e+00 | |||||||
mannose-1-phosphate guanyltransferase; Provisional Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 582.32 E-value: 0e+00
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| CpsB | COG0836 | Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-348 | 0e+00 | |||||||
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 547.74 E-value: 0e+00
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| GDP-M1P_Guanylyltransferase | cd02509 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-277 | 5.90e-135 | |||||||
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes. Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 390.40 E-value: 5.90e-135
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| MannoseP_isomer | pfam01050 | Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ... |
314-464 | 8.52e-102 | |||||||
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483. Pssm-ID: 426015 [Multi-domain] Cd Length: 151 Bit Score: 301.26 E-value: 8.52e-102
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| Name | Accession | Description | Interval | E-value | |||||||
| GMP_PMI | TIGR01479 | mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
1-468 | 0e+00 | |||||||
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] Pssm-ID: 273648 [Multi-domain] Cd Length: 468 Bit Score: 808.86 E-value: 0e+00
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| cpsB | PRK15460 | mannose-1-phosphate guanyltransferase; Provisional |
1-468 | 0e+00 | |||||||
mannose-1-phosphate guanyltransferase; Provisional Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 582.32 E-value: 0e+00
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| CpsB | COG0836 | Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-348 | 0e+00 | |||||||
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 547.74 E-value: 0e+00
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| GDP-M1P_Guanylyltransferase | cd02509 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-277 | 5.90e-135 | |||||||
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes. Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 390.40 E-value: 5.90e-135
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| MannoseP_isomer | pfam01050 | Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ... |
314-464 | 8.52e-102 | |||||||
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483. Pssm-ID: 426015 [Multi-domain] Cd Length: 151 Bit Score: 301.26 E-value: 8.52e-102
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-285 | 2.82e-73 | |||||||
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars. Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 231.37 E-value: 2.82e-73
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| cupin_PMI_typeII_C | cd02213 | Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ... |
335-462 | 1.90e-71 | |||||||
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif. Pssm-ID: 380343 [Multi-domain] Cd Length: 126 Bit Score: 222.43 E-value: 1.90e-71
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| ManC | COG0662 | Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; |
362-463 | 4.57e-38 | |||||||
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440426 [Multi-domain] Cd Length: 114 Bit Score: 134.88 E-value: 4.57e-38
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| NTP_transferase | cd04181 | NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
4-272 | 1.16e-09 | |||||||
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 58.36 E-value: 1.16e-09
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| cupin_MJ1618 | cd02214 | Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ... |
358-457 | 1.33e-09 | |||||||
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. Pssm-ID: 380344 [Multi-domain] Cd Length: 100 Bit Score: 55.22 E-value: 1.33e-09
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| Cupin_2 | pfam07883 | Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
380-448 | 2.97e-09 | |||||||
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 53.42 E-value: 2.97e-09
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| cupin_TM1459-like | cd02222 | Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ... |
375-446 | 4.71e-09 | |||||||
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer. Pssm-ID: 380351 [Multi-domain] Cd Length: 91 Bit Score: 53.22 E-value: 4.71e-09
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| QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
374-450 | 8.84e-09 | |||||||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 52.93 E-value: 8.84e-09
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| COG3837 | COG3837 | Uncharacterized conserved protein, cupin superfamily [Function unknown]; |
373-450 | 9.00e-09 | |||||||
Uncharacterized conserved protein, cupin superfamily [Function unknown]; Pssm-ID: 443048 [Multi-domain] Cd Length: 115 Bit Score: 53.48 E-value: 9.00e-09
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| cupin_TcmJ-like | cd06991 | TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ... |
380-446 | 5.51e-07 | |||||||
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380396 [Multi-domain] Cd Length: 105 Bit Score: 48.06 E-value: 5.51e-07
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| cupin_XRE_C | cd02209 | XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ... |
371-446 | 6.29e-07 | |||||||
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380339 [Multi-domain] Cd Length: 90 Bit Score: 47.12 E-value: 6.29e-07
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| cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
380-448 | 1.29e-06 | |||||||
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation. Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 45.94 E-value: 1.29e-06
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| cupin_DddK | cd06988 | Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
380-448 | 5.44e-06 | |||||||
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380393 [Multi-domain] Cd Length: 76 Bit Score: 44.15 E-value: 5.44e-06
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| CDP-ME_synthetase | cd02516 | CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-68 | 1.13e-05 | |||||||
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 46.36 E-value: 1.13e-05
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| OxdD | COG2140 | Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ... |
372-475 | 1.65e-05 | |||||||
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis Pssm-ID: 441743 [Multi-domain] Cd Length: 115 Bit Score: 43.80 E-value: 1.65e-05
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| NTP_transf_3 | pfam12804 | MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
4-141 | 7.84e-05 | |||||||
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain. Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 42.95 E-value: 7.84e-05
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| IspD | COG1211 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-68 | 1.56e-04 | |||||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440824 Cd Length: 224 Bit Score: 43.19 E-value: 1.56e-04
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| cupin_OxDC | cd02240 | Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ... |
381-468 | 4.95e-04 | |||||||
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380367 [Multi-domain] Cd Length: 145 Bit Score: 40.54 E-value: 4.95e-04
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| cupin_OxDC_C | cd20305 | Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ... |
380-465 | 7.24e-04 | |||||||
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380439 [Multi-domain] Cd Length: 153 Bit Score: 39.88 E-value: 7.24e-04
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| cupin_TM1287-like | cd02221 | Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ... |
380-446 | 9.62e-04 | |||||||
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer. Pssm-ID: 380350 [Multi-domain] Cd Length: 93 Bit Score: 38.22 E-value: 9.62e-04
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| AllE | COG3257 | Ureidoglycine aminohydrolase [Nucleotide transport and metabolism]; |
372-445 | 1.05e-03 | |||||||
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism]; Pssm-ID: 442488 [Multi-domain] Cd Length: 262 Bit Score: 40.96 E-value: 1.05e-03
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| COG1213 | COG1213 | Choline kinase [Lipid transport and metabolism]; |
4-55 | 4.78e-03 | |||||||
Choline kinase [Lipid transport and metabolism]; Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 38.68 E-value: 4.78e-03
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| cupin_Bh2720-like | cd02223 | Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ... |
376-445 | 4.84e-03 | |||||||
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold. Pssm-ID: 380352 [Multi-domain] Cd Length: 98 Bit Score: 36.37 E-value: 4.84e-03
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| cupin_yp_001338853-like | cd07008 | Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ... |
383-448 | 7.39e-03 | |||||||
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. Pssm-ID: 380411 [Multi-domain] Cd Length: 101 Bit Score: 36.08 E-value: 7.39e-03
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| cupin_UGlyAH_N | cd02211 | (S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ... |
372-442 | 9.50e-03 | |||||||
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features. Pssm-ID: 380341 [Multi-domain] Cd Length: 117 Bit Score: 35.96 E-value: 9.50e-03
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