Fatty acid desaturase [Pseudomonas aeruginosa]
Protein Classification
fatty acid desaturase family protein( domain architecture ID 1056)
fatty acid desaturase (FADS) family protein similar to membrane FADSs, which are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains, and to beta-carotene ketolase/oxygenases (CrtW-like) and hydroxylases (CrtR-like)
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Membrane-FADS-like super family | cl00615 | The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ... |
25-311 | 8.13e-106 | |||||
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. The actual alignment was detected with superfamily member cd03509: Pssm-ID: 445012 [Multi-domain] Cd Length: 288 Bit Score: 310.06 E-value: 8.13e-106
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| Name | Accession | Description | Interval | E-value | |||||
| DesA_FADS-like | cd03509 | Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, ... |
25-311 | 8.13e-106 | |||||
Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, DesA-like, yet uncharacterized subgroup of membrane fatty acid desaturase proteins found in alpha-, beta-, and gamma-proteobacteria. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase. Pssm-ID: 239586 [Multi-domain] Cd Length: 288 Bit Score: 310.06 E-value: 8.13e-106
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| DesA | COG3239 | Fatty acid desaturase [Lipid transport and metabolism]; |
10-272 | 3.13e-20 | |||||
Fatty acid desaturase [Lipid transport and metabolism]; Pssm-ID: 442471 [Multi-domain] Cd Length: 319 Bit Score: 89.02 E-value: 3.13e-20
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| FA_desaturase | pfam00487 | Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ... |
60-272 | 3.14e-08 | |||||
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme. Pssm-ID: 425713 [Multi-domain] Cd Length: 252 Bit Score: 53.50 E-value: 3.14e-08
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| Name | Accession | Description | Interval | E-value | |||||
| DesA_FADS-like | cd03509 | Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, ... |
25-311 | 8.13e-106 | |||||
Fatty acid desaturase protein family subgroup, a delta-12 acyl-lipid desaturase-like, DesA-like, yet uncharacterized subgroup of membrane fatty acid desaturase proteins found in alpha-, beta-, and gamma-proteobacteria. Sequences of this domain family appear to be structurally related to membrane fatty acid desaturases and alkane hydroxylases. They all share in common extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXXH, HXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within homologs, stearoyl CoA desaturase and alkane hydroxylase. Pssm-ID: 239586 [Multi-domain] Cd Length: 288 Bit Score: 310.06 E-value: 8.13e-106
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| DesA | COG3239 | Fatty acid desaturase [Lipid transport and metabolism]; |
10-272 | 3.13e-20 | |||||
Fatty acid desaturase [Lipid transport and metabolism]; Pssm-ID: 442471 [Multi-domain] Cd Length: 319 Bit Score: 89.02 E-value: 3.13e-20
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| FA_desaturase | pfam00487 | Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ... |
60-272 | 3.14e-08 | |||||
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a double bond at the delta position of fatty acids. There seem to be two distinct families of fatty acid desaturases which do not seem to be evolutionary related: Family 1 composed of Stearoyl-CoA desaturases (SCD) and Family 2 composed of Bacterial fatty acid desaturases, Plant stearoyl-acyl-carrier-protein desaturase and Cyanobacterial DesA. Members of this entry are ER integral membrane proteins that share the same mushroom-shaped fold consisting of four transmembrane helices (TM1-TM4) which anchor them to the membrane, capped by a cytosolic domain containing a unique 9-10 histidine- coordinating di metal (di-iron) catalytic centre. The structure of mouse stearoyl-CoA desaturase (SDC) revealed that TM2 and TM4 are longer than TM1 and TM3 and protrude into the cytosolic domain, providing three of the nine histidine residues that coordinate the two metal ions, while the other histidine residues are provided by the soluble domain in this enzyme. Pssm-ID: 425713 [Multi-domain] Cd Length: 252 Bit Score: 53.50 E-value: 3.14e-08
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| Membrane-FADS-like | cd01060 | The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ... |
49-128 | 8.19e-06 | |||||
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane hydroxylases, beta carotene ketolases (CrtW-like), hydroxylases (CrtR-like), and other related proteins. They are present in all groups of organisms with the exception of archaea. Membrane FADSs are non-heme, iron-containing, oxygen-dependent enzymes involved in regioselective introduction of double bonds in fatty acyl aliphatic chains. They play an important role in the maintenance of the proper structure and functioning of biological membranes. Alkane hydroxylases are bacterial, integral-membrane di-iron enzymes that share a requirement for iron and oxygen for activity similar to that of membrane FADSs, and are involved in the initial oxidation of inactivated alkanes. Beta-carotene ketolase and beta-carotene hydroxylase are carotenoid biosynthetic enzymes for astaxanthin and zeaxanthin, respectively. This superfamily domain has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of these sequences also reveals three regions of conserved histidine cluster motifs that contain eight histidine residues: HXXX(X)H, HXX(X)HH, and HXXHH (an additional conserved histidine residue is seen between clusters 2 and 3). Spectroscopic and genetic evidence point to a nitrogen-rich coordination environment located in the cytoplasm with as many as eight histidines coordinating the two iron ions and a carboxylate residue bridging the two metals in the Pseudomonas oleovorans alkane hydroxylase (AlkB). In addition, the eight histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the rat stearoyl CoA delta-9 desaturase. Pssm-ID: 238511 [Multi-domain] Cd Length: 122 Bit Score: 44.38 E-value: 8.19e-06
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