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Conserved domains on  [gi|489193138|ref|WP_003102475|]
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MULTISPECIES: alkane 1-monooxygenase AlkB1 [Pseudomonas]

Protein Classification

alkane 1-monooxygenase( domain architecture ID 10131413)

alkane 1-monooxygenase catalyzes the hydroxylation of n-alkanes and fatty acids in the presence of a NADH-rubredoxin reductase and rubredoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alkane-hydroxylase cd03512
Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement ...
 44-360 1.23e-133

Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points 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. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins.


:

Pssm-ID: 239589  Cd Length: 314  Bit Score: 384.70  E-value: 1.23e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  44 WAFSLVIAVFGIGPLLDMLFGRDPANPDEETQTPQLlgqGYYVLLTLATVPVLIGTLVWAAGVFVAfQEWGWLGRLGWIL 123
Cdd:cd03512    2 WAWLGLLFITVLIPLLDALLGLDLSNPPEEPPLEKD---RYYRWLLYLLLPLQFALLFLGVWAVST-GDLSALEKVGLIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 124 SMGTVMGAVGIVVAHELIHKDSALEQAAGGILLAAVCYAGFKVEHVRGHHVHVSTPEDASSARFGQSVYQFLPHAYKYNF 203
Cdd:cd03512   78 SLGLLSGVIGINTAHELIHRRSRLERWLGKLLLASLLYGHFAIEHVRGHHRYVATPEDPATARRGESFYRFLPRALVGSF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 204 LNAWRLEAVRLRKKGLPVFGWQNELIWWYLLSLALLVGFGWAFGWLGMVFFLGQAFVAVTLLEIINYVEHYGLHRRKGED 283
Cdd:cd03512  158 RSAWKLEKKRLRRKGRSPWSPRNEVLRYLALAVALLALAAALGGLAGLLFLLIQAFYAKSLLELVNYIEHYGLLRKKLAN 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193138 284 GRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAKRPYQVLRHYDDSPQMPSGYAGMVVLALIPPLWRAVMDPKV 360
Cdd:cd03512  238 GRYEPVGPRHSWNSNHIVSNLLLFNLQRHSDHHAHPTRPYQALRPFPEAPQLPSGYPVMALLALIPPLWRRVMDPRV 314
 
Name Accession Description Interval E-value
Alkane-hydroxylase cd03512
Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement ...
 44-360 1.23e-133

Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points 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. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins.


Pssm-ID: 239589  Cd Length: 314  Bit Score: 384.70  E-value: 1.23e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  44 WAFSLVIAVFGIGPLLDMLFGRDPANPDEETQTPQLlgqGYYVLLTLATVPVLIGTLVWAAGVFVAfQEWGWLGRLGWIL 123
Cdd:cd03512    2 WAWLGLLFITVLIPLLDALLGLDLSNPPEEPPLEKD---RYYRWLLYLLLPLQFALLFLGVWAVST-GDLSALEKVGLIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 124 SMGTVMGAVGIVVAHELIHKDSALEQAAGGILLAAVCYAGFKVEHVRGHHVHVSTPEDASSARFGQSVYQFLPHAYKYNF 203
Cdd:cd03512   78 SLGLLSGVIGINTAHELIHRRSRLERWLGKLLLASLLYGHFAIEHVRGHHRYVATPEDPATARRGESFYRFLPRALVGSF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 204 LNAWRLEAVRLRKKGLPVFGWQNELIWWYLLSLALLVGFGWAFGWLGMVFFLGQAFVAVTLLEIINYVEHYGLHRRKGED 283
Cdd:cd03512  158 RSAWKLEKKRLRRKGRSPWSPRNEVLRYLALAVALLALAAALGGLAGLLFLLIQAFYAKSLLELVNYIEHYGLLRKKLAN 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193138 284 GRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAKRPYQVLRHYDDSPQMPSGYAGMVVLALIPPLWRAVMDPKV 360
Cdd:cd03512  238 GRYEPVGPRHSWNSNHIVSNLLLFNLQRHSDHHAHPTRPYQALRPFPEAPQLPSGYPVMALLALIPPLWRRVMDPRV 314
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 114-346 1.14e-18

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: 84.71  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  114 GWLGRLGWILsMGTVMGAVGIVVAHELIHK------------DSALEQAAGgiLLAAVCYAGFKVEHvRGHHVHVSTPED 181
Cdd:pfam00487   1 SWLALLLALL-LGLFLLGITGSLAHEASHGalfkkrrlnrwlNDLLGRLAG--LPLGISYSAWRIAH-LVHHRYTNGPDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  182 ----ASSARFGQSVYQFLPHAYKYNFLNAWRLEAV------RLRKKGLPVFGWQNELIWWYLLS-----LALLVGFGWAF 246
Cdd:pfam00487  77 dpdtAPLASRFRGLLRYLLRWLLGLLVLAWLLALVlplwlrRLARRKRPIKSRRRRWRLIAWLLllaawLGLWLGFLGLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  247 GWLGMVFFLGQAFVAVTLLEIINYVEHYGLhrrkgeDGRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAKRPYQVL 326
Cdd:pfam00487 157 GLLLLLWLLPLLVFGFLLALIFNYLEHYGG------DWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRL 230

                         250       260
                  ....*....|....*....|..
gi 489193138  327 R--HYDDSPQMPSGYAGMVVLA 346
Cdd:pfam00487 231 PklHRRLREALPEHGLPYRSLG 252
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
89-323 5.09e-10

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 60.13  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  89 TLATVPVLIGTLVWAAGVFVAFQeWGWLGRLGWILsMGTVMGAVGIVvAHELIH----KDSALEQAAGGI--LLAAVCYA 162
Cdd:COG3239   30 DWRYLLKLALTLALLAALWLLLS-WSWLALLAALL-LGLALAGLFSL-GHDAGHgslfRSRWLNDLLGRLlgLPLGTPYD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 163 GFKVEHVRgHHVHVSTPE---DASSARFGQSVYQFLPHAYKYNFLN----AWRLEAVRLRKKGLPVFGWQNELIWWYLLS 235
Cdd:COG3239  107 AWRRSHNR-HHAYTNDPGkdpDIGYGVQAWRPLYLFQHLLRFFLLGlgglYWLLALDFLPLRGRLELKERRLEALLLLLF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 236 LALLVGFGWAFGWLG-MVFFLGQAFVAVTLLEIINYVEHYGLHRRKGEDGRyeRTNHTHSWNSNFVFtNLVLFHLQRHSD 314
Cdd:COG3239  186 LAALLALLLALGWWAvLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD--QLLGSRNIRGGRLL-RWLFGNLNYHIE 262


                 ....*....
gi 489193138 315 HHAFAKRPY 323
Cdd:COG3239  263 HHLFPSIPW 271
 
Name Accession Description Interval E-value
Alkane-hydroxylase cd03512
Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement ...
 44-360 1.23e-133

Alkane hydroxylase is a bacterial, integral-membrane di-iron enzyme that shares a requirement for iron and oxygen for activity similar to that of the non-heme integral-membrane acyl coenzyme A (CoA) desaturases and acyl lipid desaturases. The alk genes in Pseudomonas oleovorans encode conversion of alkanes to acyl CoA. The alkane omega-hydroxylase (AlkB) system is responsible for the initial oxidation of inactivated alkanes. It is a three-component system comprising a soluble NADH-rubredoxin reductase (AlkT), a soluble rubredoxin (AlkG), and the integral membrane oxygenase (AlkB). AlkB utilizes the oxygen rebound mechanism to hydroxylate alkanes. This mechanism involves homolytic cleavage of the C-H bond by an electrophilic metal-oxo intermediate to generate a substrate-based radical. As with other members of this superfamily, this domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. The active site structure of AlkB is not known, however, spectroscopic and genetic evidence points 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. Like all other members of this superfamily, there are eight conserved histidines seen in the histidine cluster motifs: HXXXH, HXXXHH, and HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase. Also included in this CD are terminal alkane hydroxylases (AlkM), xylene monooxygenase hydroxylases (XylM), p-cymene monooxygenase hydroxylases (CymAa), and other related proteins.


Pssm-ID: 239589  Cd Length: 314  Bit Score: 384.70  E-value: 1.23e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  44 WAFSLVIAVFGIGPLLDMLFGRDPANPDEETQTPQLlgqGYYVLLTLATVPVLIGTLVWAAGVFVAfQEWGWLGRLGWIL 123
Cdd:cd03512    2 WAWLGLLFITVLIPLLDALLGLDLSNPPEEPPLEKD---RYYRWLLYLLLPLQFALLFLGVWAVST-GDLSALEKVGLIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 124 SMGTVMGAVGIVVAHELIHKDSALEQAAGGILLAAVCYAGFKVEHVRGHHVHVSTPEDASSARFGQSVYQFLPHAYKYNF 203
Cdd:cd03512   78 SLGLLSGVIGINTAHELIHRRSRLERWLGKLLLASLLYGHFAIEHVRGHHRYVATPEDPATARRGESFYRFLPRALVGSF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 204 LNAWRLEAVRLRKKGLPVFGWQNELIWWYLLSLALLVGFGWAFGWLGMVFFLGQAFVAVTLLEIINYVEHYGLHRRKGED 283
Cdd:cd03512  158 RSAWKLEKKRLRRKGRSPWSPRNEVLRYLALAVALLALAAALGGLAGLLFLLIQAFYAKSLLELVNYIEHYGLLRKKLAN 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489193138 284 GRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAKRPYQVLRHYDDSPQMPSGYAGMVVLALIPPLWRAVMDPKV 360
Cdd:cd03512  238 GRYEPVGPRHSWNSNHIVSNLLLFNLQRHSDHHAHPTRPYQALRPFPEAPQLPSGYPVMALLALIPPLWRRVMDPRV 314
FA_desaturase pfam00487
Fatty acid desaturase; Fatty acid desaturases are enzymes that catalyze the insertion of a ...
 114-346 1.14e-18

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: 84.71  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  114 GWLGRLGWILsMGTVMGAVGIVVAHELIHK------------DSALEQAAGgiLLAAVCYAGFKVEHvRGHHVHVSTPED 181
Cdd:pfam00487   1 SWLALLLALL-LGLFLLGITGSLAHEASHGalfkkrrlnrwlNDLLGRLAG--LPLGISYSAWRIAH-LVHHRYTNGPDK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  182 ----ASSARFGQSVYQFLPHAYKYNFLNAWRLEAV------RLRKKGLPVFGWQNELIWWYLLS-----LALLVGFGWAF 246
Cdd:pfam00487  77 dpdtAPLASRFRGLLRYLLRWLLGLLVLAWLLALVlplwlrRLARRKRPIKSRRRRWRLIAWLLllaawLGLWLGFLGLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  247 GWLGMVFFLGQAFVAVTLLEIINYVEHYGLhrrkgeDGRYERTNHTHSWNSNFVFTNLVLFHLQRHSDHHAFAKRPYQVL 326
Cdd:pfam00487 157 GLLLLLWLLPLLVFGFLLALIFNYLEHYGG------DWGERPVETTRSIRSPNWWLNLLTGNLNYHIEHHLFPGVPWYRL 230

                         250       260
                  ....*....|....*....|..
gi 489193138  327 R--HYDDSPQMPSGYAGMVVLA 346
Cdd:pfam00487 231 PklHRRLREALPEHGLPYRSLG 252
DesA COG3239
Fatty acid desaturase [Lipid transport and metabolism];
89-323 5.09e-10

Fatty acid desaturase [Lipid transport and metabolism];


Pssm-ID: 442471 [Multi-domain]  Cd Length: 319  Bit Score: 60.13  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138  89 TLATVPVLIGTLVWAAGVFVAFQeWGWLGRLGWILsMGTVMGAVGIVvAHELIH----KDSALEQAAGGI--LLAAVCYA 162
Cdd:COG3239   30 DWRYLLKLALTLALLAALWLLLS-WSWLALLAALL-LGLALAGLFSL-GHDAGHgslfRSRWLNDLLGRLlgLPLGTPYD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 163 GFKVEHVRgHHVHVSTPE---DASSARFGQSVYQFLPHAYKYNFLN----AWRLEAVRLRKKGLPVFGWQNELIWWYLLS 235
Cdd:COG3239  107 AWRRSHNR-HHAYTNDPGkdpDIGYGVQAWRPLYLFQHLLRFFLLGlgglYWLLALDFLPLRGRLELKERRLEALLLLLF 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 236 LALLVGFGWAFGWLG-MVFFLGQAFVAVTLLEIINYVEHYGLHRRKGEDGRyeRTNHTHSWNSNFVFtNLVLFHLQRHSD 314
Cdd:COG3239  186 LAALLALLLALGWWAvLLFWLLPLLVAGLLLGLRFYLEHRGEDTGDGEYRD--QLLGSRNIRGGRLL-RWLFGNLNYHIE 262


                 ....*....
gi 489193138 315 HHAFAKRPY 323
Cdd:COG3239  263 HHLFPSIPW 271
Membrane-FADS-like cd01060
The membrane fatty acid desaturase (Membrane_FADS)-like CD includes membrane FADSs, alkane ...
 119-318 2.48e-03

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: 37.45  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 119 LGWILSMGTVMGAVGIVVAHELIH----KDSALEQAAGGILLAA--VCYAGFKVEHVRgHHVHVSTPE-DASSArfgqsv 191
Cdd:cd01060    1 LLLALLLGLLGGLGLTVLAHELGHrsffRSRWLNRLLGALLGLAlgGSYGWWRRSHRR-HHRYTNTPGkDPDSA------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489193138 192 yqflphaykynflnawrleavrlrkkglpvfgwqneliwwyllslallvgfgwafgwlgmvfflgqafvavtlleiINYV 271
Cdd:cd01060   74 ----------------------------------------------------------------------------VNYL 77

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489193138 272 EHYGLHRRKGEDGRYERtnhTHSWNSNFVFTNLVLFHLQRHSDHHAF 318
Cdd:cd01060   78 EHYGGDRPFDTDGEWLR---TTDNSRNGWLNLLLTGGLGYHNEHHLF 121
DUF2530 pfam10745
Protein of unknown function (DUF2530); This family of proteins with unknown function appears ...
 88-136 9.07e-03

Protein of unknown function (DUF2530); This family of proteins with unknown function appears to be restricted to mycobacteria.


Pssm-ID: 431470  Cd Length: 73  Bit Score: 34.59  E-value: 9.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489193138   88 LTLATVPVLIGTLVWAAGVFVAFQEWGWLGRLGWILSMGTVMGAVGIVV 136
Cdd:pfam10745   9 LTDPWPVIIVGTLLWLVATVVVLVVGPALDSWLPTCLAGLGVGVLGTGI 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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