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Conserved domains on  [gi|495708302|ref|WP_008432881|]
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MULTISPECIES: hypothetical protein [unclassified Pseudomonas]

Protein Classification

phytanoyl-CoA dioxygenase family protein( domain architecture ID 1903680)

phytanoyl-CoA dioxygenase (PhyH) family protein may act as a dioxygenase that catalyzes the oxidation of a substrate without the reduction of one oxygen atom from dioxygen into a water molecule

CATH:  2.60.120.620
EC:  1.14.-.-
Gene Ontology:  GO:0051213|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 229-275 4.26e-04

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd05940:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 449  Bit Score: 41.57  E-value: 4.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495708302 229 FKGRFSVHRVTRVEGATERNTAIFAYSEKPGIIGRAQRTKQLYGRLS 275
Cdd:cd05940  214 FKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLA 260
PhyH super family cl44208
Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary ...
 34-255 8.16e-04

Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG5285:

Pssm-ID: 444095  Cd Length: 237  Bit Score: 40.02  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302  34 ALIEHARAELAEDGCCLLKNFLRPAALEQARleglalsgktfysvRKVNAYFTEddtslpHDDPRRTFMERTSGFVTRDM 113
Cdd:COG5285    1 LLTDEQIAFFERDGYLVLRGVLSPEEVAALR--------------AALDRLLAE------APDEGDLEYSEADGGRLRRI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 114 IAP---DAIIHRLYVSPMMKRFIGACLNePEIFEYADpfaglVINVMP--DGTEQPWHFD------TNEFIVSMM----- 177
Cdd:COG5285   61 YNLhrrDPAFRDLARHPRILAVAEQLLG-PDVRLHHS-----QLFFKPpgGGGATPWHQDfpywplEPPRAVTVWialdd 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 178 -TqkPEAGGLfEYAP-----MIRSRTQENlgavGKVVRGEDRSRVQELELNPGDLQIFKGRfSVHRVTRVEGATERNTAI 251
Cdd:COG5285  135 vT--EENGCL-RVVPgshrwGLLPHRDDD----GSLDDALDEEEAVPVELKAGDVLIFHGL-TLHGSGPNRSDRPRRALV 206


                 ....
gi 495708302 252 FAYS 255
Cdd:COG5285  207 LRYN 210
 
Name Accession Description Interval E-value
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 229-275 4.26e-04

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 41.57  E-value: 4.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495708302 229 FKGRFSVHRVTRVEGATERNTAIFAYSEKPGIIGRAQRTKQLYGRLS 275
Cdd:cd05940  214 FKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLA 260
PhyH COG5285
Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary ...
 34-255 8.16e-04

Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444095  Cd Length: 237  Bit Score: 40.02  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302  34 ALIEHARAELAEDGCCLLKNFLRPAALEQARleglalsgktfysvRKVNAYFTEddtslpHDDPRRTFMERTSGFVTRDM 113
Cdd:COG5285    1 LLTDEQIAFFERDGYLVLRGVLSPEEVAALR--------------AALDRLLAE------APDEGDLEYSEADGGRLRRI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 114 IAP---DAIIHRLYVSPMMKRFIGACLNePEIFEYADpfaglVINVMP--DGTEQPWHFD------TNEFIVSMM----- 177
Cdd:COG5285   61 YNLhrrDPAFRDLARHPRILAVAEQLLG-PDVRLHHS-----QLFFKPpgGGGATPWHQDfpywplEPPRAVTVWialdd 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 178 -TqkPEAGGLfEYAP-----MIRSRTQENlgavGKVVRGEDRSRVQELELNPGDLQIFKGRfSVHRVTRVEGATERNTAI 251
Cdd:COG5285  135 vT--EENGCL-RVVPgshrwGLLPHRDDD----GSLDDALDEEEAVPVELKAGDVLIFHGL-TLHGSGPNRSDRPRRALV 206


                 ....
gi 495708302 252 FAYS 255
Cdd:COG5285  207 LRYN 210
PhyH pfam05721
Phytanoyl-CoA dioxygenase (PhyH); This family is made up of several eukaryotic phytanoyl-CoA ...
 45-232 5.78e-03

Phytanoyl-CoA dioxygenase (PhyH); This family is made up of several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins, ectoine hydroxylases and a number of bacterial deoxygenases. PhyH is a peroxisomal enzyme catalysing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD) which is an inherited neurological syndrome biochemically characterized by the accumulation of phytanic acid in plasma and tissues.


Pssm-ID: 399029  Cd Length: 213  Bit Score: 37.43  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302   45 EDGCCLLKNFLRPAALEQARLEGLALSGKTFYSVRKVNAYFTEddtslphddprrTFMERTSGFVTRDMIAPDAIIHRLY 124
Cdd:pfam05721   3 EDGYLVIEGFLSPEEVAALRAEAERLLDRAAESGPDKDDFFDE------------KAAGDETGLLEKSITKRDHFLHPFY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302  125 VSPMMKRFIGAclNEPEIFEYADPFAGLVINVMPD-GTE-QPWH-------FDTNEFIVSMMTQ----KPEAGGLF---- 187
Cdd:pfam05721  71 LADLARAILGS--PVYVANVLQSMYQDLSIFKQPGtGGEvSPWHqdytflpTRPAELVVNVWIAlddaTEENGCLRvipg 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495708302  188 ----EYAPMIRSRTQENLGAVGKVVRGEDRSRVQELELNPGDLQIFKGR 232
Cdd:pfam05721 149 shkwEVGPLARRLPEDDYYAEDDEAPKRDEEPAVPVPMKAGDAVLFHPR 197
 
Name Accession Description Interval E-value
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 229-275 4.26e-04

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 41.57  E-value: 4.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495708302 229 FKGRFSVHRVTRVEGATERNTAIFAYSEKPGIIGRAQRTKQLYGRLS 275
Cdd:cd05940  214 FKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLA 260
PhyH COG5285
Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary ...
 34-255 8.16e-04

Ectoine hydroxylase-related dioxygenase, phytanoyl-CoA dioxygenase (PhyH) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 444095  Cd Length: 237  Bit Score: 40.02  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302  34 ALIEHARAELAEDGCCLLKNFLRPAALEQARleglalsgktfysvRKVNAYFTEddtslpHDDPRRTFMERTSGFVTRDM 113
Cdd:COG5285    1 LLTDEQIAFFERDGYLVLRGVLSPEEVAALR--------------AALDRLLAE------APDEGDLEYSEADGGRLRRI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 114 IAP---DAIIHRLYVSPMMKRFIGACLNePEIFEYADpfaglVINVMP--DGTEQPWHFD------TNEFIVSMM----- 177
Cdd:COG5285   61 YNLhrrDPAFRDLARHPRILAVAEQLLG-PDVRLHHS-----QLFFKPpgGGGATPWHQDfpywplEPPRAVTVWialdd 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302 178 -TqkPEAGGLfEYAP-----MIRSRTQENlgavGKVVRGEDRSRVQELELNPGDLQIFKGRfSVHRVTRVEGATERNTAI 251
Cdd:COG5285  135 vT--EENGCL-RVVPgshrwGLLPHRDDD----GSLDDALDEEEAVPVELKAGDVLIFHGL-TLHGSGPNRSDRPRRALV 206


                 ....
gi 495708302 252 FAYS 255
Cdd:COG5285  207 LRYN 210
PhyH pfam05721
Phytanoyl-CoA dioxygenase (PhyH); This family is made up of several eukaryotic phytanoyl-CoA ...
 45-232 5.78e-03

Phytanoyl-CoA dioxygenase (PhyH); This family is made up of several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins, ectoine hydroxylases and a number of bacterial deoxygenases. PhyH is a peroxisomal enzyme catalysing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD) which is an inherited neurological syndrome biochemically characterized by the accumulation of phytanic acid in plasma and tissues.


Pssm-ID: 399029  Cd Length: 213  Bit Score: 37.43  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302   45 EDGCCLLKNFLRPAALEQARLEGLALSGKTFYSVRKVNAYFTEddtslphddprrTFMERTSGFVTRDMIAPDAIIHRLY 124
Cdd:pfam05721   3 EDGYLVIEGFLSPEEVAALRAEAERLLDRAAESGPDKDDFFDE------------KAAGDETGLLEKSITKRDHFLHPFY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495708302  125 VSPMMKRFIGAclNEPEIFEYADPFAGLVINVMPD-GTE-QPWH-------FDTNEFIVSMMTQ----KPEAGGLF---- 187
Cdd:pfam05721  71 LADLARAILGS--PVYVANVLQSMYQDLSIFKQPGtGGEvSPWHqdytflpTRPAELVVNVWIAlddaTEENGCLRvipg 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495708302  188 ----EYAPMIRSRTQENLGAVGKVVRGEDRSRVQELELNPGDLQIFKGR 232
Cdd:pfam05721 149 shkwEVGPLARRLPEDDYYAEDDEAPKRDEEPAVPVPMKAGDAVLFHPR 197
 
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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