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Conserved domains on  [gi|1330817586|gb|PNE67301|]
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ferritin [Burkholderia cenocepacia]

Protein Classification

ferritin family protein( domain architecture ID 38)

ferritin family protein similar to rubrerythrin, a non-heme di-iron that is involved in oxidative stress defense as a peroxide scavenger in a wide range of organisms

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ferritin_like super family cl00264
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 17-187 6.76e-06

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


The actual alignment was detected with superfamily member cd01050:

Pssm-ID: 469698  Cd Length: 297  Bit Score: 46.49  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  17 RWDMEKDI-PWDKfDASLLTDEQAKTIKMNAITEwSALP-----ATEMFLRDNQHDSDFSAFMSVWFFEEQKHSLVLMEY 90
Cdd:cd01050    39 SEDFDLDVkELRE-RAAELPDDARVALVGNLLTE-EALPtyhsmLNRLFGLDDESPTAWARWVRRWTAEENRHGDLLNKY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  91 L---RRFKPEMVptEEELHA-VRFQFDPA---PPLETLMLHFCGEIRLNHWYRCAAD--WHTEPVIKQIYETISRDEARH 161
Cdd:cd01050   117 LyltGRVDPRAL--ERTRQYlIGSGFDPGtdnSPYRGFVYTSFQELATRISHRNTARlaGAGDPVLAKLLGRIAADEARH 194

                         170       180
                  ....*....|....*....|....*.
gi 1330817586 162 GGAYLRYMKKALNNCGDVARAAFAKI 187
Cdd:cd01050   195 EAFYRDIVEALFELDPDGAVLAFADM 220
 
Name Accession Description Interval E-value
Acyl_ACP_Desat cd01050
Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase ...
 17-187 6.76e-06

Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase (Acyl_ACP_Desat) is a mu-oxo-bridged diiron-carboxylate enzyme, which belongs to a broad superfamily of ferritin-like proteins and catalyzes the NADPH and O2-dependent formation of a cis-double bond in acyl-ACPs. Acyl-ACP desaturases are found in higher plants and a few bacterial species (Mycobacterium tuberculosis, M. leprae, M. avium and Streptomyces avermitilis, S. coelicolor). In plants, Acyl-ACP desaturase is a plastid-localized, covalently ACP linked, soluble desaturase that introduces the first double bound into saturated fatty acids, resulting in the corresponding monounsaturated fatty acid. Members of this class of soluble desaturases are specific for a particular substrate chain length and introduce the double bond between specific carbon atoms. For example, delta 9 stearoyl-ACP is specific for stearic acid and introduces a double bond between carbon 9 and 10 to yield oleic acid in the ACP-bound form. The enzymatic reaction requires molecular oxygen, NAD(P)H, NAD(P)H ferredoxin oxido-reductase and ferredoxin. The enzyme is active in the homodimeric form; the monomer consists mainly of alpha-helices with the catalytic diiron center buried within a four-helix bundle. Integral membrane fatty acid desaturases that introduce double bonds into fatty acid chains, acyl-CoA desaturases of animals, yeasts, and fungi, and acyl-lipid desaturases of cyanobacteria and higher plants, are distinct from soluble acyl-ACP desaturases, lack diiron centers, and are not included in this CD.


Pssm-ID: 153109  Cd Length: 297  Bit Score: 46.49  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  17 RWDMEKDI-PWDKfDASLLTDEQAKTIKMNAITEwSALP-----ATEMFLRDNQHDSDFSAFMSVWFFEEQKHSLVLMEY 90
Cdd:cd01050    39 SEDFDLDVkELRE-RAAELPDDARVALVGNLLTE-EALPtyhsmLNRLFGLDDESPTAWARWVRRWTAEENRHGDLLNKY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  91 L---RRFKPEMVptEEELHA-VRFQFDPA---PPLETLMLHFCGEIRLNHWYRCAAD--WHTEPVIKQIYETISRDEARH 161
Cdd:cd01050   117 LyltGRVDPRAL--ERTRQYlIGSGFDPGtdnSPYRGFVYTSFQELATRISHRNTARlaGAGDPVLAKLLGRIAADEARH 194

                         170       180
                  ....*....|....*....|....*.
gi 1330817586 162 GGAYLRYMKKALNNCGDVARAAFAKI 187
Cdd:cd01050   195 EAFYRDIVEALFELDPDGAVLAFADM 220
 
Name Accession Description Interval E-value
Acyl_ACP_Desat cd01050
Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase ...
 17-187 6.76e-06

Acyl ACP desaturase, ferritin-like diiron-binding domain; Acyl-Acyl Carrier Protein Desaturase (Acyl_ACP_Desat) is a mu-oxo-bridged diiron-carboxylate enzyme, which belongs to a broad superfamily of ferritin-like proteins and catalyzes the NADPH and O2-dependent formation of a cis-double bond in acyl-ACPs. Acyl-ACP desaturases are found in higher plants and a few bacterial species (Mycobacterium tuberculosis, M. leprae, M. avium and Streptomyces avermitilis, S. coelicolor). In plants, Acyl-ACP desaturase is a plastid-localized, covalently ACP linked, soluble desaturase that introduces the first double bound into saturated fatty acids, resulting in the corresponding monounsaturated fatty acid. Members of this class of soluble desaturases are specific for a particular substrate chain length and introduce the double bond between specific carbon atoms. For example, delta 9 stearoyl-ACP is specific for stearic acid and introduces a double bond between carbon 9 and 10 to yield oleic acid in the ACP-bound form. The enzymatic reaction requires molecular oxygen, NAD(P)H, NAD(P)H ferredoxin oxido-reductase and ferredoxin. The enzyme is active in the homodimeric form; the monomer consists mainly of alpha-helices with the catalytic diiron center buried within a four-helix bundle. Integral membrane fatty acid desaturases that introduce double bonds into fatty acid chains, acyl-CoA desaturases of animals, yeasts, and fungi, and acyl-lipid desaturases of cyanobacteria and higher plants, are distinct from soluble acyl-ACP desaturases, lack diiron centers, and are not included in this CD.


Pssm-ID: 153109  Cd Length: 297  Bit Score: 46.49  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  17 RWDMEKDI-PWDKfDASLLTDEQAKTIKMNAITEwSALP-----ATEMFLRDNQHDSDFSAFMSVWFFEEQKHSLVLMEY 90
Cdd:cd01050    39 SEDFDLDVkELRE-RAAELPDDARVALVGNLLTE-EALPtyhsmLNRLFGLDDESPTAWARWVRRWTAEENRHGDLLNKY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  91 L---RRFKPEMVptEEELHA-VRFQFDPA---PPLETLMLHFCGEIRLNHWYRCAAD--WHTEPVIKQIYETISRDEARH 161
Cdd:cd01050   117 LyltGRVDPRAL--ERTRQYlIGSGFDPGtdnSPYRGFVYTSFQELATRISHRNTARlaGAGDPVLAKLLGRIAADEARH 194

                         170       180
                  ....*....|....*....|....*.
gi 1330817586 162 GGAYLRYMKKALNNCGDVARAAFAKI 187
Cdd:cd01050   195 EAFYRDIVEALFELDPDGAVLAFADM 220
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
 65-169 3.90e-03

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 36.71  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330817586  65 HDSDFSAFMSVWFFEEQKHSLVLMEYLRRFKPEMVPTEEELHAVRFQFDPAP-PLETLMLHFCGEIRLNHWYRCAADWHT 143
Cdd:cd00657    25 PDPDLKDELLEIADEERRHADALAERLRELGGTPPLPPAHLLAAYALPKTSDdPAEALRAALEVEARAIAAYRELIEQAD 104

                          90       100
                  ....*....|....*....|....*.
gi 1330817586 144 EPVIKQIYETISRDEARHGGAYLRYM 169
Cdd:cd00657   105 DPELRRLLERILADEQRHAAWFRKLL 130
 
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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