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Conserved domains on  [gi|1524359881|gb|AZD26615|]
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magnesium-protoporphyrin IX monomethyl ester oxidative cyclase, partial [Elettaria sp. CSB-2018]

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, ...
 1-83 2.10e-62

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 PLN02508:

Pssm-ID: 469698  Cd Length: 357  Bit Score: 192.28  E-value: 2.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:PLN02508  155 FKPKFIFYATYLSEKIGYWRYITIYRHLQANPDYQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 234


                  ...
gi 1524359881  81 CLS 83
Cdd:PLN02508  235 CLS 237
 
Name Accession Description Interval E-value
PLN02508 PLN02508
magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase
 1-83 2.10e-62

magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase


Pssm-ID: 178124  Cd Length: 357  Bit Score: 192.28  E-value: 2.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:PLN02508  155 FKPKFIFYATYLSEKIGYWRYITIYRHLQANPDYQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 234


                  ...
gi 1524359881  81 CLS 83
Cdd:PLN02508  235 CLS 237
ACSF cd01047
Aerobic Cyclase System Fe-containing subunit (ACSF), ferritin-like diiron-binding domain; ...
 1-83 4.41e-61

Aerobic Cyclase System Fe-containing subunit (ACSF), ferritin-like diiron-binding domain; Aerobic Cyclase System, Fe-containing subunit (ACSF) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Rubrivivax gelatinosus acsF codes for a conserved, putative binuclear iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethyl ester. AcsF and homologs have a leucine zipper and two copies of the conserved glutamate and histidine residues predicted to act as ligands for iron in the Ex(29-35)DExRH motifs. Several homologs of AcsF are found in a wide range of photosynthetic organisms, including Chlamydomonas reinhardtii Crd1 and Pharbitis nil PNZIP, suggesting that this aerobic oxidative cyclization mechanism is conserved from bacteria to plants.


Pssm-ID: 153106  Cd Length: 323  Bit Score: 187.89  E-value: 4.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:cd01047   139 FKPKFIFYATYLSEKIGYWRYITIYRHLERNPENQFHPIFKYFENWCQDENRHGDFFAALLRAQPHLLNDGKNKLWIRFF 218


                  ...
gi 1524359881  81 CLS 83
Cdd:cd01047   219 LLS 221
Ycf59 COG5759
Mg-protoporphyrin IX monomethyl ester cyclase BchE, aerobic (=Ycf59) [Coenzyme transport and ...
 1-83 1.27e-59

Mg-protoporphyrin IX monomethyl ester cyclase BchE, aerobic (=Ycf59) [Coenzyme transport and metabolism];


Pssm-ID: 444469  Cd Length: 352  Bit Score: 185.07  E-value: 1.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:COG5759   157 FKPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRFYPIFKWFENWCQDENRHGDFFAALMRSQPKLLNGWKNRLWIRFF 236


                  ...
gi 1524359881  81 CLS 83
Cdd:COG5759   237 LLA 239
AcsF TIGR02029
magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase; This model respresents ...
 1-83 1.80e-53

magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase; This model respresents the oxidative cyclase responsible for forming the distinctive E-ring of the chlorin ring system under aerobic conditions. This enzyme is believed to utilize a binuclear iron center and molecular oxygen. There are two isoforms of this enzyme in some plants and cyanobacterai which are differentially regulated based on the levels of copper and oxygen. This step is essential in the biosynthesis of both bacteriochlorophyll and chlorophyll under aerobic conditions (a separate enzyme, BchE, acts under anaerobic conditions). This enzyme is found in plants, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131084  Cd Length: 337  Bit Score: 168.82  E-value: 1.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:TIGR02029 149 FRPKFIYYATYLSEKIGYWRYITIYRHLEENPENQFYPIFKYFESWCQDENRHGDAFAALMRSQPQLLNNWKAKLWSRFF 228


                  ...
gi 1524359881  81 CLS 83
Cdd:TIGR02029 229 LLS 231
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 1-61 6.11e-17

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 69.69  E-value: 6.11e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524359881   1 FKPKFIFYATYLSE--KIGYWRYISIYRHLKANPEFQLYP-IFKYFENWCQDENRHGDFFSALL 61
Cdd:pfam02915  74 FPPKFLTTATNLEEaiEGEYAEEEEMYRFYEELAEKEGYPeARKLFEDLAEAEKRHEERFRKLL 137
 
Name Accession Description Interval E-value
PLN02508 PLN02508
magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase
 1-83 2.10e-62

magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase


Pssm-ID: 178124  Cd Length: 357  Bit Score: 192.28  E-value: 2.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:PLN02508  155 FKPKFIFYATYLSEKIGYWRYITIYRHLQANPDYQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 234


                  ...
gi 1524359881  81 CLS 83
Cdd:PLN02508  235 CLS 237
ACSF cd01047
Aerobic Cyclase System Fe-containing subunit (ACSF), ferritin-like diiron-binding domain; ...
 1-83 4.41e-61

Aerobic Cyclase System Fe-containing subunit (ACSF), ferritin-like diiron-binding domain; Aerobic Cyclase System, Fe-containing subunit (ACSF) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Rubrivivax gelatinosus acsF codes for a conserved, putative binuclear iron-cluster-containing protein involved in aerobic oxidative cyclization of Mg-protoporphyrin IX monomethyl ester. AcsF and homologs have a leucine zipper and two copies of the conserved glutamate and histidine residues predicted to act as ligands for iron in the Ex(29-35)DExRH motifs. Several homologs of AcsF are found in a wide range of photosynthetic organisms, including Chlamydomonas reinhardtii Crd1 and Pharbitis nil PNZIP, suggesting that this aerobic oxidative cyclization mechanism is conserved from bacteria to plants.


Pssm-ID: 153106  Cd Length: 323  Bit Score: 187.89  E-value: 4.41e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:cd01047   139 FKPKFIFYATYLSEKIGYWRYITIYRHLERNPENQFHPIFKYFENWCQDENRHGDFFAALLRAQPHLLNDGKNKLWIRFF 218


                  ...
gi 1524359881  81 CLS 83
Cdd:cd01047   219 LLS 221
PRK13654 PRK13654
magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional
 1-83 1.07e-59

magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional


Pssm-ID: 237458  Cd Length: 355  Bit Score: 185.10  E-value: 1.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:PRK13654  159 FPPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRFHPIFKFFENWCQDENRHGDFFALLMRAQPKLLKGWVNRLWIRFF 238


                  ...
gi 1524359881  81 CLS 83
Cdd:PRK13654  239 LLA 241
Ycf59 COG5759
Mg-protoporphyrin IX monomethyl ester cyclase BchE, aerobic (=Ycf59) [Coenzyme transport and ...
 1-83 1.27e-59

Mg-protoporphyrin IX monomethyl ester cyclase BchE, aerobic (=Ycf59) [Coenzyme transport and metabolism];


Pssm-ID: 444469  Cd Length: 352  Bit Score: 185.07  E-value: 1.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:COG5759   157 FKPKFIFYATYLSEKIGYWRYITIYRHLEKHPEHRFYPIFKWFENWCQDENRHGDFFAALMRSQPKLLNGWKNRLWIRFF 236


                  ...
gi 1524359881  81 CLS 83
Cdd:COG5759   237 LLA 239
ycf59 CHL00185
magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional
 1-83 2.59e-55

magnesium-protoporphyrin IX monomethyl ester cyclase; Provisional


Pssm-ID: 177087  Cd Length: 351  Bit Score: 173.76  E-value: 2.59e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:CHL00185  155 FSPKFIFYATYLSEKIGYWRYITIYRHLEKNPEYRIYPIFKFFESWCQDENRHGDFFAALLKSQPHLLNGWKARLWCRFF 234


                  ...
gi 1524359881  81 CLS 83
Cdd:CHL00185  235 LLS 237
AcsF TIGR02029
magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase; This model respresents ...
 1-83 1.80e-53

magnesium-protoporphyrin IX monomethyl ester aerobic oxidative cyclase; This model respresents the oxidative cyclase responsible for forming the distinctive E-ring of the chlorin ring system under aerobic conditions. This enzyme is believed to utilize a binuclear iron center and molecular oxygen. There are two isoforms of this enzyme in some plants and cyanobacterai which are differentially regulated based on the levels of copper and oxygen. This step is essential in the biosynthesis of both bacteriochlorophyll and chlorophyll under aerobic conditions (a separate enzyme, BchE, acts under anaerobic conditions). This enzyme is found in plants, cyanobacteria and other photosynthetic bacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131084  Cd Length: 337  Bit Score: 168.82  E-value: 1.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524359881   1 FKPKFIFYATYLSEKIGYWRYISIYRHLKANPEFQLYPIFKYFENWCQDENRHGDFFSALLKAQPQFLNDWKAKLWSRFF 80
Cdd:TIGR02029 149 FRPKFIYYATYLSEKIGYWRYITIYRHLEENPENQFYPIFKYFESWCQDENRHGDAFAALMRSQPQLLNNWKAKLWSRFF 228


                  ...
gi 1524359881  81 CLS 83
Cdd:TIGR02029 229 LLS 231
Rubrerythrin pfam02915
Rubrerythrin; This domain has a ferritin-like fold.
 1-61 6.11e-17

Rubrerythrin; This domain has a ferritin-like fold.


Pssm-ID: 397180  Cd Length: 137  Bit Score: 69.69  E-value: 6.11e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524359881   1 FKPKFIFYATYLSE--KIGYWRYISIYRHLKANPEFQLYP-IFKYFENWCQDENRHGDFFSALL 61
Cdd:pfam02915  74 FPPKFLTTATNLEEaiEGEYAEEEEMYRFYEELAEKEGYPeARKLFEDLAEAEKRHEERFRKLL 137
 
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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