NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446211236|ref|WP_000289091|]
View 

MULTISPECIES: bacterioferritin-associated ferredoxin [Acinetobacter]

Protein Classification

bacterioferritin-associated ferredoxin( domain architecture ID 14448173)

bacterioferritin-associated ferredoxin is a (2Fe-2S)-binding protein that may participate either in the release/delivery of iron from/to bacterioferritin (or other iron complexes), or in the iron-dependent regulation of bacterioferritin expression

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Fer2_BFD cd19945
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ...
 1-54 1.50e-21

bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


:

Pssm-ID: 381078 [Multi-domain]  Cd Length: 54  Bit Score: 78.01  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 446211236  1 MYVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:cd19945   1 MYVCLCNGITDKQIRQAVAQGATSLRELREQLGVGSQCGKCARMARQVLEEELA 54
 
Name Accession Description Interval E-value
Fer2_BFD cd19945
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ...
 1-54 1.50e-21

bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381078 [Multi-domain]  Cd Length: 54  Bit Score: 78.01  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 446211236  1 MYVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:cd19945   1 MYVCLCNGITDKQIRQAVAQGATSLRELREQLGVGSQCGKCARMARQVLEEELA 54
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
1-54 4.74e-17

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 66.76  E-value: 4.74e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 446211236  1 MYVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:COG2906   1 MYVCLCNGVTDRQIRAAIAEGATSLEELRAALGAGTQCGSCVPEARELLAEALA 54
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
 2-51 2.12e-12

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 54.84  E-value: 2.12e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446211236   2 YVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISE 51
Cdd:pfam04324  1 IVCRCFGVTDGEIRDAIREGLTTVEEVKRRTKAGTGCGSCRPAIEEILAE 50
PRK10509 PRK10509
bacterioferritin-associated ferredoxin; Provisional
 1-56 6.72e-11

bacterioferritin-associated ferredoxin; Provisional


Pssm-ID: 182506 [Multi-domain]  Cd Length: 64  Bit Score: 51.66  E-value: 6.72e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 446211236  1 MYVCLCRGITDQDIKDAI-ENGAESYREIRDLLDLGTCCGRCAPEARAIISEELAEI 56
Cdd:PRK10509  1 MYVCLCNGVSDKKIRQAVrQFHPQSFQQLRKFVPVGNQCGKCIRAAREVMQDELMQM 57
 
Name Accession Description Interval E-value
Fer2_BFD cd19945
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ...
 1-54 1.50e-21

bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381078 [Multi-domain]  Cd Length: 54  Bit Score: 78.01  E-value: 1.50e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 446211236  1 MYVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:cd19945   1 MYVCLCNGITDKQIRQAVAQGATSLRELREQLGVGSQCGKCARMARQVLEEELA 54
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
1-54 4.74e-17

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 66.76  E-value: 4.74e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 446211236  1 MYVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:COG2906   1 MYVCLCNGVTDRQIRAAIAEGATSLEELRAALGAGTQCGSCVPEARELLAEALA 54
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
 2-51 2.12e-12

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 54.84  E-value: 2.12e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446211236   2 YVCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISE 51
Cdd:pfam04324  1 IVCRCFGVTDGEIRDAIREGLTTVEEVKRRTKAGTGCGSCRPAIEEILAE 50
PRK10509 PRK10509
bacterioferritin-associated ferredoxin; Provisional
 1-56 6.72e-11

bacterioferritin-associated ferredoxin; Provisional


Pssm-ID: 182506 [Multi-domain]  Cd Length: 64  Bit Score: 51.66  E-value: 6.72e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 446211236  1 MYVCLCRGITDQDIKDAI-ENGAESYREIRDLLDLGTCCGRCAPEARAIISEELAEI 56
Cdd:PRK10509  1 MYVCLCNGVSDKKIRQAVrQFHPQSFQQLRKFVPVGNQCGKCIRAAREVMQDELMQM 57
NasA-like_Fer2_BFD-like cd19948
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ...
 3-51 2.28e-04

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381081 [Multi-domain]  Cd Length: 53  Bit Score: 34.81  E-value: 2.28e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 446211236  3 VCLCRGITDQDIKDAI-ENGAESYREIRDLLDLGTCCGRCAPEARAIISE 51
Cdd:cd19948   4 VCACFSVGENTIRRAIaDNGLTSVAQVGTCLKAGTNCGSCVPEIQKLLSE 53
Fer2_BFD-like cd19942
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ...
 1-45 3.00e-04

[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.


Pssm-ID: 381075 [Multi-domain]  Cd Length: 49  Bit Score: 34.34  E-value: 3.00e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 446211236  1 MYVCLCRGITDQDIKDAIENGaESYREIRDLLDL--GTCCGRCAPEA 45
Cdd:cd19942   1 ALVCECFAVTEKELREAIRKG-GLKTVEELLTGTgaGGGCGVCHPHV 46
HyaA_family_Fer2_BFD-like cd19951
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized ...
 3-49 4.88e-04

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized proteins having a C-terminal Ni,Fe-hydrogenase I small subunit (HyaA) family domain; The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381084 [Multi-domain]  Cd Length: 54  Bit Score: 34.01  E-value: 4.88e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 446211236  3 VCLCRGITDQDIKDAI-ENGAESYREIRDLLDLGTCCGRCAPEARAII 49
Cdd:cd19951   4 VCSCEHVYYQDLIDIIvSCAITSFAELKEFSEAGRVCGRCKKDVDDII 51
GlpA-like_Fer2_BFD-like cd19946
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ...
 3-51 8.38e-04

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381079 [Multi-domain]  Cd Length: 55  Bit Score: 33.28  E-value: 8.38e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 446211236  3 VCLCRGITDQDIKDAIENGAesyreIRDLLDL--------GTCCGR-CAPEARAIISE 51
Cdd:cd19946   3 VCRCEEVTEGEIRDAIRRGA-----ARDLDGLkrrtragmGRCQGRfCAPRVAELLAR 55
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 3-54 1.54e-03

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 34.32  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446211236   3 VCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAIISEELA 54
Cdd:PRK14989 424 ICSCFDVTKGDLIAAINKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELA 475
Fer2_BFD-like cd19950
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ...
 3-49 3.83e-03

[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; uncharacterized subgroup; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1.


Pssm-ID: 381083  Cd Length: 51  Bit Score: 31.70  E-value: 3.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 446211236  3 VCLCRGITDQDIKDAIENGAESYREIRDLLDLGTCCGRCAPEARAII 49
Cdd:cd19950   4 VCTCNDLYIDDIEEAIAEGETEYEEIFAYNDTQPRCGECIDHVQEIV 50
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH