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Conserved domains on  [gi|1134132574|ref|WP_076375569|]
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siderophore-interacting protein [Filimonas lacunae]

Protein Classification

ferredoxin reductase domain-containing protein( domain architecture ID 835)

ferredoxin reductase (FNR) domain-containing protein may bind FAD and/or NAD(P)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ViuB super family cl34463
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 65-229 6.27e-08

NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG2375:

Pssm-ID: 441942 [Multi-domain]  Cd Length: 260  Bit Score: 51.80  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  65 RDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTIeylGISG-TSHKPLPEN--QWVFIGDNSSIGHFLA-LQQ 139
Cdd:COG2375    84 RTYTVRRFDPEAGELDIdFVLHGDGGPASRWAARARPGDRV---GILGpGGSFVPPPDadWYLLAGDETALPAIARiLEA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574 140 LA--TPG---IEISGaialpPQHHRQFAEYLSLPVTIVNASEKGGSTTLTHWLQQQR--YSNAAIYIAGHIPTSVTLRSQ 212
Cdd:COG2375   161 LPadARGtavIEVPD-----AADEQPLPAPAGVEVTWLHRGGAPPGSALLDAVRALElpDGDVYAWVAGEASAVRALRRH 235

                         170
                  ....*....|....*...
gi 1134132574 213 AKQNRNIE-GRVKVQGFW 229
Cdd:COG2375   236 LRDERGLPrDRVRASGYW 253
 
Name Accession Description Interval E-value
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 65-229 6.27e-08

NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];


Pssm-ID: 441942 [Multi-domain]  Cd Length: 260  Bit Score: 51.80  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  65 RDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTIeylGISG-TSHKPLPEN--QWVFIGDNSSIGHFLA-LQQ 139
Cdd:COG2375    84 RTYTVRRFDPEAGELDIdFVLHGDGGPASRWAARARPGDRV---GILGpGGSFVPPPDadWYLLAGDETALPAIARiLEA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574 140 LA--TPG---IEISGaialpPQHHRQFAEYLSLPVTIVNASEKGGSTTLTHWLQQQR--YSNAAIYIAGHIPTSVTLRSQ 212
Cdd:COG2375   161 LPadARGtavIEVPD-----AADEQPLPAPAGVEVTWLHRGGAPPGSALLDAVRALElpDGDVYAWVAGEASAVRALRRH 235

                         170
                  ....*....|....*...
gi 1134132574 213 AKQNRNIE-GRVKVQGFW 229
Cdd:COG2375   236 LRDERGLPrDRVRASGYW 253
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 65-229 3.95e-07

Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 49.18  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  65 RDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTIEYLGISGTSHKPLPENQWVFIGDNSSIGHFLA-LQQLAt 142
Cdd:cd06193    65 RTYTVRRFDPEAGELDIdFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPDADWYLLAGDETALPAIAAiLEELP- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574 143 PGIEISGAIALPPQHHRQfaeYLSLP----VT-IVNASEKGGSTTLTHWLQQQR-YSNAAIYIAGHIPTSVTLRSQAKQN 216
Cdd:cd06193   144 ADARGTALIEVPDAADEQ---PLPAPagveVTwLHRGGAEAGELALLAVRALAPpAGDGYVWIAGEAGAVRALRRHLREE 220

                         170
                  ....*....|....
gi 1134132574 217 RNIE-GRVKVQGFW 229
Cdd:cd06193   221 RGVPrAQVYASGYW 234
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
29-111 4.00e-03

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 36.11  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  29 EPATFVEIDVHLPETDmRQWNASVQHmkckvaPATyRDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTieyL 107
Cdd:pfam08021  41 PGQTPPAVPPTLGEDG-PIWPPEDQR------PVM-RTYTVRAYDPEAGELDIdFVLHGDEGPAARWAAQAQPGDV---L 109


                  ....
gi 1134132574 108 GISG 111
Cdd:pfam08021 110 GIVG 113
 
Name Accession Description Interval E-value
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 65-229 6.27e-08

NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];


Pssm-ID: 441942 [Multi-domain]  Cd Length: 260  Bit Score: 51.80  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  65 RDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTIeylGISG-TSHKPLPEN--QWVFIGDNSSIGHFLA-LQQ 139
Cdd:COG2375    84 RTYTVRRFDPEAGELDIdFVLHGDGGPASRWAARARPGDRV---GILGpGGSFVPPPDadWYLLAGDETALPAIARiLEA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574 140 LA--TPG---IEISGaialpPQHHRQFAEYLSLPVTIVNASEKGGSTTLTHWLQQQR--YSNAAIYIAGHIPTSVTLRSQ 212
Cdd:COG2375   161 LPadARGtavIEVPD-----AADEQPLPAPAGVEVTWLHRGGAPPGSALLDAVRALElpDGDVYAWVAGEASAVRALRRH 235

                         170
                  ....*....|....*...
gi 1134132574 213 AKQNRNIE-GRVKVQGFW 229
Cdd:COG2375   236 LRDERGLPrDRVRASGYW 253
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 65-229 3.95e-07

Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 49.18  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  65 RDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTIEYLGISGTSHKPLPENQWVFIGDNSSIGHFLA-LQQLAt 142
Cdd:cd06193    65 RTYTVRRFDPEAGELDIdFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPDADWYLLAGDETALPAIAAiLEELP- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574 143 PGIEISGAIALPPQHHRQfaeYLSLP----VT-IVNASEKGGSTTLTHWLQQQR-YSNAAIYIAGHIPTSVTLRSQAKQN 216
Cdd:cd06193   144 ADARGTALIEVPDAADEQ---PLPAPagveVTwLHRGGAEAGELALLAVRALAPpAGDGYVWIAGEAGAVRALRRHLREE 220

                         170
                  ....*....|....
gi 1134132574 217 RNIE-GRVKVQGFW 229
Cdd:cd06193   221 RGVPrAQVYASGYW 234
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 21-141 2.88e-04

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 40.89  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  21 TVLDVRFWEPATFVE---IDVHLPETDMRQWnasvqhmkckvapatyRDYTPACWDAGTHTCTLFINTSHQGAGSKWAGS 97
Cdd:cd00322    11 RLFRLQLPNGFSFKPgqyVDLHLPGDGRGLR----------------RAYSIASSPDEEGELELTVKIVPGGPFSAWLHD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1134132574  98 LQKGDTIEYLGISGTSHKPLPENQW-VFIGDNSSIGHFLA-LQQLA 141
Cdd:cd00322    75 LKPGDEVEVSGPGGDFFLPLEESGPvVLIAGGIGITPFRSmLRHLA 120
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
29-111 4.00e-03

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 36.11  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134132574  29 EPATFVEIDVHLPETDmRQWNASVQHmkckvaPATyRDYTPACWDAGTHTCTL-FINTSHQGAGSKWAGSLQKGDTieyL 107
Cdd:pfam08021  41 PGQTPPAVPPTLGEDG-PIWPPEDQR------PVM-RTYTVRAYDPEAGELDIdFVLHGDEGPAARWAAQAQPGDV---L 109


                  ....
gi 1134132574 108 GISG 111
Cdd:pfam08021 110 GIVG 113
 
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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