NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1175241556|ref|WP_081789351|]
View 

MULTISPECIES: siderophore-interacting protein [Kutzneria]

Protein Classification

siderophore-interacting protein( domain architecture ID 11457194)

siderophore-interacting protein plays a role in iron homeostasis

CATH:  3.40.50.80|2.40.30.10
EC:  1.16.1.-
Gene Ontology:  GO:0071949|GO:0071949|GO:0015891
PubMed:  39155116

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 2-199 2.13e-28

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: 107.66  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556   2 PSAPALLARRRARPVTVDSVEELSPGLRLVTFTGEPLSGTPWT-PGCAVGIRV----------------------GRRVT 58
Cdd:COG2375     4 TTPARVRRPLRLRELTVVRVERLSPHMRRVTLGGEDLAGFASPgPDDHVKLFFpppgggepvlptlddglalpgeERPVM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  59 RHYTVAEVAGGGSRLGIVFQLHRGDGPGTRWARSLAAGDRVALLGPRRLSRCRRGLA-YFLVGDASAVGLFQSLAESVPA 137
Cdd:COG2375    84 RTYTVRRFDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPPDADwYLLAGDETALPAIARILEALPA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175241556 138 SAEVCGVIEVPAEDlDGASLLVPG---VTVVASAGRP-GEALLARLREERVPVGAV-AHLAGHVRTV 199
Cdd:COG2375   164 DARGTAVIEVPDAA-DEQPLPAPAgveVTWLHRGGAPpGSALLDAVRALELPDGDVyAWVAGEASAV 229
 
Name Accession Description Interval E-value
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 2-199 2.13e-28

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: 107.66  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556   2 PSAPALLARRRARPVTVDSVEELSPGLRLVTFTGEPLSGTPWT-PGCAVGIRV----------------------GRRVT 58
Cdd:COG2375     4 TTPARVRRPLRLRELTVVRVERLSPHMRRVTLGGEDLAGFASPgPDDHVKLFFpppgggepvlptlddglalpgeERPVM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  59 RHYTVAEVAGGGSRLGIVFQLHRGDGPGTRWARSLAAGDRVALLGPRRLSRCRRGLA-YFLVGDASAVGLFQSLAESVPA 137
Cdd:COG2375    84 RTYTVRRFDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPPDADwYLLAGDETALPAIARILEALPA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175241556 138 SAEVCGVIEVPAEDlDGASLLVPG---VTVVASAGRP-GEALLARLREERVPVGAV-AHLAGHVRTV 199
Cdd:COG2375   164 DARGTAVIEVPDAA-DEQPLPAPAgveVTWLHRGGAPpGSALLDAVRALELPDGDVyAWVAGEASAV 229
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 18-189 5.25e-20

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: 85.01  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  18 VDSVEELSPGLRLVTFTGEPLSGTP-WTPGCAVGIRV----------------------GRRVTRHYTVAEVAGGGSRLG 74
Cdd:cd06193     1 VVRVERLTPHMRRITLGGPDLAGFPsDGPDQHVKLLFpdpgqappvlpvlgrrrwppeePRPVMRTYTVRRFDPEAGELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  75 IVFQLHRGDGPGTRWARSLAAGDRVALLGPRRLSRCRRGLA-YFLVGDASAVGLFQSLAESVPASAEVCGVIEVPAEDlD 153
Cdd:cd06193    81 IDFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPDADwYLLAGDETALPAIAAILEELPADARGTALIEVPDAA-D 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1175241556 154 GASLLVP-GVTV---VASAGRPGEALLARLREERVPVGAV 189
Cdd:cd06193   160 EQPLPAPaGVEVtwlHRGGAEAGELALLAVRALAPPAGDG 199
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
17-105 2.84e-10

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 56.14  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  17 TVDSVEELSPGLRLVTFTGEPLSGTPWT------------PGCAVGI--------------RVGRRVTRHYTVAEVAGGG 70
Cdd:pfam08021   1 QVVRVTRLSPHMRRITFTGPGLAGFPSDgtdqhiklffppPGQTPPAvpptlgedgpiwppEDQRPVMRTYTVRAYDPEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1175241556  71 SRLGIVFQLHRGDGPGTRWARSLAAGDRVALLGPR 105
Cdd:pfam08021  81 GELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPG 115
 
Name Accession Description Interval E-value
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 2-199 2.13e-28

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: 107.66  E-value: 2.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556   2 PSAPALLARRRARPVTVDSVEELSPGLRLVTFTGEPLSGTPWT-PGCAVGIRV----------------------GRRVT 58
Cdd:COG2375     4 TTPARVRRPLRLRELTVVRVERLSPHMRRVTLGGEDLAGFASPgPDDHVKLFFpppgggepvlptlddglalpgeERPVM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  59 RHYTVAEVAGGGSRLGIVFQLHRGDGPGTRWARSLAAGDRVALLGPRRLSRCRRGLA-YFLVGDASAVGLFQSLAESVPA 137
Cdd:COG2375    84 RTYTVRRFDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPPDADwYLLAGDETALPAIARILEALPA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175241556 138 SAEVCGVIEVPAEDlDGASLLVPG---VTVVASAGRP-GEALLARLREERVPVGAV-AHLAGHVRTV 199
Cdd:COG2375   164 DARGTAVIEVPDAA-DEQPLPAPAgveVTWLHRGGAPpGSALLDAVRALELPDGDVyAWVAGEASAV 229
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 18-189 5.25e-20

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: 85.01  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  18 VDSVEELSPGLRLVTFTGEPLSGTP-WTPGCAVGIRV----------------------GRRVTRHYTVAEVAGGGSRLG 74
Cdd:cd06193     1 VVRVERLTPHMRRITLGGPDLAGFPsDGPDQHVKLLFpdpgqappvlpvlgrrrwppeePRPVMRTYTVRRFDPEAGELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  75 IVFQLHRGDGPGTRWARSLAAGDRVALLGPRRLSRCRRGLA-YFLVGDASAVGLFQSLAESVPASAEVCGVIEVPAEDlD 153
Cdd:cd06193    81 IDFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPDADwYLLAGDETALPAIAAILEELPADARGTALIEVPDAA-D 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1175241556 154 GASLLVP-GVTV---VASAGRPGEALLARLREERVPVGAV 189
Cdd:cd06193   160 EQPLPAPaGVEVtwlHRGGAEAGELALLAVRALAPPAGDG 199
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
17-105 2.84e-10

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 56.14  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  17 TVDSVEELSPGLRLVTFTGEPLSGTPWT------------PGCAVGI--------------RVGRRVTRHYTVAEVAGGG 70
Cdd:pfam08021   1 QVVRVTRLSPHMRRITFTGPGLAGFPSDgtdqhiklffppPGQTPPAvpptlgedgpiwppEDQRPVMRTYTVRAYDPEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1175241556  71 SRLGIVFQLHRGDGPGTRWARSLAAGDRVALLGPR 105
Cdd:pfam08021  81 GELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPG 115
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 20-104 7.86e-06

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: 45.13  E-value: 7.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  20 SVEELSPGLRLVTFtgEPLSGTPWTPGCAVGIRV---GRRVTRHYTVAEVAGGGSRLGIVFQLHRGdGPGTRWARSLAAG 96
Cdd:cd00322     2 ATEDVTDDVRLFRL--QLPNGFSFKPGQYVDLHLpgdGRGLRRAYSIASSPDEEGELELTVKIVPG-GPFSAWLHDLKPG 78


                  ....*...
gi 1175241556  97 DRVALLGP 104
Cdd:cd00322    79 DEVEVSGP 86
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
11-105 8.98e-06

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 45.17  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  11 RRARPVTVDSVEELSPGLRLVTFT-GEPLSGTPWTPGCAVGIRV---GRRVTRHYTVAEVAGGGS-RLGIvfqLHRGDGP 85
Cdd:COG1018     1 AGFRPLRVVEVRRETPDVVSFTLEpPDGAPLPRFRPGQFVTLRLpidGKPLRRAYSLSSAPGDGRlEITV---KRVPGGG 77

                          90       100
                  ....*....|....*....|.
gi 1175241556  86 GTRWA-RSLAAGDRVALLGPR 105
Cdd:COG1018    78 GSNWLhDHLKVGDTLEVSGPR 98
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 17-104 2.00e-05

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 44.08  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  17 TVDSVEELSPGLRLVTFTGePLSGTPWTPGCAVGIRV-GRRVTRHYTVAEVAGGGSRLGIVFQLHrgdGPGTRWARSLAA 95
Cdd:COG0543     1 KVVSVERLAPDVYLLRLEA-PLIALKFKPGQFVMLRVpGDGLRRPFSIASAPREDGTIELHIRVV---GKGTRALAELKP 76


                  ....*....
gi 1175241556  96 GDRVALLGP 104
Cdd:COG0543    77 GDELDVRGP 85
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 16-134 2.75e-03

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 37.70  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175241556  16 VTVDSVEELSPGLRLVTFTGEPLSGTPWTPGCAVGIRV-GRRVTRHYTVAEVAGGGSRLGIVFQLHRGDGPGTRWARSLA 94
Cdd:cd06212     3 GTVVAVEALTHDIRRLRLRLEEPEPIKFFAGQYVDITVpGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDDGLA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1175241556  95 AGDRVALLGP-----RRLSRCRRGLayfLVGDASAV----GLFQSLAES 134
Cdd:cd06212    83 VGDPVTVTGPygtctLRESRDRPIV---LIGGGSGMapllSLLRDMAAS 128
 
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