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Conserved domains on  [gi|576482761|gb|EUA76286|]
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siderophore-interacting FAD-binding domain protein [Mycobacterium xenopi 4042]

Protein Classification

siderophore-interacting protein( domain architecture ID 10547131)

siderophore-interacting protein plays a role in iron homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
5-123 2.23e-42

Siderophore-interacting FAD-binding domain;


:

Pssm-ID: 311811  Cd Length: 118  Bit Score: 137.80  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761    5 EVVRREQLAPHLVRVVLGGSGFDTFvPNDFTDSYVKLVFVADDVDVAALPRPLTLDSFSGLPVEKQPVIRTMTVRRADPA 84
Cdd:pfam08021   1 QVVRVTRLSPHMRRITFTGPGLAGF-PSDGTDQHIKLFFPPPGQTPPAVPPTLGEDGPIWPPEDQRPVMRTYTVRAYDPE 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 576482761   85 ARELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAY 123
Cdd:pfam08021  80 AGELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPGGAD 118
 
Name Accession Description Interval E-value
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
5-123 2.23e-42

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 137.80  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761    5 EVVRREQLAPHLVRVVLGGSGFDTFvPNDFTDSYVKLVFVADDVDVAALPRPLTLDSFSGLPVEKQPVIRTMTVRRADPA 84
Cdd:pfam08021   1 QVVRVTRLSPHMRRITFTGPGLAGF-PSDGTDQHIKLFFPPPGQTPPAVPPTLGEDGPIWPPEDQRPVMRTYTVRAYDPE 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 576482761   85 ARELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAY 123
Cdd:pfam08021  80 AGELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPGGAD 118
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 1-127 5.68e-42

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: 141.17  E-value: 5.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761   1 MHSFEVVRREQLAPHLVRVVLGGSGFDTFVPNDFtDSYVKLVFVADDVDVAALPrplTLDSFSGLPVEKQPVIRTMTVRR 80
Cdd:COG2375   15 LRELTVVRVERLSPHMRRVTLGGEDLAGFASPGP-DDHVKLFFPPPGGGEPVLP---TLDDGLALPGEERPVMRTYTVRR 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 576482761  81 ADPAARELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAYAPTP 127
Cdd:COG2375   91 FDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPP 137
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 6-128 4.78e-37

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: 127.76  E-value: 4.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761   6 VVRREQLAPHLVRVVLGGSGFDTFvPNDFTDSYVKLVFVADDvdvAALPRPLTLDSFSGLPVEKQPVIRTMTVRRADPAA 85
Cdd:cd06193    1 VVRVERLTPHMRRITLGGPDLAGF-PSDGPDQHVKLLFPDPG---QAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 576482761  86 RELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAYAPTPP 128
Cdd:cd06193   77 GELDIDFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPD 119
 
Name Accession Description Interval E-value
FAD_binding_9 pfam08021
Siderophore-interacting FAD-binding domain;
5-123 2.23e-42

Siderophore-interacting FAD-binding domain;


Pssm-ID: 311811  Cd Length: 118  Bit Score: 137.80  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761    5 EVVRREQLAPHLVRVVLGGSGFDTFvPNDFTDSYVKLVFVADDVDVAALPRPLTLDSFSGLPVEKQPVIRTMTVRRADPA 84
Cdd:pfam08021   1 QVVRVTRLSPHMRRITFTGPGLAGF-PSDGTDQHIKLFFPPPGQTPPAVPPTLGEDGPIWPPEDQRPVMRTYTVRAYDPE 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 576482761   85 ARELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAY 123
Cdd:pfam08021  80 AGELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPGGAD 118
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 1-127 5.68e-42

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: 141.17  E-value: 5.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761   1 MHSFEVVRREQLAPHLVRVVLGGSGFDTFVPNDFtDSYVKLVFVADDVDVAALPrplTLDSFSGLPVEKQPVIRTMTVRR 80
Cdd:COG2375   15 LRELTVVRVERLSPHMRRVTLGGEDLAGFASPGP-DDHVKLFFPPPGGGEPVLP---TLDDGLALPGEERPVMRTYTVRR 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 576482761  81 ADPAARELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAYAPTP 127
Cdd:COG2375   91 FDPEAGELDIDFVLHGDGGPASRWAARARPGDRVGILGPGGSFVPPP 137
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 6-128 4.78e-37

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: 127.76  E-value: 4.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 576482761   6 VVRREQLAPHLVRVVLGGSGFDTFvPNDFTDSYVKLVFVADDvdvAALPRPLTLDSFSGLPVEKQPVIRTMTVRRADPAA 85
Cdd:cd06193    1 VVRVERLTPHMRRITLGGPDLAGF-PSDGPDQHVKLLFPDPG---QAPPVLPVLGRRRWPPEEPRPVMRTYTVRRFDPEA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 576482761  86 RELTVDIVVHGEHGVAGPWAATAEPGQPMYLMGPGGAYAPTPP 128
Cdd:cd06193   77 GELDIDFVLHGDEGPASRWAASAQPGDTLGIAGPGGSFLPPPD 119
 
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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