Conserved Protein Domain Family
FNR_iron_sulfur_binding

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cd06191: FNR_iron_sulfur_binding 
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR 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 methnae 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 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Statistics
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PSSM-Id: 99788
View PSSM: cd06191
Aligned: 4 rows
Threshold Bit Score: 303.294
Threshold Setting Gi: 145594608
Created: 9-Apr-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
 
Feature 1:FAD binding pocket [chemical binding site]
Evidence:
  • Comment:contacts primarily in N-terminal region
  • Comment:based on Acinetobacter sp. Benzoate dioxygenase reductase (1KRH) and Methylococcus capsulatus Methane monooxygenase (1TVC)

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                          #              ####              ### #   ###  
P76081         7 LTVAKVESETRDavtiTFAVPQPlqeayRFRPGQHLTLKasfdg-eelrRCYSICRsyl--pgeISVAVKAIegGRFSRY 83  Escherichia coli
YP_001509835  19 ARLAEVRDETPTartlVLDVPGWp----GHLSGQRVDVRltaadgystrRSYSLAApga--gdrVELTVQRVpgGEVSPY 92  Frankia sp. EAN...
NP_521624     36 LVCCHVRQETHDvksfFFRSPAGrt--fLFEPGQFITLEldieg-etinRCYTLSSspar-phtISITVKRVpgGKVSNW 111 Ralstonia solan...
YP_001158905  58 GRIVEVRPETPDaa-tVVIQPGRdw--qGHRPGQYVRLGvdvng-vrqwRAYSVTSapgdrhdpITITVKAIpdGLVSNH 133 Salinispora tro...
Feature 1                                               #  #                                     
P76081        84 AREHIrqGMTLEVMVPq-GHFGYQpqaerqGRYLAIAAGSGITPMLAIIATTlqtepesQFTLIYGNRTsqsMMFRQALA 162 Escherichia coli
YP_001509835  93 LTEIFsvGDPVEIRGPigGWFVWRpa--dpEPVLLVAGGSGIVPLMAMVRARrsaasrvPFRLICSVRSpadLYYADELR 170 Frankia sp. EAN...
NP_521624    112 LHDNLqpGAAIRVLGPa-GEFTCArh--paRKYLFLSAGSGVTPLMSMSRAHhdlaedrDIVFVHSARTpddIIFARELE 188 Ralstonia solan...
YP_001158905 134 LVRHAqpGTIVQLDQAq-GDFVLPat--ppARVLLVTAGSGITPVMGMLRSGalt--gsDVTLVHSAPTaadVIFGGALR 208 Salinispora tro...
Feature 1                                                                                       #
P76081       163 DLkdkypqRLQLLCIFsqetldsdllhgridgeklqslgaslinfrlydeaFICGPAaMMDDAETALKALGmpdkTIHLE 242 Escherichia coli
YP_001509835 171 EAara-dpGLDVTRCYtrvvpdhwtspprrlrp--adlaeagwppdltptcYVCGPTgFVEAVADALVEIGhepeRIRTE 247 Frankia sp. EAN...
NP_521624    189 LIasn-htNFRTSFVVerlgartnwpgitgfls--lpllkliapdfmereiFTCGPApYMKAVRGLLEEAGfdpaRYHEE 265 Ralstonia solan...
YP_001158905 209 ELag--agALRLVERHtrddgqlsladl-----------aalvpdhleretWACGPAgLLDALTAHWTAVGrg-eRLHTE 274 Salinispora tro...
Feature 1         #
P76081       243 RF 244 Escherichia coli
YP_001509835 248 RF 249 Frankia sp. EAN1pec
NP_521624    266 SF 267 Ralstonia solanacearum GMI1000
YP_001158905 275 QF 276 Salinispora tropica CNB-440

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