Conserved Protein Domain Family
SiR_like1

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cd06200: SiR_like1 
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Statistics
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PSSM-Id: 99797
View PSSM: cd06200
Aligned: 19 rows
Threshold Bit Score: 268.377
Threshold Setting Gi: 88812170
Created: 15-May-2008
Updated: 2-Oct-2020
Structure
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Aligned Rows:
  next features
Feature 1:FAD binding pocket [chemical binding site]
Evidence:
  • Comment:by homology to E coli sulfite reductase

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                              #                                         
AAC06216     511 WSLARRECLNPGSQGESTWLLDLRapa-nsaIQWRAGDLLEIVPHQapvrirewlqrhnldgqarvavegveqsl--eqa 587 Pseudomonas aer...
YP_587764    228 WRLVERRLLNPGSQGEAAFHLALEped-asqLAWRAGDIAEIGPCQppdvvdrllarlsldgtapvrcdsrpmtlseala 306 Ralstonia metal...
NP_421857    211 WTLAERTLLNPGSPGGEAWHLRLTpp---kgAVWQAGDIVEIGPRNdpaqvaaliaaldlpaeaadtlagl--------- 278 Caulobacter cre...
YP_001847710 551 WTLQQRDLLNPNSLGQPAYNIELTas---heAVWQAGDIAEIQPGNsperinkflqhhhilknavvdslqvsi------e 621 Acinetobacter b...
ZP_01644196  237 WTLLQREHLNPGSPGGPVYWLRLQppv-gvdVQWQAGDIAEIGPQHardsarawldaqgfdadavlddgqtl-------- 307 Stenotrophomona...
YP_001561561 578 WPLQARSLCNAGSQGAGLYVLELSppe-gvaPLWRAGALAEVLPRHgaatvqawlaaqecdgsapvqwrqqtctl--gea 654 Delftia acidovo...
NP_884093    209 WRLARRTLLNPGSQGAPCYFIELTpph-gtaPQWQAGDIAEIGPRDapd------------------------------- 256 Bordetella para...
YP_973093    588 WRLESRETLNPGSLGNPLVEITLKpavagtpLHWPAGALVDLLPRQpadavgrwlreagldgqapvqaggaperl---ad 664 Acidovorax aven...
ABK64008     585 WRLARRVLLNPGSLGGELHEITLTgp---agATWEAGALAEIIGHNadgsdg---------------------------- 633 Janthinobacteri...
ZP_01519776  220 FVLSRRRLLNPGSQGGALYQLEWTpqs-gelPPWESGDLVSLCVPAd--------------------------------- 265 Comamonas testo...
Feature 1                                      ####            # #            ####               
AAC06216     588 lagrllpdsfehlvglhpqalldaliPLSVRQYSIASLQsDGDLQLIVRQEQHa---dGSLGICSGWLTEYlpLGAALTL 664 Pseudomonas aer...
YP_587764    307 trlllpdsqldiltgftpqrlvdalpALPHREYSIASLPaDGRLELLVRQTRHa---dGRLGLASGWLTEFarEGASIAL 383 Ralstonia metal...
NP_421857    279 -rlpqdaaaldalrglplealaerltALPHREYSIASLPdDGGVELIVRLMTRa---dGAPGLGSGWLCRHapIGAAIEA 354 Caulobacter cre...
YP_001847710 622 kalwnkdltgeiepfanldhlleqlpTLPTREYSIASIPsQQVLRLVVRQQYDe---sGNLGLGSGWLTQHteINQNVAL 698 Acinetobacter b...
ZP_01644196  308 larvarshlpslvppgdlpallatlqPLPHREYSIASVMaDGALDILLRRQLRa---dGTPGIGSGWLCDHavVGEPVQL 384 Stenotrophomona...
YP_001561561 655 laasvlpapgdiapgtapqavadalrPLLPRSYSVASLPqDGHVRLLVRQARHd----GGLGVASGWLTAHaaQGISVAM 730 Delftia acidovo...
NP_884093    257 ------------------------spLHAHREYSIASLPaDGAVHLLVRQMRSa---dGALGLGSGWLTHIaqTGQAIDL 309 Bordetella para...
YP_973093    665 vlarsvlpalplperlhaqacadalvPLAPRTYSIASLPeDGALQLLVRQERHa----QGLGIASGWLTAHapLGSIQTL 740 Acidovorax aven...
ABK64008     634 ---------------------dahhaQHAPRSYSLASLPsDGELQLLVRQERHagdenQGHGVCSGWLTRFapLGAGIRL 692 Janthinobacteri...
ZP_01519776  266 --------------------------PERARDYSIASITaDGSLQLLVRESTRa---dGSPGLASHWLCCGmaEGDVLSL 316 Comamonas testo...
Feature 1                                                                                        
AAC06216     665 RLRRNAGFHLPe-----dDVPLILIGNGTGLAGLRSLLRASiaAGRKRNWLLFGERNfAHDYYCRAELEQALarGELQRL 739 Pseudomonas aer...
YP_587764    384 RVRTNRSFHPPe-----dGRPLILIGNGTGLAGLRAVIKARaeAGHHRNWLLFGERSaAHDNFHAEEFQAWLsqGVLQRV 458 Ralstonia metal...
NP_421857    355 RVRVNRSFHAPe-----tKRPLILIGSGTGLAGLRAHLKARaaAGVRWNWLIFGERTaAHDYFHRAELEAWQasGLLDRL 429 Caulobacter cre...
YP_001847710 699 RIRTNESFHLId-----dNRPIICIGNGTGIAGLMSLLHTRtrHNYTENWLIFGERQrNHDFFYASTIEAWQtmGMLKRL 773 Acinetobacter b...
ZP_01644196  385 RLRRNDNFHGVa-----aDVPLLLIGNGTGIAGLRAHLHERarDGARRTWLLFGERTaEHDFHFGEELQAMLadGTLARL 459 Stenotrophomona...
YP_001561561 731 RLVENRAFEPRdeadaepDAPAIFIGNGSGYAGLRGHLLARmhAGRHRNWLLFGERQrAHDGYCEAEVSGWLaaGKLQRA 810 Delftia acidovo...
NP_884093    310 RVRANRNFHPPa-----dARPLILVGNGTGLAGLRALLKARrsAGHGRNWLVFGERSaAHDWFCRDELAQWRgeGWLEYV 384 Bordetella para...
YP_973093    741 RFVENPCFGLEgt----eGRPCLFIGNGSGLAGLRSLLRARvrAGQQRNWLLFGERQrAADTLCAGEIAHWQarGCLPRL 816 Acidovorax aven...
ABK64008     693 RLQANPAFAPAl-----vDVPCIYIGNGSGLAGLRAHLRARqrAGLARNWLLFGERQqAFDSVCGEELQGWLdaGHLARL 767 Janthinobacteri...
ZP_01519776  317 TLREHRGFRLGdn----aGRPLILIGNGSGLAGLLSHIKARvqQDRNDQWLLFGERSpQHDAFCAEQLAAWVeqGRLARL 392 Comamonas testo...
Feature 1                                                                                      
AAC06216     740 DLAFSRDQae---kIYVQDRLHEaaDELRRWIDEGAALYVCGSLqGMAGGVDRVLReVLGEEALQRLAdEGRYRRDVY 814 Pseudomonas aerug...
YP_587764    459 DHAWSRDGam---pRYVQDAVSAqaATIAAWVEQGASIYVCGSLqGMAAGVQDALLrILGESTLQRLTeAGSYRRDVY 533 Ralstonia metalli...
NP_421857    430 DLAFSRDQae---rVYVQHRLREsaDILRRWVANGAAIYVCGSLeGMSREAHTALVeILGAPMLERLTdEGRYRRDVY 504 Caulobacter cresc...
YP_001847710 774 DLAFSRDQeq---rVYVQDIIRQnaAELINWIERGAVLYVCGSIdGMASGVDQALIhILGEEQVDELRqQGRYRRDVY 848 Acinetobacter bau...
ZP_01644196  460 DAVFSRSGga---hRYVQDRLLAeaATLRQWVDEGTTILVCGSLqGMAPAVDAVIEqVLGAEGKEALQlAGRYRRDVY 534 Stenotrophomonas ...
YP_001561561 811 DFIYSRDQar---rRYVQDALREaaEPLRDWIADGAVLYVCGSAdGMAAGVDAALAdILGATAVEDLIvEGRYRRDVY 885 Delftia acidovora...
NP_884093    385 DAVFSRDApq---rRYVQDLLREraERVRDWIREGAAVYVCGSLhGMAEGVHQALAdILGPAQLQALQhAGRYRRDVY 459 Bordetella parape...
YP_973093    817 DLAFSRDAda--phRYVQDALRAamPELRRWLDDGAVVFVCGSAeGMGAGVDHVLSdALGAEGMDALIdAGRYRRDVY 892 Acidovorax avenae...
ABK64008     768 DRVFSRDGdevgkrQYVQDRLRAcaDELRDWLAQGAIVYVCGSLqGMAAGIDAVLQeVLGQEGLDALLaAGRYRRDVY 845 Janthinobacterium...
ZP_01519776  393 DQAWSRNGkd---sRYVQDLLRShaEEVRQWVERGAAIYVCGSLnGMGQGVHLTLQaILGEAKVAELLgSGRYRRDVY 467 Comamonas testost...

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