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Conserved domains on  [gi|218546561|gb|ACK98929|]
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sulfite reductase [NADPH] flavoprotein alpha-component, partial [Aeromonas salmonicida subsp. masoucida]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FNR_like super family cl06868
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 1-81 1.74e-11

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).


The actual alignment was detected with superfamily member PRK10953:

Pssm-ID: 447143 [Multi-domain]  Cd Length: 600  Bit Score: 57.81  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218546561   1 VWFDNDADLVGEVLALSGRSGDE-ATAHG---SLREVLTRNLELTRLHGGFITGLAEISGNAALKDLAGDKAQVNALVAS 76
Cdd:PRK10953 279 VWYQNDPALVKELVELLWLKGDEpVTVDGktlPLAEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAALQHYAAT 358


                 ....*
gi 218546561  77 AQVVD 81
Cdd:PRK10953 359 TPIVD 363
 
Name Accession Description Interval E-value
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
1-81 1.74e-11

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 57.81  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218546561   1 VWFDNDADLVGEVLALSGRSGDE-ATAHG---SLREVLTRNLELTRLHGGFITGLAEISGNAALKDLAGDKAQVNALVAS 76
Cdd:PRK10953 279 VWYQNDPALVKELVELLWLKGDEpVTVDGktlPLAEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAALQHYAAT 358


                 ....*
gi 218546561  77 AQVVD 81
Cdd:PRK10953 359 TPIVD 363
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 1-81 4.89e-10

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.


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 53.77  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218546561   1 VWFDNDADLVGEVLALSGRSGDE--ATAHG---SLREVLTRNLELTRLHGGFITGLAEISGNAALKDLAGDKaqvnALVA 75
Cdd:cd06199   39 VYPTNDPALVDELLAALGLSGDEpvSTVGGgtlPLREALIKHYEITTLLLALLESYAADTGALELLALAALE----AVLA 114


                 ....*.
gi 218546561  76 SAQVVD 81
Cdd:cd06199  115 FAELRD 120
 
Name Accession Description Interval E-value
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
1-81 1.74e-11

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 57.81  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218546561   1 VWFDNDADLVGEVLALSGRSGDE-ATAHG---SLREVLTRNLELTRLHGGFITGLAEISGNAALKDLAGDKAQVNALVAS 76
Cdd:PRK10953 279 VWYQNDPALVKELVELLWLKGDEpVTVDGktlPLAEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAALQHYAAT 358


                 ....*
gi 218546561  77 AQVVD 81
Cdd:PRK10953 359 TPIVD 363
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 1-81 4.89e-10

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.


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 53.77  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218546561   1 VWFDNDADLVGEVLALSGRSGDE--ATAHG---SLREVLTRNLELTRLHGGFITGLAEISGNAALKDLAGDKaqvnALVA 75
Cdd:cd06199   39 VYPTNDPALVDELLAALGLSGDEpvSTVGGgtlPLREALIKHYEITTLLLALLESYAADTGALELLALAALE----AVLA 114


                 ....*.
gi 218546561  76 SAQVVD 81
Cdd:cd06199  115 FAELRD 120
PRK06214 PRK06214
sulfite reductase subunit alpha;
5-61 2.43e-04

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 37.36  E-value: 2.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 218546561   5 NDADLVGEVLALSGRSGDEATAHGSLREVLTRNLELTRLHGGFITGLAEISGNAALK 61
Cdd:PRK06214 214 NDPALVDAVIAALGAPPEFPIGGKTLREALLEDVSLGPAPDGLFELLSYITGGAARK 270
 
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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