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Conserved domains on  [gi|756975319|ref|WP_042663544|]
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ferredoxin--NADP reductase, partial [Haloferax sp. ATB1]

Protein Classification

ferredoxin--NADP reductase( domain architecture ID 11436905)

ferredoxin--NADP reductase, may act on an iron-sulfur protein as electron donor with NADP(+) as acceptor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
5-97 1.47e-22

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


:

Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.92  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG---FEAEPGQFVKLSAEVDGESYARFYTLSSPGVGDTFEVTVGIDPEeaGPFSRHL- 80
Cdd:COG1018    6 LRVVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG--GGGSNWLh 83

                         90
                 ....*....|....*..
gi 756975319  81 DSLVAGDDVEISGPFGR 97
Cdd:COG1018   84 DHLKVGDTLEVSGPRGD 100
 
Name Accession Description Interval E-value
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
5-97 1.47e-22

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.92  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG---FEAEPGQFVKLSAEVDGESYARFYTLSSPGVGDTFEVTVGIDPEeaGPFSRHL- 80
Cdd:COG1018    6 LRVVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG--GGGSNWLh 83

                         90
                 ....*....|....*..
gi 756975319  81 DSLVAGDDVEISGPFGR 97
Cdd:COG1018   84 DHLKVGDTLEVSGPRGD 100
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 9-109 2.44e-20

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: 82.11  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   9 AVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEVDGESYARFYTL-SSPGVGDTFEVTVGIDPeeAGPFSRHLDSLVAGD 87
Cdd:cd00322    2 ATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIaSSPDEEGELELTVKIVP--GGPFSAWLHDLKPGD 79

                         90       100
                 ....*....|....*....|....
gi 756975319  88 DVEISGPFG--RSYYDGESRVVVL 109
Cdd:cd00322   80 EVEVSGPGGdfFLPLEESGPVVLI 103
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
6-100 1.66e-08

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 48.35  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319    6 TVAAVSDVGPGTVAIEFETPDGFEAE---PGQFVKLSAEVDGESYARFYT-LSSPGVGDTFEVTVGIDPeeAGPFSRHLD 81
Cdd:pfam00970   3 TLVEKELVSHDTRIFRFALPHPDQVLglpVGQHLFLRLPIDGELVIRSYTpISSDDDKGYLELLVKVYP--GGKMSQYLD 80

                          90
                  ....*....|....*....
gi 756975319   82 SLVAGDDVEISGPFGRSYY 100
Cdd:pfam00970  81 ELKIGDTIDFKGPLGRFEY 99
PLN02252 PLN02252
nitrate reductase [NADPH]
 33-108 4.51e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 46.98  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319  33 GQFVKLSAEVDGESYARFYTLSSpGVGDT--FEVTV-----GIDPE--EAGPFSRHLDSLVAGDDVEISGPFGRSYYDGE 103
Cdd:PLN02252 668 GKHVFLCATINGKLCMRAYTPTS-SDDEVghFELVIkvyfkNVHPKfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGR 746


                 ....*
gi 756975319 104 SRVVV 108
Cdd:PLN02252 747 GSFLV 751
 
Name Accession Description Interval E-value
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
5-97 1.47e-22

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 87.92  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG---FEAEPGQFVKLSAEVDGESYARFYTLSSPGVGDTFEVTVGIDPEeaGPFSRHL- 80
Cdd:COG1018    6 LRVVEVRRETPDVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG--GGGSNWLh 83

                         90
                 ....*....|....*..
gi 756975319  81 DSLVAGDDVEISGPFGR 97
Cdd:COG1018   84 DHLKVGDTLEVSGPRGD 100
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 9-109 2.44e-20

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: 82.11  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   9 AVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEVDGESYARFYTL-SSPGVGDTFEVTVGIDPeeAGPFSRHLDSLVAGD 87
Cdd:cd00322    2 ATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIaSSPDEEGELELTVKIVP--GGPFSAWLHDLKPGD 79

                         90       100
                 ....*....|....*....|....
gi 756975319  88 DVEISGPFG--RSYYDGESRVVVL 109
Cdd:cd00322   80 EVEVSGPGGdfFLPLEESGPVVLI 103
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 5-97 4.87e-14

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. 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 portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin 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.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 65.69  E-value: 4.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG--FEAEPGQFVKLSAEVDGESYARFYTLSS-PGVGDTFEVTVG-IDPeeaGPFSRHL 80
Cdd:cd06215    1 LRCVKIIQETPDVKTFRFAAPDGslFAYKPGQFLTLELEIDGETVYRAYTLSSsPSRPDSLSITVKrVPG---GLVSNWL 77

                         90
                 ....*....|....*...
gi 756975319  81 -DSLVAGDDVEISGPFGR 97
Cdd:cd06215   78 hDNLKVGDELWASGPAGE 95
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 5-97 3.54e-13

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 63.35  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG---FEAEPGQFVKLSAEVDGESYARFYT-LSSPGVGDTFEVTVGIDPEeaGPFSRHL 80
Cdd:cd06183    1 FKLVSKEDISHDTRIFRFELPSPdqvLGLPVGQHVELKAPDDGEQVVRPYTpISPDDDKGYFDLLIKIYPG--GKMSQYL 78

                         90
                 ....*....|....*..
gi 756975319  81 DSLVAGDDVEISGPFGR 97
Cdd:cd06183   79 HSLKPGDTVEIRGPFGK 95
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 5-97 4.98e-13

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. 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 and 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.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 62.95  E-value: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFETPDG----FEAEPGQFVKLSAEVDGESYARFYTLSS-PGVGdtfEVTVGIDPEEAGPFSRH 79
Cdd:cd06214    4 LTVAEVVRETADAVSITFDVPEElrdaFRYRPGQFLTLRVPIDGEEVRRSYSICSsPGDD---ELRITVKRVPGGRFSNW 80

                         90
                 ....*....|....*....
gi 756975319  80 L-DSLVAGDDVEISGPFGR 97
Cdd:cd06214   81 AnDELKAGDTLEVMPPAGR 99
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 7-96 1.16e-12

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. 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.


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 61.86  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   7 VAAVSDVGPGTVAIEFETPDGFEA-EPGQFVKLSAEVDGESYARFYTLSSP--GVGDTFEVTVGIDPEeaGPFSRHL-DS 82
Cdd:cd06216   22 VVAVRPETADMVTLTLRPNRGWPGhRAGQHVRLGVEIDGVRHWRSYSLSSSptQEDGTITLTVKAQPD--GLVSNWLvNH 99

                         90
                 ....*....|....
gi 756975319  83 LVAGDDVEISGPFG 96
Cdd:cd06216  100 LAPGDVVELSQPQG 113
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 6-96 2.65e-12

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).


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 61.00  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETP--DGFEAEPGQFVKLSAEVDGESYARFYTLSSPGVGDTFEVTVGIDPeeAGPFSRHL-DS 82
Cdd:cd06191    2 RVAEVRSETPDAVTIVFAVPgpLQYGFRPGQHVTLKLDFDGEELRRCYSLCSSPAPDEISITVKRVP--GGRVSNYLrEH 79

                         90
                 ....*....|....
gi 756975319  83 LVAGDDVEISGPFG 96
Cdd:cd06191   80 IQPGMTVEVMGPQG 93
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 6-109 4.94e-12

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. 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 between 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.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 60.36  E-value: 4.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETPDG--FEAEPGQFVKLSAEV-DGESYARFYTLSSPGVGDTF-EVTVgiDPEEAGPFSRHL- 80
Cdd:cd06217    5 RVTEIIQETPTVKTFRLAVPDGvpPPFLAGQHVDLRLTAiDGYTAQRSYSIASSPTQRGRvELTV--KRVPGGEVSPYLh 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 756975319  81 DSLVAGDDVEISGPFGRSYYDG-ESRVVVL 109
Cdd:cd06217   83 DEVKVGDLLEVRGPIGTFTWNPlHGDPVVL 112
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 6-99 1.89e-11

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 58.72  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETPD-GFEAEPGQFVKLSaeVDGESYARFYTLSS-PGVGDTFEVTVGIdpeeAGPFSRHLDSL 83
Cdd:COG0543    1 KVVSVERLAPDVYLLRLEAPLiALKFKPGQFVMLR--VPGDGLRRPFSIASaPREDGTIELHIRV----VGKGTRALAEL 74

                         90
                 ....*....|....*.
gi 756975319  84 VAGDDVEISGPFGRSY 99
Cdd:COG0543   75 KPGDELDVRGPLGNGF 90
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
6-100 1.66e-08

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 48.35  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319    6 TVAAVSDVGPGTVAIEFETPDGFEAE---PGQFVKLSAEVDGESYARFYT-LSSPGVGDTFEVTVGIDPeeAGPFSRHLD 81
Cdd:pfam00970   3 TLVEKELVSHDTRIFRFALPHPDQVLglpVGQHLFLRLPIDGELVIRSYTpISSDDDKGYLELLVKVYP--GGKMSQYLD 80

                          90
                  ....*....|....*....
gi 756975319   82 SLVAGDDVEISGPFGRSYY 100
Cdd:pfam00970  81 ELKIGDTIDFKGPLGRFEY 99
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 4-103 3.56e-08

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 49.55  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   4 IVTVAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEVDG-ESYARFYTLSSPGVGDTFEVTVGIDPEEAGpFSRHLDS 82
Cdd:cd06196    2 TVTLLSIEPVTHDVKRLRFDKPEGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDDVLEFVIKSYPDHDG-VTEQLGR 80

                         90       100
                 ....*....|....*....|.
gi 756975319  83 LVAGDDVEISGPFGRSYYDGE 103
Cdd:cd06196   81 LQPGDTLLIEDPWGAIEYKGP 101
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 22-109 4.22e-08

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 49.48  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319  22 FETPDGF---EAEPGQFVKLSAEVDGESY--ARFYTLSSPGVGDTFEVTVgiDPEEAGPFSRHL-DSLVAGDDVEISGPF 95
Cdd:cd06184   26 LEPADGGplpPFLPGQYLSVRVKLPGLGYrqIRQYSLSDAPNGDYYRISV--KREPGGLVSNYLhDNVKVGDVLEVSAPA 103

                         90
                 ....*....|....*
gi 756975319  96 GRSYYDGES-RVVVL 109
Cdd:cd06184  104 GDFVLDEASdRPLVL 118
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 6-100 5.74e-08

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 49.25  E-value: 5.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETPDGFEAE--PGQFVKLSAEvDGESYARFYTLSSPGVGDTFEVTVGIDPEEAGPFSRHlDSL 83
Cdd:cd06211   10 TVVEIEDLTPTIKGVRLKLDEPEEIEfqAGQYVNLQAP-GYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVH-KQL 87

                         90
                 ....*....|....*..
gi 756975319  84 VAGDDVEISGPFGRSYY 100
Cdd:cd06211   88 KEGDELEISGPYGDFFV 104
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 17-99 1.90e-07

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 47.60  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319  17 TVAIEFETPDGFEAEPGQFVKLSAEVDGEsyARFYTLSSPGVGDTFEVTVgidpEEAGPFSRHLDSLVAGDDVEISGPFG 96
Cdd:cd06221   15 TLRLEDDDEELFTFKPGQFVMLSLPGVGE--APISISSDPTRRGPLELTI----RRVGRVTEALHELKPGDTVGLRGPFG 88


                 ...
gi 756975319  97 RSY 99
Cdd:cd06221   89 NGF 91
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 6-97 3.41e-07

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.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 46.79  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEVD-GESYARFYTLSSPGVGDTFEVTVGIDPEeaGPFSRHLDSLV 84
Cdd:cd06195    1 TVLKRRDWTDDLFSFRVTRDIPFRFQAGQFTKLGLPNDdGKLVRRAYSIASAPYEENLEFYIILVPD--GPLTPRLFKLK 78

                         90
                 ....*....|....
gi 756975319  85 AGDDVEIS-GPFGR 97
Cdd:cd06195   79 PGDTIYVGkKPTGF 92
PLN02252 PLN02252
nitrate reductase [NADPH]
 33-108 4.51e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 46.98  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319  33 GQFVKLSAEVDGESYARFYTLSSpGVGDT--FEVTV-----GIDPE--EAGPFSRHLDSLVAGDDVEISGPFGRSYYDGE 103
Cdd:PLN02252 668 GKHVFLCATINGKLCMRAYTPTS-SDDEVghFELVIkvyfkNVHPKfpNGGLMSQYLDSLPIGDTIDVKGPLGHIEYAGR 746


                 ....*
gi 756975319 104 SRVVV 108
Cdd:PLN02252 747 GSFLV 751
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 7-103 9.27e-07

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. 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.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 45.72  E-value: 9.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   7 VAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEvDGEsyARFYTL-SSPGVGDTFEVTVGIDPEeaGPFSRHLDSLVA 85
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPDRPLPYLPGQYVNLRRA-GGL--ARSYSPtSLPDGDNELEFHIRRKPN--GAFSGWLGEEAR 75

                         90
                 ....*....|....*....
gi 756975319  86 -GDDVEISGPFGRSYYDGE 103
Cdd:cd06194   76 pGHALRLQGPFGQAFYRPE 94
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 6-100 1.65e-06

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 45.24  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   6 TVAAVSDVGPGTVAIEFETPDG--FEAEPGQFVKLSAEVDGESYARF---------------------YTL-SSPGVGDT 61
Cdd:COG2871  135 TVVSNENVTTFIKELVLELPEGeeIDFKAGQYIQIEVPPYEVDFKDFdipeeekfglfdkndeevtraYSMaNYPAEKGI 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 756975319  62 FEVTVGIDPEEA----GPFSRHLDSLVAGDDVEISGPFGRSYY 100
Cdd:COG2871  215 IELNIRIATPPMdvppGIGSSYIFSLKPGDKVTISGPYGEFFL 257
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 7-105 3.92e-05

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 41.00  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   7 VAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEvDGESyaRFYTL-SSPGVGDTFEVTVGIDPEeaGPFSRH-LDSLV 84
Cdd:cd06189    3 VESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLLLD-DGDK--RPFSIaSAPHEDGEIELHIRAVPG--GSFSDYvFEELK 77

                         90       100
                 ....*....|....*....|.
gi 756975319  85 AGDDVEISGPFGRSYYDGESR 105
Cdd:cd06189   78 ENGLVRIEGPLGDFFLREDSD 98
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 26-92 6.30e-05

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 40.45  E-value: 6.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319  26 DGFEAepGQFVKLSAEVDGESYARFYTLSSPGVGDTFE---VTVgidPEeaGPFSRHLDSLVAGDDVEIS 92
Cdd:PRK10926  29 DPFTA--GQFTKLGLEIDGERVQRAYSYVNAPDNPDLEfylVTV---PE--GKLSPRLAALKPGDEVQVV 91
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 7-97 2.01e-04

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 39.23  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   7 VAAVSDVGPGTVAIEFETPDG-FEAEPGQFVKLSAEVDGESYARFYTLSSPGVG-DTFEVTVgidpEEAGPFSRHLDSLV 84
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKAPLAaRLFRPGQFVFLRNFESPGLERIPLSLAGVDPEeGTISLLV----EIRGPKTKLIAELK 76

                         90
                 ....*....|...
gi 756975319  85 AGDDVEISGPFGR 97
Cdd:cd06192   77 PGEKLDVMGPLGN 89
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 4-97 3.39e-04

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 38.32  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   4 IVTVAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAevdgesyarfytlssPGVGDTFEVTVGI---DPEEA------- 73
Cdd:PRK00054   6 NMKIVENKEIAPNIYTLVLDGEKVFDMKPGQFVMVWV---------------PGVEPLLERPISIsdiDKNEItilyrkv 70

                         90       100
                 ....*....|....*....|....
gi 756975319  74 GPFSRHLDSLVAGDDVEISGPFGR 97
Cdd:PRK00054  71 GEGTKKLSKLKEGDELDIRGPLGN 94
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 8-94 1.70e-03

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 36.31  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   8 AAVSDVGPGTVAIEFETPDGF---EAEPGQFVKLSAevdGESYARFYTL-SSPGVGDTFEVTVGIDPEEAGPfSRHL-DS 82
Cdd:cd06185    1 VRIRDEAPDIRSFELEAPDGAplpAFEPGAHIDVHL---PNGLVRQYSLcGDPADRDRYRIAVLREPASRGG-SRYMhEL 76

                         90
                 ....*....|..
gi 756975319  83 LVAGDDVEISGP 94
Cdd:cd06185   77 LRVGDELEVSAP 88
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 7-104 2.12e-03

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 36.03  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   7 VAAVSDVGPGTVAIEFETPDGFEAEPGQFVKLSAEvDGESYARFYTLSS-PGVGDTFEVTVGIDPEeaGPFSRHL-DSLV 84
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVP-GRPRTWRAYSPANpPNEDGEIEFHVRAVPG--GRVSNALhDELK 77

                         90       100
                 ....*....|....*....|
gi 756975319  85 AGDDVEISGPFGRSYYDGES 104
Cdd:cd06187   78 VGDRVRLSGPYGTFYLRRDH 97
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
 48-96 3.27e-03

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) 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 between 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. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. 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.


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 35.76  E-value: 3.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756975319  48 ARFYTLSSPGVGD-----TFEVTV--------GIDPEEAGPFSRHLDSLVAGDDVEISGPFG 96
Cdd:cd06208   64 LRLYSIASSRYGDdgdgkTLSLCVkrlvytdpETDETKKGVCSNYLCDLKPGDDVQITGPVG 125
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 5-99 3.37e-03

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 35.69  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   5 VTVAAVSDVGPGTVAIEFEtpDGFEAEPGQFVKLSAEVDGEsyarfYTLSSPGVGDTFEVTVgidpEEAGPFSRHLDSLV 84
Cdd:cd06220    1 VTIKEVIDETPTVKTFVFD--WDFDFKPGQFVMVWVPGVDE-----IPMSLSYIDGPNSITV----KKVGEATSALHDLK 69

                         90
                 ....*....|....*
gi 756975319  85 AGDDVEISGPFGRSY 99
Cdd:cd06220   70 EGDKLGIRGPYGNGF 84
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 8-109 4.36e-03

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 35.31  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975319   8 AAVSDVGPgTVAIEFETP-DGFEAEPGQFVKLSAEVDGESYARFYTLSS-PGVGDTFEVTVGidpeEAGPFSRHL-DSLV 84
Cdd:cd06198    1 ARVTEVRP-TTTLTLEPRgPALGHRAGQFAFLRFDASGWEEPHPFTISSaPDPDGRLRFTIK----ALGDYTRRLaERLK 75

                         90       100
                 ....*....|....*....|....*
gi 756975319  85 AGDDVEISGPFGRSYYDGESRVVVL 109
Cdd:cd06198   76 PGTRVTVEGPYGRFTFDDRRARQIW 100
 
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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