NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24655635|ref|NP_611419|]
View 

uncharacterized protein Dmel_CG11257 [Drosophila melanogaster]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10445791)

cytochrome b5 reductase family protein such as NADH-cytochrome b5 reductase that catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor; the cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes

Graphical summary

 Zoom to residue level

show extra options Â»

Show site features     Horizontal zoom: Ã—

List of domain hits

Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
295-533 1.71e-61

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: 202.03  E-value: 1.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 295 YEVVHSKDFNHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVDHTYLrlenirssrSECLHFLIKRYPN 374
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDD---------KGYFDLLIKIYPG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 375 GPVSSHLQKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRiESLQLLYFNKTNEDIWL 454
Cdd:cd06183  72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDK-TKISLLYANRTEEDILL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 455 KEKLHELHTD-DERFSCTNYVSQSEDNPQ----RIALELLAPLFQKNQPERcTYVLICGPSGFNT-AALDILSQLDVKAN 528
Cdd:cd06183 151 REELDELAKKhPDRFKVHYVLSRPPEGWKggvgFITKEMIKEHLPPPPSED-TLVLVCGPPPMIEgAVKGLLKELGYKKD 229

                ....*
gi 24655635 529 QIHVF 533
Cdd:cd06183 230 NVFKF 234
p23_NCB5OR cd06490
p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. ...
190-276 1.06e-37

p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. NCB5OR is widely expressed in human organs and tissues and is localized in the ER (endoplasmic reticulum). It appears to play a critical role in maintaining viable pancreatic beta cells. Mice homozygous for a targeted knockout (KO) of the gene encoding NCB5OR develop an early-onset nonautoimmune diabetes phenotype with a non-inflammatory beta-cell deficiency. The role of NCB5OR in beta cells may be in maintaining or regulating their redox status. Proteins in this group in addition contain an N-terminal cytochrome b5 domain and a C-terminal cytochrome b5 oxidoreductase domain. The gene encoding NCB5OR has been considered as a positional candidate for type II diabetes and other diabetes subtypes related to B-cell dysfunction, however variation in its coding region does not appear not to be a major contributor to the pathogenesis of these diseases.


:

Pssm-ID: 107240  Cd Length: 87  Bit Score: 133.61  E-value: 1.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 190 FDWIQQRSELTLIFYTRSLANPGLVVRRKDLQ-QLSVRVLVQHNWHSFDFQLTNNVEWPPkLAKIGSETGKIELVFVKEE 268
Cdd:cd06490   1 YDWFQTDSEVTIVVYTKSKGNPADIVIVDDQQrELRVEIILGDKSYLLHLDLSNEVQWPC-EVRISTETGKIELVLKKKE 79

                ....*...
gi 24655635 269 AEPWPTYG 276
Cdd:cd06490  80 PEKWTSLG 87
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
91-163 2.27e-23

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 93.45  E-value: 2.27e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635    91 SRTELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLF-DEVHAWVNYPQLLGKCYVGPLK 163
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKYRIGELA 74
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
295-533 1.71e-61

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: 202.03  E-value: 1.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 295 YEVVHSKDFNHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVDHTYLrlenirssrSECLHFLIKRYPN 374
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDD---------KGYFDLLIKIYPG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 375 GPVSSHLQKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRiESLQLLYFNKTNEDIWL 454
Cdd:cd06183  72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDK-TKISLLYANRTEEDILL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 455 KEKLHELHTD-DERFSCTNYVSQSEDNPQ----RIALELLAPLFQKNQPERcTYVLICGPSGFNT-AALDILSQLDVKAN 528
Cdd:cd06183 151 REELDELAKKhPDRFKVHYVLSRPPEGWKggvgFITKEMIKEHLPPPPSED-TLVLVCGPPPMIEgAVKGLLKELGYKKD 229

                ....*
gi 24655635 529 QIHVF 533
Cdd:cd06183 230 NVFKF 234
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
290-532 8.01e-39

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 141.47  E-value: 8.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 290 DETFEYEVVHSKDFNHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVDhtylrlenirSSRSECLHFLI 369
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSS----------APGDGRLEITV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 370 KRYPNGPVSSHLQ-KLETGSRVHWSAPRGSFQLSDLTAhRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKT 448
Cdd:COG1018  71 KRVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPA-RPLLLIAGGIGITPFLSMLRTLLARGPFR--PVTLVYGARS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 449 NEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ-RIALELLAPLFqKNQPERCTYvlICGPSGFNTAALDILSQLDVKA 527
Cdd:COG1018 148 PADLAFRDELEALAARHPRLRLHPVLSREPAGLQgRLDAELLAALL-PDPADAHVY--LCGPPPMMEAVRAALAELGVPE 224

                ....*
gi 24655635 528 NQIHV 532
Cdd:COG1018 225 ERIHF 229
p23_NCB5OR cd06490
p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. ...
190-276 1.06e-37

p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. NCB5OR is widely expressed in human organs and tissues and is localized in the ER (endoplasmic reticulum). It appears to play a critical role in maintaining viable pancreatic beta cells. Mice homozygous for a targeted knockout (KO) of the gene encoding NCB5OR develop an early-onset nonautoimmune diabetes phenotype with a non-inflammatory beta-cell deficiency. The role of NCB5OR in beta cells may be in maintaining or regulating their redox status. Proteins in this group in addition contain an N-terminal cytochrome b5 domain and a C-terminal cytochrome b5 oxidoreductase domain. The gene encoding NCB5OR has been considered as a positional candidate for type II diabetes and other diabetes subtypes related to B-cell dysfunction, however variation in its coding region does not appear not to be a major contributor to the pathogenesis of these diseases.


Pssm-ID: 107240  Cd Length: 87  Bit Score: 133.61  E-value: 1.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 190 FDWIQQRSELTLIFYTRSLANPGLVVRRKDLQ-QLSVRVLVQHNWHSFDFQLTNNVEWPPkLAKIGSETGKIELVFVKEE 268
Cdd:cd06490   1 YDWFQTDSEVTIVVYTKSKGNPADIVIVDDQQrELRVEIILGDKSYLLHLDLSNEVQWPC-EVRISTETGKIELVLKKKE 79

                ....*...
gi 24655635 269 AEPWPTYG 276
Cdd:cd06490  80 PEKWTSLG 87
PLN02252 PLN02252
nitrate reductase [NADPH]
83-533 4.56e-27

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 115.93  E-value: 4.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   83 TGGRLVPVSrtELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLFDEVH---AWvnypQLLGKCYV 159
Cdd:PLN02252 515 TGSKQYTMS--EVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHsdkAK----KMLEDYRI 588
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  160 GPL--KDNETKPAKESPQITNVILQPPEIVPRfdwiqqrseltlifytRSLANPGLVVRRKDLQqlsvrvlvqhnwhsfd 237
Cdd:PLN02252 589 GELvtTGAAASSSASSHPLSAISTASALAAAS----------------PAPGRPVALNPREKIP---------------- 636
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  238 FQLTNnvewppklakigsetgKIELvfvkeeaepwptygthvsnrldssrlhdetfeyevvhskdfNHDS--FELCLQSV 315
Cdd:PLN02252 637 CRLVE----------------KISL-----------------------------------------SHDVrlFRFALPSE 659
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  316 GQKvlMVLPAGYHVDIEVPLEGRVIQRSYTPVdhtylrlenirSSRSE--CLHFLIK--------RYPNG-PVSSHLQKL 384
Cdd:PLN02252 660 DHV--LGLPVGKHVFLCATINGKLCMRAYTPT-----------SSDDEvgHFELVIKvyfknvhpKFPNGgLMSQYLDSL 726
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  385 ETGSRVHWSAP--------RGSFQLSDLTAH-RNILLLAAGSGLTPILSLIQPILKRNTNRIEsLQLLYFNKTNEDIWLK 455
Cdd:PLN02252 727 PIGDTIDVKGPlghieyagRGSFLVNGKPKFaKKLAMLAGGTGITPMYQVIQAILRDPEDKTE-MSLVYANRTEDDILLR 805
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  456 EKLHEL---HTDdeRFSCTNYVSQSED-----NPQRIALEllapLFQKNQPERC--TYVLICGPSGF-NTAALDILSQLD 524
Cdd:PLN02252 806 EELDRWaaeHPD--RLKVWYVVSQVKRegwkySVGRVTEA----MLREHLPEGGdeTLALMCGPPPMiEFACQPNLEKMG 879

                 ....*....
gi 24655635  525 VKANQIHVF 533
Cdd:PLN02252 880 YDKDSILVF 888
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
91-163 2.27e-23

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 93.45  E-value: 2.27e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635    91 SRTELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLF-DEVHAWVNYPQLLGKCYVGPLK 163
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKYRIGELA 74
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
89-146 2.72e-16

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 74.30  E-value: 2.72e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24655635  89 PVSRTELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLFDEVHA 146
Cdd:COG5274  17 TYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
304-399 1.07e-11

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 61.44  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   304 NHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVdhtylrlenirSSRSEC--LHFLIKRYPNGPVSSHL 381
Cdd:pfam00970  11 SHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPI-----------SSDDDKgyLELLVKVYPGGKMSQYL 79
                          90
                  ....*....|....*...
gi 24655635   382 QKLETGSRVHWSAPRGSF 399
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRF 97
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
93-169 4.98e-08

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 55.47  E-value: 4.98e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655635   93 TELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGvDELMRGVGRDATKLFDEVHAWVNYpQLLGKCYVGPLKDNETKP 169
Cdd:PLN03198 109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTW-KILQDFYIGDVDNVEPTP 183
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
295-533 1.71e-61

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: 202.03  E-value: 1.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 295 YEVVHSKDFNHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVDHTYLrlenirssrSECLHFLIKRYPN 374
Cdd:cd06183   1 FKLVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPDDGEQVVRPYTPISPDDD---------KGYFDLLIKIYPG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 375 GPVSSHLQKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRiESLQLLYFNKTNEDIWL 454
Cdd:cd06183  72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKDPEDK-TKISLLYANRTEEDILL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 455 KEKLHELHTD-DERFSCTNYVSQSEDNPQ----RIALELLAPLFQKNQPERcTYVLICGPSGFNT-AALDILSQLDVKAN 528
Cdd:cd06183 151 REELDELAKKhPDRFKVHYVLSRPPEGWKggvgFITKEMIKEHLPPPPSED-TLVLVCGPPPMIEgAVKGLLKELGYKKD 229

                ....*
gi 24655635 529 QIHVF 533
Cdd:cd06183 230 NVFKF 234
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
290-532 8.01e-39

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 141.47  E-value: 8.01e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 290 DETFEYEVVHSKDFNHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVDhtylrlenirSSRSECLHFLI 369
Cdd:COG1018   1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSS----------APGDGRLEITV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 370 KRYPNGPVSSHLQ-KLETGSRVHWSAPRGSFQLSDLTAhRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKT 448
Cdd:COG1018  71 KRVPGGGGSNWLHdHLKVGDTLEVSGPRGDFVLDPEPA-RPLLLIAGGIGITPFLSMLRTLLARGPFR--PVTLVYGARS 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 449 NEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ-RIALELLAPLFqKNQPERCTYvlICGPSGFNTAALDILSQLDVKA 527
Cdd:COG1018 148 PADLAFRDELEALAARHPRLRLHPVLSREPAGLQgRLDAELLAALL-PDPADAHVY--LCGPPPMMEAVRAALAELGVPE 224

                ....*
gi 24655635 528 NQIHV 532
Cdd:COG1018 225 ERIHF 229
p23_NCB5OR cd06490
p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. ...
190-276 1.06e-37

p23_like domain found in NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR) and similar proteins. NCB5OR is widely expressed in human organs and tissues and is localized in the ER (endoplasmic reticulum). It appears to play a critical role in maintaining viable pancreatic beta cells. Mice homozygous for a targeted knockout (KO) of the gene encoding NCB5OR develop an early-onset nonautoimmune diabetes phenotype with a non-inflammatory beta-cell deficiency. The role of NCB5OR in beta cells may be in maintaining or regulating their redox status. Proteins in this group in addition contain an N-terminal cytochrome b5 domain and a C-terminal cytochrome b5 oxidoreductase domain. The gene encoding NCB5OR has been considered as a positional candidate for type II diabetes and other diabetes subtypes related to B-cell dysfunction, however variation in its coding region does not appear not to be a major contributor to the pathogenesis of these diseases.


Pssm-ID: 107240  Cd Length: 87  Bit Score: 133.61  E-value: 1.06e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 190 FDWIQQRSELTLIFYTRSLANPGLVVRRKDLQ-QLSVRVLVQHNWHSFDFQLTNNVEWPPkLAKIGSETGKIELVFVKEE 268
Cdd:cd06490   1 YDWFQTDSEVTIVVYTKSKGNPADIVIVDDQQrELRVEIILGDKSYLLHLDLSNEVQWPC-EVRISTETGKIELVLKKKE 79

                ....*...
gi 24655635 269 AEPWPTYG 276
Cdd:cd06490  80 PEKWTSLG 87
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
325-532 1.43e-32

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: 124.48  E-value: 1.43e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 325 AGYHVDIEVPLEGRVIQRSYTpvdhtylrlenIRSSRSEC--LHFLIKRYPNGPVSSHLQKLETGSRVHWSAPRGSFQLs 402
Cdd:cd00322  25 PGQYVDLHLPGDGRGLRRAYS-----------IASSPDEEgeLELTVKIVPGGPFSAWLHDLKPGDEVEVSGPGGDFFL- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 403 DLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ 482
Cdd:cd00322  93 PLEESGPVVLIAGGIGITPFRSMLRHLAADKPGG--EITLLYGARTPADLLFLDELEELAKEGPNFRLVLALSRESEAKL 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24655635 483 RIALELLAPLFQKNQPERC--TYVLICGPSGFNTAALDILSQLDVKANQIHV 532
Cdd:cd00322 171 GPGGRIDREAEILALLPDDsgALVYICGPPAMAKAVREALVSLGVPEERIHT 222
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
325-532 8.56e-29

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: 114.18  E-value: 8.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 325 AGYHVDIEVPLEGRVIQRSY----TPVDHtYLRLenirssrseclhfLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSF 399
Cdd:cd06214  35 PGQFLTLRVPIDGEEVRRSYsicsSPGDD-ELRI-------------TVKRVPGGRFSNWAnDELKAGDTLEVMPPAGRF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 400 QLSDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKLHEL---HTDdeRFSCTNYVSQ 476
Cdd:cd06214 101 TLPPLPGARHYVLFAAGSGITPVLSILKTALAREPAS--RVTLVYGNRTEASVIFREELADLkarYPD--RLTVIHVLSR 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24655635 477 SEDNP----QRIALELLAPLF-QKNQPERCTYVLICGPSGFNTAALDILSQLDVKANQIHV 532
Cdd:cd06214 177 EQGDPdllrGRLDAAKLNALLkNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHR 237
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
325-532 8.88e-28

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: 111.55  E-value: 8.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 325 AGYHVDIEVPLEGRVIQRSYTPVdhtylrleNIRSSRSECLHFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSD 403
Cdd:cd06216  48 AGQHVRLGVEIDGVRHWRSYSLS--------SSPTQEDGTITLTVKAQPDGLVSNWLvNHLAPGDVVELSQPQGDFVLPD 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 404 lTAHRNILLLAAGSGLTPILSLIQPILKRntNRIESLQLLYFNKTNED-IWLKE-----------KLHELHTDDE---RF 468
Cdd:cd06216 120 -PLPPRLLLIAAGSGITPVMSMLRTLLAR--GPTADVVLLYYARTREDvIFADElralaaqhpnlRLHLLYTREEldgRL 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635 469 SCTnyvsqsednpqriALELLAPLFQKNQperctyVLICGPSGFNTAALDILSQLDVKANqIHV 532
Cdd:cd06216 197 SAA-------------HLDAVVPDLADRQ------VYACGPPGFLDAAEELLEAAGLADR-LHT 240
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
305-531 2.56e-27

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: 109.99  E-value: 2.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 305 HDSFELCLQSVGQKVLMVLPaGYHVDIEVPLEGRVIQRSYTpvdhtylrlenIRSS--RSECLHFLIKRYPNGPVSSHL- 381
Cdd:cd06215  11 PDVKTFRFAAPDGSLFAYKP-GQFLTLELEIDGETVYRAYT-----------LSSSpsRPDSLSITVKRVPGGLVSNWLh 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 382 QKLETGSRVHWSAPRGSFQLSDLTAhRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKLHEL 461
Cdd:cd06215  79 DNLKVGDELWASGPAGEFTLIDHPA-DKLLLLSAGSGITPMMSMARWLLDTRPDA--DIVFIHSARSPADIIFADELEEL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 462 HTDDERFSCTNYVSQSED----------NPQRiaLELLAPLFqknqPERCTYVliCGPSGFNTAALDILSQLDVKANQIH 531
Cdd:cd06215 156 ARRHPNFRLHLILEQPAPgawggyrgrlNAEL--LALLVPDL----KERTVFV--CGPAGFMKAVKSLLAELGFPMSRFH 227
PLN02252 PLN02252
nitrate reductase [NADPH]
83-533 4.56e-27

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 115.93  E-value: 4.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   83 TGGRLVPVSrtELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLFDEVH---AWvnypQLLGKCYV 159
Cdd:PLN02252 515 TGSKQYTMS--EVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHsdkAK----KMLEDYRI 588
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  160 GPL--KDNETKPAKESPQITNVILQPPEIVPRfdwiqqrseltlifytRSLANPGLVVRRKDLQqlsvrvlvqhnwhsfd 237
Cdd:PLN02252 589 GELvtTGAAASSSASSHPLSAISTASALAAAS----------------PAPGRPVALNPREKIP---------------- 636
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  238 FQLTNnvewppklakigsetgKIELvfvkeeaepwptygthvsnrldssrlhdetfeyevvhskdfNHDS--FELCLQSV 315
Cdd:PLN02252 637 CRLVE----------------KISL-----------------------------------------SHDVrlFRFALPSE 659
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  316 GQKvlMVLPAGYHVDIEVPLEGRVIQRSYTPVdhtylrlenirSSRSE--CLHFLIK--------RYPNG-PVSSHLQKL 384
Cdd:PLN02252 660 DHV--LGLPVGKHVFLCATINGKLCMRAYTPT-----------SSDDEvgHFELVIKvyfknvhpKFPNGgLMSQYLDSL 726
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  385 ETGSRVHWSAP--------RGSFQLSDLTAH-RNILLLAAGSGLTPILSLIQPILKRNTNRIEsLQLLYFNKTNEDIWLK 455
Cdd:PLN02252 727 PIGDTIDVKGPlghieyagRGSFLVNGKPKFaKKLAMLAGGTGITPMYQVIQAILRDPEDKTE-MSLVYANRTEDDILLR 805
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  456 EKLHEL---HTDdeRFSCTNYVSQSED-----NPQRIALEllapLFQKNQPERC--TYVLICGPSGF-NTAALDILSQLD 524
Cdd:PLN02252 806 EELDRWaaeHPD--RLKVWYVVSQVKRegwkySVGRVTEA----MLREHLPEGGdeTLALMCGPPPMiEFACQPNLEKMG 879

                 ....*....
gi 24655635  525 VKANQIHVF 533
Cdd:PLN02252 880 YDKDSILVF 888
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
91-163 2.27e-23

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 93.45  E-value: 2.27e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635    91 SRTELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLF-DEVHAWVNYPQLLGKCYVGPLK 163
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKYRIGELA 74
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
325-531 9.73e-23

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: 96.95  E-value: 9.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 325 AGYHVDIEVPLE-GRVIQRSYT----PVDHTYLRLenirssrseclhfLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGS 398
Cdd:cd06217  33 AGQHVDLRLTAIdGYTAQRSYSiassPTQRGRVEL-------------TVKRVPGGEVSPYLhDEVKVGDLLEVRGPIGT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 399 FQLSDLTAHRnILLLAAGSGLTPILSLIQPILKRNTNRIesLQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSE 478
Cdd:cd06217 100 FTWNPLHGDP-VVLLAGGSGIVPLMSMIRYRRDLGWPVP--FRLLYSARTAEDVIFRDELEQLARRHPNLHVTEALTRAA 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24655635 479 DN-----PQRIALELLAPLFQKNQPERCtYVliCGPSGFNTAALDILSQLDVKANQIH 531
Cdd:cd06217 177 PAdwlgpAGRITADLIAELVPPLAGRRV-YV--CGPPAFVEAATRLLLELGVPRDRIR 231
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
293-532 1.47e-21

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 93.55  E-value: 1.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 293 FEYEVVHSKDFNHDSFELCLQSVGQKVLMVLPaGYHVDIEVPleGRVIQRSYTpvdhtylrLENIrSSRSECLHFLIKRY 372
Cdd:cd06212   1 FVGTVVAVEALTHDIRRLRLRLEEPEPIKFFA-GQYVDITVP--GTEETRSFS--------MANT-PADPGRLEFIIKKY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 373 PNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDlTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNED 451
Cdd:cd06212  69 PGGLFSSFLdDGLAVGDPVTVTGPYGTCTLRE-SRDRPIVLIGGGSGMAPLLSLLRDMAASGSDR--PVRFFYGARTARD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 452 IWLKEKLHELHTDDERFSCTNYVSQSEDN-PQRIALELLAPLFQKNQPE-RCTYVLICGPSGFNTAALDILSQLDVKANQ 529
Cdd:cd06212 146 LFYLEEIAALGEKIPDFTFIPALSESPDDeGWSGETGLVTEVVQRNEATlAGCDVYLCGPPPMIDAALPVLEMSGVPPDQ 225

                ...
gi 24655635 530 IHV 532
Cdd:cd06212 226 IFY 228
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
329-533 4.86e-20

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: 89.54  E-value: 4.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 329 VDIEVPLEGRVIQRSYT---PVDHTYLRlenirssrseclhFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLsDL 404
Cdd:cd06184  45 VRVKLPGLGYRQIRQYSlsdAPNGDYYR-------------ISVKREPGGLVSNYLhDNVKVGDVLEVSAPAGDFVL-DE 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 405 TAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ-- 482
Cdd:cd06184 111 ASDRPLVLISAGVGITPMLSMLEALAAEGPGR--PVTFIHAARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDRee 188
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24655635 483 ------RIALELLAPLFQKNQPErctyVLICGPSGFNTAALDILSQLDVKANQIH--VF 533
Cdd:cd06184 189 dydhagRIDLALLRELLLPADAD----FYLCGPVPFMQAVREGLKALGVPAERIHyeVF 243
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
297-532 2.35e-16

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: 78.02  E-value: 2.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 297 VVHSKDFNHDSFELCLQSVGQkvlMVLPAGYHVDIEVPlEGRVIQRSYTPVdhtylrlenIRSSRSECLHFLIKRYPNGP 376
Cdd:cd06187   1 VVSVERLTHDIAVVRLQLDQP---LPFWAGQYVNVTVP-GRPRTWRAYSPA---------NPPNEDGEIEFHVRAVPGGR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 377 VSSHL-QKLETGSRVHWSAPRGSFQLSDlTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLK 455
Cdd:cd06187  68 VSNALhDELKVGDRVRLSGPYGTFYLRR-DHDRPVLCIAGGTGLAPLRAIVEDALRRGEPR--PVHLFFGARTERDLYDL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 456 EKLHELHTDDERFSCTNYVSQSEDNPQ-------RIALELLAPLfqkNQPErctyVLICGPSGFNTAALDILSQLDVKAN 528
Cdd:cd06187 145 EGLLALAARHPWLRVVPVVSHEEGAWTgrrglvtDVVGRDGPDW---ADHD----IYICGPPAMVDATVDALLARGAPPE 217

                ....
gi 24655635 529 QIHV 532
Cdd:cd06187 218 RIHF 221
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
89-146 2.72e-16

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 74.30  E-value: 2.72e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24655635  89 PVSRTELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGVDELMRGVGRDATKLFDEVHA 146
Cdd:COG5274  17 TYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
295-509 4.00e-16

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 79.11  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  295 YEVVHSKDFNHDS--FELCLQSVGQKvlMVLPAGYHVDIEV----PLEGRVIQRSYTPVdhtylrlenirSSRSECLH-- 366
Cdd:PTZ00319  36 FKLIKKTEVTHDTfiFRFALHSPTQR--LGLPIGQHIVFRCdcttPGKPETVQHSYTPI-----------SSDDEKGYvd 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  367 FLIK--------RYPNG-PVSSHLQKLETGSRVHWSAPRGSFQL---SDLTAHRN-----------ILLLAAGSGLTPIL 423
Cdd:PTZ00319 103 FLIKvyfkgvhpSFPNGgRLSQHLYHMKLGDKIEMRGPVGKFEYlgnGTYTVHKGkgglktmhvdaFAMIAGGTGITPML 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  424 SLIQPILKRNTNRIEsLQLLYFNKTNEDIWLKEKLHELHTDDeRFSCTnYVSQSEDNPQ------RIALEL----LAPLF 493
Cdd:PTZ00319 183 QIIHAIKKNKEDRTK-VFLVYANQTEDDILLRKELDEAAKDP-RFHVW-YTLDREATPEwkygtgYVDEEMlrahLPVPD 259
                        250
                 ....*....|....*.
gi 24655635  494 QKNQPERCTYVLICGP 509
Cdd:PTZ00319 260 PQNSGIKKVMALMCGP 275
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
297-531 1.97e-14

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: 72.94  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 297 VVHSKDFNHDSFELCLQSVGQKVLMVLPaGYHVDIEVPLEGRVIQRSYTPVdhtylrleniRSSRSECLHFLIKRYPNGP 376
Cdd:cd06191   3 VAEVRSETPDAVTIVFAVPGPLQYGFRP-GQHVTLKLDFDGEELRRCYSLC----------SSPAPDEISITVKRVPGGR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 377 VSSHLQK-LETGSRVHWSAPRGSFQLSDLTAHRnILLLAAGSGLTPILSLIQPilKRNTNRIESLQLLYFNKTNEDIWLK 455
Cdd:cd06191  72 VSNYLREhIQPGMTVEVMGPQGHFVYQPQPPGR-YLLVAAGSGITPLMAMIRA--TLQTAPESDFTLIHSARTPADMIFA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 456 EKLHELHTDDERFSCTNYVSQ----SEDNPQRIALEL-LAPLFQKNQPERCTYvlICGPSGFNTAALDILSQLDVKANQI 530
Cdd:cd06191 149 QELRELADKPQRLRLLCIFTRetldSDLLHGRIDGEQsLGAALIPDRLEREAF--ICGPAGMMDAVETALKELGMPPERI 226

                .
gi 24655635 531 H 531
Cdd:cd06191 227 H 227
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
296-532 6.89e-14

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 71.43  E-value: 6.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 296 EVVHSKDFNHDSFELCLQSVGQKvLMVLPaGYHVDIEVPleGRVIQRSYTPVDHtylrlenirSSRSECLHFLIKRYpnG 375
Cdd:COG0543   1 KVVSVERLAPDVYLLRLEAPLIA-LKFKP-GQFVMLRVP--GDGLRRPFSIASA---------PREDGTIELHIRVV--G 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 376 PVSSHLQKLETGSRVHWSAPRGS-FQLSDltAHRNILLLAAGSGLTPILSLIQPILKRNtNRIEslqLLYFNKTNEDIWL 454
Cdd:COG0543  66 KGTRALAELKPGDELDVRGPLGNgFPLED--SGRPVLLVAGGTGLAPLRSLAEALLARG-RRVT---LYLGARTPEDLYL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 455 KEKLHELHtdDERFSCTnyvsqSEDNPQRI---ALELLAPLFQKNQPercTYVLICGPSGFNTAALDILSQLDVKANQIH 531
Cdd:COG0543 140 LDELEALA--DFRVVVT-----TDDGWYGRkgfVTDALKELLAEDSG---DDVYACGPPPMMKAVAELLLERGVPPERIY 209

                .
gi 24655635 532 V 532
Cdd:COG0543 210 V 210
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
378-531 1.16e-13

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 73.00  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 378 SSHLQKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAGSGLTPILSLIQPiLKRNTNRIESLQLLYFNKTNEDIWLKEK 457
Cdd:COG4097 289 TRRLGRLKPGTRVYVEGPYGRFTFDRRDTAPRQVWIAGGIGITPFLALLRA-LAARPGDQRPVDLFYCVRDEEDAPFLEE 367
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635 458 LHELHTDDERFScTNYVSQSEDnpQRIALELLAplfQKNQPERCTYVLICGPSGFNTAALDILSQLDVKANQIH 531
Cdd:COG4097 368 LRALAARLAGLR-LHLVVSDED--GRLTAERLR---RLVPDLAEADVFFCGPPGMMDALRRDLRALGVPARRIH 435
p23_CS_SGT1_like cd06466
p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 ...
191-276 1.49e-13

p23_like domain similar to the C-terminal CHORD-SGT1 (CS) domain of Sgt1 (suppressor of G2 allele of Skp1). Sgt1 interacts with multiple protein complexes and has the features of a cochaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. ScSgt1 is needed for the G1/S and G2/M cell-cycle transitions, and for assembly of the core kinetochore complex (CBF3) via activation of Ctf13, the F-box protein. Binding of Hsp82 (a yeast Hsp90 homologue) to ScSgt1, promotes the binding of Sgt1 to Skp1 and of Skp1 to Ctf13. Some proteins in this group have an SGT1-specific (SGS) domain at the extreme C-terminus. The ScSgt1-SGS domain binds adenylate cyclase. The hSgt1-SGS domain interacts with some S100 family proteins, and studies suggest that the interaction of hSgt1 with Hsp90 and Hsp70 may be regulated by S100A6 in a Ca2+ dependent fashion. This group also includes the p23_like domains of Melusin and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). Melusin is a vertebrate protein which interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107223  Cd Length: 84  Bit Score: 66.07  E-value: 1.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 191 DWIQQRSELTLIFYTRSLANPGLVVRRKDlQQLSVRVLV-QHNWHSFDFQLTNNVEwpPKLAKIGSETGKIELVFVKEEA 269
Cdd:cd06466   1 DWYQTDTSVTVTIYAKNVDKEDVKVEFNE-QSLSVSIILpGGSEYQLELDLFGPID--PEQSKVSVLPTKVEITLKKAEP 77

                ....*..
gi 24655635 270 EPWPTYG 276
Cdd:cd06466  78 GSWPSLE 84
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
307-532 1.89e-13

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: 69.43  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 307 SFELclQSVGQKVLMVLPAGYHVDIEVPlEGRViqRSY----TPVD-HTY----LRLENirsSR--SECLHflikrypng 375
Cdd:cd06185  12 SFEL--EAPDGAPLPAFEPGAHIDVHLP-NGLV--RQYslcgDPADrDRYriavLREPA---SRggSRYMH--------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 376 pvsshlQKLETGSRVHWSAPRGSFQLSDltAHRNILLLAAGSGLTPILSLIQPiLKRntnRIESLQLLYFNKTNEDIWLK 455
Cdd:cd06185  75 ------ELLRVGDELEVSAPRNLFPLDE--AARRHLLIAGGIGITPILSMARA-LAA---RGADFELHYAGRSREDAAFL 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655635 456 EKLHELHTDDERFsctnYVSqseDNPQRIAlelLAPLFQKNQPERCTYVliCGPSGFNTAALDILSQLDVKANQIHV 532
Cdd:cd06185 143 DELAALPGDRVHL----HFD---DEGGRLD---LAALLAAPPAGTHVYV--CGPEGMMDAVRAAAAALGWPEARLHF 207
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
336-508 2.76e-13

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: 69.52  E-value: 2.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 336 EGRVIQRSYTPVDHTYlrlenirssrSECLHFLIKRYPNGPVSSHLQKLETGSRVHWSA-PRGSFQLSDLTAHRNILLLA 414
Cdd:cd06195  39 DGKLVRRAYSIASAPY----------EENLEFYIILVPDGPLTPRLFKLKPGDTIYVGKkPTGFLTLDEVPPGKRLWLLA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 415 AGSGLTPILS-LIQPILKRNTNRIESLQ-------LLYFNKTNEdiwLKEKLHelhtddERFSCTNYVSQSEDNP---QR 483
Cdd:cd06195 109 TGTGIAPFLSmLRDLEIWERFDKIVLVHgvryaeeLAYQDEIEA---LAKQYN------GKFRYVPIVSREKENGaltGR 179
                       170       180       190
                ....*....|....*....|....*....|.
gi 24655635 484 IAlELLAP--LFQK----NQPERcTYVLICG 508
Cdd:cd06195 180 IP-DLIESgeLEEHaglpLDPET-SHVMLCG 208
PRK13289 PRK13289
NO-inducible flavohemoprotein;
316-531 4.14e-13

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 70.98  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  316 GQKVLMVLPAGYhVDIEVPLEGRVIQ--RSYT----PVDHTYlrleniRSSrseclhflIKRYPNGPVSSHL-QKLETGS 388
Cdd:PRK13289 179 GGPVADFKPGQY-LGVRLDPEGEEYQeiRQYSlsdaPNGKYY------RIS--------VKREAGGKVSNYLhDHVNVGD 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  389 RVHWSAPRGSFQLsDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieslQLLYFNKT-NEDIW-LKEKLHELHTDDE 466
Cdd:PRK13289 244 VLELAAPAGDFFL-DVASDTPVVLISGGVGITPMLSMLETLAAQQPKR----PVHFIHAArNGGVHaFRDEVEALAARHP 318
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24655635  467 RFSCTNYVSQ--SEDNPQ-------RIALELLaplfQKNQPERCTYVLICGPSGFNTAALDILSQLDVKANQIH 531
Cdd:PRK13289 319 NLKAHTWYREptEQDRAGedfdsegLMDLEWL----EAWLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIH 388
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
360-531 5.10e-13

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: 68.34  E-value: 5.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 360 SRSECLHFLIKRYPNGPVSSH-LQKLETGSRVHWSAPRGSFQLSDLTaHRNILLLAAGSGLTPILSLIQPILKRNTNRIE 438
Cdd:cd06189  51 HEDGEIELHIRAVPGGSFSDYvFEELKENGLVRIEGPLGDFFLREDS-DRPLILIAGGTGFAPIKSILEHLLAQGSKRPI 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 439 SlqlLYF-NKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQR-------IALELLAPLfqknqpERCTyVLICGPS 510
Cdd:cd06189 130 H---LYWgARTEEDLYLDELLEAWAEAHPNFTYVPVLSEPEEGWQGrtglvheAVLEDFPDL------SDFD-VYACGSP 199
                       170       180
                ....*....|....*....|.
gi 24655635 511 GFNTAALDILSQLDVKANQIH 531
Cdd:cd06189 200 EMVYAARDDFVEKGLPEENFF 220
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
365-532 2.11e-12

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: 67.25  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 365 LHFLIKRYpnGPVSSHLQKLETGSRVHWSAPRG-SFQLsDLTAHRNILLLAAGSGLTPILSLIQPILkRNTNRIESLQLL 443
Cdd:cd06221  58 LELTIRRV--GRVTEALHELKPGDTVGLRGPFGnGFPV-EEMKGKDLLLVAGGLGLAPLRSLINYIL-DNREDYGKVTLL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 444 YFNKTNEDIWLKEKLHELHT-DDERFSCTnyVSQSED--------NPQRIALELLAPLFqknqpercTYVLICGPSGFNT 514
Cdd:cd06221 134 YGARTPEDLLFKEELKEWAKrSDVEVILT--VDRAEEgwtgnvglVTDLLPELTLDPDN--------TVAIVCGPPIMMR 203
                       170
                ....*....|....*...
gi 24655635 515 AALDILSQLDVKANQIHV 532
Cdd:cd06221 204 FVAKELLKLGVPEEQIWV 221
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
297-531 4.31e-12

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. 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 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: 99809  Cd Length: 227  Bit Score: 65.80  E-value: 4.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 297 VVHSKDFNHDSFELCLQSvgqKVLMVLPAGYHVDIEVPLEGRViqRSY---TPVDhtylrlenirssRSECLHFLIKRYP 373
Cdd:cd06213   5 IVAQERLTHDIVRLTVQL---DRPIAYKAGQYAELTLPGLPAA--RSYsfaNAPQ------------GDGQLSFHIRKVP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 374 NGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTAHrnILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDI 452
Cdd:cd06213  68 GGAFSGWLfGADRTGERLTVRGPFGDFWLRPGDAP--ILCIAGGSGLAPILAILEQARAAGTKR--DVTLLFGARTQRDL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 453 WlkeKLHELHTDDE----RFSCTNYVS-QSEDNPQRIALELLAPLFQKNQPERCTYVLiCGPSGFNTAALDILSQLDVKA 527
Cdd:cd06213 144 Y---ALDEIAAIAArwrgRFRFIPVLSeEPADSSWKGARGLVTEHIAEVLLAATEAYL-CGPPAMIDAAIAVLRALGIAR 219

                ....
gi 24655635 528 NQIH 531
Cdd:cd06213 220 EHIH 223
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
292-531 4.44e-12

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 65.69  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 292 TFEYEVVHSKDFNHDSFELCLQSVGQKVLMVLPaGYHVDIEVPleGRVIQRSYTPvdhtylrlenirSSRSECLH--FLI 369
Cdd:cd06209   1 TFEATVTEVERLSDSTIGLTLELDEAGALAFLP-GQYVNLQVP--GTDETRSYSF------------SSAPGDPRleFLI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 370 KRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTahRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKT 448
Cdd:cd06209  66 RLLPGGAMSSYLrDRAQPGDRLTLTGPLGSFYLREVK--RPLLMLAGGTGLAPFLSMLDVLAEDGSAH--PVHLVYGVTR 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 449 NEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQRI--ALELLAPLfQKNQPERCTYvlICGPSGFNTAALDILSQLDVK 526
Cdd:cd06209 142 DADLVELDRLEALAERLPGFSFRTVVADPDSWHPRKgyVTDHLEAE-DLNDGDVDVY--LCGPPPMVDAVRSWLDEQGIE 218

                ....*
gi 24655635 527 ANQIH 531
Cdd:cd06209 219 PANFY 223
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
304-399 1.07e-11

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 61.44  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   304 NHDSFELCLQSVGQKVLMVLPAGYHVDIEVPLEGRVIQRSYTPVdhtylrlenirSSRSEC--LHFLIKRYPNGPVSSHL 381
Cdd:pfam00970  11 SHDTRIFRFALPHPDQVLGLPVGQHLFLRLPIDGELVIRSYTPI-----------SSDDDKgyLELLVKVYPGGKMSQYL 79
                          90
                  ....*....|....*...
gi 24655635   382 QKLETGSRVHWSAPRGSF 399
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRF 97
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
365-530 1.16e-11

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: 64.18  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 365 LHFLIKRYPN-GPVSSHLQKLETGSRVHWSAPRGSFQLsdltaHRNILLLAAGSGLTPILSLIQPILKRNtnRIESLQLL 443
Cdd:cd06196  61 LEFVIKSYPDhDGVTEQLGRLQPGDTLLIEDPWGAIEY-----KGPGVFIAGGAGITPFIAILRDLAAKG--KLEGNTLI 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 444 YFNKTNEDIWLKEKLHELHTDDerfsCTNYVSQSEDNP---QRIALELLAplfQKNQPERCTYvLICGPSGFNTAALDIL 520
Cdd:cd06196 134 FANKTEKDIILKDELEKMLGLK----FINVVTDEKDPGyahGRIDKAFLK---QHVTDFNQHF-YVCGPPPMEEAINGAL 205
                       170
                ....*....|
gi 24655635 521 SQLDVKANQI 530
Cdd:cd06196 206 KELGVPEDSI 215
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
292-532 8.53e-10

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 59.28  E-value: 8.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 292 TFEYEVVHSKDFNHDSFELCLQSVGQKVLMV---LPAGYHVDIEVPleGRVIQRSYTPVDhtylrLENIRSSrsecLHFL 368
Cdd:cd06210   1 VREAEIVAVDRVSSNVVRLRLQPDDAEGAGIaaeFVPGQFVEIEIP--GTDTRRSYSLAN-----TPNWDGR----LEFL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 369 IKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDlTAHRNILLLAAGSGLTPILSLIQPILKRNTNrieSLQLLYFNK 447
Cdd:cd06210  70 IRLLPGGAFSTYLeTRAKVGQRLNLRGPLGAFGLRE-NGLRPRWFVAGGTGLAPLLSMLRRMAEWGEP---QEARLFFGV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 448 TNED-IWLKEKLHELHTDDERFSCTNYVSQSEDN---PQRIALELLAPLFQKNQPERCTYVliCGPSGFNTAALDILSQL 523
Cdd:cd06210 146 NTEAeLFYLDELKRLADSLPNLTVRICVWRPGGEwegYRGTVVDALREDLASSDAKPDIYL--CGPPGMVDAAFAAAREA 223

                ....*....
gi 24655635 524 DVKANQIHV 532
Cdd:cd06210 224 GVPDEQVYL 232
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
365-531 1.08e-09

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 58.80  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 365 LHFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTAhRNILLLAAGSGLTPILSLIQPILKRNTNRIESLQLL 443
Cdd:cd06190  55 WEFIIKRKPGGAASNALfDNLEPGDELELDGPYGLAYLRPDED-RDIVCIAGGSGLAPMLSILRGAARSPYLSDRPVDLF 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 444 YFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ--------RIAlELLAPLFQKNQPERCTYVliCGPSGFNTA 515
Cdd:cd06190 134 YGGRTPSDLCALDELSALVALGARLRVTPAVSDAGSGSAagwdgptgFVH-EVVEATLGDRLAEFEFYF--AGPPPMVDA 210
                       170
                ....*....|....*..
gi 24655635 516 ALDIL-SQLDVKANQIH 531
Cdd:cd06190 211 VQRMLmIEGVVPFDQIH 227
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
327-531 1.58e-09

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The 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 of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 58.85  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 327 YHVDIEVPLEGRVIQRSYTPVDHTYlRLENiRSSRSECLHFLIK---------RYPNGPVSSHLQKLETGSRVHWSAPRG 397
Cdd:cd06188  65 YRADWDKFGLWQLVFKHDEPVSRAY-SLAN-YPAEEGELKLNVRiatpppgnsDIPPGIGSSYIFNLKPGDKVTASGPFG 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 398 SFQLSDltAHRNILLLAAGSGLTPILSLIQPILKR-NTNRieSLQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVS- 475
Cdd:cd06188 143 EFFIKD--TDREMVFIGGGAGMAPLRSHIFHLLKTlKSKR--KISFWYGARSLKELFYQEEFEALEKEFPNFKYHPVLSe 218
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24655635 476 -QSEDNPQ----RIALELLAPLFQKN-QPERCTYVLiCGPSGFNTAALDILSQLDVKANQIH 531
Cdd:cd06188 219 pQPEDNWDgytgFIHQVLLENYLKKHpAPEDIEFYL-CGPPPMNSAVIKMLDDLGVPRENIA 279
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
288-531 1.81e-09

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: 58.10  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 288 LHDETFEYEVVHSKDFNHDSFELCLQSVGQKVlMVLPAGYHVDIEVPleGRVIQRSYTpvdhtylrlenIRSSRSECLH- 366
Cdd:cd06211   2 LNVKDFEGTVVEIEDLTPTIKGVRLKLDEPEE-IEFQAGQYVNLQAP--GYEGTRAFS-----------IASSPSDAGEi 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 367 -FLIKRYPNGPVSSHLQK-LETGSRVHWSAPRGSFQLSDlTAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLY 444
Cdd:cd06211  68 eLHIRLVPGGIATTYVHKqLKEGDELEISGPYGDFFVRD-SDQRPIIFIAGGSGLSSPRSMILDLLERGDTR--KITLFF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 445 FNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQ-----RIALELLAPLFQKNQPERCTYvlICGPSGFNTAALDI 519
Cdd:cd06211 145 GARTRAELYYLDEFEALEKDHPNFKYVPALSREPPESNwkgftGFVHDAAKKHFKNDFRGHKAY--LCGPPPMIDACIKT 222
                       250
                ....*....|..
gi 24655635 520 LSQLDVKANQIH 531
Cdd:cd06211 223 LMQGRLFERDIY 234
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
342-512 1.94e-09

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: 58.05  E-value: 1.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 342 RSYTPVDhtylrleniRSSRSECLHFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAGSGLT 420
Cdd:cd06194  40 RSYSPTS---------LPDGDNELEFHIRRKPNGAFSGWLgEEARPGHALRLQGPFGQAFYRPEYGEGPLLLVGAGTGLA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 421 PILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQRIALELLAPLfqknQPE- 499
Cdd:cd06194 111 PLWGIARAALRQGHQG--EIRLVHGARDPDDLYLHPALLWLAREHPNFRYIPCVSEGSQGDPRVRAGRIAAH----LPPl 184
                       170
                ....*....|....
gi 24655635 500 -RCTYVLICGPSGF 512
Cdd:cd06194 185 tRDDVVYLCGAPSM 198
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
412-518 4.05e-09

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 54.19  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   412 LLAAGSGLTPILSLIQPILKRNTNRIESLqLLYFNKTNEDIWLKEKLHEL-HTDDERFSCTNYVSQSEDNPQ----RIAL 486
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAILEDPKDPTQVV-LVFGNRNEDDILYREELDELaEKHPGRLTVVYVVSRPEAGWTggkgRVQD 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 24655635   487 ELLAPLFQKNQPErcTYVLICGPSGFNTAALD 518
Cdd:pfam00175  80 ALLEDHLSLPDEE--THVYVCGPPGMIKAVRK 109
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
382-531 5.85e-09

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: 56.50  E-value: 5.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 382 QKLETGSRVHWSAPRGSFQLSDltAHRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLLYFNKTNEDIWLKEKL--- 458
Cdd:cd06198  72 ERLKPGTRVTVEGPYGRFTFDD--RRARQIWIAGGIGITPFLALLEALAARGDAR--PVTLFYCVRDPEDAVFLDELral 147
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655635 459 -----HELHTDDERfsctnyvsqsEDNPQRIALELLAPLFQKNQPErctyVLICGPSGFNTAALDILSQLDVKANQIH 531
Cdd:cd06198 148 aaaagVVLHVIDSP----------SDGRLTLEQLVRALVPDLADAD----VWFCGPPGMADALEKGLRALGVPARRFH 211
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
348-531 1.63e-08

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 56.26  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  348 DHTyLRLENIRSS--RSECLHFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTAHRnILLLAAGSGLTPILS 424
Cdd:PRK10684  51 AET-LRAYTLSSTpgVSEFITLTVRRIDDGVGSQWLtRDVKRGDYLWLSDAMGEFTCDDKAEDK-YLLLAAGCGVTPIMS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  425 LIQPILKrntNRIES-LQLLYFNKTNEDIWLKEKLHELHTDDERFSCTnYVSQSEDNPQRIALELLAPLFQKNQPERCTY 503
Cdd:PRK10684 129 MRRWLLK---NRPQAdVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLT-LVAENNATEGFIAGRLTRELLQQAVPDLASR 204
                        170       180
                 ....*....|....*....|....*....
gi 24655635  504 -VLICGPSGFNTAALDILSQLDVKANQIH 531
Cdd:PRK10684 205 tVMTCGPAPYMDWVEQEVKALGVTADRFF 233
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
93-169 4.98e-08

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 55.47  E-value: 4.98e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24655635   93 TELARHNKIDDAWMAIRGRVFNVTRYMDFHPGGvDELMRGVGRDATKLFDEVHAWVNYpQLLGKCYVGPLKDNETKP 169
Cdd:PLN03198 109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGG-SVISTYFGRDGTDAFSSFHAASTW-KILQDFYIGDVDNVEPTP 183
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
361-509 1.02e-06

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 50.58  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  361 RSECLHFLIKRYpnGPVSSHLQKLETGSRVHWSAPRGS-FQLSDLTAHrNILLLAAGSGLTPILSLIQPILKrNTNRIES 439
Cdd:PRK08345  64 RKGFFELCIRRA--GRVTTVIHRLKEGDIVGVRGPYGNgFPVDEMEGM-DLLLIAGGLGMAPLRSVLLYAMD-NRWKYGN 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  440 LQLLYFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQSEDNPQRIALE-----------LLAPLFQKNQPERCTYVLICG 508
Cdd:PRK08345 140 ITLIYGAKYYEDLLFYDELIKDLAEAENVKIIQSVTRDPEWPGCHGLPqgfiervckgvVTDLFREANTDPKNTYAAICG 219

                 .
gi 24655635  509 P 509
Cdd:PRK08345 220 P 220
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
402-513 2.14e-05

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 45.76  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 402 SDLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRIeSLQLLYF----NKTNEDIWLKEKLHELHTDDERFSCTNYVSQs 477
Cdd:cd06186 101 EDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKTS-RTRRVKLvwvvRDREDLEWFLDELRAAQELEVDGEIEIYVTR- 178
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 24655635 478 ednpqrialellaplfqknqperctyVLICGPSGFN 513
Cdd:cd06186 179 --------------------------VVVCGPPGLV 188
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
407-479 5.77e-05

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 43.48  E-value: 5.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24655635   407 HRNILLLAAGSGLTPILSLIQPILKR-NTNRIESLQLLYFNKTNEDI-WLKEKLHEL-HTDDERFSCTNYVSQSED 479
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKsKKLKTKKIKFYWVVRDLSSLeWFKDVLNELeELKELNIEIHIYLTGEYE 76
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
403-454 6.21e-05

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 45.99  E-value: 6.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24655635  403 DLTAHRNILLLAAGSGLTPILSLIQPILKRNTNRIES---LQLLYFNKTNEDIWL 454
Cdd:PLN02844 419 DFLRYDSLLLVAGGIGITPFLSILKEIASQSSSRYRFpkrVQLIYVVKKSQDICL 473
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
365-509 2.01e-04

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 43.58  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  365 LHFLIKRYPNGPVSSHL-QKLETGSRVHWSAPRGSFQLSDLTahRNILLLAAGSGLTPILSLIQPILKRNTNRieSLQLL 443
Cdd:PRK11872 168 LQFLIRLLPDGVMSNYLrERCQVGDEILFEAPLGAFYLREVE--RPLVFVAGGTGLSAFLGMLDELAEQGCSP--PVHLY 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655635  444 YFNKTNEDIWLKEKLHELHTDDERFSCTNYVSQ-SEDNPQRIAleLLAPLFQKNQ-PERCTYVLICGP 509
Cdd:PRK11872 244 YGVRHAADLCELQRLAAYAERLPNFRYHPVVSKaSADWQGKRG--YIHEHFDKAQlRDQAFDMYLCGP 309
p23_like cd06463
Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) ...
192-274 4.52e-04

Proteins containing this p23_like domain include p23 and its Saccharomyces cerevisiae (Sc) homolog Sba1. Both are co-chaperones for the heat shock protein (Hsp) 90. p23 binds Hsp90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis. Both p23 and Sba1p can regulate telomerase activity. This group includes domains similar to the C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1). Sgt1 interacts with multiple protein complexes and has the features of a co-chaperone. Human (h) Sgt1 interacts with both Hsp70 and Hsp90, and has been shown to bind Hsp90 through its CS domain. Saccharomyces cerevisiae (Sc) Sgt1 is a subunit of both core kinetochore and SCF (Skp1-Cul1-F-box) ubiquitin ligase complexes. Sgt1 is required for pathogen resistance in plants. This group also includes the p23_like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR). hB-ind1 plays a role in the signaling pathway mediated by the small GTPase Rac1, NUDC is needed for nuclear movement, Melusin interacts with two splice variants of beta1 integrin, and NCB5OR plays a part in maintaining viable pancreatic beta cells.


Pssm-ID: 107220  Cd Length: 84  Bit Score: 39.19  E-value: 4.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 192 WIQQRSELTLIFYTRSLANPGLVVRRKDlQQLSVRVLV-QHNWHSFDFQLTNNVEwpPKLAKIGSETGKIELVFVK-EEA 269
Cdd:cd06463   1 WYQTLDEVTITIPLKDVTKKDVKVEFTP-KSLTVSVKGgGGKEYLLEGELFGPID--PEESKWTVEDRKIEITLKKkEPG 77

                ....*
gi 24655635 270 EPWPT 274
Cdd:cd06463  78 EWWPR 82
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
352-526 4.54e-04

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 42.68  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  352 LRLENIRSSR------SECLHFLIKR--YPN-------GPVSSHLQKLETGSRVHWSAPRGSFQLSDLTAHRNILLLAAG 416
Cdd:PLN03115 145 LRLYSIASSAlgdfgdSKTVSLCVKRlvYTNdqgeivkGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLATG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635  417 SGLTPILSLIQPIL--KRNTNRIESLQLLYFN-KTNEDIWLKEKLHEL-HTDDERFSCTNYVSQSEDNPQ--------RI 484
Cdd:PLN03115 225 TGIAPFRSFLWKMFfeKHDDYKFNGLAWLFLGvPTSSSLLYKEEFEKMkEKAPENFRLDFAVSREQTNAKgekmyiqtRM 304
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24655635  485 A--LELLAPLFQKNQpercTYVLICGPSGFNTAALDILSQLDVK 526
Cdd:PLN03115 305 AeyAEELWELLKKDN----TYVYMCGLKGMEKGIDDIMVSLAAK 344
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
408-509 1.70e-03

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 41.30  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635   408 RNILLLAAGSGLTPILSLIQPILKRN-TNRIESLQLLYFNKTNEDIWLKEKLHELHTDD-ERFSCT----NYVSQSEDNP 481
Cdd:PTZ00306 1032 RKLALIAGGTGVAPMLQIIRAALKKPyVDSIESIRLIYAAEDVSELTYRELLESYRKENpGKFKCHfvlnNPPEGWTDGV 1111
                          90       100
                  ....*....|....*....|....*...
gi 24655635   482 QRIALELLAPLFQKnqPERCTYVLICGP 509
Cdd:PTZ00306 1112 GFVDRALLQSALQP--PSKDLLVAICGP 1137
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
370-510 1.80e-03

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.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 40.72  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 370 KRYPNGPVSSHLQKLETGSRVHWSAPRGSFQL-SDLTAhrNILLLAAGSGLTPILSLIQP--ILKRNTNRIESLqLLYF- 445
Cdd:cd06207 194 GRSRYGLCSSYLAGLKVGQRVTVFIKKSSFKLpKDPKK--PIIMVGPGTGLAPFRAFLQEraALLAQGPEIGPV-LLYFg 270
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655635 446 NKT-NEDIWLKEKLHELHTDDerfSCTN-YVSQSEDNPQRI--------ALELLAPLFQknqpERCTYVLICGPS 510
Cdd:cd06207 271 CRHeDKDYLYKEELEEYEKSG---VLTTlGTAFSRDQPKKVyvqdlireNSDLVYQLLE----EGAGVIYVCGST 338
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
367-527 2.07e-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: 39.92  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 367 FLIKRYpnGPVSSHLQKLETGSRVHWSAPRGS-FQLSDltahRNILLLAAGSGLTPILsliqPILKRNTNRIESLQLLYF 445
Cdd:cd06220  53 ITVKKV--GEATSALHDLKEGDKLGIRGPYGNgFELVG----GKVLLIGGGIGIAPLA----PLAERLKKAADVTVLLGA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655635 446 nKTNEDIWLKEKL---HELH--TDDERFSCTNYVSqsednpqrialELLAPLFQKNqPERctyVLICGPSGFNTAALDIL 520
Cdd:cd06220 123 -RTKEELLFLDRLrksDELIvtTDDGSYGFKGFVT-----------DLLKELDLEE-YDA---IYVCGPEIMMYKVLEIL 186

                ....*..
gi 24655635 521 SQLDVKA 527
Cdd:cd06220 187 DERGVRA 193
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure