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Conserved domains on  [gi|1352513|sp|P35228|]
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RecName: Full=Nitric oxide synthase, inducible; AltName: Full=Hepatocyte NOS; Short=HEP-NOS; AltName: Full=Inducible NO synthase; Short=Inducible NOS; Short=iNOS; AltName: Full=NOS type II; AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2

Protein Classification

NADPH cytochrome P450 oxidoreductase family protein; NADPH--cytochrome P450 reductase( domain architecture ID 10092407)

NADPH cytochrome P450 oxidoreductase family protein may serve as an electron donor in several oxygenase systems, catalyzing the transfer of two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN| NADPH--cytochrome P450 reductase, also called NADPH--hemoprotein reductase, is required for electron transfer from NADP to cytochrome P450 in microsomes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
84-496 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


:

Pssm-ID: 238410  Cd Length: 412  Bit Score: 935.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    84 HVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPtPPDELLPQAIEFVNQYYGSFKEAKIEEHL 163
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGR-PKEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   164 ARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSA 243
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   244 ITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPP 323
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   324 DLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLET 403
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   404 HKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNY 483
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 1352513   484 VLSPFYYYQVEAW 496
Cdd:cd00795  400 VLSPSYEYQPDPW 412
FNR_like super family cl06868
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
736-1132 0e+00

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


The actual alignment was detected with superfamily member cd06202:

Pssm-ID: 447143 [Multi-domain]  Cd Length: 406  Bit Score: 640.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   736 RLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGS---- 811
Cdd:cd06202    1 KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERSTalgi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   812 --YWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQ-PSEYSKWKFTNSPTFLEVLEEFPS 888
Cdd:cd06202   81 ikTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKgSSEYEDWKWYKNPNILEVLEEFPS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   889 LRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFH 968
Cdd:cd06202  161 LQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   969 LPEDPSHPCILIGPGTGIAPFRSFWQQRLHD---SQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAY 1045
Cdd:cd06202  241 LPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDlrmSEDPGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTAL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1046 SRLPGKPKVYVQDILRQQlASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHE 1125
Cdd:cd06202  321 SREPGKPKTYVQDLLKEQ-AESVYDALVREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHE 399

                 ....*..
gi 1352513  1126 DIFGAVF 1132
Cdd:cd06202  400 DIFGVTL 406
Flavodoxin_1 pfam00258
Flavodoxin;
541-672 1.36e-36

Flavodoxin;


:

Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 134.80  E-value: 1.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     541 ILFATETGKSEALAWDLGALF-SCAFNPKVVCMDKYR--LSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELN- 616
Cdd:pfam00258    1 IFYGSQTGNTEKLAEAIAEGLgEAGFEVDVVDLDDVDetLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLEd 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352513     617 ---NKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDEL---SGQEDAFRSW 672
Cdd:pfam00258   81 gdlSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
 
Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
84-496 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


Pssm-ID: 238410  Cd Length: 412  Bit Score: 935.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    84 HVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPtPPDELLPQAIEFVNQYYGSFKEAKIEEHL 163
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGR-PKEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   164 ARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSA 243
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   244 ITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPP 323
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   324 DLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLET 403
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   404 HKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNY 483
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 1352513   484 VLSPFYYYQVEAW 496
Cdd:cd00795  400 VLSPSYEYQPDPW 412
NO_synthase pfam02898
Nitric oxide synthase, oxygenase domain;
135-497 0e+00

Nitric oxide synthase, oxygenase domain;


Pssm-ID: 460742  Cd Length: 362  Bit Score: 755.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     135 PPDELLPQAIEFVNQYYGSFKEAkIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDA 214
Cdd:pfam02898    1 PKEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     215 RSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLG 294
Cdd:pfam02898   80 RHVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     295 WKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYM 374
Cdd:pfam02898  160 WKGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYM 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     375 GTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSR 454
Cdd:pfam02898  240 GTEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAG 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1352513     455 GGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWK 497
Cdd:pfam02898  320 RGCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPWK 362
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
736-1132 0e+00

The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.


Pssm-ID: 99799 [Multi-domain]  Cd Length: 406  Bit Score: 640.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   736 RLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGS---- 811
Cdd:cd06202    1 KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERSTalgi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   812 --YWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQ-PSEYSKWKFTNSPTFLEVLEEFPS 888
Cdd:cd06202   81 ikTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKgSSEYEDWKWYKNPNILEVLEEFPS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   889 LRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFH 968
Cdd:cd06202  161 LQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   969 LPEDPSHPCILIGPGTGIAPFRSFWQQRLHD---SQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAY 1045
Cdd:cd06202  241 LPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDlrmSEDPGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTAL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1046 SRLPGKPKVYVQDILRQQlASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHE 1125
Cdd:cd06202  321 SREPGKPKTYVQDLLKEQ-AESVYDALVREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHE 399

                 ....*..
gi 1352513  1126 DIFGAVF 1132
Cdd:cd06202  400 DIFGVTL 406
COG4362 COG4362
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
134-492 0e+00

Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];


Pssm-ID: 443495  Cd Length: 360  Bit Score: 571.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   134 TPPDELLPQAIEFVNQYYGSFKEAKiEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFD 213
Cdd:COG4362    1 TEQEALLAEAEEFLRQCYKELGKSE-EEVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   214 ARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDL 293
Cdd:COG4362   80 RRHVTTPEEVFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   294 GWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWY 373
Cdd:COG4362  160 GWRGPRTAFDVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   374 MGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRS 453
Cdd:COG4362  240 MGTEIGARNLADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKA 319
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 1352513   454 RGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQ 492
Cdd:COG4362  320 GREVTGDWSWLIPPMSGATTHVFHRYYDNEILKPNFFYQ 358
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
532-1128 9.76e-156

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 476.18  E-value: 9.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   532 TMASRVRVTILFATETGKSEALAWDLGA-LFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLF 610
Cdd:COG0369   22 AAAAGTPLTILYGSQTGNAEGLAEQLAErAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFLH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   611 MLKE--LNNkFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDelSGQEDAFRSW---AVQTFKAACETFD 685
Cdd:COG0369  102 SKKApkLDG-LRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWlaaVLAALAEALGAAA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   686 VRGKQHIQIPKLYTSnvtwdphhyrlvqdsqpldlskalssmhaKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGqGL 765
Cdd:COG0369  179 AAAAAAAAAAPAYSR-----------------------------KNPFPATVLENRELTGRGSAKETRHIEIDLPGS-GL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   766 NYLPGEHLGVCPGNQPALVQGILERVvdGPTPHQTVRLEalDEsgsywvsdkrlpPCSLSQALTYFLDITTPPTQLLlQK 845
Cdd:COG0369  229 SYEPGDALGVWPENDPALVDELLARL--GLDGDEPVTLD--GE------------PLSLREALTEHLELTRLTPPLL-EK 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   846 LAQvATEEPErqrLEALCQPSEYSKWK-FTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLT 924
Cdd:COG0369  292 YAE-LTGNAE---LAALLADEDKAALReYLAGRQLLDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLT 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   925 VAVVTYHTrdgQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRlhdsQHKG 1004
Cdd:COG0369  368 VGVVRYEA---SGRERKGVASTYLADLEEGDTVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQER----EARG 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1005 VRgGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLpGKPKVYVQDILRQQlASEVLRVLhKEPGHLYVCGD 1084
Cdd:COG0369  441 AS-GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRD-QAEKIYVQHRLLEQ-GAELWAWL-EEGAHVYVCGD 516
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 1352513  1085 V-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:COG0369  517 AsRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
726-947 1.63e-100

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 316.97  E-value: 1.63e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     726 SMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDgQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEA 805
Cdd:pfam00667    1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISG-SGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     806 LDEsgsyWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPS---EYSKWKFTNSPTFLEV 882
Cdd:pfam00667   80 LDE----RVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAgarEYKRWKLNHAPTLLEV 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352513     883 LEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTrDGQGPLHHGVCSTW 947
Cdd:pfam00667  156 LEEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYET-DGEGRIHYGVCSNW 219
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
534-1128 3.53e-77

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 266.59  E-value: 3.53e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    534 ASRVRVTILFATETGKSEALAWDL-GALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFML 612
Cdd:PRK10953   59 AEMPGITLISASQTGNARRVAEQLrDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    613 K--ELNNKfRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD-ELSGQEDAFRSWAVQTFKAacetfdvrgk 689
Cdd:PRK10953  139 KapKLENT-AFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDADvEYQAAASEWRARVVDALKS---------- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    690 qhiQIPKLYTSnvtwdphhyrlVQDSQPLDLSKALSSMHAKNV-FTMRLKSRQNLQSPTSSRATILVELSCEDgQGLNYL 768
Cdd:PRK10953  208 ---RAPAVAAP-----------SQSVATGAVNEIHTSPYSKEApLTASLSVNQKITGRNSEKDVRHIEIDLGD-SGLRYQ 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    769 PGEHLGVCPGNQPALVQGILErvvdgptphqtvrLEALDESGSYWVSDKRLPpcsLSQALTYFLDITTPpTQLLLQKLAQ 848
Cdd:PRK10953  273 PGDALGVWYQNDPALVKELVE-------------LLWLKGDEPVTVDGKTLP---LAEALQWHFELTVN-TANIVENYAT 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    849 VATEEperqRLEALC----QPSEYSKwkftNSPtFLEVLEEFPSlRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLT 924
Cdd:PRK10953  336 LTRSE----TLLPLVgdkaALQHYAA----TTP-IVDMVRFAPA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHIT 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    925 VAVVTYhtrDGQGPLHHGVCSTWL-NSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQhk 1003
Cdd:PRK10953  406 VGVVRY---DIEGRARAGGASSFLaDRLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGA-- 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   1004 gvrGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRlPGKPKVYVQDILRQQLAsEVLRVLhKEPGHLYVCG 1083
Cdd:PRK10953  481 ---PGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSR-DQKEKIYVQDKLREQGA-ELWRWI-NDGAHIYVCG 554
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 1352513   1084 DV-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:PRK10953  555 DAnRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
Flavodoxin_1 pfam00258
Flavodoxin;
541-672 1.36e-36

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 134.80  E-value: 1.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     541 ILFATETGKSEALAWDLGALF-SCAFNPKVVCMDKYR--LSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELN- 616
Cdd:pfam00258    1 IFYGSQTGNTEKLAEAIAEGLgEAGFEVDVVDLDDVDetLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLEd 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352513     617 ---NKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDEL---SGQEDAFRSW 672
Cdd:pfam00258   81 gdlSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
PRK08105 PRK08105
flavodoxin; Provisional
582-660 4.80e-09

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 56.05  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    582 EERLLLVVTSTFGNGDCPGN----GEKLKKSLFMLKELnnkfRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMG 657
Cdd:PRK08105   48 QDELVLVVTSTTGQGDLPDSivplFQALKDTAGYQPNL----RYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERL 123

                  ...
gi 1352513    658 EGD 660
Cdd:PRK08105  124 EID 126
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
539-650 1.29e-04

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 42.97  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   539 VTILFATETGKSEALAWDLGALFScAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGnGDCPGNGEKLKKSLfmLKELNNK 618
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAEALG-AAGVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDFLEEL--KEDLSGK 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 1352513   619 fRYAVFGLG-SSMYPRfcaFAHDIDQKLSHLGA 650
Cdd:COG0716   77 -KVALFGTGdSSGYGD---ALGELKELLEEKGA 105
 
Name Accession Description Interval E-value
NOS_oxygenase_euk cd00795
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
84-496 0e+00

Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.


Pssm-ID: 238410  Cd Length: 412  Bit Score: 935.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    84 HVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPtPPDELLPQAIEFVNQYYGSFKEAKIEEHL 163
Cdd:cd00795    1 FVRVKNWETGSILYDTLHSKATQDGPCTERRCLGSIMDPKKLTRRPRDGR-PKEELLPQAKDFINQYYSSIKRSGSEAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   164 ARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSA 243
Cdd:cd00795   80 ARLEEVTKEIEATGTYQLTEDELIFGAKQAWRNAPRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   244 ITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPP 323
Cdd:cd00795  160 ITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   324 DLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLET 403
Cdd:cd00795  240 ELVLEVPIEHPKYEWFKELGLKWYALPAVSNMLLEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   404 HKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNY 483
Cdd:cd00795  320 RKTSSLWKDKALVEINVAVLHSFQKANVTIVDHHSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNY 399
                        410
                 ....*....|...
gi 1352513   484 VLSPFYYYQVEAW 496
Cdd:cd00795  400 VLSPSYEYQPDPW 412
NOS_oxygenase cd00575
Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron ...
138-492 0e+00

Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOSs also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. While prokaryotes can produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS, a few prokaryotes also have a NOS which consists solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.


Pssm-ID: 238321  Cd Length: 356  Bit Score: 789.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   138 ELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSC 217
Cdd:cd00575    1 ELLPQAKDFINQYYSSIKRSGSEAHEARLEEVEKEIEATGTYQLTEEELIYGAKMAWRNAPRCIGRIQWSKLQVFDARDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   218 STAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKP 297
Cdd:cd00575   81 TTAQEMFEAICNHIKYATNGGNIRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIQLGWKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   298 KYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTE 377
Cdd:cd00575  161 KGGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFAELGLKWYALPAVSNMLLEIGGLEFPAAPFNGWYMGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   378 IGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGC 457
Cdd:cd00575  241 IGVRNLCDTQRYNILEKVARKMGLDTRKNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAESFMKHLENEYRARGGC 320
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 1352513   458 PADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQ 492
Cdd:cd00575  321 PADWVWLVPPMSGSLTPVFHQEMLNYVLSPSFFYQ 355
NO_synthase pfam02898
Nitric oxide synthase, oxygenase domain;
135-497 0e+00

Nitric oxide synthase, oxygenase domain;


Pssm-ID: 460742  Cd Length: 362  Bit Score: 755.14  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     135 PPDELLPQAIEFVNQYYGSFKEAkIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDA 214
Cdd:pfam02898    1 PKEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     215 RSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLG 294
Cdd:pfam02898   80 RHVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     295 WKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYM 374
Cdd:pfam02898  160 WKGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYM 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     375 GTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSR 454
Cdd:pfam02898  240 GTEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAG 319
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1352513     455 GGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWK 497
Cdd:pfam02898  320 RGCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPWK 362
Nitric_oxide_synthase cd06202
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ...
736-1132 0e+00

The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.


Pssm-ID: 99799 [Multi-domain]  Cd Length: 406  Bit Score: 640.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   736 RLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGS---- 811
Cdd:cd06202    1 KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERSTalgi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   812 --YWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQ-PSEYSKWKFTNSPTFLEVLEEFPS 888
Cdd:cd06202   81 ikTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKgSSEYEDWKWYKNPNILEVLEEFPS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   889 LRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFH 968
Cdd:cd06202  161 LQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   969 LPEDPSHPCILIGPGTGIAPFRSFWQQRLHD---SQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAY 1045
Cdd:cd06202  241 LPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDlrmSEDPGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTAL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1046 SRLPGKPKVYVQDILRQQlASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHE 1125
Cdd:cd06202  321 SREPGKPKTYVQDLLKEQ-AESVYDALVREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHE 399

                 ....*..
gi 1352513  1126 DIFGAVF 1132
Cdd:cd06202  400 DIFGVTL 406
COG4362 COG4362
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
134-492 0e+00

Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];


Pssm-ID: 443495  Cd Length: 360  Bit Score: 571.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   134 TPPDELLPQAIEFVNQYYGSFKEAKiEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFD 213
Cdd:COG4362    1 TEQEALLAEAEEFLRQCYKELGKSE-EEVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   214 ARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDL 293
Cdd:COG4362   80 RRHVTTPEEVFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   294 GWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWY 373
Cdd:COG4362  160 GWRGPRTAFDVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   374 MGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRS 453
Cdd:COG4362  240 MGTEIGARNLADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKA 319
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 1352513   454 RGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQ 492
Cdd:COG4362  320 GREVTGDWSWLIPPMSGATTHVFHRYYDNEILKPNFFYQ 358
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
532-1128 9.76e-156

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 476.18  E-value: 9.76e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   532 TMASRVRVTILFATETGKSEALAWDLGA-LFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLF 610
Cdd:COG0369   22 AAAAGTPLTILYGSQTGNAEGLAEQLAErAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFLH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   611 MLKE--LNNkFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDelSGQEDAFRSW---AVQTFKAACETFD 685
Cdd:COG0369  102 SKKApkLDG-LRYAVLGLGDSSYETFCQTGKDFDARLEELGATRLLPRVDCD--VDYEEAAEAWlaaVLAALAEALGAAA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   686 VRGKQHIQIPKLYTSnvtwdphhyrlvqdsqpldlskalssmhaKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGqGL 765
Cdd:COG0369  179 AAAAAAAAAAPAYSR-----------------------------KNPFPATVLENRELTGRGSAKETRHIEIDLPGS-GL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   766 NYLPGEHLGVCPGNQPALVQGILERVvdGPTPHQTVRLEalDEsgsywvsdkrlpPCSLSQALTYFLDITTPPTQLLlQK 845
Cdd:COG0369  229 SYEPGDALGVWPENDPALVDELLARL--GLDGDEPVTLD--GE------------PLSLREALTEHLELTRLTPPLL-EK 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   846 LAQvATEEPErqrLEALCQPSEYSKWK-FTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLT 924
Cdd:COG0369  292 YAE-LTGNAE---LAALLADEDKAALReYLAGRQLLDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLT 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   925 VAVVTYHTrdgQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRlhdsQHKG 1004
Cdd:COG0369  368 VGVVRYEA---SGRERKGVASTYLADLEEGDTVPVFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQER----EARG 440
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1005 VRgGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLpGKPKVYVQDILRQQlASEVLRVLhKEPGHLYVCGD 1084
Cdd:COG0369  441 AS-GKNWLFFGDRHFTTDFLYQTELQAWLKDGVLTRLDLAFSRD-QAEKIYVQHRLLEQ-GAELWAWL-EEGAHVYVCGD 516
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 1352513  1085 V-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:COG0369  517 AsRMAKDVDAALLDIIAEHGGLSEEEAEEYLAELRAEKRYQRDVY 561
NOS_oxygenase_prok cd00794
Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by ...
139-492 2.21e-151

Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. Nitric oxide synthases are homodimers. Most prokaryotes produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS. However, a few prokaryotes also have a NOS, consisting solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.


Pssm-ID: 238409  Cd Length: 353  Bit Score: 456.51  E-value: 2.21e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   139 LLPQAIEFVNQYYgsfKEAKIEEHLA-RVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSC 217
Cdd:cd00794    2 LFKEARAFLTNMY---EELGETGELNkRLAAVESEIDETGTYTHTTEELVYGAKMAWRNSNRCIGRLFWESLNVRDARDV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   218 STAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIrGDPANVEFTQLCIDLGWKP 297
Cdd:cd00794   79 RTEEEVAEALLDHITEATNGGKIRPYITIFAPEAPGKDGPRIWNNQLIRYAGYERPGANI-GDPASAKFTRLAERLGWKG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   298 KYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTE 377
Cdd:cd00794  158 KGTNFDVLPLIIQLPGDRPKWFELPNDAVKEVPITHPHYPKIRKLGLKWYAVPIISDMDLEIGGIHYPAAPFNGWYMGTE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   378 IGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGC 457
Cdd:cd00794  238 IGARNLADEYRYNLLPKVAEALGLDTLKNRSLWKDRALVELNVAVLHSFKKAGVSIVDHHTAAKQFERFEEREARAGRKV 317
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 1352513   458 PADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQ 492
Cdd:cd00794  318 TGKWSWLIPPLSPATTHIFHRGYDNTEVHPNFFYQ 352
CYPOR cd06204
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
729-1127 1.49e-103

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: 99801 [Multi-domain]  Cd Length: 416  Bit Score: 332.68  E-value: 1.49e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   729 AKNVFTMRLKSRQNLQSPtSSRATILVELSCeDGQGLNYLPGEHLGVCPGNQPALVQgILERVVDGPTPHQTVRLEALDE 808
Cdd:cd06204    2 AKNPFLAPVAVSRELFTG-SDRSCLHIEFDI-SGSGIRYQTGDHLAVWPTNPSEEVE-RLLKVLGLDDRDTVISLKSLDE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   809 SGSYWVsdkRLP-PCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPS--EYSKWKFTNSPTFLEVLEE 885
Cdd:cd06204   79 PASKKV---PFPcPTTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLASEGkdEYAKWIVEPHRNLLEVLQD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   886 FPSLRVSA---GFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTrdGQGPLHHGVCSTWLNSLKPQDP------ 956
Cdd:cd06204  156 FPSAKPTPppfDFLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPT--PTGRIIKGVATNWLLALKPALNgekppt 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   957 ---------------VPCFVRNaSGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHdSQHKGVRGGRMTLVFGCRRPDE 1021
Cdd:cd06204  234 pyylsgprkkgggskVPVFVRR-SNFRLPTKPSTPVIMIGPGTGVAPFRGFIQERAA-LKESGKKVGPTLLFFGCRHPDE 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1022 DHIYQEEMLEMAQKGVLHAVHTAYSRLPGKpKVYVQDILRQQlASEVLRVLHkEPGHLYVCGDVR-MARDVAHTLKQLVA 1100
Cdd:cd06204  312 DFIYKDELEEYAKLGGLLELVTAFSREQPK-KVYVQHRLAEH-AEQVWELIN-EGAYIYVCGDAKnMARDVEKTLLEILA 388
                        410       420
                 ....*....|....*....|....*..
gi 1352513  1101 AKLKLNEEQVEDYFFQLKSQKRYHEDI 1127
Cdd:cd06204  389 EQGGMTETEAEEYVKKLKTRGRYQEDV 415
FAD_binding_1 pfam00667
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ...
726-947 1.63e-100

FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.


Pssm-ID: 395540 [Multi-domain]  Cd Length: 219  Bit Score: 316.97  E-value: 1.63e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     726 SMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDgQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEA 805
Cdd:pfam00667    1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISG-SGLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     806 LDEsgsyWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPS---EYSKWKFTNSPTFLEV 882
Cdd:pfam00667   80 LDE----RVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSSDAgarEYKRWKLNHAPTLLEV 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352513     883 LEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTrDGQGPLHHGVCSTW 947
Cdd:pfam00667  156 LEEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYET-DGEGRIHYGVCSNW 219
SiR cd06199
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
736-1128 2.18e-91

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain.


Pssm-ID: 99796 [Multi-domain]  Cd Length: 360  Bit Score: 297.60  E-value: 2.18e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   736 RLKSRQNLQSPTSSRATILVELSCEdGQGLNYLPGEHLGVCPGNQPALVQGILERV-VDGPTPHQTVRLEALdesgsywv 814
Cdd:cd06199    1 TVLENRLLTGPGSEKETRHIELDLE-GSGLSYEPGDALGVYPTNDPALVDELLAALgLSGDEPVSTVGGGTL-------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   815 sdkrlppcSLSQALTYFLDITTPPTQLLlQKLAQvATEEPERQRLEALCQPSEYSKWKftnspTFLEVLEEFPSlRVSAG 894
Cdd:cd06199   72 --------PLREALIKHYEITTLLLALL-ESYAA-DTGALELLALAALEAVLAFAELR-----DVLDLLPIPPA-RLTAE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   895 FLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQgplHHGVCSTWLNS-LKPQDPVPCFVRNASGFHLPEDP 973
Cdd:cd06199  136 ELLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESHGRE---RKGVASTFLADrLKEGDTVPVFVQPNPHFRLPEDP 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   974 SHPCILIGPGTGIAPFRSFWQQRLHdSQHKgvrgGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRlPGKPK 1053
Cdd:cd06199  213 DAPIIMVGPGTGIAPFRAFLQEREA-TGAK----GKNWLFFGERHFATDFLYQDELQQWLKDGVLTRLDTAFSR-DQAEK 286
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352513  1054 VYVQDILRQQlASEVLRVLhKEPGHLYVCGDV-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:cd06199  287 VYVQDRMREQ-GAELWAWL-EEGAHFYVCGDAkRMAKDVDAALLDIIATEGGMDEEEAEAYLKELKKEKRYQRDVY 360
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
736-1123 9.25e-88

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: 288.79  E-value: 9.25e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   736 RLKSRQNLQSPTSSRATILVELSCeDGQGLNYLPGEHLGVCPGNQPALVQGILERVvdGPTPHQTVRLEALDESgsywVS 815
Cdd:cd06207    1 KVTENKRLTPADYDRSTRHIEFDL-GGSGLSYETGDNLGIYPENSDALVDEFLARL--GLDGDDVVRVEPNEQQ----RG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   816 DKRLP-PCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAG 894
Cdd:cd06207   74 KPPFPePISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLASREGRTEYKRYEKYTYLEVLKDFPSVRPTLE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   895 FLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTrdGQGPLHHGVCSTWLNSLKPQDPVPCFVRnASGFHLPEDPS 974
Cdd:cd06207  154 QLLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKT--PSGRSRYGLCSSYLAGLKVGQRVTVFIK-KSSFKLPKDPK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   975 HPCILIGPGTGIAPFRSFWQQRLHDSQhKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKpKV 1054
Cdd:cd06207  231 KPIIMVGPGTGLAPFRAFLQERAALLA-QGPEIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVLTTLGTAFSRDQPK-KV 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1055 YVQDILRQQlASEVLRVLHKEPGHLYVCGDV-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRY 1123
Cdd:cd06207  309 YVQDLIREN-SDLVYQLLEEGAGVIYVCGSTwKMPPDVQEAFEEILKKHGGGDEELAEKKIEELEERGRY 377
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
863-1128 5.77e-86

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. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. 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: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 279.22  E-value: 5.77e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   863 CQPSEYSKWKFtnsptFLEV-LEEFPSLRVSAGFLLSQLPI--LKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGqgPL 939
Cdd:cd06182    8 LTPPDSPRSTR-----HLEFdLSGNSVLKYQPGDHLGVIPPnpLQPRYYSIASSPDVDPGEVHLCVRVVSYEAPAG--RI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   940 HHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDsQHKGVRGGRMTLVFGCRRP 1019
Cdd:cd06182   81 RKGVCSNFLAGLQLGAKVTVFIRPAPSFRLPKDPTTPIIMVGPGTGIAPFRGFLQERAAL-RANGKARGPAWLFFGCRNF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1020 DEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQlASEVLRVLHKEpGHLYVCGDVR-MARDVAHTLKQL 1098
Cdd:cd06182  160 ASDYLYREELQEALKDGALTRLDVAFSREQAEPKVYVQDKLKEH-AEELRRLLNEG-AHIYVCGDAKsMAKDVEDALVKI 237
                        250       260       270
                 ....*....|....*....|....*....|
gi 1352513  1099 VAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:cd06182  238 IAKAGGVDESDAEEYLKELEDEGRYVEDVW 267
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
743-1128 4.08e-83

These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase 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: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 276.06  E-value: 4.08e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   743 LQSPTSSRATILVELSCEDGqgLNYLPGEHLGVCPGNQPALVQGILERVvdGPTPHQTVRLEALDESGsywvsdkRLP-- 820
Cdd:cd06206    8 LTAPGVGPSKRHLELRLPDG--MTYRAGDYLAVLPRNPPELVRRALRRF--GLAWDTVLTISASGSAT-------GLPlg 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   821 -PCSLSQALTYFLDITTPPTQLLLQKLAQvATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQ 899
Cdd:cd06206   77 tPISVSELLSSYVELSQPATRRQLAALAE-ATRCPDTKALLERLAGEAYAAEVLAKRVSVLDLLERFPSIALPLATFLAM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   900 LPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPlHHGVCSTWLNSLKPQDPVPCFVR-NASGFHLPEDPSHPCI 978
Cdd:cd06206  156 LPPMRPRQYSISSSPLVDPGHATLTVSVLDAPALSGQGR-YRGVASSYLSSLRPGDSIHVSVRpSHSAFRPPSDPSTPLI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   979 LIGPGTGIAPFRSFWQQRlHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLhAVHTAYSRLPGKPKVYVQD 1058
Cdd:cd06206  235 MIAAGTGLAPFRGFLQER-AALLAQGRKLAPALLFFGCRHPDHDDLYRDELEEWEAAGVV-SVRRAYSRPPGGGCRYVQD 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352513  1059 ILRQQlaSEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKL----NEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:cd06206  313 RLWAE--REEVWELWEQGARVYVCGDGRMAPGVREVLKRIYAEKDERgggsDDEEAEEWLEELRNKGRYATDVF 384
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
534-1128 3.53e-77

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 266.59  E-value: 3.53e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    534 ASRVRVTILFATETGKSEALAWDL-GALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFML 612
Cdd:PRK10953   59 AEMPGITLISASQTGNARRVAEQLrDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    613 K--ELNNKfRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD-ELSGQEDAFRSWAVQTFKAacetfdvrgk 689
Cdd:PRK10953  139 KapKLENT-AFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDRVDADvEYQAAASEWRARVVDALKS---------- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    690 qhiQIPKLYTSnvtwdphhyrlVQDSQPLDLSKALSSMHAKNV-FTMRLKSRQNLQSPTSSRATILVELSCEDgQGLNYL 768
Cdd:PRK10953  208 ---RAPAVAAP-----------SQSVATGAVNEIHTSPYSKEApLTASLSVNQKITGRNSEKDVRHIEIDLGD-SGLRYQ 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    769 PGEHLGVCPGNQPALVQGILErvvdgptphqtvrLEALDESGSYWVSDKRLPpcsLSQALTYFLDITTPpTQLLLQKLAQ 848
Cdd:PRK10953  273 PGDALGVWYQNDPALVKELVE-------------LLWLKGDEPVTVDGKTLP---LAEALQWHFELTVN-TANIVENYAT 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    849 VATEEperqRLEALC----QPSEYSKwkftNSPtFLEVLEEFPSlRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLT 924
Cdd:PRK10953  336 LTRSE----TLLPLVgdkaALQHYAA----TTP-IVDMVRFAPA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHIT 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    925 VAVVTYhtrDGQGPLHHGVCSTWL-NSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQhk 1003
Cdd:PRK10953  406 VGVVRY---DIEGRARAGGASSFLaDRLEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADGA-- 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   1004 gvrGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRlPGKPKVYVQDILRQQLAsEVLRVLhKEPGHLYVCG 1083
Cdd:PRK10953  481 ---PGKNWLFFGNPHFTEDFLYQVEWQRYVKEGLLTRIDLAWSR-DQKEKIYVQDKLREQGA-ELWRWI-NDGAHIYVCG 554
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 1352513   1084 DV-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIF 1128
Cdd:PRK10953  555 DAnRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY 600
methionine_synthase_red cd06203
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ...
737-1127 2.62e-76

Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. 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. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. 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: 99800 [Multi-domain]  Cd Length: 398  Bit Score: 257.64  E-value: 2.62e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   737 LKSRQNLQSPTSSRATILVELSCEdGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEAL-DESGSYWVS 815
Cdd:cd06203    2 ISSAKKLTEGDDVKTVVDLTLDLS-PTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVpNTKKKNAKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   816 DKRLP-PCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALC---QPSEYSKWKFTNSPTFLEVLEEFPSLRV 891
Cdd:cd06203   81 PVHIPkVVTLRTILTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCskqGSEDYTDFVRKRGLSLLDLLEAFPSCRP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   892 SAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRdgqgplhhGVCSTWLNSL-----KPQDPVPCFVRNASG 966
Cdd:cd06203  161 PLSLLIEHLPRLQPRPYSIASSPLEGPGKLRFIFSVVEFPAK--------GLCTSWLESLclsasSHGVKVPFYLRSSSR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   967 FHLPED-PSHPCILIGPGTGIAPFRSFWQQR-LHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTA 1044
Cdd:cd06203  233 FRLPPDdLRRPIIMVGPGTGVAPFLGFLQHReKLKESHTETVFGEAWLFFGCRHRDRDYLFRDELEEFLEEGILTRLIVA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1045 YSRLP--GKPKVYVQDILRQQLAsEVLRVLHKEPGHLYVCGDVR-MARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQK 1121
Cdd:cd06203  313 FSRDEndGSTPKYVQDKLEERGK-KLVDLLLNSNAKIYVCGDAKgMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKED 391

                 ....*.
gi 1352513  1122 RYHEDI 1127
Cdd:cd06203  392 RYLEDV 397
PRK06214 PRK06214
sulfite reductase subunit alpha;
730-1128 6.42e-70

sulfite reductase subunit alpha;


Pssm-ID: 235745 [Multi-domain]  Cd Length: 530  Bit Score: 243.83  E-value: 6.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    730 KNVFTMRLKSRQNLQSPTSSRATILVELSCEDGqGLNYLPGEHLGVCPGNQPALVQGILERV---VDGPTPHQTVRlEAL 806
Cdd:PRK06214  166 DNPVEATFLSRRRLNKPGSEKETWHVEIDLAGS-GLDYEVGDSLGLFPANDPALVDAVIAALgapPEFPIGGKTLR-EAL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    807 DESgsywvsdkrlppCSLSqaltyfldittPPTQLLLQKLAQVaTEEPERQRLEALCQ---PSEyskwkftNSPTF--LE 881
Cdd:PRK06214  244 LED------------VSLG-----------PAPDGLFELLSYI-TGGAARKKARALAAgedPDG-------DAATLdvLA 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    882 VLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYhtrDGQGPLHHGVCSTWL-NSLKPQDPVPCF 960
Cdd:PRK06214  293 ALEKFPGIRPDPEAFVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRY---EIGSRLRLGVASTFLgERLAPGTRVRVY 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    961 VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLhdsqhkgVRG--GRMTLVFGCRRPDEDHIYQEEMLEMAQKGVL 1038
Cdd:PRK06214  370 VQKAHGFALPADPNTPIIMVGPGTGIAPFRAFLHERA-------ATKapGRNWLFFGHQRSATDFFYEDELNGLKAAGVL 442
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   1039 HAVHTAYSRlPGKPKVYVQDILRQQlASEVLRVLhKEPGHLYVCGDV-RMARDVAHTLKQLVAAKLKLNEEQVEDYFFQL 1117
Cdd:PRK06214  443 TRLSLAWSR-DGEEKTYVQDRMREN-GAELWKWL-EEGAHFYVCGDAkRMAKDVERALVDIVAQFGGRSPDEAVAFVAEL 519
                         410
                  ....*....|.
gi 1352513   1118 KSQKRYHEDIF 1128
Cdd:PRK06214  520 KKAGRYQADVY 530
Flavodoxin_1 pfam00258
Flavodoxin;
541-672 1.36e-36

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 134.80  E-value: 1.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     541 ILFATETGKSEALAWDLGALF-SCAFNPKVVCMDKYR--LSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELN- 616
Cdd:pfam00258    1 IFYGSQTGNTEKLAEAIAEGLgEAGFEVDVVDLDDVDetLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLEd 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352513     617 ---NKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDEL---SGQEDAFRSW 672
Cdd:pfam00258   81 gdlSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGPLGEGDEDpqeDGLEEAFEAW 142
CYPOR_like_FNR cd06208
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ...
904-1124 9.01e-36

These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99804 [Multi-domain]  Cd Length: 286  Bit Score: 137.84  E-value: 9.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   904 KPRFYSISSSR---DHTPTEIHLTVAVVTYhTRDGQGPLHHGVCSTWLNSLKPQDPVpcFVRNASG--FHLPEDPSHPCI 978
Cdd:cd06208   63 KLRLYSIASSRygdDGDGKTLSLCVKRLVY-TDPETDETKKGVCSNYLCDLKPGDDV--QITGPVGktMLLPEDPNATLI 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   979 LIGPGTGIAPFRSFWQQRLHDsQHKGVR-GGRMTLVFGCRRPDEdHIYQEEMLEMAQK--GVLHaVHTAYSRLPGK---P 1052
Cdd:cd06208  140 MIATGTGIAPFRSFLRRLFRE-KHADYKfTGLAWLFFGVPNSDS-LLYDDELEKYPKQypDNFR-IDYAFSREQKNadgG 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352513  1053 KVYVQDILRQQlASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLvaAKLKLNEEQVEDyffQLKSQKRYH 1124
Cdd:cd06208  217 KMYVQDRIAEY-AEEIWNLLDKDNTHVYICGLKGMEPGVDDALTSV--AEGGLAWEEFWE---SLKKKGRWH 282
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
871-1128 1.44e-34

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 134.38  E-value: 1.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   871 WKFTNSPTF---LEVLEEFPS----LRVSAGFLLSQLP--ILKPRFYSI-SSSRDHTpTEIhltvaVVTYHTrdgqgplh 940
Cdd:cd06201   57 GAAVQAPTAilrFKPAKRKLSgkglPSFEAGDLLGILPpgSDVPRFYSLaSSSSDGF-LEI-----CVRKHP-------- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   941 HGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDpSHPCILIGPGTGIAPFRSFwqQRLHDSQHKgvrggrMTLVFGCRRPD 1020
Cdd:cd06201  123 GGLCSGYLHGLKPGDTIKAFIRPNPSFRPAKG-AAPVILIGAGTGIAPLAGF--IRANAARRP------MHLYWGGRDPA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1021 EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGkpKVYVQDILRQQlASEVLRVLHkEPGHLYVCGDVRMARDVAHTL-KQLV 1099
Cdd:cd06201  194 SDFLYEDELDQYLADGRLTQLHTAFSRTPD--GAYVQDRLRAD-AERLRRLIE-DGAQIMVCGSRAMAQGVAAVLeEILA 269
                        250       260
                 ....*....|....*....|....*....
gi 1352513  1100 AAKLKLneeqvedyfFQLKSQKRYHEDIF 1128
Cdd:cd06201  270 PQPLSL---------DELKLQGRYAEDVY 289
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
878-1102 4.95e-34

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: 130.64  E-value: 4.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   878 TFLEVLEEFPSLRVSAG----FLLSQLPILKPRFYSISSSRDHtPTEIHLTVAVVTyhtrdgqgplhHGVCSTWLNSLKP 953
Cdd:cd00322   10 VRLFRLQLPNGFSFKPGqyvdLHLPGDGRGLRRAYSIASSPDE-EGELELTVKIVP-----------GGPFSAWLHDLKP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   954 QDPVPCFVRnASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQhkgvrGGRMTLVFGCRRPDeDHIYQEEMLEMA 1033
Cdd:cd00322   78 GDEVEVSGP-GGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKP-----GGEITLLYGARTPA-DLLFLDELEELA 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352513  1034 QKGVLHAVHTAYSRLPGKPKVYVQDILRQqlASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAK 1102
Cdd:cd00322  151 KEGPNFRLVLALSRESEAKLGPGGRIDRE--AEILALLPDDSGALVYICGPPAMAKAVREALVSLGVPE 217
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
889-1128 3.91e-32

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99797  Cd Length: 245  Bit Score: 125.85  E-value: 3.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   889 LRVSAGFLLSQLP--ILKPRFYSISSsrdhTPTEIHLTVaVVTYHTRDGQGPlhhGVCSTWLNSLKPQ-DPVPCFVRNAS 965
Cdd:cd06200   30 AQWQAGDIAEIGPrhPLPHREYSIAS----LPADGALEL-LVRQVRHADGGL---GLGSGWLTRHAPIgASVALRLRENP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   966 GFHLPEDPShPCILIGPGTGIAPFRSFWQQRLHDSQHkgvrggRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAY 1045
Cdd:cd06200  102 GFHLPDDGR-PLILIGNGTGLAGLRSHLRARARAGRH------RNWLLFGERQAAHDFFCREELEAWQAAGHLARLDLAF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1046 SRlPGKPKVYVQDILRQqlASEVLRVLHKEPGHLYVCGDVR-MARDVAHTLKQLvaaklkLNEEQVEdyffQLKSQKRYH 1124
Cdd:cd06200  175 SR-DQAQKRYVQDRLRA--AADELRAWVAEGAAIYVCGSLQgMAPGVDAVLDEI------LGEEAVE----ALLAAGRYR 241

                 ....
gi 1352513  1125 EDIF 1128
Cdd:cd06200  242 RDVY 245
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
979-1093 3.34e-27

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: 106.96  E-value: 3.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513     979 LIGPGTGIAPFRSFWQQRLHDSQHKgvrgGRMTLVFGCRRPDeDHIYQEEMLEMAQK--GVLHAVHTAySRLPGKP---K 1053
Cdd:pfam00175    1 MIAGGTGIAPVRSMLRAILEDPKDP----TQVVLVFGNRNED-DILYREELDELAEKhpGRLTVVYVV-SRPEAGWtggK 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1352513    1054 VYVQDILRQQLASevlrvLHKEPGHLYVCGDVRMARDVAH 1093
Cdd:pfam00175   75 GRVQDALLEDHLS-----LPDEETHVYVCGPPGMIKAVRK 109
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
906-1098 6.92e-21

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 92.93  E-value: 6.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSrdhtPTEIHLTVAVVtyhtRDGQGPLhhgvcSTWLN-SLKPQDPVpcFVRNASG-FHLPEDPSHPCILIGPG 983
Cdd:COG1018   53 RAYSLSSA----PGDGRLEITVK----RVPGGGG-----SNWLHdHLKVGDTL--EVSGPRGdFVLDPEPARPLLLIAGG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   984 TGIAPFRSFWQQRLHDSqhkgvRGGRMTLVFGCRRPdEDHIYQEEMLEMAQK-GVLHaVHTAYSRLPGKPKVYV-QDILR 1061
Cdd:COG1018  118 IGITPFLSMLRTLLARG-----PFRPVTLVYGARSP-ADLAFRDELEALAARhPRLR-LHPVLSREPAGLQGRLdAELLA 190
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1352513  1062 QQLASEvlrvlhkEPGHLYVCGDVRMARDVAHTLKQL 1098
Cdd:COG1018  191 ALLPDP-------ADAHVYLCGPPPMMEAVRAALAEL 220
PLN03116 PLN03116
ferredoxin--NADP+ reductase; Provisional
904-1128 2.11e-16

ferredoxin--NADP+ reductase; Provisional


Pssm-ID: 215586 [Multi-domain]  Cd Length: 307  Bit Score: 81.30  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    904 KPRFYSISSSR---DHTPTEIHLTVAVVTY---HTRDgQGPLHHGVCSTWLNSLKPQDPVPcfVRNASG--FHLPE-DPS 974
Cdd:PLN03116   80 NVRLYSIASTRygdDFDGKTASLCVRRAVYydpETGK-EDPAKKGVCSNFLCDAKPGDKVQ--ITGPSGkvMLLPEeDPN 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    975 HPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPDEdHIYQEEMLEMAQKGVLH-AVHTAYSRLPGKP- 1052
Cdd:PLN03116  157 ATHIMVATGTGIAPFRGFLRRMFMEDVPAFKFGGLAWLFLGVANSDS-LLYDDEFERYLKDYPDNfRYDYALSREQKNKk 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352513   1053 --KVYVQDILrQQLASEVLRVLHKePGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEdyffQLKSQKRYHEDIF 1128
Cdd:PLN03116  236 ggKMYVQDKI-EEYSDEIFKLLDN-GAHIYFCGLKGMMPGIQDTLKRVAEERGESWEEKLS----GLKKNKQWHVEVY 307
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
906-1098 4.35e-15

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: 76.06  E-value: 4.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSRDHTPTEIhltvavvtYHTRDGQGPLhhgvcSTWLNSLKPQDPVpcFV-RNASGFhLPEDPSHPC---ILIG 981
Cdd:cd06195   45 RAYSIASAPYEENLEF--------YIILVPDGPL-----TPRLFKLKPGDTI--YVgKKPTGF-LTLDEVPPGkrlWLLA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFwqqrLHDSQHKGvRGGRMTLVFGCRRPdEDHIYQEEMLEMAQKGV--LHaVHTAYSR--LPGKPKVYVQ 1057
Cdd:cd06195  109 TGTGIAPFLSM----LRDLEIWE-RFDKIVLVHGVRYA-EELAYQDEIEALAKQYNgkFR-YVPIVSRekENGALTGRIP 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1352513  1058 DILRQ-QLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQL 1098
Cdd:cd06195  182 DLIESgELEEHAGLPLDPETSHVMLCGNPQMIDDTQELLKEK 223
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
905-1098 1.71e-14

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 74.51  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   905 PRFYSISSSrDHTPTEIHLTVAVVtyhtrdgqgplhhGVCSTWLNSLKPQDPVpcFVR----NasGFHLPEDPsHPCILI 980
Cdd:COG0543   42 RRPFSIASA-PREDGTIELHIRVV-------------GKGTRALAELKPGDEL--DVRgplgN--GFPLEDSG-RPVLLV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   981 GPGTGIAPFRSFwQQRLHDsqhkgvRGGRMTLVFGCRRPDeDHIYQEEMLEMAQKGVLHAVHTAYSRLPGkpkvYVQDIL 1060
Cdd:COG0543  103 AGGTGLAPLRSL-AEALLA------RGRRVTLYLGARTPE-DLYLLDELEALADFRVVVTTDDGWYGRKG----FVTDAL 170
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 1352513  1061 RQQLASEvlrvlhkEPGHLYVCGDVRMARDVAHTLKQL 1098
Cdd:COG0543  171 KELLAED-------SGDDVYACGPPPMMKAVAELLLER 201
PLN03115 PLN03115
ferredoxin--NADP(+) reductase; Provisional
904-1128 3.12e-14

ferredoxin--NADP(+) reductase; Provisional


Pssm-ID: 215585 [Multi-domain]  Cd Length: 367  Bit Score: 75.81  E-value: 3.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    904 KPRFYSISSSR--DHTPTE-IHLTVAVVTYhTRDgQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILI 980
Cdd:PLN03115  144 KLRLYSIASSAlgDFGDSKtVSLCVKRLVY-TND-QGEIVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIML 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    981 GPGTGIAPFRSF-WqqRLHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKG-----VLHAVHTAYSRLPGKpKV 1054
Cdd:PLN03115  222 ATGTGIAPFRSFlW--KMFFEKHDDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKApenfrLDFAVSREQTNAKGE-KM 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352513   1055 YVQDILrQQLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAaklklnEEQVE--DYFFQLKSQKRYHEDIF 1128
Cdd:PLN03115  299 YIQTRM-AEYAEELWELLKKDNTYVYMCGLKGMEKGIDDIMVSLAA------KDGIDwfEYKKQLKKAEQWNVEVY 367
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
905-1098 9.87e-13

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


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 71.43  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   905 PRFYSISSSRDhTPTEIHLTVAVVTyhTRDGQGPlhhGVCSTWLNSLKPQDPVpcfvrNASG----FHLPEDPShPCILI 980
Cdd:COG2871  200 TRAYSMANYPA-EKGIIELNIRIAT--PPMDVPP---GIGSSYIFSLKPGDKV-----TISGpygeFFLRDSDR-EMVFI 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   981 GPGTGIAPFRSFwqqrLHDSQHKGVRGGRMTLVFGCRRPDEdHIYQEEMLEMAQKgvlHA---VHTAYSR-LPG----KP 1052
Cdd:COG2871  268 GGGAGMAPLRSH----IFDLLERGKTDRKITFWYGARSLRE-LFYLEEFRELEKE---HPnfkFHPALSEpLPEdnwdGE 339
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 1352513  1053 KVYVQDILRQQLASEvlrvlHKEP-GHL-YVCGDVRMARDVAHTLKQL 1098
Cdd:COG2871  340 TGFIHEVLYENYLKD-----HPAPeDCEaYLCGPPPMIDAVIKMLDDL 382
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
906-1098 1.37e-12

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: 69.64  E-value: 1.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSsRDHTPTEIHLTVAVVTyhTRDGQGPLHHGVCSTWLNSLKPQDPVpcfvrNASG----FHLPEDPsHPCILIG 981
Cdd:cd06188   87 RAYSLAN-YPAEEGELKLNVRIAT--PPPGNSDIPPGIGSSYIFNLKPGDKV-----TASGpfgeFFIKDTD-REMVFIG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFWQQRLhdsqhKGVRGGR-MTLVFGCRRPDEdHIYQEEMLEMAQKGVLHAVHTAYSR-LPGK----PKVY 1055
Cdd:cd06188  158 GGAGMAPLRSHIFHLL-----KTLKSKRkISFWYGARSLKE-LFYQEEFEALEKEFPNFKYHPVLSEpQPEDnwdgYTGF 231
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 1352513  1056 VQDILRQQLASEvlrvlHKEPG--HLYVCGDVRMARDVAHTLKQL 1098
Cdd:cd06188  232 IHQVLLENYLKK-----HPAPEdiEFYLCGPPPMNSAVIKMLDDL 271
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
908-1098 2.86e-10

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 63.76  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   908 YSISSSRDHTPtEIHLTVAVVTYHTRdgqgplhhgvcstWLNSLKPQDPVpcFVRNASG-FHLPEDPSHPC-ILIGPGTG 985
Cdd:COG4097  266 FSISSAPGGDG-RLRFTIKALGDFTR-------------RLGRLKPGTRV--YVEGPYGrFTFDRRDTAPRqVWIAGGIG 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   986 IAPFRSfwqqRLHDSQHKGVRGGRMTLVFGCRRPDEDhIYQEEMLEMAQKgvlhavhTAYSRLpgkpkVYVQDILRQQLA 1065
Cdd:COG4097  330 ITPFLA----LLRALAARPGDQRPVDLFYCVRDEEDA-PFLEELRALAAR-------LAGLRL-----HLVVSDEDGRLT 392
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 1352513  1066 SEVLRVLHKEPGH--LYVCGDVRMARDVAHTLKQL 1098
Cdd:COG4097  393 AERLRRLVPDLAEadVFFCGPPGMMDALRRDLRAL 427
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
905-1098 3.20e-10

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: 61.79  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   905 PRFYSISSSrdhtPTEIHLTVAVvtyhtRDGQGplhhGVCSTWLN-SLKPQDPVPcfVRNASG-FHLPEDP-SHPCILIG 981
Cdd:cd06214   51 RRSYSICSS----PGDDELRITV-----KRVPG----GRFSNWANdELKAGDTLE--VMPPAGrFTLPPLPgARHYVLFA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFWQQRLHDSqhkgvRGGRMTLVFGCRRPDeDHIYQEEMLEMAQK--GVLHAVHTaYSRLPGKPKVYvQDI 1059
Cdd:cd06214  116 AGSGITPVLSILKTALARE-----PASRVTLVYGNRTEA-SVIFREELADLKARypDRLTVIHV-LSREQGDPDLL-RGR 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 1352513  1060 LRQQLASEVLRVLHKEPG--HLYVCGDVRMARDVAHTLKQL 1098
Cdd:cd06214  188 LDAAKLNALLKNLLDATEfdEAFLCGPEPMMDAVEAALLEL 228
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
906-1101 1.20e-09

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: 59.97  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSrdhtPTE---IHLTVAVVtyhtrdgqgplHHGVCSTWL-NSLKPQDPVpcFVRNASG-FHLPEDPSHPCILI 980
Cdd:cd06217   51 RSYSIASS----PTQrgrVELTVKRV-----------PGGEVSPYLhDEVKVGDLL--EVRGPIGtFTWNPLHGDPVVLL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   981 GPGTGIAPFRSFWQQRLHDSQHkgvrgGRMTLVFGCRRPdEDHIYQEEMLEMA-QKGVLHaVHTAYSRLPGK----PKVY 1055
Cdd:cd06217  114 AGGSGIVPLMSMIRYRRDLGWP-----VPFRLLYSARTA-EDVIFRDELEQLArRHPNLH-VTEALTRAAPAdwlgPAGR 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1352513  1056 VQDILRQQLASEVlrvlhkEPGHLYVCGDVRMardVAHTLKQLVAA 1101
Cdd:cd06217  187 ITADLIAELVPPL------AGRRVYVCGPPAF---VEAATRLLLEL 223
PRK08105 PRK08105
flavodoxin; Provisional
582-660 4.80e-09

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 56.05  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    582 EERLLLVVTSTFGNGDCPGN----GEKLKKSLFMLKELnnkfRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMG 657
Cdd:PRK08105   48 QDELVLVVTSTTGQGDLPDSivplFQALKDTAGYQPNL----RYGVIALGDSSYDNFCGAGKQFDALLQEQGAKRVGERL 123

                  ...
gi 1352513    658 EGD 660
Cdd:PRK08105  124 EID 126
PRK06703 PRK06703
flavodoxin; Provisional
538-675 8.14e-09

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 55.54  E-value: 8.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    538 RVTILFATETGKSEALAWDLGALFScAFNPKVVC--MDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLkEL 615
Cdd:PRK06703    3 KILIAYASMSGNTEDIADLIKVSLD-AFDHEVVLqeMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDFHEDLENI-DL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    616 NNKfRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGAS--------QLTPMGEGDELSGQE--DAFRSWAVQ 675
Cdd:PRK06703   81 SGK-KVAVFGSGDTAYPLFCEAVTIFEERLVERGAElvqeglkiELAPETDEDVEKCSNfaIAFAEKFAQ 149
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
906-1083 1.60e-08

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: 56.85  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSRDHTPTEIHLTVAVVTyhtrdgqgplhHGVCSTWL-NSLKPQDpvpcFVR--NASG-FHLPEDPSHPCILIG 981
Cdd:cd06216   65 RSYSLSSSPTQEDGTITLTVKAQP-----------DGLVSNWLvNHLAPGD----VVElsQPQGdFVLPDPLPPRLLLIA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFWQQrLHDSQHkgvrGGRMTLVFGCRRPdEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKpkvyvQDILR 1061
Cdd:cd06216  130 AGSGITPVMSMLRT-LLARGP----TADVVLLYYARTR-EDVIFADELRALAAQHPNLRLHLLYTREELD-----GRLSA 198
                        170       180
                 ....*....|....*....|..
gi 1352513  1062 QQLASEvlrVLHKEPGHLYVCG 1083
Cdd:cd06216  199 AHLDAV---VPDLADRQVYACG 217
PRK09004 PRK09004
FMN-binding protein MioC; Provisional
577-655 2.40e-08

FMN-binding protein MioC; Provisional


Pssm-ID: 181608 [Multi-domain]  Cd Length: 146  Bit Score: 54.07  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    577 LSCLEEERLLLVVTSTFGNGDCPGNgeklKKSLFmlKELNNK------FRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGA 650
Cdd:PRK09004   41 LDDLSASGLWLIVTSTHGAGDLPDN----LQPFF--EELQEQkpdlsqVRFAAIGIGSSEYDTFCGAIDKLEQLLKAKGA 114

                  ....*
gi 1352513    651 SQLTP 655
Cdd:PRK09004  115 KQIGE 119
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
905-1098 1.46e-07

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: 53.37  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   905 PRFYSISSsrdhTPTEIHLtvavVTYHTRDGQGplhhGVCSTWL-NSLKPQDPVpcFVRNASG-FHLPEDPSHPCILIGP 982
Cdd:cd06187   41 WRAYSPAN----PPNEDGE----IEFHVRAVPG----GRVSNALhDELKVGDRV--RLSGPYGtFYLRRDHDRPVLCIAG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   983 GTGIAPFRSFwqqrLHDSQHKGvRGGRMTLVFGCRRPDEdhIY-QEEMLEMAQKgvlHA---VHTAYSRLPGKPKvyvqd 1058
Cdd:cd06187  107 GTGLAPLRAI----VEDALRRG-EPRPVHLFFGARTERD--LYdLEGLLALAAR---HPwlrVVPVVSHEEGAWT----- 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 1352513  1059 iLRQQLASEVLRVLHKEP-GH-LYVCGDVRMARDVAHTLKQL 1098
Cdd:cd06187  172 -GRRGLVTDVVGRDGPDWaDHdIYICGPPAMVDATVDALLAR 212
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
908-1111 1.70e-07

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: 53.03  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   908 YSISSSRDHTPtEIHLTVAVVTYHTRDGQgplhhgvcstwlNSLKPQDPV----P--CFVRnasgfhlpEDPSHPCILIG 981
Cdd:cd06198   44 FTISSAPDPDG-RLRFTIKALGDYTRRLA------------ERLKPGTRVtvegPygRFTF--------DDRRARQIWIA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFWQQRLHDSQHKGVrggrmTLVFGCRRPDEDhIYQEEMLEMAQKG--VLHAVHTaysrlPGKPKVYVQDI 1059
Cdd:cd06198  103 GGIGITPFLALLEALAARGDARPV-----TLFYCVRDPEDA-VFLDELRALAAAAgvVLHVIDS-----PSDGRLTLEQL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1352513  1060 LRQqlasevlRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVE 1111
Cdd:cd06198  172 VRA-------LVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
942-1110 1.63e-06

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: 50.64  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   942 GVCSTWLNSLKPQDPVpcFVRNASG-FHLPEDPSHPCI-LIGPGTGIAPFRSFWQQRLHDSQHKgvrgGRMTLVFGCRRP 1019
Cdd:cd06183   72 GKMSQYLHSLKPGDTV--EIRGPFGkFEYKPNGKVKHIgMIAGGTGITPMLQLIRAILKDPEDK----TKISLLYANRTE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1020 dEDHIYQEEMLEMAQKGVLH-AVHTAYSRLPGKPKVYV----QDILRQQLASevlrvLHKEPGHLYVCGDVRMardVAHT 1094
Cdd:cd06183  146 -EDILLREELDELAKKHPDRfKVHYVLSRPPEGWKGGVgfitKEMIKEHLPP-----PPSEDTLVLVCGPPPM---IEGA 216
                        170
                 ....*....|....*.
gi 1352513  1095 LKQLvAAKLKLNEEQV 1110
Cdd:cd06183  217 VKGL-LKELGYKKDNV 231
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
905-1092 3.07e-06

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: 49.57  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   905 PRFYSISSSRDHTPT-EIHLTVavvtyhtrdgqgpLHHGVCSTWL-------NSLKPQDPVpcfvrnASGFHLPEDPSHP 976
Cdd:cd06194   39 ARSYSPTSLPDGDNElEFHIRR-------------KPNGAFSGWLgeearpgHALRLQGPF------GQAFYRPEYGEGP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   977 CILIGPGTGIAPFRSFWQQRLHdSQHKgvrgGRMTLVFGCRRPDeDHIYQEEMLEMA-QKGVLHAVHTAYSRLPGKPKVY 1055
Cdd:cd06194  100 LLLVGAGTGLAPLWGIARAALR-QGHQ----GEIRLVHGARDPD-DLYLHPALLWLArEHPNFRYIPCVSEGSQGDPRVR 173
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 1352513  1056 VQDILRQQLASevlrvlhKEPGHLYVCGDVRMARDVA 1092
Cdd:cd06194  174 AGRIAAHLPPL-------TRDDVVYLCGAPSMVNAVR 203
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
909-1036 5.25e-06

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: 49.14  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   909 SISSSRDHTPTeIHLTVAVVtyhtrdgqgplhhGVCSTWLNSLKPQDPVpcFVRNA--SGFHLPEDPSHPCILIGPGTGI 986
Cdd:cd06221   47 SISSDPTRRGP-LELTIRRV-------------GRVTEALHELKPGDTV--GLRGPfgNGFPVEEMKGKDLLLVAGGLGL 110
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 1352513   987 APFRSFWQQRLhdsQHKGvRGGRMTLVFGCRRPdEDHIYQEEMLEMAQKG 1036
Cdd:cd06221  111 APLRSLINYIL---DNRE-DYGKVTLLYGARTP-EDLLFKEELKEWAKRS 155
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
947-1097 1.62e-05

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. 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: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 47.54  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   947 WLNSLKPQDPVPCFVRNASGFHLPeDPSHPCILIGPGTGIAPFRsFWQQRLHDsqhkgvRGGRMTLVFGCRrpDEDHIYQ 1026
Cdd:cd06218   72 LLSELKAGDELDVLGPLGNGFDLP-DDDGKVLLVGGGIGIAPLL-FLAKQLAE------RGIKVTVLLGFR--SADDLFL 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352513  1027 EEmlEMAQKGVLHAVHT---AYSRlpgkpKVYVQDILRQQLAsevlrvlHKEPGHLYVCGDVRMARDVAHTLKQ 1097
Cdd:cd06218  142 VE--EFEALGAEVYVATddgSAGT-----KGFVTDLLKELLA-------EARPDVVYACGPEPMLKAVAELAAE 201
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
906-1109 2.57e-05

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: 46.75  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSrdHTPTEIHLTVAVVTyhtrdgqgplhHGVCSTWL-NSLKPQDPVPcfVRNASG-FHLPEDPSHPCILIGPG 983
Cdd:cd06191   47 RCYSLCSS--PAPDEISITVKRVP-----------GGRVSNYLrEHIQPGMTVE--VMGPQGhFVYQPQPPGRYLLVAAG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   984 TGIAPFRSFWQqrlhdSQHKGVRGGRMTLVFGCRRPDeDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQ 1063
Cdd:cd06191  112 SGITPLMAMIR-----ATLQTAPESDFTLIHSARTPA-DMIFAQELRELADKPQRLRLLCIFTRETLDSDLLHGRIDGEQ 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1352513  1064 LASEVLRVLHKEPgHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQ 1109
Cdd:cd06191  186 SLGAALIPDRLER-EAFICGPAGMMDAVETALKELGMPPERIHTER 230
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
906-1035 3.33e-05

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: 46.43  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   906 RFYSISSSrDHTPTEIHLTVAVVtyhtrDGqgplhhGVCSTWLN-SLKPQDPVPCfvRNASG-FHLPEDPSHPCILIGPG 983
Cdd:cd06215   47 RAYTLSSS-PSRPDSLSITVKRV-----PG------GLVSNWLHdNLKVGDELWA--SGPAGeFTLIDHPADKLLLLSAG 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1352513   984 TGIAPFRSFWQQrLHDSQHKgvrgGRMTLVFGCRRPdEDHIYQEEMLEMAQK 1035
Cdd:cd06215  113 SGITPMMSMARW-LLDTRPD----ADIVFIHSARSP-ADIIFADELEELARR 158
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
904-1104 7.10e-05

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


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 45.62  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   904 KPRFYSISSSrDHTPTEIHLtvavvtyHTRDGQGplhhGVCST-WLNSLKPQDPVPcfVRNASG-FHLPEDPSHPCILIG 981
Cdd:cd06189   40 DKRPFSIASA-PHEDGEIEL-------HIRAVPG----GSFSDyVFEELKENGLVR--IEGPLGdFFLREDSDRPLILIA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   982 PGTGIAPFRSFWQQRLHDSQHKGVrggrmTLVFGCRRPdEDHIYQEEMLEMAQKgvlHA---VHTAYSRLPGKPKV---Y 1055
Cdd:cd06189  106 GGTGFAPIKSILEHLLAQGSKRPI-----HLYWGARTE-EDLYLDELLEAWAEA---HPnftYVPVLSEPEEGWQGrtgL 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1352513  1056 VQDILRQQLAS----EVlrvlhkepghlYVCGDVRMARDvahTLKQLVAAKLK 1104
Cdd:cd06189  177 VHEAVLEDFPDlsdfDV-----------YACGSPEMVYA---ARDDFVEKGLP 215
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
539-650 1.29e-04

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 42.97  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   539 VTILFATETGKSEALAWDLGALFScAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGnGDCPGNGEKLKKSLfmLKELNNK 618
Cdd:COG0716    1 ILIVYGSTTGNTEKVAEAIAEALG-AAGVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDFLEEL--KEDLSGK 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 1352513   619 fRYAVFGLG-SSMYPRfcaFAHDIDQKLSHLGA 650
Cdd:COG0716   77 -KVALFGTGdSSGYGD---ALGELKELLEEKGA 105
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
967-1034 8.62e-04

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 42.94  E-value: 8.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352513    967 FHLPEDPSHPCILIGPGTGIAPFRSFwqqrLHDSQHKGVRggR-MTLVFGCRRPDEdhIYqeeMLEMAQ 1034
Cdd:PRK07609  197 FFLREDSDKPIVLLASGTGFAPIKSI----VEHLRAKGIQ--RpVTLYWGARRPED--LY---LSALAE 254
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
942-1097 1.46e-03

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 41.61  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513    942 GVCSTWLNSLKPQDPVpCFVRNASGFH-LPEDPshPC---ILIGPGTGIAPFRSFWQQrlhdsqHKGV-RGGRMTLVFGC 1016
Cdd:PRK10926   73 GKLSPRLAALKPGDEV-QVVSEAAGFFvLDEVP--DCetlWMLATGTAIGPYLSILQE------GKDLeRFKNLVLVHAA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   1017 RRPdEDHIYQEEMLEMAQK--GVLHaVHTAYSR------LPGK-PKVyvqdILRQQLASEVLRVLHKEPGHLYVCGDVRM 1087
Cdd:PRK10926  144 RYA-ADLSYLPLMQELEQRyeGKLR-IQTVVSRetapgsLTGRvPAL----IESGELEAAVGLPMDAETSHVMLCGNPQM 217
                         170
                  ....*....|
gi 1352513   1088 ARDVAHTLKQ 1097
Cdd:PRK10926  218 VRDTQQLLKE 227
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
938-1111 1.74e-03

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: 41.07  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   938 PLHHGVCSTwLNSLKPQDPVpcfvrnasgfhLPEDP------SHPCILIGPGTGIAPFRSFWQQRLHDSQHKGvrggrMT 1011
Cdd:cd06196   69 PDHDGVTEQ-LGRLQPGDTL-----------LIEDPwgaieyKGPGVFIAGGAGITPFIAILRDLAAKGKLEG-----NT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1012 LVFGCRRPDeDHIYQEEMLEMAQKGVLHAVhtaySRLPgKPKVYVQDILRQQLASEVlrvlHKEPGHLYVCGDVRMARDV 1091
Cdd:cd06196  132 LIFANKTEK-DIILKDELEKMLGLKFINVV----TDEK-DPGYAHGRIDKAFLKQHV----TDFNQHFYVCGPPPMEEAI 201
                        170       180
                 ....*....|....*....|
gi 1352513  1092 AHTLKQLVAaklklNEEQVE 1111
Cdd:cd06196  202 NGALKELGV-----PEDSIV 216
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
942-1098 4.52e-03

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: 39.88  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513   942 GVCSTWLNSL-KPQDPVPCfvrnaSG----FHLpEDPSHPCILIGPGTGIAPFRSFWQQ-RLHDSQHKgvrggrMTLVFG 1015
Cdd:cd06209   71 GAMSSYLRDRaQPGDRLTL-----TGplgsFYL-REVKRPLLMLAGGTGLAPFLSMLDVlAEDGSAHP------VHLVYG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352513  1016 CRRPDeDHIYQEEMLEMAQKGVLHAVHTAYSRLP-GKP-KVYVQDilrqqlasevlrvlHKEPGHL-------YVCGDVR 1086
Cdd:cd06209  139 VTRDA-DLVELDRLEALAERLPGFSFRTVVADPDsWHPrKGYVTD--------------HLEAEDLndgdvdvYLCGPPP 203
                        170
                 ....*....|..
gi 1352513  1087 MARDVAHTLKQL 1098
Cdd:cd06209  204 MVDAVRSWLDEQ 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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