NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|411531966|gb|AFW19939|]
View 

assimilatory nitrate reductase, partial [Halomonas sp. WP5m-6]

Protein Classification

molybdopterin oxidoreductase family protein( domain architecture ID 11465282)

molybdopterin oxidoreductase family protein similar to Bacillus subtilis formate dehydrogenase YrhE and oxidoreductase YjgC

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
1-259 1.50e-100

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


:

Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 307.20  E-value: 1.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   1 QLAAHMDYHTPGARELVSRFWAtehlAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLV 80
Cdd:COG3383  347 VLPGYRDVTDPEHRAKVADAWG----VPPLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFL 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  81 IVSECVaNTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFseAFSYTHPWEIF 160
Cdd:COG3383  423 VVQDIF-LTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLGY--GFDYDSPEEVF 499

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 161 DEHARLSGyensgetqrlfDISglvGLGQAAYDALAPIQWPVTQQAPRGTARLFEDgRFATANGRAKLLPITPRPPAQPL 240
Cdd:COG3383  500 DEIARLTP-----------DYS---GISYERLEALGGVQWPCPSEDHPGTPRLFTG-RFPTPDGKARFVPVEYRPPAELP 564

                        250
                 ....*....|....*....
gi 411531966 241 SDDYPLRLNTGRVRDQWHT 259
Cdd:COG3383  565 DEEYPLVLTTGRLLDQWHT 583
 
Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
1-259 1.50e-100

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 307.20  E-value: 1.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   1 QLAAHMDYHTPGARELVSRFWAtehlAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLV 80
Cdd:COG3383  347 VLPGYRDVTDPEHRAKVADAWG----VPPLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFL 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  81 IVSECVaNTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFseAFSYTHPWEIF 160
Cdd:COG3383  423 VVQDIF-LTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLGY--GFDYDSPEEVF 499

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 161 DEHARLSGyensgetqrlfDISglvGLGQAAYDALAPIQWPVTQQAPRGTARLFEDgRFATANGRAKLLPITPRPPAQPL 240
Cdd:COG3383  500 DEIARLTP-----------DYS---GISYERLEALGGVQWPCPSEDHPGTPRLFTG-RFPTPDGKARFVPVEYRPPAELP 564

                        250
                 ....*....|....*....
gi 411531966 241 SDDYPLRLNTGRVRDQWHT 259
Cdd:COG3383  565 DEEYPLVLTTGRLLDQWHT 583
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 1-236 1.07e-96

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239155 [Multi-domain]  Cd Length: 565  Bit Score: 294.13  E-value: 1.07e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   1 QLAAHMDYHTPGARELVSRFWATEhlAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLV 80
Cdd:cd02754  343 LLPGHRSVNNPEHRAEVAKFWGVP--EGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFV 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  81 IVSECVANTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSYTHPWEIF 160
Cdd:cd02754  421 VVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEVF 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411531966 161 DEHARLSGyensgetQRLFDISGLvglgqaAYDALA--PIQWPVTQQAPRGTARLFEDGRFATANGRAKLLPITPRPP 236
Cdd:cd02754  501 EEYRRLSR-------GRGADLSGL------SYERLRdgGVQWPCPDGPPEGTRRLFEDGRFPTPDGRARFVAVPYRPP 565
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
20-144 2.17e-36

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 132.14  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   20 FWATEHLAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLPFADIVL 99
Cdd:pfam00384 235 GAASPVGALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTAKYADVIL 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 411531966  100 PASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKR 144
Cdd:pfam00384 315 PAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
2-259 1.60e-19

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 87.65  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   2 LAAHMDYHTPGARELVSRFWATehlaPA--LPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCP- 78
Cdd:PRK13532 429 LPADMVVTNPKHREIAEKIWKL----PEgtIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNINEERLPGWRNPd 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  79 -LVIVSECVANTDLLPfADIVLPASGWSEKDGTVTNSERRIS--RQQgmLPPPGEAKHDWWILCEVAKRLGFSEAFsyth 155
Cdd:PRK13532 505 nFIVVSDPYPTVSALA-ADLILPTAMWVEKEGAYGNAERRTQfwRQQ--VKAPGEAKSDLWQLVEFSKRFKTEEVW---- 577

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 156 PWEIFDEHARLSG-------YENsGETQR-------------------------LFDISGLVGLGQaAYDaLAP------ 197
Cdd:PRK13532 578 PEELLAKKPEYRGktlydvlFAN-GQVDKfplselaegylndeakhfgfyvqkgLFEEYASFGRGH-GHD-LAPfdtyhk 654

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411531966 198 ---IQWPV-----TQ---------QAPRGTARLFedgrFATANGRAKLLPITPRPPAQPLSDDYPLRLNTGRVRDQWHT 259
Cdd:PRK13532 655 vrgLRWPVvdgkeTLwryregydpYVKAGEGFKF----YGKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHT 729
 
Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
1-259 1.50e-100

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 307.20  E-value: 1.50e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   1 QLAAHMDYHTPGARELVSRFWAtehlAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLV 80
Cdd:COG3383  347 VLPGYRDVTDPEHRAKVADAWG----VPPLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFL 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  81 IVSECVaNTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFseAFSYTHPWEIF 160
Cdd:COG3383  423 VVQDIF-LTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLGY--GFDYDSPEEVF 499

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 161 DEHARLSGyensgetqrlfDISglvGLGQAAYDALAPIQWPVTQQAPRGTARLFEDgRFATANGRAKLLPITPRPPAQPL 240
Cdd:COG3383  500 DEIARLTP-----------DYS---GISYERLEALGGVQWPCPSEDHPGTPRLFTG-RFPTPDGKARFVPVEYRPPAELP 564

                        250
                 ....*....|....*....
gi 411531966 241 SDDYPLRLNTGRVRDQWHT 259
Cdd:COG3383  565 DEEYPLVLTTGRLLDQWHT 583
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 1-236 1.07e-96

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239155 [Multi-domain]  Cd Length: 565  Bit Score: 294.13  E-value: 1.07e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   1 QLAAHMDYHTPGARELVSRFWATEhlAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLV 80
Cdd:cd02754  343 LLPGHRSVNNPEHRAEVAKFWGVP--EGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFV 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  81 IVSECVANTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSYTHPWEIF 160
Cdd:cd02754  421 VVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEVF 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411531966 161 DEHARLSGyensgetQRLFDISGLvglgqaAYDALA--PIQWPVTQQAPRGTARLFEDGRFATANGRAKLLPITPRPP 236
Cdd:cd02754  501 EEYRRLSR-------GRGADLSGL------SYERLRdgGVQWPCPDGPPEGTRRLFEDGRFPTPDGRARFVAVPYRPP 565
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
43-259 1.14e-61

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 205.08  E-value: 1.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  43 DAIERGE---ITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLpFADIVLPASGWSEKDGTVTNSE-RRI 118
Cdd:COG0243  357 EAILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETAR-YADIVLPATTWLERDDIVTNSEdRRV 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 119 SRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSY-THPWEIFDEHARLSGYEnsgetqrlfdisglvGLGQAAYDALAP 197
Cdd:COG0243  436 HLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWgRTEEDYLRELLEATRGR---------------GITFEELREKGP 500

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411531966 198 IQWPVTQQAPrgtarLFEDGRFATANGRAKLLP-----------ITPRPPAQPLSDDYPLRLNTGRVRDQWHT 259
Cdd:COG0243  501 VQLPVPPEPA-----FRNDGPFPTPSGKAEFYSetlalpplpryAPPYEGAEPLDAEYPLRLITGRSRDQWHS 568
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
 29-235 2.15e-48

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239154 [Multi-domain]  Cd Length: 512  Bit Score: 167.00  E-value: 2.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  29 ALPD-APGYkavelfdaiergeITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVAnTDLLPFADIVLPASGWSEK 107
Cdd:cd02753  336 ALPNvLPGY-------------VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFL-TETAELADVVLPAASFAEK 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 108 DGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAfsYTHPWEIFDEHARL----SG--YEnsgetqRLFDI 181
Cdd:cd02753  402 DGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGF--YSHPEEIFDEIARLtpqyAGisYE------RLERP 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 411531966 182 SGLvglgqaaydalapiQWPVTQQAPRGTARLFEDgRFATANGRAKLLPITPRP 235
Cdd:cd02753  474 GGL--------------QWPCPDEDHPGTPILHTE-RFATPDGKARFMPVEYRP 512
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
20-144 2.17e-36

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 132.14  E-value: 2.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   20 FWATEHLAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLPFADIVL 99
Cdd:pfam00384 235 GAASPVGALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTAKYADVIL 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 411531966  100 PASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKR 144
Cdd:pfam00384 315 PAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 57-145 1.30e-28

Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.


Pssm-ID: 238218 [Multi-domain]  Cd Length: 374  Bit Score: 111.65  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  57 ATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLpFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWW 136
Cdd:cd00368  287 GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWE 365


                 ....*....
gi 411531966 137 ILCEVAKRL 145
Cdd:cd00368  366 ILRELAKRL 374
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
 28-225 1.52e-21

The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239167 [Multi-domain]  Cd Length: 501  Bit Score: 93.08  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  28 PALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALA-KCPLVIVSEcVANTDLLPFADIVLPASGWSE 106
Cdd:cd02766  307 PALTGNIGVPGGGAFYSNSGPPVKALWVYNSNPVAQAPDSNKVRKGLArEDLFVVVHD-QFMTDTARYADIVLPATTFLE 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 107 KDGTVTnSE--RRISRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSYTHPWEIFDEHARLSGYENSGETQRLFDISGL 184
Cdd:cd02766  386 HEDVYA-SYwhYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFEESDEEWLDQALDGTGLPLEGIDLERLLGPRK 464

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 411531966 185 VGLGQAAydalapiqwpvtqqaprgtarlFEDGRFATANGR 225
Cdd:cd02766  465 AGFPLVA----------------------WEDRGFPTPSGK 483
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 25-174 3.76e-21

NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440657 [Multi-domain]  Cd Length: 453  Bit Score: 91.82  E-value: 3.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  25 HLAPALPDAPgykavELFDAIERGEITALWVMATNPAVSmpDGEKVRRALAKCPLVIVSECVAnTDLLPFADIVLPASGW 104
Cdd:COG1034  313 ALLGALPDAA-----AILEAAEAGKLKALVLLGADPYDL--DPAAALAALAKADFVVVLDHFG-SATAERADVVLPAAAF 384

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 105 SEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGfsEAFSYTHPWEIFDEHARLSGYENSGE 174
Cdd:COG1034  385 AEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALG--AGLPYDSLEEVRAELAAEAPATVSAE 452
MopB_NDH-1_NuoG2-N7 cd02771
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ...
 26-166 5.94e-20

MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239172 [Multi-domain]  Cd Length: 472  Bit Score: 88.60  E-value: 5.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  26 LAP--ALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEkVRRALAKCPLVIVSEcVANTDLLPFADIVLPASG 103
Cdd:cd02771  313 LLLlgGHVTEPGLDLDGALAALEDGSADALIVLGNDLYRSAPERR-VEAALDAAEFVVVLD-HFLTETAERADVVLPAAS 390

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411531966 104 WSEKDGTVTNSERRISR-QQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSythPWEIFDEHARL 166
Cdd:cd02771  391 FAEKSGTFVNYEGRAQRfFKAYDDPAGDARSDWRWLHALAAKLGGKLVPS---DAAILDEIIAL 451
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
2-259 1.60e-19

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 87.65  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966   2 LAAHMDYHTPGARELVSRFWATehlaPA--LPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCP- 78
Cdd:PRK13532 429 LPADMVVTNPKHREIAEKIWKL----PEgtIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNINEERLPGWRNPd 504

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  79 -LVIVSECVANTDLLPfADIVLPASGWSEKDGTVTNSERRIS--RQQgmLPPPGEAKHDWWILCEVAKRLGFSEAFsyth 155
Cdd:PRK13532 505 nFIVVSDPYPTVSALA-ADLILPTAMWVEKEGAYGNAERRTQfwRQQ--VKAPGEAKSDLWQLVEFSKRFKTEEVW---- 577

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 156 PWEIFDEHARLSG-------YENsGETQR-------------------------LFDISGLVGLGQaAYDaLAP------ 197
Cdd:PRK13532 578 PEELLAKKPEYRGktlydvlFAN-GQVDKfplselaegylndeakhfgfyvqkgLFEEYASFGRGH-GHD-LAPfdtyhk 654

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411531966 198 ---IQWPV-----TQ---------QAPRGTARLFedgrFATANGRAKLLPITPRPPAQPLSDDYPLRLNTGRVRDQWHT 259
Cdd:PRK13532 655 vrgLRWPVvdgkeTLwryregydpYVKAGEGFKF----YGKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHT 729
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
 50-150 1.40e-15

The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239160 [Multi-domain]  Cd Length: 477  Bit Score: 75.81  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  50 ITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLpFADIVLPASGWSEKDGTVTNSERRI--SRQQGMLPP 127
Cdd:cd02759  330 VKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAM-LADIVLPVAMSLERPGLRGGFEAENfvQLRQKAVEP 408

                         90       100
                 ....*....|....*....|...
gi 411531966 128 PGEAKHDWWILCEVAKRLGFSEA 150
Cdd:cd02759  409 YGEAKSDYEIVLELGKRLGPEEA 431
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
 59-152 6.70e-14

Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239153 [Multi-domain]  Cd Length: 649  Bit Score: 70.89  E-value: 6.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  59 NPAVSMPDGEKVRRALAKCPLVIVSecvantDLLP-----FAD-------------IVLPASGWSEKDGTVTNSERRISR 120
Cdd:cd02752  342 NPNSSFPNANKVRRALDKLDWLVVI------DPFPtetaaFWKnpgmdpksiqtevFLLPAACQYEKEGSITNSGRWLQW 415

                         90       100       110
                 ....*....|....*....|....*....|..
gi 411531966 121 QQGMLPPPGEAKHDWWILCEVAKRLGFSEAFS 152
Cdd:cd02752  416 RYKVVEPPGEAKSDGDILVELAKRLGFLYEKE 447
MopB_Arsenite-Ox cd02756
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ...
 48-235 1.53e-13

Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239157 [Multi-domain]  Cd Length: 676  Bit Score: 69.82  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  48 GEITALWVMATNPAVSMPDG-----------EKVRRALAKCP----------------------LVIVSECVANTDLLPF 94
Cdd:cd02756  433 GKGKVLWVIGCDPYKTTPNAqrlretinhrsKLVTDAVEAALyagtydreamvcligdaiqpggLFIVVQDIYPTKLAED 512

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  95 ADIVLPASGWSEKDGTVTN-SERRISRQQGMLPPPGEAKHDWWILCEVAKRL----------GFSEAFSYTHPWEIfDEH 163
Cdd:cd02756  513 AHVILPAAANGEMNETSMNgHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeegkgGSAQYQFFGFIWKT-EED 591

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966 164 ARLSGYE---NSGETQRLFDISGLVGLGQAAYDALAP-----IQWPVTQQAPRG---TARLFEDGRFATANGRAKLLPIT 232
Cdd:cd02756  592 NFMDGSQefaDGGEFSEDYYVLGQERYEGVTYNRLKAvgvngIQLPVTTDTVTKilvTNVLRTEGVFDTEDGKAYVIDLA 671


                 ...
gi 411531966 233 PRP 235
Cdd:cd02756  672 PWP 674
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 43-155 2.18e-13

The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239152 [Multi-domain]  Cd Length: 609  Bit Score: 69.18  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  43 DAIER--GEITA------------LWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVAnTDLLPFADIVLPASGWSEKD 108
Cdd:cd02751  386 DALLNpgKEFTAngklktypdikmIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFW-TASARYADIVLPATTSLERN 464

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 411531966 109 ---GTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRLGFSEAFSYTH 155
Cdd:cd02751  465 digLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGR 514
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
 42-138 1.52e-12

MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.


Pssm-ID: 239169 [Multi-domain]  Cd Length: 386  Bit Score: 66.54  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  42 FDAIERGEITALWVMATNPAVSMPDGekvRRALAKCPLVIVSECVANtDLLPFADIVLPASGWSEKDGTVTNSERRISRQ 121
Cdd:cd02768  287 LALLEPGKAKLLLLGEDELDRSNPPA---AVALAAADAFVVYQGHHG-DTGAQADVILPAAAFTEKSGTYVNTEGRVQRF 362

                         90
                 ....*....|....*..
gi 411531966 122 QGMLPPPGEAKHDWWIL 138
Cdd:cd02768  363 KKAVSPPGDAREDWKIL 379
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 24-145 1.23e-11

The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239168 [Multi-domain]  Cd Length: 574  Bit Score: 64.25  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  24 EHLAPALPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPL-VIVSECVANTDLLPFAD-IVLPA 101
Cdd:cd02767  379 EVFGFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLtVHVATKLNRSHLVHGEEaLILPC 458

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411531966 102 SGWSEKDG--------TVTNSERRISRQQGMLPP-------------------PGEAKHDWWILCEVAKRL 145
Cdd:cd02767  459 LGRTEIDMqaggaqavTVEDSMSMTHTSRGRLKPasrvllseeaivagiagarLGEAKPEWEILVEDYDRI 529
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
 11-118 6.52e-11

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 62.27  E-value: 6.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  11 PGARELVSRFWATehlaPALPDAPGYKAVELFDAIERGEITALWVMATNPAvSMPDGEKVRRALAKCPLViVSECVANTD 90
Cdd:PRK07860 518 PAARAEVAAAWGV----DELPAAPGRDTAGILAAAAAGELGALLVGGVEPA-DLPDPAAALAALDAAGFV-VSLELRHSA 591

                         90       100
                 ....*....|....*....|....*...
gi 411531966  91 LLPFADIVLPASGWSEKDGTVTNSERRI 118
Cdd:PRK07860 592 VTERADVVLPVAPVAEKAGTFLNWEGRL 619
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
 50-152 8.53e-11

The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239156 [Multi-domain]  Cd Length: 454  Bit Score: 61.54  E-value: 8.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  50 ITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSEcVANTDLLPFADIVLPASGWSEKDGTVT----NSERRISRQQGMl 125
Cdd:cd02755  331 IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAID-ILPSDTALYADVILPEATYLERDEPFSdkggPAPAVATRQRAI- 408

                         90       100
                 ....*....|....*....|....*..
gi 411531966 126 PPPGEAKHDWWILCEVAKRLGFSEAFS 152
Cdd:cd02755  409 EPLYDTRPGWDILKELARRLGLFGTPS 435
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
 48-154 2.81e-10

The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239166 [Multi-domain]  Cd Length: 567  Bit Score: 60.19  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  48 GEITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSEcVANTDLLPFADIVLPASGWSEKDGTVTNSERR--ISRQQGML 125
Cdd:cd02765  385 GQIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVD-IFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAI 463

                         90       100
                 ....*....|....*....|....*....
gi 411531966 126 PPPGEAKHDWWILCEVAKRLGFSEAFSYT 154
Cdd:cd02765  464 EPLFESKSDFEIEKGLAERLGLGDYFPKT 492
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
 54-158 5.80e-10

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 59.30  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  54 WVMA-TNPAVSMPDGEKVRRALAKCPLVIVSEcVANTDLLPFADIVLPASGWSEKDGTVTNSERRIS----RQQgMLPPP 128
Cdd:PRK15488 433 WVMSrHNPMQTVTDRADVVKALKKLDLVVVCD-VYLSESAAYADVVLPESTYLERDEEISDKSGKNPayalRQR-VVEPI 510

                         90       100       110
                 ....*....|....*....|....*....|
gi 411531966 129 GEAKHDWWILCEVAKRLGFSEAFsythPWE 158
Cdd:PRK15488 511 GDTKPSWQIFKELGEKMGLGQYY----PWQ 536
MopB_Res-Cmplx1_Nad11 cd02773
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ...
 93-145 7.26e-10

MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239174 [Multi-domain]  Cd Length: 375  Bit Score: 58.43  E-value: 7.26e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411531966  93 PFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWILCEVAKRL 145
Cdd:cd02773  323 QIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 41-145 1.29e-09

The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239163 [Multi-domain]  Cd Length: 539  Bit Score: 58.18  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  41 LFDAIER---GEITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSEcVANTDLLPFADIVLPASGWSEKD-GTVTNSE- 115
Cdd:cd02762  366 LAEEILTdgpGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVD-VYMTETTRHADYILPPASQLEKPhATFFNLEf 444

                         90       100       110
                 ....*....|....*....|....*....|..
gi 411531966 116 -RRISR-QQGMLPPPGEAKHDWWILCEVAKRL 145
Cdd:cd02762  445 pRNAFRyRRPLFPPPPGTLPEWEILARLVEAL 476
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
 40-164 1.32e-09

This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239171 [Multi-domain]  Cd Length: 617  Bit Score: 58.10  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  40 ELFDAIERGE------------------ITALWVMATNPAVSMPDG-----EKVRRALAKCPLVIVSECVANTDLlPFAD 96
Cdd:cd02770  381 MWTDAIERGEemtaddggvkgadklksnIKMIWNYAGNTLINQHSDdnnttRALLDDESKCEFIVVIDNFMTPSA-RYAD 459

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411531966  97 IVLPASGWSEKDGTVTNS-----ERRISRQQgMLPPPGEAKHDWWILCEVAKRLGFSEAFSYTHPWEIFDEHA 164
Cdd:cd02770  460 ILLPDTTELEREDIVLTSnagmmEYLIYSQK-AIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEEL 531
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
 48-159 1.55e-09

Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239151 [Multi-domain]  Cd Length: 461  Bit Score: 57.71  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  48 GEITALWVMATNPAVSMPDGEKVRRA--LAKCPLVIVSECVANTDLLpFADIVLPASGWSEK-DGTVTNSERRISRQQGM 124
Cdd:cd02750  332 GQPRVLFVWRGNLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTAL-YSDIVLPAATWYEKhDLSTTDMHPFIHPFSPA 410

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 411531966 125 LPPPGEAKHDWWILCEVAKRLGFSEA-----FSYTHPWEI 159
Cdd:cd02750  411 VDPLWEAKSDWEIFKALAKKVPWRTLtgrqqFYLDHDWFL 450
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 59-170 2.50e-09

The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239170 [Multi-domain]  Cd Length: 609  Bit Score: 57.27  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  59 NPAVSMPDGEKVRRALAKCPLVIVSECVAnTDLLPFADIVLPASGWSEK-DGTVTNSERRISRQQGMLPPPGEAKHDWWI 137
Cdd:cd02769  418 NPFHHHQDLNRLIRAWQKPETVIVHEPFW-TATARHADIVLPATTSLERnDIGGSGDNRYIVAMKQVVEPVGEARDDYDI 496

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 411531966 138 LCEVAKRLGFSEAFSYT--------HPWEIFDEHARLSGYE 170
Cdd:cd02769  497 FADLAERLGVEEQFTEGrdemewlrHLYEESRAQAAARGVE 537
MopB_CT_Nitrate-R-NapA-like cd02791
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 242-259 7.77e-07

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs


Pssm-ID: 239192 [Multi-domain]  Cd Length: 122  Bit Score: 46.80  E-value: 7.77e-07
                         10
                 ....*....|....*...
gi 411531966 242 DDYPLRLNTGRVRDQWHT 259
Cdd:cd02791    1 AEYPLWLNTGRVRDQWHT 18
MopB_Arsenate-R cd02757
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ...
 58-161 8.19e-07

This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239158 [Multi-domain]  Cd Length: 523  Bit Score: 49.75  E-value: 8.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  58 TNPAVSMPDGEKVRRALAKCPLVIVSECVANtDLLPFADIVLPASGWSEKDG---TVTNSERRISRQQGMLPPPGEAKHD 134
Cdd:cd02757  367 DNPVFSNPDGMSWEEALAKIPFHVHLSPFMS-ETTYFADIVLPDGHHFERWDvmsQENNLHPWLSIRQPVVKSLGEVREE 445

                         90       100       110
                 ....*....|....*....|....*....|
gi 411531966 135 WWILCEVAKRL---GFSEAFSYtHPWEIFD 161
Cdd:cd02757  446 TEILIELAKKLdpkGSDGMKRY-APGQFKD 474
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
 242-259 1.91e-05

This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 238282 [Multi-domain]  Cd Length: 120  Bit Score: 42.88  E-value: 1.91e-05
                         10
                 ....*....|....*...
gi 411531966 242 DDYPLRLNTGRVRDQWHT 259
Cdd:cd00508    1 EEYPLVLTTGRLLEHWHT 18
MopB_Phenylacetyl-CoA-OR cd02760
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ...
 58-152 3.53e-05

The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239161 [Multi-domain]  Cd Length: 760  Bit Score: 44.58  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  58 TNPAVSMPDGEKVRRALAKCPLViVSECVANTDLLPFADIVLPASGWSEKDGTVTN----------SERRISRQQGMLPP 127
Cdd:cd02760  522 TNPAISFWDTATLVDNIAKFPFT-VSFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfveqfwEHRGVVLRQPAVEP 600

                         90       100
                 ....*....|....*....|....*
gi 411531966 128 PGEAKHDWWILCEVAKRLGFSEAFS 152
Cdd:cd02760  601 QGEARDFTWISTELAKRTGLLADYN 625
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
15-129 8.61e-05

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 43.50  E-value: 8.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  15 ELVSRFWATEHLAPalPDAPGYKAVELFDAIERGEITALWVMATNPAVSMPDGEKVRRALAKCPLVIVSECVANTDLLPF 94
Cdd:PRK09939 423 EFLARLGERYGFTP--PHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLT 500

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 411531966  95 A--DIVLPASGWSEKDG--------TVTNSERRISRQQGMLPPPG 129
Cdd:PRK09939 501 ArhSYILPVLGRSEIDMqksgaqavTVEDSMSMIHASRGVLKPAG 545
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
 66-138 1.22e-04

MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239173 [Multi-domain]  Cd Length: 414  Bit Score: 42.73  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411531966  66 DGEKVRRALAKCPLVIVSECVANTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQGMLPPPGEAKHDWWIL 138
Cdd:cd02772  335 NPAQALAALNQAEFVVALSAFASAALLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
PRK15102 PRK15102
trimethylamine-N-oxide reductase TorA;
57-152 6.39e-04

trimethylamine-N-oxide reductase TorA;


Pssm-ID: 237909 [Multi-domain]  Cd Length: 825  Bit Score: 40.81  E-value: 6.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  57 ATNPAVSMPDGEKVRRALAKCPLVIVSEcVANTDLLPFADIVLPASGWSEK---DGTVTNSERRISRQQGMLPPPGEAKH 133
Cdd:PRK15102 475 GTNPWHRHQDRNRMKEAFRKLETVVAID-NQWTATCRFADIVLPACTQFERndiDQYGSYSNRGIIAMKKVVEPLFESRS 553

                         90
                 ....*....|....*....
gi 411531966 134 DWWILCEVAKRLGFSEAFS 152
Cdd:PRK15102 554 DFDIFRELCRRFGREKEYT 572
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 56-146 4.85e-03

The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239164 [Multi-domain]  Cd Length: 679  Bit Score: 37.89  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411531966  56 MATNPAVSMPdgeKVRRALA--------KCPLVIVSECVaNTDLLPFADIVLPASGWSEKDGTVTNSERRISRQQG---- 123
Cdd:cd02763  432 MAWNSSMNTP---EVREMLTdkdasgnyKIPFIIVCDAF-YSEMVAFADLVLPDTTYLERHDAMSLLDRPISEADGpvda 507

                         90       100
                 ....*....|....*....|....*..
gi 411531966 124 ----MLPPPGEAKHDWWILCEVAKRLG 146
Cdd:cd02763  508 irvpIVEPKGDVKPFQEVLIELGTRLG 534
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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