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Conserved domains on  [gi|1134962969|gb|APX78175|]
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sulfate ABC transporter substrate-binding protein [Achromobacter insolitus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Molybdopterin-Binding super family cl09928
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 4-196 2.22e-79

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.


The actual alignment was detected with superfamily member TIGR01553:

Pssm-ID: 447860 [Multi-domain]  Cd Length: 1009  Bit Score: 254.84  E-value: 2.22e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969    4 MNRRQFFKVTGATLAGSSLALLGAAPGTAMAEVRQYKLARMTETRNTCPYCSVACGLLMYGLGDGSKNARASIMHIEGDP 83
Cdd:TIGR01553    2 ISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGDP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   84 DHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSWDDALTRITKLMKADRDANFVEKTADGKTVNRWLTTG 163
Cdd:TIGR01553   82 DHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGIA 161

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1134962969  164 MLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:TIGR01553  162 SVGSSAMDNEECWLYQKWLRSLGLFYIEHQARI 194
 
Name Accession Description Interval E-value
formate-DH-alph TIGR01553
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ...
 4-196 2.22e-79

formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273689 [Multi-domain]  Cd Length: 1009  Bit Score: 254.84  E-value: 2.22e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969    4 MNRRQFFKVTGATLAGSSLALLGAAPGTAMAEVRQYKLARMTETRNTCPYCSVACGLLMYGLGDGSKNARASIMHIEGDP 83
Cdd:TIGR01553    2 ISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGDP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   84 DHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSWDDALTRITKLMKADRDANFVEKTADGKTVNRWLTTG 163
Cdd:TIGR01553   82 DHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGIA 161

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1134962969  164 MLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:TIGR01553  162 SVGSSAMDNEECWLYQKWLRSLGLFYIEHQARI 194
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
 48-196 2.03e-73

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: 233.06  E-value: 2.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  48 RNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSW 127
Cdd:cd02752     1 RTICPYCSVGCGLIAY-----VQNGV--WVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134962969 128 DDALTRITKLMKADRDANFVEKTADGKTVNRWLTTGMLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:cd02752    74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARI 142
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
26-195 1.41e-31

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 119.95  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  26 GAAPGTAMAEVRQyklarMTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:COG0243     8 AAGAGAAALEAAG-----TKTVKTTCPGCGVGCGLGVK-----VEDGR--VVRVRGDPDHPVNRGRLCAKGAALDERLYS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969 106 PNRLKYPEYR--APGSDKWVRMSWDDALTRITKLMKAdrdanfVEKTADGKTVnrWLTTGMLAASASSNEVGYITHKTVR 183
Cdd:COG0243    76 PDRLTYPMKRvgPRGSGKFERISWDEALDLIAEKLKA------IIDEYGPEAV--AFYTSGGSAGRLSNEAAYLAQRFAR 147

                         170
                  ....*....|..
gi 1134962969 184 SMGILAFDNQAR 195
Cdd:COG0243   148 ALGTNNLDDNSR 159
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
 44-105 2.82e-20

Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.


Pssm-ID: 197994 [Multi-domain]  Cd Length: 55  Bit Score: 79.99  E-value: 2.82e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969   44 MTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:smart00926   1 EKWVPTVCPLCGVGCGLLVE-----VKDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
Molybdop_Fe4S4 pfam04879
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ...
 44-105 3.11e-20

Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.


Pssm-ID: 428168 [Multi-domain]  Cd Length: 55  Bit Score: 79.64  E-value: 3.11e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  44 MTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:pfam04879   1 MKVVKTICPYCGVGCGLEVH-----VKDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
 3-138 1.43e-11

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 62.38  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   3 NMNRRQFFKVTGATLAGSSLALLgaAPGT-AMAEVRQYKlARMTETRNTCPYCSVACGLlmyglgdgskNARA---SIMH 78
Cdd:PRK15488    2 SLSRRDFLKGAGAGCAACALGSL--LPGAlAANEIAQLK-GKTKLTPSICEMCSTRCPI----------EARVvngKNVF 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  79 IEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSWDDALTRITKLM 138
Cdd:PRK15488   69 IQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKL 130
 
Name Accession Description Interval E-value
formate-DH-alph TIGR01553
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ...
 4-196 2.22e-79

formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits of 32 and 20 kDa. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273689 [Multi-domain]  Cd Length: 1009  Bit Score: 254.84  E-value: 2.22e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969    4 MNRRQFFKVTGATLAGSSLALLGAAPGTAMAEVRQYKLARMTETRNTCPYCSVACGLLMYGLGDGSKNARASIMHIEGDP 83
Cdd:TIGR01553    2 ISRRAFLKLTAGGATLSAFGGLGFDLAPAKAQARALKTVDAKQTTSVCCYCSVSCGLLVYSSSHTGDNKTNRAIHVEGDP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   84 DHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSWDDALTRITKLMKADRDANFVEKTADGKTVNRWLTTG 163
Cdd:TIGR01553   82 DHPINRGSLCPKGASTWDLVNNERRPANPLYRAPGSDQWEEISWDWAIDTIARRVKDTRDATFVTKDAKGQVVNRCDGIA 161

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1134962969  164 MLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:TIGR01553  162 SVGSSAMDNEECWLYQKWLRSLGLFYIEHQARI 194
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
 48-196 2.03e-73

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: 233.06  E-value: 2.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  48 RNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSW 127
Cdd:cd02752     1 RTICPYCSVGCGLIAY-----VQNGV--WVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGSGKWEEISW 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134962969 128 DDALTRITKLMKADRDANFVEKTADGKTVNRWLTTGMLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:cd02752    74 DEALDEIARKMKDIRDASFVEKNAAGVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARI 142
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 48-196 1.25e-33

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: 122.82  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  48 RNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSDKWVRMSW 127
Cdd:cd00368     1 PSVCPFCGVGCGILVY-----VKDGK--VVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISW 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134962969 128 DDALTRITKLMKADRDANFVEKTAdgktvnrwlttgMLAASASSNEVGYITHKTVRSMGILAFDNQARV 196
Cdd:cd00368    74 DEALDEIAEKLKEIREKYGPDAIA------------FYGGGGASNEEAYLLQKLLRALGSNNVDSHARL 130
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
26-195 1.41e-31

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 119.95  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  26 GAAPGTAMAEVRQyklarMTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:COG0243     8 AAGAGAAALEAAG-----TKTVKTTCPGCGVGCGLGVK-----VEDGR--VVRVRGDPDHPVNRGRLCAKGAALDERLYS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969 106 PNRLKYPEYR--APGSDKWVRMSWDDALTRITKLMKAdrdanfVEKTADGKTVnrWLTTGMLAASASSNEVGYITHKTVR 183
Cdd:COG0243    76 PDRLTYPMKRvgPRGSGKFERISWDEALDLIAEKLKA------IIDEYGPEAV--AFYTSGGSAGRLSNEAAYLAQRFAR 147

                         170
                  ....*....|..
gi 1134962969 184 SMGILAFDNQAR 195
Cdd:COG0243   148 ALGTNNLDDNSR 159
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
44-196 8.48e-30

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


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 114.98  E-value: 8.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  44 MTETRNTCPYCSVACGLLMYGLGDGsknarasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGsdKWV 123
Cdd:COG3383     4 MKKVKTVCPYCGVGCGIDLEVKDGK-------IVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGG--EFR 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134962969 124 RMSWDDALTRITKLMKADRDanfvEKTADGktvnrwltTGMLAASASSNEVGYITHKTVRS-MGILAFDNQARV 196
Cdd:COG3383    75 EVSWDEALDLVAERLREIQA----EHGPDA--------VAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARL 136
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
 50-196 3.07e-24

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: 98.82  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYGlgdgsKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGsdKWVRMSWDD 129
Cdd:cd02753     3 VCPYCGVGCGLELWV-----KDNK--IVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNG--KFVEASWDE 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134962969 130 ALTRITKLMKADRDANFVEKTAdgktvnrwlttgMLAASASSNEVGYITHKTVRS-MGILAFDNQARV 196
Cdd:cd02753    74 ALSLVASRLKEIKDKYGPDAIA------------FFGSAKCTNEENYLFQKLARAvGGTNNVDHCARL 129
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 48-195 4.88e-23

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: 95.37  E-value: 4.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  48 RNTCPYCSVACGLLMYGLGDGSKNARasimhieGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSdKWVRMSW 127
Cdd:cd02754     1 KTTCPYCGVGCGVEIGVKDGKVVAVR-------GDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG-ELVPVSW 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134962969 128 DDALTRITKLMKADRDANFVEKTAdgktvnrWLTTGMLaasasSNEVGYITHKTVRS-MGILAFDNQAR 195
Cdd:cd02754    73 DEALDLIAERFKAIQAEYGPDSVA-------FYGSGQL-----LTEEYYAANKLAKGgLGTNNIDTNSR 129
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
 50-134 4.71e-21

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: 89.67  E-value: 4.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRA--PGSDKWVRMSW 127
Cdd:cd02759     3 TCPGCHSGCGVLVY-----VKDGK--LVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGENKWERISW 75


                  ....*..
gi 1134962969 128 DDALTRI 134
Cdd:cd02759    76 DEALDEI 82
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
 44-105 2.82e-20

Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.


Pssm-ID: 197994 [Multi-domain]  Cd Length: 55  Bit Score: 79.99  E-value: 2.82e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969   44 MTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:smart00926   1 EKWVPTVCPLCGVGCGLLVE-----VKDGR--VVRVRGDPDHPVNRGRLCPKGRAGLEQVYS 55
Molybdop_Fe4S4 pfam04879
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ...
 44-105 3.11e-20

Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.


Pssm-ID: 428168 [Multi-domain]  Cd Length: 55  Bit Score: 79.64  E-value: 3.11e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  44 MTETRNTCPYCSVACGLLMYglgdgSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHS 105
Cdd:pfam04879   1 MKVVKTICPYCGVGCGLEVH-----VKDGK--IVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
 48-143 6.63e-19

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: 83.45  E-value: 6.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  48 RNTCPY-CSVACGLLMYGLGDGsknarasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRA-PGSDKWVRM 125
Cdd:cd02766     1 RSVCPLdCPDTCSLLVTVEDGR-------IVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVgRKGGQWERI 73

                          90
                  ....*....|....*...
gi 1134962969 126 SWDDALTRITKLMKADRD 143
Cdd:cd02766    74 SWDEALDTIAAKLKEIKA 91
MopB_Arsenate-R cd02757
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ...
 50-176 2.24e-17

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: 79.02  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYglgdgSKNARASimHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRA---PGSD---KWV 123
Cdd:cd02757     5 TCQGCTAWCGLQAY-----VEDGRVT--KVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprKGRDvdpKFV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134962969 124 RMSWDDALT----RITKLMKADRDANFVEKTADGKTVNRWLTTGMLAASASSNEVGY 176
Cdd:cd02757    78 PISWDEALDtiadKIRALRKENEPHKIMLHRGRYGHNNSILYGRFTKMIGSPNNISH 134
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 50-144 2.48e-17

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: 78.98  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYGlgDGSKNARasimhIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGSdkWVRMSWDD 129
Cdd:cd02762     3 ACILCEANCGLVVTV--EDGRVAS-----IRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRRRGGS--FEEIDWDE 73

                          90
                  ....*....|....*
gi 1134962969 130 ALTRITKLMKADRDA 144
Cdd:cd02762    74 AFDEIAERLRAIRAR 88
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
 49-179 1.24e-15

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: 73.87  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  49 NTCPYCSVACGLLMYglgdgSKNARAsiMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMS 126
Cdd:cd02755     3 SICEMCSSRCGILAR-----VEDGRV--VKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGerGEGKFREAS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1134962969 127 WDDALTRITKLMKADRDANFVEKTA--DGKTVNRWLTTGMLAASASSNevgYITH 179
Cdd:cd02755    76 WDEALQYIASKLKEIKEQHGPESVLfgGHGGCYSPFFKHFAAAFGSPN---IFSH 127
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 50-145 4.20e-15

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: 72.56  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYgLGDGSknarasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSW 127
Cdd:cd02763     3 TCYMCACRCGIRVH-LRDGK------VRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGprGSGQFEEIEW 75

                          90
                  ....*....|....*...
gi 1134962969 128 DDALTRITKLMKADRDAN 145
Cdd:cd02763    76 EEAFSIATKRLKAARATD 93
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
 3-138 1.43e-11

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 62.38  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   3 NMNRRQFFKVTGATLAGSSLALLgaAPGT-AMAEVRQYKlARMTETRNTCPYCSVACGLlmyglgdgskNARA---SIMH 78
Cdd:PRK15488    2 SLSRRDFLKGAGAGCAACALGSL--LPGAlAANEIAQLK-GKTKLTPSICEMCSTRCPI----------EARVvngKNVF 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  79 IEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSWDDALTRITKLM 138
Cdd:PRK15488   69 IQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGerGEGKWQEISWDEAYQEIAAKL 130
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
 80-139 1.92e-10

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: 59.26  E-value: 1.92e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  80 EGDPDHPVNRGtlCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSWDDALTRITKLMK 139
Cdd:cd02770    33 DDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVGkrGEGKFVRISWDEALDTIASELK 92
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
3-140 2.50e-10

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 58.76  E-value: 2.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   3 NMNRRQFFK----VTGATLAGSSL-ALLGAAPGTAMAEVRQYKLArmtetrntCPYCSVACGLLMyglgdGSKNARasIM 77
Cdd:PRK13532    2 KLSRRDFMKanaaAAAAAAAGLSLpAVANAVVGSAQTAIKWDKAP--------CRFCGTGCGVLV-----GTKDGR--VV 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  78 HIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYP-------EYRAPGsdKWVRMSWDDALTRITKLMKA 140
Cdd:PRK13532   67 ATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQPllrmkdgKYDKEG--EFTPVSWDQAFDVMAEKFKK 134
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
 83-149 4.10e-10

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: 58.10  E-value: 4.10e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  83 PDH-PvnRGtlCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSWDDALTRItklmkADRDANFVEK 149
Cdd:cd02750    44 PDYnP--RG--CQRGASFSWYLYSPDRVKYPLKRVGarGEGKWKRISWDEALELI-----ADAIIDTIKK 104
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 ...
 50-144 1.45e-09

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: 56.24  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLmYGLGDGSknarasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRapGSDKWVRMSWDD 129
Cdd:cd02771     3 ICHHCSVGCNIS-LGERYGE------LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR--RGGTLVPVSWNE 73

                          90
                  ....*....|....*
gi 1134962969 130 ALTRITKLMKADRDA 144
Cdd:cd02771    74 ALDVAAARLKEAKDK 88
MopB_PHLH cd02764
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ...
 6-143 2.13e-09

The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.


Pssm-ID: 239165 [Multi-domain]  Cd Length: 524  Bit Score: 55.96  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   6 RRQFFKVTGATLAGSSLALLGAaPGTAMAEVRQyklarMTETRNT---CPYCSVACgLLMYGLGDGSKNARASIMHIEGD 82
Cdd:cd02764     1 RRGFLKLMGASLAMASAAACRY-PVEKIVPYVI-----WPENIVPgetVYYATSLV-PAGEGQGVLVKTVDGRPIKIEGN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134962969  83 PDHPVNRGTLCPKGAALIDFIHSPNRLKYPeYRAPGSDKWVRMSWDDALTRITKLMKADRD 143
Cdd:cd02764    74 PDHPASLGGTSARAQASVLSLYDPDRAQGP-LRRGIDGAYVASDWADFDAKVAEQLKAVKD 133
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
 44-144 3.89e-09

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: 55.23  E-value: 3.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  44 MTETRNTCPYCSVACGLLMyglgdGSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRAPGsdKWV 123
Cdd:COG1034   215 LKKTPSICPHCSVGCNIRV-----DVRGGK--VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDG--ELV 285

                          90       100
                  ....*....|....*....|.
gi 1134962969 124 RMSWDDALTRITKLMKADRDA 144
Cdd:COG1034   286 EASWEEALAAAAEGLKALKKA 306
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 108-195 4.77e-08

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: 51.92  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969 108 RLKYPEYRAPGSDKWVRMSWDDALTRITKLMKAdrdanfvekTADGKTVnrWLTTGMlaasaSSNEVGYITHKTVRSMGI 187
Cdd:cd02767    64 RLTYPMRYDAGSDHYRPISWDEAFAEIAARLRA---------LDPDRAA--FYTSGR-----ASNEAAYLYQLFARAYGT 127


                  ....*...
gi 1134962969 188 LAFDNQAR 195
Cdd:cd02767   128 NNLPDCSN 135
MopB_Tetrathionate-Ra cd02758
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ...
 50-135 6.64e-08

The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239159 [Multi-domain]  Cd Length: 735  Bit Score: 51.57  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  50 TCPYCSVACGLLMYglgdgSKNARASIMHIEGDPDHPVN---------------------------RGTLCPKGAALIDF 102
Cdd:cd02758     3 SCLGCWTQCGIRVR-----VDKETGKVLRIAGNPYHPLNtapslpyntplkeslylslvgenglkaRATACARGNAGLQY 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1134962969 103 IHSPNRLKYPEYRA--PGSDKWVRMSWDDALTRIT 135
Cdd:cd02758    78 LYDPYRVLQPLKRVgpRGSGKWKPISWEQLIEEVV 112
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
 51-191 8.13e-08

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: 51.13  E-value: 8.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  51 CPYCSVACGLLMyglgdGSKNARasIMHIEGDPDHPVNRGTLCPKGAALIDFIHSPNRLKYPEYRapGSDKWVRMSWDDA 130
Cdd:cd02768     4 DVHDALGSNIRV-----DVRGGE--VMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK--KGGKLVPVSWEEA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134962969 131 LTRItklmkadrdANFVEKTADGKtvnrwltTGMLAASASSNEVGYITHKTVRSMGILAFD 191
Cdd:cd02768    75 LKTV---------AEGLKAVKGDK-------IGGIAGPRADLESLFLLKKLLNKLGSNNID 119
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 93-134 1.02e-07

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: 51.08  E-value: 1.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134962969  93 CPKGAALIDFIHSPNRLKYPEYR------------APGSDKWVRMSWDDALTRI 134
Cdd:cd02751    32 CPRGRSVRDRVYSPDRIKYPMKRvgwlgngpgsreLRGEGEFVRISWDEALDLV 85
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
 83-134 2.89e-07

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: 49.78  E-value: 2.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134962969  83 PDHPVNRGtlCPKGAALIDFIHSPNRLKYPEYRAP--GSDKWVRMSWDDALTRI 134
Cdd:cd02765    32 PDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGerGEGKFERITWDEALDTI 83
MopB_Phenylacetyl-CoA-OR cd02760
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ...
 51-149 8.42e-07

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: 48.43  E-value: 8.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  51 CPYCSVACGLLMYGLGDGSknarasIMHIEGDPD----HPVnRGTLCPKGAALIDFIHSPNRLKYPEYRA---------P 117
Cdd:cd02760     4 CYNCVAGPDFMAVKVVDGV------ATEIEPNFAaediHPA-RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkkgrnedP 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1134962969 118 GsdkWVRMSWDDALTRITKLMKADRDANFVEK 149
Cdd:cd02760    77 G---FVPISWDEALDLVAAKLRRVREKGLLDE 105
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
 4-179 2.02e-06

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 47.33  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969   4 MNRRQFFKVT---GATLAGSSLALlgaaPGTAMAEVRQYKLARMTETRNTCPYCSVACG----LLMYGLgDGSknarasI 76
Cdd:PRK14990   14 VSRRGLVKTTaigGLAMASSALTL----PFSRIAHAVDSAIPTKSDEKVIWSACTVNCGsrcpLRMHVV-DGE------I 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969  77 MHIEGDPDHPVNRGTL-----CPKGAALIDFIHSPNRLKYPEYR--APGSDKWVRMSWDDAL----TRITKLMKADRDA- 144
Cdd:PRK14990   83 KYVETDNTGDDNYDGLhqvraCLRGRSMRRRVYNPDRLKYPMKRvgARGEGKFERISWEEAYdiiaTNMQRLIKEYGNEs 162

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1134962969 145 ---NFVEKTADGKTVNRWLTTGMLAASASSNEVGYITH 179
Cdd:PRK14990  163 iylNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNH 200
MopB_Arsenite-Ox cd02756
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ...
 82-145 1.40e-04

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: 41.70  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134962969  82 DPDHPVNRGTLCPKGAALIDFIHSP------NRLKYPEYRApgSDKWVRMSWDDALTRITKLMKA--DRDAN 145
Cdd:cd02756    85 DKECPVNSGNYSTRGGTNAERIWSPdnrvgeTRLTTPLVRR--GGQLQPTTWDDAIDLVARVIKGilDKDGN 154
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
108-192 4.62e-04

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 40.08  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134962969 108 RLKYPEYRApGSDKWVRMSWDDALTRITKLMKADRDANFVEKTADGKTVNRWLTTGMLAASAS------SNEVGYITHKT 181
Cdd:pfam00384   1 RLKYPMVRR-GDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDVESLYALKKllnrlgSKNGNTEDHNG 79

                          90
                  ....*....|.
gi 1134962969 182 VRSMGILAFDN 192
Cdd:pfam00384  80 DLCTAAAAAFG 90
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 80-144 3.02e-03

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: 37.63  E-value: 3.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1134962969  80 EGDPDhPvnrgtlCPKGAALIDFIHSPNRLKYPEYR-------------APGSDKWVRMSWDDALTRITKLMKADRDA 144
Cdd:cd02769    25 EEDPD-P------SPLLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKT 95
 
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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