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Conserved domains on  [gi|301015936|pdb|3MMA|E]
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Chain E, Sulfite reductase, dissimilatory-type subunit beta

Protein Classification

dsrB family protein( domain architecture ID 11493565)

dsrB family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 22-366 0e+00

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


:

Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 633.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E         22 VIAKNYGKWKYHEVVKPGVIKRVAESGDVIYVVRFGTPRLLSIYTVRELCDIADKYSDGYLRWTSRNNVEFFVTDESKID 101
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        102 DLINEVQErVGFPCGGTWDAVKGeyglsNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANM 181
Cdd:TIGR02066  81 PLIDELEE-VGFPVGGTGDAVKG-----NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        182 CGAVHASDIAIVGIHRTPPIPNDEAIRKTCEIPSTVAACPTGALKP--DMKNKTIKVDVEKCMYCGNCYTMCPGMPLFDP 259
Cdd:TIGR02066 155 CGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPrrDGKNKSLEVDVEKCIYCGNCYTMCPAMPIFDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        260 ENDGAAIMVGGKLSEARRMPELSKVVVPWVPNEPPRWPTLVKYVKQILEAWAANANKHERLIEWVDRIGWERFFELTGLE 339
Cdd:TIGR02066 235 ENDGAAIWVGGKLSNARVMPELSKVVVPWIPNNPPRWPELVAYVKKILEAWKANAKKHERLIEWVERIGWERFFELVGLP 314

                         330       340
                  ....*....|....*....|....*..
3MMA_E        340 FTQHLIDDYRITPYFYSEFRASTQFKW 366
Cdd:TIGR02066 315 FTQHHIDDWRIAPYFYSTFRASTQFKF 341
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 22-366 0e+00

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 633.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E         22 VIAKNYGKWKYHEVVKPGVIKRVAESGDVIYVVRFGTPRLLSIYTVRELCDIADKYSDGYLRWTSRNNVEFFVTDESKID 101
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        102 DLINEVQErVGFPCGGTWDAVKGeyglsNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANM 181
Cdd:TIGR02066  81 PLIDELEE-VGFPVGGTGDAVKG-----NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        182 CGAVHASDIAIVGIHRTPPIPNDEAIRKTCEIPSTVAACPTGALKP--DMKNKTIKVDVEKCMYCGNCYTMCPGMPLFDP 259
Cdd:TIGR02066 155 CGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPrrDGKNKSLEVDVEKCIYCGNCYTMCPAMPIFDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        260 ENDGAAIMVGGKLSEARRMPELSKVVVPWVPNEPPRWPTLVKYVKQILEAWAANANKHERLIEWVDRIGWERFFELTGLE 339
Cdd:TIGR02066 235 ENDGAAIWVGGKLSNARVMPELSKVVVPWIPNNPPRWPELVAYVKKILEAWKANAKKHERLIEWVERIGWERFFELVGLP 314

                         330       340
                  ....*....|....*....|....*..
3MMA_E        340 FTQHLIDDYRITPYFYSEFRASTQFKW 366
Cdd:TIGR02066 315 FTQHHIDDWRIAPYFYSTFRASTQFKF 341
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 127-339 5.21e-30

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 112.36  E-value: 5.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        127 GLSNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANMCGAVHASDIAIVGIHRtppipndea 206
Cdd:pfam01077   3 NVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWK--------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        207 irktceipstvaacptgalkpdmknktikvdvekcmycgncytmcpgmplfDPENDGAAIMVGGKLSEARRMPELSKvVV 286
Cdd:pfam01077  74 ---------------------------------------------------DGGEIGFNILVGGGLGRTPGAAATLK-VV 101

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
3MMA_E        287 PWVPNEpprwpTLVKYVKQILEAWA----ANANKHERLIEWVDRIGWERFFELTGLE 339
Cdd:pfam01077 102 PFVPEE-----DVLEVIEAILEVYRdhgdRENRKKERLKYLIERLGLEKFREEVEER 153
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 217-256 1.42e-10

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 56.60  E-value: 1.42e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
3MMA_E      217 VAACPTGALKPDmkNKTIKVDVEKCMYCGNCYTMCPGMPL 256
Cdd:COG2221  24 VAVCPTGAISLD--DGKLVIDEEKCIGCGACIRVCPTGAI 61
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 171-266 4.47e-10

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 56.82  E-value: 4.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E      171 CRI-SLACCANMCGAVHASdIAIVGIHRTPPIPNDEAIR-KTCEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCY 248
Cdd:cd10550  11 CRTcELACSLKHEGVFNPS-LSRIRVVRFEPEGLDVPVVcRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCV 89

                        90
                ....*....|....*....
3MMA_E      249 TMCP-GMPLFDPENDGAAI 266
Cdd:cd10550  90 EACPfGAIRVDPETGKAIK 108
PRK09898 PRK09898
ferredoxin-like protein;
209-260 5.68e-07

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 49.83  E-value: 5.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
3MMA_E       209 KTCEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:PRK09898 124 RQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPwMMATVNTE 176
 
Name Accession Description Interval E-value
dsrB TIGR02066
sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes ...
 22-366 0e+00

sulfite reductase, dissimilatory-type beta subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the beta subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131121 [Multi-domain]  Cd Length: 341  Bit Score: 633.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E         22 VIAKNYGKWKYHEVVKPGVIKRVAESGDVIYVVRFGTPRLLSIYTVRELCDIADKYSDGYLRWTSRNNVEFFVTDESKID 101
Cdd:TIGR02066   1 VVKKNYGKWKYHEVVKPGVIKHVAESGDVIYTVKAGTPRLLSVDTLRKLCDIADKYSDGYLRWTIRNNVEFLVSDESKIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        102 DLINEVQErVGFPCGGTWDAVKGeyglsNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANM 181
Cdd:TIGR02066  81 PLIDELEE-VGFPVGGTGDAVKG-----NIVHTQGWLHCHIPAIDASGIVKAVMDELYEYFTDHKLPAMVRISLSCCANM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        182 CGAVHASDIAIVGIHRTPPIPNDEAIRKTCEIPSTVAACPTGALKP--DMKNKTIKVDVEKCMYCGNCYTMCPGMPLFDP 259
Cdd:TIGR02066 155 CGGVHASDIAIVGIHRKPPKINHEAVRNVCEIPSVVAACPTGALKPrrDGKNKSLEVDVEKCIYCGNCYTMCPAMPIFDP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        260 ENDGAAIMVGGKLSEARRMPELSKVVVPWVPNEPPRWPTLVKYVKQILEAWAANANKHERLIEWVDRIGWERFFELTGLE 339
Cdd:TIGR02066 235 ENDGAAIWVGGKLSNARVMPELSKVVVPWIPNNPPRWPELVAYVKKILEAWKANAKKHERLIEWVERIGWERFFELVGLP 314

                         330       340
                  ....*....|....*....|....*..
3MMA_E        340 FTQHLIDDYRITPYFYSEFRASTQFKW 366
Cdd:TIGR02066 315 FTQHHIDDWRIAPYFYSTFRASTQFKF 341
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 127-339 5.21e-30

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 112.36  E-value: 5.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        127 GLSNIVHTQGWIHCHTPAIDASGIVKAVMDELYEYFTDHKLPAMCRISLACCANMCGAVHASDIAIVGIHRtppipndea 206
Cdd:pfam01077   3 NVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWK--------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        207 irktceipstvaacptgalkpdmknktikvdvekcmycgncytmcpgmplfDPENDGAAIMVGGKLSEARRMPELSKvVV 286
Cdd:pfam01077  74 ---------------------------------------------------DGGEIGFNILVGGGLGRTPGAAATLK-VV 101

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
3MMA_E        287 PWVPNEpprwpTLVKYVKQILEAWA----ANANKHERLIEWVDRIGWERFFELTGLE 339
Cdd:pfam01077 102 PFVPEE-----DVLEVIEAILEVYRdhgdRENRKKERLKYLIERLGLEKFREEVEER 153
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 52-109 1.01e-11

Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.


Pssm-ID: 377044 [Multi-domain]  Cd Length: 67  Bit Score: 59.85  E-value: 1.01e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
3MMA_E         52 YVVRFGTP-RLLSIYTVRELCDIADKYSDGYLRWTSRNNVEFFVTDESKIDDLINEVQE 109
Cdd:pfam03460   8 YMVRVRVPgGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEELAE 66
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 217-256 1.42e-10

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 56.60  E-value: 1.42e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
3MMA_E      217 VAACPTGALKPDmkNKTIKVDVEKCMYCGNCYTMCPGMPL 256
Cdd:COG2221  24 VAVCPTGAISLD--DGKLVIDEEKCIGCGACIRVCPTGAI 61
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 171-266 4.47e-10

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 56.82  E-value: 4.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E      171 CRI-SLACCANMCGAVHASdIAIVGIHRTPPIPNDEAIR-KTCEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCY 248
Cdd:cd10550  11 CRTcELACSLKHEGVFNPS-LSRIRVVRFEPEGLDVPVVcRQCEDAPCVEACPVGAISRDEETGAVVVDEDKCIGCGMCV 89

                        90
                ....*....|....*....
3MMA_E      249 TMCP-GMPLFDPENDGAAI 266
Cdd:cd10550  90 EACPfGAIRVDPETGKAIK 108
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 194-261 2.02e-07

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 49.69  E-value: 2.02e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3MMA_E      194 GIHRTPPIPNDEAIRKT----CEIPSTVAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPEN 261
Cdd:cd04410  32 RIKVIEGGGLERAFLPVscmhCEDPPCVKACPTGAIYKD-EDGIVLIDEDKCIGCGSCVEACPyGAIVFDPEP 103
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 211-260 4.59e-07

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 48.90  E-value: 4.59e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
3MMA_E      211 CEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:cd10553  61 CENPWCVKACPTGAMQKREKDGIVYVDQELCIGCKACIEACPwGIPQWNPA 111
PRK09898 PRK09898
ferredoxin-like protein;
209-260 5.68e-07

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 49.83  E-value: 5.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
3MMA_E       209 KTCEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:PRK09898 124 RQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPwMMATVNTE 176
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 211-260 1.83e-06

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 47.39  E-value: 1.83e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
3MMA_E      211 CEIPSTVAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:cd16366  73 CTDAGCLAACPTGAIIRT-ETGTVVVDPETCIGCGYCVNACPfDIPRFDEE 122
PRK13795 PRK13795
hypothetical protein; Provisional
 217-261 2.33e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 49.22  E-value: 2.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
3MMA_E       217 VAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCPGMPLFDPEN 261
Cdd:PRK13795 590 VGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVVKYKDKRN 634
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
211-252 3.70e-06

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 45.80  E-value: 3.70e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
3MMA_E      211 CEIPSTVAACPTGALKPDmkNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1142  55 CEDAPCAEVCPVGAITRD--DGAVVVDEEKCIGCGLCVLACP 94
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 217-252 4.04e-06

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 43.97  E-value: 4.04e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
3MMA_E      217 VAACPTGALK--PDMKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1143  11 VRVCPVDAITieDGEPGKVYVIDPDKCIGCGLCVEVCP 48
NapF COG1145
Ferredoxin [Energy production and conversion];
217-252 4.63e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 47.41  E-value: 4.63e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
3MMA_E      217 VAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1145 191 VKVCPTGAIRLKDGKPQIVVDPDKCIGCGACVKVCP 226
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
168-252 4.79e-06

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.10  E-value: 4.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E      168 PAMCRISLACCANMCGAVHASDIAIVGI----HRTPPIPNDEAIRKTCEipSTVAACPTGALKpdMKNKTIKVDVEKCMY 243
Cdd:COG4624  49 SCCPRCCLCCCCCCRCCVAISCIQVRGIiiidKRGPSIIRDKEKCKNCY--PCVRACPVKAIK--VDDGKAEIDEEKCIS 124


                ....*....
3MMA_E      244 CGNCYTMCP 252
Cdd:COG4624 125 CGQCVAVCP 133
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 178-252 7.07e-06

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 45.08  E-value: 7.07e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3MMA_E      178 CANMC--GAVHASDIaivgIHRTPPIPNDEAIRKTCEIPST--VAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:cd10549  48 CVEVCptGAIELTPE----GKEYVPKEKEAEIDEEKCIGCGlcVKVCPVDAITLE-DELEIVIDKEKCIGCGICAEVCP 121
PLN02431 PLN02431
ferredoxin--nitrite reductase
 68-194 7.71e-06

ferredoxin--nitrite reductase


Pssm-ID: 178050 [Multi-domain]  Cd Length: 587  Bit Score: 47.85  E-value: 7.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E        68 RELCDIADKYSDGYLRWTSRNNVEFFVTDESKIDDLINE--VQERVGFPcggtwdavkgEYGLSNIVHTQGWIHCHTPAI 145
Cdd:PLN02431 413 DELARLADEYGSGELRLTVEQNIIIPNVPNSKVEALLAEplLQRFSPNP----------GLLLKGLVACTGNQFCGQAII 482

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
3MMA_E       146 DASGIVKAVMDELYEYFTdhkLPAMCRISLACCANMCGAVHASDIAIVG 194
Cdd:PLN02431 483 ETKARALKVTEELERLVE---VPRPVRMHWTGCPNSCGQVQVADIGFMG 528
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
217-252 8.17e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 43.18  E-value: 8.17e-06
                        10        20        30
                ....*....|....*....|....*....|....*.
3MMA_E      217 VAACPTGALKpdMKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG2768  20 VKVCPVGAIS--IEDGKAVIDPEKCIGCGACIEVCP 53
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 182-252 8.38e-06

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 45.33  E-value: 8.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E      182 CGAVHAS-DIAIVGIHRTPPIPNDEAIR----------KTCEIPSTVAACPTGALKpdMKNKTIKVDVEKCMYCGNCYTM 250
Cdd:cd10554  19 CAAAHSGkGIFEAGTDGLPFLPRLRVVKtgevtapvqcRQCEDAPCANVCPVGAIS--QEDGVVQVDEERCIGCKLCVLA 96


                ..
3MMA_E      251 CP 252
Cdd:cd10554  97 CP 98
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 217-252 1.93e-05

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 43.54  E-value: 1.93e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
3MMA_E      217 VAACPTGALKPDMKNKTIK---VDVEKCMYCGNCYTMCP 252
Cdd:cd10549  15 VKACPTDAIELGPNGAIARgpeIDEDKCVFCGACVEVCP 53
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 211-260 3.67e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 43.32  E-value: 3.67e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
3MMA_E      211 CEIPSTVAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:cd16371  57 CENPACVKVCPTGAITKR-EDGIVVVDQDKCIGCGYCVWACPyGAPQYNPE 106
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 217-252 3.72e-05

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 41.25  E-value: 3.72e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
3MMA_E      217 VAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1149  20 VEVCPEGAIKLD-DGGAPVVDPDLCTGCGACVGVCP 54
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 211-266 4.85e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 42.64  E-value: 4.85e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
3MMA_E      211 CEIPSTVAACPTGALKPdMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPENDGAAI 266
Cdd:cd16370  56 CEDPPCAEACPTGALEP-RKGGGVVLDKEKCIGCGNCVKACIvGAIFWDEETNKPII 111
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 217-252 5.04e-05

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 40.59  E-value: 5.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
3MMA_E        217 VAACPTGALKPD-----MKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:pfam12838   8 VAACPVGAITLDevgekKGTKTVVIDPERCVGCGACVAVCP 48
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 211-260 6.04e-05

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 43.40  E-value: 6.04e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
3MMA_E      211 CEIPSTVAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPE 260
Cdd:COG0437  63 CDDPPCVKVCPTGATYKR-EDGIVLVDYDKCIGCRYCVAACPyGAPRFNPE 112
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 211-261 7.70e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 42.26  E-value: 7.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
3MMA_E      211 CEIPSTVAACPTGALKPDMKNKTIkVDVEKCMYCGNCYTMCP-GMPLFDPEN 261
Cdd:cd16374  46 CEDAPCMEVCPTGAIYRDEDGAVL-VDPDKCIGCGMCAMACPfGVPRFDPSL 96
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 211-261 1.82e-04

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 41.09  E-value: 1.82e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
3MMA_E      211 CEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPEN 261
Cdd:cd10563  60 CDEPPCVKACMSGAMHKDPETGIVIHDEEKCVGCWMCVMVCPyGAIRPDKER 111
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 211-262 2.66e-04

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 41.13  E-value: 2.66e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
3MMA_E      211 CEIPSTVAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPEND 262
Cdd:cd10562  73 CTDAACVKVCPTGALYKT-ENGAVVVDEDKCIGCGYCVAACPfDVPRYDETTN 124
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 266-335 3.19e-04

Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439925 [Multi-domain]  Cd Length: 519  Bit Score: 42.41  E-value: 3.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MMA_E      266 IMVGGKLSEARRmpeLSKVVVPWVPNEpprwpTLVKYVKQILEAWAANANKHERLIEWVDRIGWERFFEL 335
Cdd:COG0155 453 LYLGGGLGGDAR---LGRKYGPKVPAD-----EIPDALERLLEAYLAEREEGESFGDFVRRVGIEPLKEL 514
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 217-252 3.30e-04

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.88  E-value: 3.30e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
3MMA_E      217 VAACPTGALKPDmKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1144  39 WIVCPDGAIRVD-DGKYYGIDYDYCKGCGICAEVCP 73
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 211-269 3.82e-04

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 40.98  E-value: 3.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3MMA_E      211 CEIPSTVAACPTGALkpdMKNKT--IKVDVEKCMYCGNCYTMCP-GMPLFDPENDGAAIMVG 269
Cdd:cd10551  56 CENPPCVKVCPTGAT---YKREDgiVLVDYDKCIGCRYCMAACPyGARYFNPEEPHEFGEVP 114
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 217-252 4.13e-04

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.49  E-value: 4.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
3MMA_E      217 VAACPTGALKPDmkNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG4231  31 VKVCPADAIEEG--DGKAVIDPDLCIGCGSCVQVCP 64
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 217-252 4.86e-04

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 38.00  E-value: 4.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
3MMA_E        217 VAACPT-----GALKPDMKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:pfam13237  16 TAACPAgltrvGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 211-262 5.77e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 40.06  E-value: 5.77e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
3MMA_E      211 CEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPEND 262
Cdd:cd16369  54 CEDPTCAEVCPADAIKVTEDGVVQSALKPRCIGCSNCVNACPfGVPKYDEERN 106
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 217-252 7.07e-04

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.77  E-value: 7.07e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
3MMA_E      217 VAACPTGALKPDMK-NKTIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1146  17 VEVCPVDVLELDEEgKKALVINPEECIGCGACELVCP 53
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 229-260 7.66e-04

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 37.40  E-value: 7.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
3MMA_E      229 MKNKTIKVDVEKCMYCGNCYTMCP---------GMPLFDPE 260
Cdd:COG1149   1 VKRKIPVIDEEKCIGCGLCVEVCPegaiklddgGAPVVDPD 41
PRK06273 PRK06273
ferredoxin; Provisional
 210-257 1.72e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 38.92  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MMA_E       210 TCEIPSTVA------------ACPTGA-----LKPD------MKNKTIKVDVEKCMYCGNCYTMCPGMPLF 257
Cdd:PRK06273  39 TVELPKKVFeelcigcggcanVCPTKAiemipVEPVkitegyVKTKIPKIDYEKCVYCLYCHDFCPVFALF 109
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
211-261 2.49e-03

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 39.27  E-value: 2.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
3MMA_E       211 CEIPSTVAACPTGALKPDMKNKTIKVDVEKCMYCGNCYTMCP-GMPLFDPEN 261
Cdd:PRK10882 115 CVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPfNVPKYDYNN 166
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
215-252 2.93e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.15  E-value: 2.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
3MMA_E       215 STVAACPTGALKpdMKNKTIKVDVEKCMYCGNCYTMCP 252
Cdd:PRK07118 146 SCVAACPFDAIH--IENGLPVVDEDKCTGCGACVKACP 181
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 234-252 7.35e-03

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 33.76  E-value: 7.35e-03
                          10
                  ....*....|....*....
3MMA_E        234 IKVDVEKCMYCGNCYTMCP 252
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCP 19
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
209-252 7.39e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 38.30  E-value: 7.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
3MMA_E      209 KTCeipstVAACPTGALKPDMKNKtIKVDVEKCMYCGNCYTMCP 252
Cdd:COG1148 502 GRC-----VEVCPYGAISIDEKGV-AEVNPALCKGCGTCAAACP 539
 
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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