NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446741216|ref|WP_000818472|]
View 

MULTISPECIES: 4Fe-4S binding protein [Enterobacteriaceae]

Protein Classification

4Fe-4S binding protein( domain architecture ID 11417435)

4Fe-4S binding protein similar to Escherichia coli electron transport protein YccM

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
19-289 1.78e-54

Polyferredoxin NapH [Energy production and conversion];


:

Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 179.87  E-value: 1.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  19 KLPWNDWRNATTWRKATQLLLLAmnIYIAITFWYWvryyetasSTTFVARPGGIEGWLPIAGLMNLKYSLTtgqlpsvhA 98
Cdd:COG0348    2 SYPRLVKGRFRRLRRLVQLLFLL--LFLLGPWLRW--------LGDPAVLLDLAERRFYLFGLFWDFYLLA--------L 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  99 AAMLLLVAFIVISLLLKKAFCSWLCPVGTLSELIGDLGNKLFGRQCVLPRWLDIPLRGVKYLLLSFFLYIALLMPAQAIH 178
Cdd:COG0348   64 LLIGAALALFLLTLLFGRVWCGWVCPQGVLTELFSWLERKLGDRRLKLPWSLSKILRWLKYIILALWLLLALLTGLTFFG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 179 YFmlSPYSVVmdVKMLDFFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRRNAESCIDCGKCA 258
Cdd:COG0348  144 YF--SPIGTL--LRLLLFGVLGLWLLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDRGDCIDCGLCV 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446741216 259 KNCPSRIPVDKlIQVRTVECTGCMTCVESCP 289
Cdd:COG0348  220 KVCPMGIDIRK-GEINQSECINCGRCIDACP 249
 
Name Accession Description Interval E-value
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
19-289 1.78e-54

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 179.87  E-value: 1.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  19 KLPWNDWRNATTWRKATQLLLLAmnIYIAITFWYWvryyetasSTTFVARPGGIEGWLPIAGLMNLKYSLTtgqlpsvhA 98
Cdd:COG0348    2 SYPRLVKGRFRRLRRLVQLLFLL--LFLLGPWLRW--------LGDPAVLLDLAERRFYLFGLFWDFYLLA--------L 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  99 AAMLLLVAFIVISLLLKKAFCSWLCPVGTLSELIGDLGNKLFGRQCVLPRWLDIPLRGVKYLLLSFFLYIALLMPAQAIH 178
Cdd:COG0348   64 LLIGAALALFLLTLLFGRVWCGWVCPQGVLTELFSWLERKLGDRRLKLPWSLSKILRWLKYIILALWLLLALLTGLTFFG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 179 YFmlSPYSVVmdVKMLDFFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRRNAESCIDCGKCA 258
Cdd:COG0348  144 YF--SPIGTL--LRLLLFGVLGLWLLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDRGDCIDCGLCV 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446741216 259 KNCPSRIPVDKlIQVRTVECTGCMTCVESCP 289
Cdd:COG0348  220 KVCPMGIDIRK-GEINQSECINCGRCIDACP 249
napH_ TIGR02163
ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, ...
 87-290 1.27e-22

ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, found next to NapG,in operons that encode the periplasmic nitrate reductase. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this protein are designated MauN and are found in methylamine utilization operons in species that appear to lack a periplasmic nitrate reductase.


Pssm-ID: 274004 [Multi-domain]  Cd Length: 255  Bit Score: 95.11  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216   87 SLTTGQLPsvhaAAMLLLVAFIVI---SLLLKKAFCSWLCPVGtlseLIGDLGNKLfGRQCVLPRWLDIPlRGVKYLLLS 163
Cdd:TIGR02163  51 ILLAGHSP----PTNALIGALIIVafyALFGGRAFCSWVCPVN----LVTDFAAWL-RRKLGINKIIKLP-RNLRYWVLV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  164 FFLYIALLMPAQAIHYFmlSPYSVVMDVkmldFFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFK 243
Cdd:TIGR02163 121 LFLLLSFLSGLLIWEWF--NPVGILHRG----IIFGMGAGIWLILLVFLFDLLFSERGWCGHLCPLGAFYGLIGRKSLIK 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446741216  244 IR-RNAESCIDCGKCAKNCPS----RIPVDKL--IQVRTVECTGCMTCVESCPV 290
Cdd:TIGR02163 195 IAaSDREKCTNCMDCFNVCPEpqvlRMPLKKGgsTLVLSGDCTLCGRCIDVCHE 248
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 31-289 1.71e-22

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 95.35  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  31 WRKATQLLLLAMNIYIAITFWyWVRYYETASSTTFvarpggieGWLPIAGLMNLKYSLTTGQLPsvhaAAMLLLVAFIVI 110
Cdd:PRK09477  11 LRRLSQLSILALFLSGPWFGV-WILKGNLSSSLLF--------DTIPLTDPLATLQSLAAGHLP----ATVALIGALIIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 111 S---LLLKKAFCSWLCPVgtlsELIGDLGNKLfGRQCVLPRWLDIPlRGVKYLLLSFFLYIALLMPAQAihYFMLSPysv 187
Cdd:PRK09477  78 VfyaLAGGRAFCSWVCPV----NLVTDLANWL-RRKLGLNQSATLP-RNLRYWLLVLVLVGSALTGTLA--WEWINP--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 188 vmdVKMLD--FFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRR-NAESCIDCGKCAKNCPSR 264
Cdd:PRK09477 147 ---VSMLHrgLVFGFGSGWWLILAIFLFDLFVVEHGWCGHLCPLGAFYGLIGKKSLIRVKAhDRQKCTRCMDCFHVCPEP 223

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446741216 265 -------IPVDKLIQVRTVECTGCMTCVESCP 289
Cdd:PRK09477 224 qvlrpplKGKQSPSQVTSGDCITCGRCIDVCS 255
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 223-290 4.30e-10

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: 57.02  E-value: 4.30e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446741216 223 CRYLCPYGAL-MGVVSLLSPFKIRR---NAESCIDCGKCAKNCPS---RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:cd10549   48 CVEVCPTGAIeLTPEGKEYVPKEKEaeiDEEKCIGCGLCVKVCPVdaiTLEDELEIVIDKEKCIGCGICAEVCPV 122
Fer4_5 pfam12801
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 96-142 7.70e-10

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: 432796 [Multi-domain]  Cd Length: 48  Bit Score: 53.72  E-value: 7.70e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446741216   96 VHAAAMLLLVAFIVISLLLKKAFCSWLCPVGTLSELIGDLGNKLFGR 142
Cdd:pfam12801   1 LGPAGLILFLAVLVLTLLFGRVFCGWLCPFGALQELLAKLLRRKLGK 47
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 249-290 5.35e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.16  E-value: 5.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446741216 249 ESCIDCGKCAKNCPSR-IpvdKLIQVRTV---ECTGCMTCVESCPV 290
Cdd:NF038196 185 DKCIGCGICAKVCPVNnI---EMEDGKPVwghNCTHCLACIHRCPK 227
 
Name Accession Description Interval E-value
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
19-289 1.78e-54

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 179.87  E-value: 1.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  19 KLPWNDWRNATTWRKATQLLLLAmnIYIAITFWYWvryyetasSTTFVARPGGIEGWLPIAGLMNLKYSLTtgqlpsvhA 98
Cdd:COG0348    2 SYPRLVKGRFRRLRRLVQLLFLL--LFLLGPWLRW--------LGDPAVLLDLAERRFYLFGLFWDFYLLA--------L 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  99 AAMLLLVAFIVISLLLKKAFCSWLCPVGTLSELIGDLGNKLFGRQCVLPRWLDIPLRGVKYLLLSFFLYIALLMPAQAIH 178
Cdd:COG0348   64 LLIGAALALFLLTLLFGRVWCGWVCPQGVLTELFSWLERKLGDRRLKLPWSLSKILRWLKYIILALWLLLALLTGLTFFG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 179 YFmlSPYSVVmdVKMLDFFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRRNAESCIDCGKCA 258
Cdd:COG0348  144 YF--SPIGTL--LRLLLFGVLGLWLLLILLAAFLLLALFLRRQWCRYLCPYGAFQGLLSDLSTLRVRYDRGDCIDCGLCV 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446741216 259 KNCPSRIPVDKlIQVRTVECTGCMTCVESCP 289
Cdd:COG0348  220 KVCPMGIDIRK-GEINQSECINCGRCIDACP 249
napH_ TIGR02163
ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, ...
 87-290 1.27e-22

ferredoxin-type protein, NapH/MauN family; Most members of this family are the NapH protein, found next to NapG,in operons that encode the periplasmic nitrate reductase. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this protein are designated MauN and are found in methylamine utilization operons in species that appear to lack a periplasmic nitrate reductase.


Pssm-ID: 274004 [Multi-domain]  Cd Length: 255  Bit Score: 95.11  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216   87 SLTTGQLPsvhaAAMLLLVAFIVI---SLLLKKAFCSWLCPVGtlseLIGDLGNKLfGRQCVLPRWLDIPlRGVKYLLLS 163
Cdd:TIGR02163  51 ILLAGHSP----PTNALIGALIIVafyALFGGRAFCSWVCPVN----LVTDFAAWL-RRKLGINKIIKLP-RNLRYWVLV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  164 FFLYIALLMPAQAIHYFmlSPYSVVMDVkmldFFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFK 243
Cdd:TIGR02163 121 LFLLLSFLSGLLIWEWF--NPVGILHRG----IIFGMGAGIWLILLVFLFDLLFSERGWCGHLCPLGAFYGLIGRKSLIK 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446741216  244 IR-RNAESCIDCGKCAKNCPS----RIPVDKL--IQVRTVECTGCMTCVESCPV 290
Cdd:TIGR02163 195 IAaSDREKCTNCMDCFNVCPEpqvlRMPLKKGgsTLVLSGDCTLCGRCIDVCHE 248
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 31-289 1.71e-22

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 95.35  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  31 WRKATQLLLLAMNIYIAITFWyWVRYYETASSTTFvarpggieGWLPIAGLMNLKYSLTTGQLPsvhaAAMLLLVAFIVI 110
Cdd:PRK09477  11 LRRLSQLSILALFLSGPWFGV-WILKGNLSSSLLF--------DTIPLTDPLATLQSLAAGHLP----ATVALIGALIIT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 111 S---LLLKKAFCSWLCPVgtlsELIGDLGNKLfGRQCVLPRWLDIPlRGVKYLLLSFFLYIALLMPAQAihYFMLSPysv 187
Cdd:PRK09477  78 VfyaLAGGRAFCSWVCPV----NLVTDLANWL-RRKLGLNQSATLP-RNLRYWLLVLVLVGSALTGTLA--WEWINP--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 188 vmdVKMLD--FFRHMGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRR-NAESCIDCGKCAKNCPSR 264
Cdd:PRK09477 147 ---VSMLHrgLVFGFGSGWWLILAIFLFDLFVVEHGWCGHLCPLGAFYGLIGKKSLIRVKAhDRQKCTRCMDCFHVCPEP 223

                        250       260       270
                 ....*....|....*....|....*....|..
gi 446741216 265 -------IPVDKLIQVRTVECTGCMTCVESCP 289
Cdd:PRK09477 224 qvlrpplKGKQSPSQVTSGDCITCGRCIDVCS 255
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 228-290 3.14e-10

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 55.44  E-value: 3.14e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446741216 228 PYGaLMGVVsllspfKIRRNAESCIDCGKCAKNCPSRI--PVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG2221    1 PYG-IIGTW------PPKIDEEKCIGCGLCVAVCPTGAisLDDGKLVIDEEKCIGCGACIRVCPT 58
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 223-290 4.30e-10

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: 57.02  E-value: 4.30e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446741216 223 CRYLCPYGAL-MGVVSLLSPFKIRR---NAESCIDCGKCAKNCPS---RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:cd10549   48 CVEVCPTGAIeLTPEGKEYVPKEKEaeiDEEKCIGCGLCVKVCPVdaiTLEDELEIVIDKEKCIGCGICAEVCPV 122
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 241-290 6.66e-10

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 55.05  E-value: 6.66e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446741216 241 PFKIrrNAESCIDCGKCAKNCPSRI--PVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG4231   16 RYVI--DEDKCTGCGACVKVCPADAieEGDGKAVIDPDLCIGCGSCVQVCPV 65
Fer4_5 pfam12801
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 96-142 7.70e-10

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: 432796 [Multi-domain]  Cd Length: 48  Bit Score: 53.72  E-value: 7.70e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446741216   96 VHAAAMLLLVAFIVISLLLKKAFCSWLCPVGTLSELIGDLGNKLFGR 142
Cdd:pfam12801   1 LGPAGLILFLAVLVLTLLFGRVFCGWLCPFGALQELLAKLLRRKLGK 47
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 242-290 1.53e-09

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 53.58  E-value: 1.53e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446741216 242 FKIRRNAESCIDCGKCAKNCPS---RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1149    4 KIPVIDEEKCIGCGLCVEVCPEgaiKLDDGGAPVVDPDLCTGCGACVGVCPT 55
NapF COG1145
Ferredoxin [Energy production and conversion];
242-290 4.53e-09

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 56.27  E-value: 4.53e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446741216 242 FKIRRNAESCIDCGKCAKNCP----SRIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1145  175 AKAVIDAEKCIGCGLCVKVCPtgaiRLKDGKPQIVVDPDKCIGCGACVKVCPV 227
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
240-290 6.10e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 52.04  E-value: 6.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446741216 240 SPFKIRRNAESCIDCGKCAKNCPSR--IPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG2768    2 SLGKPYVDEEKCIGCGACVKVCPVGaiSIEDGKAVIDPEKCIGCGACIEVCPV 54
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 243-289 8.82e-09

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: 51.10  E-value: 8.82e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446741216  243 KIRRNAESCIDCGKCAKNCPSRIPVDKLIQVRTV---------ECTGCMTCVESCP 289
Cdd:pfam13237   1 KVVIDPDKCIGCGRCTAACPAGLTRVGAIVERLEgeavrigvwKCIGCGACVEACP 56
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 242-290 3.42e-08

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 49.71  E-value: 3.42e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446741216 242 FKIRRNAESCIDCGKCAKNCPS---RIPVD--KLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVdvlELDEEgkKALVINPEECIGCGACELVCPV 54
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 242-290 4.62e-08

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: 50.05  E-value: 4.62e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446741216 242 FKIRRNAESCIDCGKCAKNCP-SRIPVD--KLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1144   23 ERPVVDEDKCIGCGLCWIVCPdGAIRVDdgKYYGIDYDYCKGCGICAEVCPV 74
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 249-290 6.52e-08

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: 48.97  E-value: 6.52e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446741216 249 ESCIDCGKCAKNCPS------RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1143    2 DKCIGCGLCVRVCPVdaitieDGEPGKVYVIDPDKCIGCGLCVEVCPT 49
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 220-290 7.04e-08

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: 50.85  E-value: 7.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 220 HAWCRYLCPYGAL----MGVVSLlspfkirrNAESCIDCGKCAKNCPSRIPVDKLIQVRTVECTGCM---------TCVE 286
Cdd:cd04410   55 DPPCVKACPTGAIykdeDGIVLI--------DEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGdrldeglepACVK 126


                 ....
gi 446741216 287 SCPV 290
Cdd:cd04410  127 ACPT 130
Fer4_18 pfam13746
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 218-301 1.06e-07

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: 404610 [Multi-domain]  Cd Length: 114  Bit Score: 49.71  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216  218 IRHAWCRYLCPYGALMGVV----SLLSPFKIRRNAES-----------------------CIDCGKCAKNCPSRIPVDKL 270
Cdd:pfam13746   1 ARENFCIYACPYGRFQSVMydedTLTVVYDAVRGEGIygrkppkaglktkelrqqkgvgdCIDCESCVQVCPTGIDIRKG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446741216  271 IQvrtVECTGCMTCVESCpvaSTLTFSLQKP 301
Cdd:pfam13746  81 LQ---LECINCGLCIDAC---NTIMGKLGKP 105
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 247-290 1.15e-07

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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 48.05  E-value: 1.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446741216  247 NAESCIDCGKCAKNCPS------RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:pfam14697   4 DEDTCIGCGKCYIACPDtshqaiVGDGKRHHTVIEDECTGCNLCVSVCPV 53
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 251-290 2.06e-07

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 51.53  E-value: 2.06e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446741216 251 CIDCGKCAKNCPsripVDKLI----QVRTV---ECTGCMTCVESCPV 290
Cdd:COG2878  139 CIGCGDCIKACP----FDAIVgaakGMHTVdedKCTGCGLCVEACPV 181
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 249-290 2.33e-07

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 50.18  E-value: 2.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446741216  249 ESCIDCGKCAKNCPsripVDKLI----QVRTV---ECTGCMTCVESCPV 290
Cdd:TIGR01944 113 DNCIGCTKCIQACP----VDAIVgaakAMHTViadECTGCDLCVEPCPT 157
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
250-307 3.30e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 51.09  E-value: 3.30e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446741216 250 SCIDCGKCAKNCPSR--IPVDKLIQVRTVECTGCMTCVESCP--VASTLTFSLQKPAANKKA 307
Cdd:PRK07118 214 GCIGCGKCVKACPAGaiTMENNLAVIDQEKCTSCGKCVEKCPtkAIRILNKPPKVKEPKKAA 275
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 251-290 5.05e-07

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: 45.98  E-value: 5.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446741216  251 CIDCGKCAKNCPS-RIPVDKLIQVRTVE--------CTGCMTCVESCPV 290
Cdd:pfam12838   1 CIGCGACVAACPVgAITLDEVGEKKGTKtvvidperCVGCGACVAVCPT 49
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 221-296 8.12e-07

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: 48.45  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 221 AWCRYLCPYGAL----MGVVSllspfkirRNAESCIDCGKCAKNCPSRIP-VDKLIQVRTvECTGCMT---------CVE 286
Cdd:cd10562   76 AACVKVCPTGALykteNGAVV--------VDEDKCIGCGYCVAACPFDVPrYDETTNKIT-KCTLCFDriengmqpaCVK 146

                         90
                 ....*....|
gi 446741216 287 SCPvASTLTF 296
Cdd:cd10562  147 TCP-TGALTF 155
Fer4_9 pfam13187
4Fe-4S dicluster domain;
251-289 1.59e-06

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 44.47  E-value: 1.59e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446741216  251 CIDCGKCAKNCPSRIPVDKL------IQVRTVECTGCMTCVESCP 289
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDLvgqtirGDIAGLACIGCGACVDACP 46
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 247-291 1.94e-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: 46.62  E-value: 1.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446741216 247 NAESCIDCGKCAKNCPS---RIPVDKLIQVRTV----ECTGCMTCVESCPVA 291
Cdd:cd10549    4 DPEKCIGCGICVKACPTdaiELGPNGAIARGPEidedKCVFCGACVEVCPTG 55
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 251-290 3.94e-06

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 46.86  E-value: 3.94e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446741216 251 CIDCGKCAKNCPsripVDKLI----QVRTV---ECTGCMTCVESCPV 290
Cdd:PRK05113 116 CIGCTKCIQACP----VDAIVgatkAMHTVisdLCTGCDLCVAPCPT 158
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 247-313 4.56e-06

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 45.51  E-value: 4.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446741216 247 NAESCIDCGKCAKNCP-SRIPV--DKLIQVRTVECTGCMTCVESCPV--ASTLTFSLQKpaanKKAFALSGW 313
Cdd:PRK09625  57 NNEICINCFNCWVYCPdAAILSrdKKLKGVDYSHCKGCGVCVEVCPTnpKSLLMFEEQI----ENETALTQW 124
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 249-290 5.35e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.16  E-value: 5.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446741216 249 ESCIDCGKCAKNCPSR-IpvdKLIQVRTV---ECTGCMTCVESCPV 290
Cdd:NF038196 185 DKCIGCGICAKVCPVNnI---EMEDGKPVwghNCTHCLACIHRCPK 227
Fer4_5 pfam12801
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 200-247 8.52e-06

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: 432796 [Multi-domain]  Cd Length: 48  Bit Score: 42.55  E-value: 8.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446741216  200 MGTATLISVTVLLIASLFIRHAWCRYLCPYGALMGVVSLLSPFKIRRN 247
Cdd:pfam12801   1 LGPAGLILFLAVLVLTLLFGRVFCGWLCPFGALQELLAKLLRRKLGKP 48
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
218-290 1.19e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 46.94  E-value: 1.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446741216 218 IRHAWCRYLCPYGALMGVVsllspFKIRRNAESCIDCGKCAKNCP--SRIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG4624   65 CVAISCIQVRGIIIIDKRG-----PSIIRDKEKCKNCYPCVRACPvkAIKVDDGKAEIDEEKCISCGQCVAVCPF 134
PRK13795 PRK13795
hypothetical protein; Provisional
 244-291 1.30e-05

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 46.91  E-value: 1.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446741216 244 IRRNAEsCIDCGKCAKNCP----SRIPVDKLIQVRTVECTGCMTCVESCPVA 291
Cdd:PRK13795 577 LRRAAE-CVGCGVCVGACPtgaiRIEEGKRKISVDEEKCIHCGKCTEVCPVV 627
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 251-292 3.66e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 42.71  E-value: 3.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446741216 251 CIDCGKCAKNCP-SRIPVDK--LIQVRTVECTGCMTCVESCPVAS 292
Cdd:cd16372   49 CNQCGECIDVCPtGAITRDAngVVMINKKLCVGCLMCVGFCPEGA 93
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 220-296 6.07e-05

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: 42.77  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 220 HAWCRYLCPYGALM----GVVsllspfkiRRNAESCIDCGKCAKNCPSRIP-VDKLIQvRTVECTGCM---------TCV 285
Cdd:cd16366   75 DAGCLAACPTGAIIrtetGTV--------VVDPETCIGCGYCVNACPFDIPrFDEETG-RVAKCTLCYdrisnglqpACV 145

                         90
                 ....*....|.
gi 446741216 286 ESCPVAStLTF 296
Cdd:cd16366  146 KTCPTGA-LTF 155
PRK06991 PRK06991
electron transport complex subunit RsxB;
227-290 7.23e-05

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 44.01  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 227 CPYGALMGVVSLLS-------PFKIRRNAE-----------SCIDCGKCAKNCPsripVDKLI----QVRTV---ECTGC 281
Cdd:PRK06991  45 CPPGGAEGIARLAAllgkpviPLDPANGVErpravavideqLCIGCTLCMQACP----VDAIVgapkQMHTVladLCTGC 120


                 ....*....
gi 446741216 282 MTCVESCPV 290
Cdd:PRK06991 121 DLCVPPCPV 129
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 238-306 7.70e-05

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 44.71  E-value: 7.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 238 LLSPFKIRRNAESCIDCGKCAKNCPSRIPVD------------KLIQVRTVeCTGCMTCVESC----PVASTLTFSLQKP 301
Cdd:cd01916  354 LPTDEEFQELAAKCTDCGWCTRACPNSLRIKeameaakegdfsGLADLFDQ-CVGCGRCEQECpkeiPIINMIEKAARER 432


                 ....*
gi 446741216 302 AANKK 306
Cdd:cd01916  433 IKEEK 437
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 223-290 7.96e-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: 42.16  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 223 CRYLCPYGAL----MGVVsllspfkiRRNAESCIDCGKCAKNCPSRIP--------VDKliqvrtveCTGCM-------- 282
Cdd:cd16371   62 CVKVCPTGAItkreDGIV--------VVDQDKCIGCGYCVWACPYGAPqynpetgkMDK--------CDMCVdrldegek 125


                 ....*....
gi 446741216 283 -TCVESCPV 290
Cdd:cd16371  126 pACVAACPT 134
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 223-262 9.46e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.08  E-value: 9.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446741216 223 CRYLCPYGALMGVVSLLSPFKIrrNAESCIDCGKCAKNCP 262
Cdd:COG1146   16 CVEVCPVDVLELDEEGKKALVI--NPEECIGCGACELVCP 53
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 223-263 1.13e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.55  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446741216 223 CRYLCPYGALMGVVSLLSPFKirrnaesCIDCGKCAKNCPS 263
Cdd:cd16372   85 CVGFCPEGAMFKHEDYPEPFK-------CIACGICVKACPT 118
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 220-289 1.53e-04

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 42.24  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 220 HAWCRYLCPYGAL----MGVVSLlspfkirrNAESCIDCGKCAKNCPSRIP--------VDKliqvrtveCTGCMT---- 283
Cdd:COG0437   65 DPPCVKVCPTGATykreDGIVLV--------DYDKCIGCRYCVAACPYGAPrfnpetgvVEK--------CTFCADrlde 128

                         90
                 ....*....|.
gi 446741216 284 -----CVESCP 289
Cdd:COG0437  129 gllpaCVEACP 139
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 198-290 1.65e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 41.14  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 198 RHMGTATLISvTVLLIASLFI----RH---AWCRYLCPYGAlmgvvsllspfkIRRNA-------ESCIDCGKCAKNCPS 263
Cdd:cd16367   34 THDGHSRLDR-NGLRFGNLLVptacRHcvdPVCMIGCPTGA------------IHRDDggevvisDACCGCGNCASACPY 100

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446741216 264 RIpvdklIQ-VRTVECTGCMT-----CVESCPV 290
Cdd:cd16367  101 GA-----IQmVRAVKCDLCAGyagpaCVSACPT 128
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 251-289 1.71e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 41.02  E-value: 1.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446741216 251 CIDCGK--CAKNCPSR-IPVDKLIQVRTV---ECTGCMTCVESCP 289
Cdd:cd10550   49 CRQCEDapCVEACPVGaISRDEETGAVVVdedKCIGCGMCVEACP 93
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 251-289 1.88e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. 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: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 41.08  E-value: 1.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446741216 251 CIDCGKCAKNCPSRI--------PVdklIQVRTVECTGCMTCVESCP 289
Cdd:cd10564   15 CTRCGDCVEACPEGIivrgdggfPE---LDFSRGECTFCGACAEACP 58
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 245-309 2.12e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 43.20  E-value: 2.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 245 RRNAESCIDC--GKCAKNCPSR--IPVDKLIQVRTVECTGCMTCVESCPVAsTLTFSLQKPAANK-KAFA 309
Cdd:PRK12769  50 QRSAVTCHHCedAPCARSCPNGaiSHVDDSIQVNQQKCIGCKSCVVACPFG-TMQIVLTPVAAGKvKATA 118
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
229-290 2.42e-04

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.92  E-value: 2.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446741216 229 YGALMGVVSLLS-------PFKIRRNAESCIDCGKCAKNCPS---RIPVDKLIQVRTVECTGCMTCVESCPV 290
Cdd:COG1148  469 TAAAARAIQLLSkgelgvePSVAEVDPEKCTGCGRCVEVCPYgaiSIDEKGVAEVNPALCKGCGTCAAACPS 540
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
251-289 2.57e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 38.63  E-value: 2.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446741216  251 CIDCGKCAKNCP------------------------SRIPVDKLIQVRTVECTGCMTCVESCP 289
Cdd:pfam13484   1 CGSCGKCIDACPtgaivgpegvldarrcisyltiekKGLIPDELRCLLGNRCYGCDICQDVCP 63
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 251-290 3.17e-04

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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 38.45  E-value: 3.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446741216  251 CIDCGKCAKNCPS----------RIPVDKLIQVRTVE-----------CTGCMTCVESCPV 290
Cdd:pfam13183   2 CIRCGACLAACPVylvtggrfpgDPRGGAAALLGRLEaleglaeglwlCTLCGACTEVCPV 62
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 222-290 5.18e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 39.93  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 222 WCRYLCPYGAL-----------MGVVSLLSPFKIrrNAESCIDCGKCAKNCPSRipvDKLIQVRTVE---------CTGC 281
Cdd:cd16373   61 ACVEVCPTGALrpldleeqkvkMGVAVIDKDRCL--AWQGGTDCGVCVEACPTE---AIAIVLEDDVlrpvvdedkCVGC 135


                 ....*....
gi 446741216 282 MTCVESCPV 290
Cdd:cd16373  136 GLCEYVCPV 144
HdrC COG1150
Heterodisulfide reductase, subunit C [Energy production and conversion];
247-289 5.30e-04

Heterodisulfide reductase, subunit C [Energy production and conversion];


Pssm-ID: 440764 [Multi-domain]  Cd Length: 79  Bit Score: 38.34  E-value: 5.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 247 NAESCIDCGKCAKNCPS---------RIP-------VDKLIQVRTV-ECTGCMTCVESCP 289
Cdd:COG1150    1 NLKKCYQCGTCTASCPVaramdynprKIIrlaqlglKEEVLKSDSIwLCVSCYTCTERCP 60
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 223-263 5.34e-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: 38.17  E-value: 5.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446741216 223 CRYLCPYGALmgvvSLLSPFKIRRNAESCIDCGKCAKNCPS 263
Cdd:COG1149   19 CVEVCPEGAI----KLDDGGAPVVDPDLCTGCGACVGVCPT 55
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
251-290 6.19e-04

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 39.52  E-value: 6.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446741216 251 CIDCGKCAKNCPSRIPVDKLIQVRTV---ECTGCMTCVESCPV 290
Cdd:PRK08764  87 CIGCTKCIQACPVDAIVGGAKHMHTViapLCTGCELCVPACPV 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 223-289 6.36e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 39.24  E-value: 6.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446741216 223 CRYLCPYGALM----GVVSLlspfkirrNAESCIDCGKCAKNCPSRIPVDKLIQVRTVECTGCMTCVESCP 289
Cdd:cd16372   55 CIDVCPTGAITrdanGVVMI--------NKKLCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACGICVKACP 117
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 247-289 6.63e-04

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N 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. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme 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.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 40.45  E-value: 6.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446741216 247 NAESCIDCGKCAKNCPSRIP-VDKLIQvRTVECTGCMT---------CVESCP 289
Cdd:cd10558   99 QSDKCIGCGYCIKGCPFDIPrISKDDN-KMYKCTLCSDrvsvglepaCVKTCP 150
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 223-289 7.00e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 39.18  E-value: 7.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446741216 223 CRYLCPYGALM-----GVVSllspfkirrNAESCIDCGKCAKNCPSR-IPVDKLIQvRTVECTGCMTCVESCP 289
Cdd:cd16370   61 CAEACPTGALEprkggGVVL---------DKEKCIGCGNCVKACIVGaIFWDEETN-KPIICIHCGYCARYCP 123
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
 223-264 8.13e-04

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 40.78  E-value: 8.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446741216  223 CRYLCPYGALMGVVSLLSPFKIRRNAESCIDCGKCAKNCPSR 264
Cdd:TIGR02494  56 CVEVCPAGTARLSELADGRNRIIIRREKCTHCGKCTEACPSG 97
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 227-262 9.33e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 37.34  E-value: 9.33e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446741216 227 CPYGALmgvvsLLSPFKIRRNAESCIDCGKCAKNCP 262
Cdd:COG2221   27 CPTGAI-----SLDDGKLVIDEEKCIGCGACIRVCP 57
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
229-272 1.20e-03

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 40.57  E-value: 1.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446741216 229 YGALMGvvsllspfkiRRNAESCIDCGKCAKNCPSRIPVDKLIQ 272
Cdd:COG1453  321 YNALGP----------GAKASACIECGACEERCPQGLDIPELLK 354
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 218-266 1.25e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 40.51  E-value: 1.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446741216 218 IRHAWCRYLCPygalMGvvslLSPFKIRRNAES-------------CIDCGKCAKNCPSRIP 266
Cdd:COG4656  367 IRCGRCVDACP----MG----LLPQQLYWYARAgdfdkaeeynlmdCIECGCCSYVCPSKIP 420
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
250-289 1.39e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.92  E-value: 1.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446741216 250 SCIDCGKCAKNCP---SRIpVDKLIQVRTVECTGCMTCVESCP 289
Cdd:PRK07118 140 GCLGLGSCVAACPfdaIHI-ENGLPVVDEDKCTGCGACVKACP 181
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 243-292 1.52e-03

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 37.89  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446741216 243 KIRRNAESCIDCGKCAKNCPS----RIPVDKLIQVRTVECTGCMTCVESCPVAS 292
Cdd:PRK08348  36 KILYDVDKCVGCRMCVTVCPAgvfvYLPEIRKVALWTGRCVFCGQCVDVCPTGA 89
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 249-289 1.62e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 39.48  E-value: 1.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446741216 249 ESCIDCGKCAKNCPSR-IPVD--KLIQVRTVECTGCMTCVESCP 289
Cdd:PRK00783 169 EDCDECEKCVEACPRGvLELKegKLVVTDLLNCSLCKLCERACP 212
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 222-297 2.01e-03

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: 38.11  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 222 WCRYLCPYGALM-----GVVSLlspfkirrNAESCIDCGKCAKNCPSRIPVDKLIQVRTVECTGCM---------TCVES 287
Cdd:cd10553   65 WCVKACPTGAMQkrekdGIVYV--------DQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMdridqglkpACVTG 136

                         90
                 ....*....|
gi 446741216 288 CPvASTLTFS 297
Cdd:cd10553  137 CT-THALSFV 145
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
249-290 2.10e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 38.32  E-value: 2.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446741216 249 ESCIDCGKCAKNCPSRipvdkLIQVRTVE-----------------CTGCMTCVESCPV 290
Cdd:PRK05888  58 ERCIACKLCAAICPAD-----AITIEAAEredgrrrttrydinfgrCIFCGFCEEACPT 111
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
220-289 2.60e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.71  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 220 HAWCRYLCPYGALM---GVVSLlspfkirrNAESCIDCGKCAKNCPSRI--PVDKLIQVRTVECTGCMT------CVESC 288
Cdd:COG1142   57 DAPCAEVCPVGAITrddGAVVV--------DEEKCIGCGLCVLACPFGAitMVGEKSRAVAVKCDLCGGreggpaCVEAC 128


                 .
gi 446741216 289 P 289
Cdd:COG1142  129 P 129
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
247-301 3.25e-03

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 39.16  E-value: 3.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446741216 247 NAESCIDCGKC-------AKNCPSRIPV-DKLIQVRTVECTGCMTCVESCPVASTLTFSLQKP 301
Cdd:PRK08318 340 DQDKCIGCGRCyiacedtSHQAIEWDEDgTRTPEVIEEECVGCNLCAHVCPVEGCITMGEVKF 402
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 243-266 3.28e-03

4Fe-4S binding domain; This 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: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 34.51  E-value: 3.28e-03
                          10        20
                  ....*....|....*....|....
gi 446741216  243 KIRRNAESCIDCGKCAKNCPSRIP 266
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGAI 24
RNAP_D cd07030
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ...
 249-288 3.40e-03

D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.


Pssm-ID: 132908 [Multi-domain]  Cd Length: 259  Bit Score: 38.79  E-value: 3.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446741216 249 ESCIDCGKCAKNCPSRIPV---DKLIQVRTVECTGCMTCVESC 288
Cdd:cd07030  169 EDCDGCGKCVEECPRGVLEleeGKVVVEDLEDCSLCKLCERAC 211
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 248-290 4.83e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 38.14  E-value: 4.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446741216 248 AESCIDCGKCAKNC--------PSRIPVDKLIqvrtveCTGCMTCVESCPV 290
Cdd:cd03110   63 QEKCIRCGNCERVCkfgailefFQKLIVDESL------CEGCGACVIICPR 107
Fer4_9 pfam13187
4Fe-4S dicluster domain;
223-262 4.91e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.84  E-value: 4.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 446741216  223 CRYLCPYGAlMGVVSLLSPFKIRRNAESCIDCGKCAKNCP 262
Cdd:pfam13187   8 CVAACPAGA-IVPDLVGQTIRGDIAGLACIGCGACVDACP 46
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 251-289 5.95e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 36.08  E-value: 5.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 446741216  251 CIDCGKCAKNCPSRIPVDK-----LIQVRTVECTGCMTCVESCP 289
Cdd:TIGR00402  36 CTRCGECASACENNILQLGqqgqpTVEFDNAECDFCGKCAEACP 79
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
227-290 6.55e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 37.99  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446741216 227 CPYGAlMGVVSLLspfkIRRNAESCIDCGKCAKNCP----------SRIPV-----DKLIQVR---TVECTGCMTCVESC 288
Cdd:PRK07118 151 CPFDA-IHIENGL----PVVDEDKCTGCGACVKACPrnvielipksARVFVacnskDKGKAVKkvcEVGCIGCGKCVKAC 225


                 ..
gi 446741216 289 PV 290
Cdd:PRK07118 226 PA 227
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 248-290 6.67e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.32  E-value: 6.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446741216 248 AESCIDCGKC--AKNCPSRIPVDKLIQVRTVE--------CTGCMTCVESCPV 290
Cdd:PRK12771 503 AARCLSCGNCfeCDNCYGACPQDAIIKLGPGRryhfdydkCTGCHICADVCPC 555
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 227-265 6.75e-03

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: 34.42  E-value: 6.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446741216  227 CPYGALMGVVSLLSP--FKIRRNAESCIDCGKCAKNCPSRI 265
Cdd:pfam12838  11 CPVGAITLDEVGEKKgtKTVVIDPERCVGCGACVAVCPTGA 51
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 251-289 6.99e-03

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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 34.74  E-value: 6.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446741216  251 CIDCGKCAKNCPSRI----------------PVDKLIQVRTVE-CTGCMTCVESCP 289
Cdd:pfam13534   2 CIQCGCCVDECPRYLlngdepkklmraaylgDLEELQANKVANlCSECGLCEYACP 57
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 223-262 7.10e-03

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: 34.72  E-value: 7.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446741216 223 CRYLCPYGAL-MGVVSLLSPFKIrrNAESCIDCGKCAKNCP 262
Cdd:COG1143   10 CVRVCPVDAItIEDGEPGKVYVI--DPDKCIGCGLCVEVCP 48
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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