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Conserved domains on  [gi|384093350|gb|AFH64786|]
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effector protein [Paenibacillus mucilaginosus K02]

Protein Classification

lactate utilization protein B( domain architecture ID 11439020)

lactate utilization protein B (LutB) is an iron-sulfur cluster-binding protein involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source

Gene Ontology:  GO:0051539|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LutB COG1139
L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and ...
 11-466 0e+00

L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and conversion];


:

Pssm-ID: 440754 [Multi-domain]  Cd Length: 465  Bit Score: 760.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  11 KERAELALNDEFLRKAVKFTTERLRLGKKNASADHGNWDEWRERGRQIRLHTIAHLDYYLNLFADNARANGVHVHFADTG 90
Cdd:COG1139   10 KERAREALADEQLRKALDRATDTLRAKRAKAVAELPDWEALREAARAIKDHALANLDEYLEQFEANATANGGHVHWARDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  91 EEAVKIALQIAENKSAKSVVKSKSMVTEELHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLS 170
Cdd:COG1139   90 EEANRIVLDIAREKGAKKVVKSKSMVTEEIGLNEALEAAGIEVVETDLGEYIVQLAGEPPSHIVMPAIHKNREQIAELFH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 171 KEAG-ETLPPDTSILAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWT 249
Cdd:COG1139  170 EKLGtEPLTDDPEELTRAAREHLREKFLEADVGITGANFAVAETGTIVLVTNEGNARLCTTLPKVHIAVMGIEKLVPTLE 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 250 DLEVMATLLPRSATGQKLTVYMSGITGPRRSKDADGPEEMHIIIVDNGRSLQLGDPEFQELLNCIRCGACLNACPVYRHI 329
Cdd:COG1139  250 DLEVFLRLLPRSATGQRITTYTSLITGPRRPGEGDGPEEFHLVLLDNGRSAMLADPEFREALRCIRCGACLNVCPVYRRV 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 330 GGHAYGGTYSGPIGAVLTPALkKNVAEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAGHDNRMETIGMKGFA 409
Cdd:COG1139  330 GGHAYGSVYPGPIGAVLTPLL-HGLEKAADLPYASTLCGACTEVCPVKIPIPELLLELRERIVEEGLTPPAEKLAMKAWA 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384093350 410 ALAGDSLRMKTALKLGKLGQKLVARDGGIRIKIGPLKGWNTYRVTPTLPKQSFREQW 466
Cdd:COG1139  409 WVMSNPKLYRLALRLARRALKLLPRGGGIRRLPGPLGGWTKGRDLPAPAKESFRDWW 465
 
Name Accession Description Interval E-value
LutB COG1139
L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and ...
 11-466 0e+00

L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and conversion];


Pssm-ID: 440754 [Multi-domain]  Cd Length: 465  Bit Score: 760.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  11 KERAELALNDEFLRKAVKFTTERLRLGKKNASADHGNWDEWRERGRQIRLHTIAHLDYYLNLFADNARANGVHVHFADTG 90
Cdd:COG1139   10 KERAREALADEQLRKALDRATDTLRAKRAKAVAELPDWEALREAARAIKDHALANLDEYLEQFEANATANGGHVHWARDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  91 EEAVKIALQIAENKSAKSVVKSKSMVTEELHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLS 170
Cdd:COG1139   90 EEANRIVLDIAREKGAKKVVKSKSMVTEEIGLNEALEAAGIEVVETDLGEYIVQLAGEPPSHIVMPAIHKNREQIAELFH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 171 KEAG-ETLPPDTSILAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWT 249
Cdd:COG1139  170 EKLGtEPLTDDPEELTRAAREHLREKFLEADVGITGANFAVAETGTIVLVTNEGNARLCTTLPKVHIAVMGIEKLVPTLE 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 250 DLEVMATLLPRSATGQKLTVYMSGITGPRRSKDADGPEEMHIIIVDNGRSLQLGDPEFQELLNCIRCGACLNACPVYRHI 329
Cdd:COG1139  250 DLEVFLRLLPRSATGQRITTYTSLITGPRRPGEGDGPEEFHLVLLDNGRSAMLADPEFREALRCIRCGACLNVCPVYRRV 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 330 GGHAYGGTYSGPIGAVLTPALkKNVAEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAGHDNRMETIGMKGFA 409
Cdd:COG1139  330 GGHAYGSVYPGPIGAVLTPLL-HGLEKAADLPYASTLCGACTEVCPVKIPIPELLLELRERIVEEGLTPPAEKLAMKAWA 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384093350 410 ALAGDSLRMKTALKLGKLGQKLVARDGGIRIKIGPLKGWNTYRVTPTLPKQSFREQW 466
Cdd:COG1139  409 WVMSNPKLYRLALRLARRALKLLPRGGGIRRLPGPLGGWTKGRDLPAPAKESFRDWW 465
TIGR00273 TIGR00273
iron-sulfur cluster-binding protein; Members of this family have a perfect 4Fe-4S binding ...
 18-455 0e+00

iron-sulfur cluster-binding protein; Members of this family have a perfect 4Fe-4S binding motif C-x(2)-C-x(2)-C-x(3)-CP followed by either a perfect or imperfect (the first Cys replaced by Ser) second copy. Members probably bind two 4fe-4S iron-sulfur clusters. [Energy metabolism, Electron transport]


Pssm-ID: 129374 [Multi-domain]  Cd Length: 432  Bit Score: 531.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   18 LNDEFLRKAVKFTTERLRLGKKNASADHGNWDEWRERGRQIRLHTIAHLDYYLNLFADNARANGVHVHFADTGEEAVKIA 97
Cdd:TIGR00273   1 IKDGILREALRNAQERLRANRKLLVEELGYWEEWRELVKEIKLKVLENLDFYLDQLKENVTQRGGHVYYAKTAEEARKII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   98 LQIAENKSAKSVVKSKSMVTEELHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLSKEAGETL 177
Cdd:TIGR00273  81 GKVAQEKNGKKVVKSKSMVSEEIGLNEVLEKIGIEVWETDLGELILQLDGDPPSHIVVPALHKNRQQIGEILKERLGYEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  178 PPDTSILAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWTDLEVMATL 257
Cdd:TIGR00273 161 EESPEVLAREARKFMREKFLSADIGISGCNFAIAETGSIFLVENEGNGRLSTTLPKTHIAVMGIEKIVPTFDDELVLKSM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  258 LPRSATGQKLTVYMSGITGPRRSKDADGPEEMHIIIVDNGRSLQLGDpEFQELLNCIRCGACLNACPVYRHIGGHAYGGT 337
Cdd:TIGR00273 241 LARSAVGTRLTAYINVLTGPRQEGDVDGPEEFHLILLDNGRSNILAT-EFREVLACIRCGACQNECPVYRHIGGHWYGSI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  338 YSGPIGAVLTPALkKNVAEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAGHDNRMETIGMKGFAALAGDSLR 417
Cdd:TIGR00273 320 YPGPIGAVWSPLL-GGYTDYKHLPYLSSLCGACREVCPVKIPLPELIREHRSDKVEKGRHSGMEKLAMKMFAKMASDGAL 398

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 384093350  418 MKTALKLGklgqKLVARDGGIRIKIGPLKGWNTYRVTP 455
Cdd:TIGR00273 399 WKFGLKMA----QFFSPLGKLLAPIGPVKEWASVRDLP 432
LUD_dom pfam02589
LUD domain; This entry represents a domain found in lactate utilization proteins B (LutB) and ...
 70-294 2.22e-57

LUD domain; This entry represents a domain found in lactate utilization proteins B (LutB) and C (LutC), as well as several uncharacterized proteins. LutB and LutC are encoded by th conserved LutABC operon in bacteria. They are involved in lactate utilization and is implicated in the oxidative conversion of L-lactate into pyruvate


Pssm-ID: 426855  Cd Length: 188  Bit Score: 188.59  E-value: 2.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   70 LNLFADNARANGVHVHFADTGEEAVKIALQIAENKsaksvvksksmvteelhlnhaleGIGVEAVETDLGEYIIqlaget 149
Cdd:pfam02589   1 LEEFKENLEANGAEVYYAKTAEEALEYILELIKEG-----------------------GVVSEGGSTDLGELGL------ 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  150 pshiiIPAIHKNRHQIAELLSKEagetlppdtsiLAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVS 229
Cdd:pfam02589  52 -----APALHSGRYEVLDLFEEK-----------LTAEAREELREKALTADVGITGANFAIAETGTLVLVDGEGNRRLLS 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384093350  230 TVPKTQITLMGMERIIPSWTDLEVMATLLPRSATGQKLTVYMSGITGPRRSKDAD--------GPEEMHIIIV 294
Cdd:pfam02589 116 FLPKVHIAVVGINKIVPDLEDAVKRLRLAPRNATRQKLTPYITFISGPSRTADIElvlvvgvhGPGELHVILV 188
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 297-383 1.97e-04

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: 43.94  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 297 GRSLQLGDPEFQELLN-CIRCGACLNACPvyrhigghayggtYSGPIGAVLTPALKKNVAEWDDIANASSLCGACYEACP 375
Cdd:cd01916  350 GEKKLPTDEEFQELAAkCTDCGWCTRACP-------------NSLRIKEAMEAAKEGDFSGLADLFDQCVGCGRCEQECP 416


                 ....*...
gi 384093350 376 VKIPLHDM 383
Cdd:cd01916  417 KEIPIINM 424
 
Name Accession Description Interval E-value
LutB COG1139
L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and ...
 11-466 0e+00

L-lactate utilization protein LutB, contains a ferredoxin-type domain [Energy production and conversion];


Pssm-ID: 440754 [Multi-domain]  Cd Length: 465  Bit Score: 760.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  11 KERAELALNDEFLRKAVKFTTERLRLGKKNASADHGNWDEWRERGRQIRLHTIAHLDYYLNLFADNARANGVHVHFADTG 90
Cdd:COG1139   10 KERAREALADEQLRKALDRATDTLRAKRAKAVAELPDWEALREAARAIKDHALANLDEYLEQFEANATANGGHVHWARDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  91 EEAVKIALQIAENKSAKSVVKSKSMVTEELHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLS 170
Cdd:COG1139   90 EEANRIVLDIAREKGAKKVVKSKSMVTEEIGLNEALEAAGIEVVETDLGEYIVQLAGEPPSHIVMPAIHKNREQIAELFH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 171 KEAG-ETLPPDTSILAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWT 249
Cdd:COG1139  170 EKLGtEPLTDDPEELTRAAREHLREKFLEADVGITGANFAVAETGTIVLVTNEGNARLCTTLPKVHIAVMGIEKLVPTLE 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 250 DLEVMATLLPRSATGQKLTVYMSGITGPRRSKDADGPEEMHIIIVDNGRSLQLGDPEFQELLNCIRCGACLNACPVYRHI 329
Cdd:COG1139  250 DLEVFLRLLPRSATGQRITTYTSLITGPRRPGEGDGPEEFHLVLLDNGRSAMLADPEFREALRCIRCGACLNVCPVYRRV 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 330 GGHAYGGTYSGPIGAVLTPALkKNVAEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAGHDNRMETIGMKGFA 409
Cdd:COG1139  330 GGHAYGSVYPGPIGAVLTPLL-HGLEKAADLPYASTLCGACTEVCPVKIPIPELLLELRERIVEEGLTPPAEKLAMKAWA 408

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384093350 410 ALAGDSLRMKTALKLGKLGQKLVARDGGIRIKIGPLKGWNTYRVTPTLPKQSFREQW 466
Cdd:COG1139  409 WVMSNPKLYRLALRLARRALKLLPRGGGIRRLPGPLGGWTKGRDLPAPAKESFRDWW 465
TIGR00273 TIGR00273
iron-sulfur cluster-binding protein; Members of this family have a perfect 4Fe-4S binding ...
 18-455 0e+00

iron-sulfur cluster-binding protein; Members of this family have a perfect 4Fe-4S binding motif C-x(2)-C-x(2)-C-x(3)-CP followed by either a perfect or imperfect (the first Cys replaced by Ser) second copy. Members probably bind two 4fe-4S iron-sulfur clusters. [Energy metabolism, Electron transport]


Pssm-ID: 129374 [Multi-domain]  Cd Length: 432  Bit Score: 531.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   18 LNDEFLRKAVKFTTERLRLGKKNASADHGNWDEWRERGRQIRLHTIAHLDYYLNLFADNARANGVHVHFADTGEEAVKIA 97
Cdd:TIGR00273   1 IKDGILREALRNAQERLRANRKLLVEELGYWEEWRELVKEIKLKVLENLDFYLDQLKENVTQRGGHVYYAKTAEEARKII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   98 LQIAENKSAKSVVKSKSMVTEELHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLSKEAGETL 177
Cdd:TIGR00273  81 GKVAQEKNGKKVVKSKSMVSEEIGLNEVLEKIGIEVWETDLGELILQLDGDPPSHIVVPALHKNRQQIGEILKERLGYEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  178 PPDTSILAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWTDLEVMATL 257
Cdd:TIGR00273 161 EESPEVLAREARKFMREKFLSADIGISGCNFAIAETGSIFLVENEGNGRLSTTLPKTHIAVMGIEKIVPTFDDELVLKSM 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  258 LPRSATGQKLTVYMSGITGPRRSKDADGPEEMHIIIVDNGRSLQLGDpEFQELLNCIRCGACLNACPVYRHIGGHAYGGT 337
Cdd:TIGR00273 241 LARSAVGTRLTAYINVLTGPRQEGDVDGPEEFHLILLDNGRSNILAT-EFREVLACIRCGACQNECPVYRHIGGHWYGSI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  338 YSGPIGAVLTPALkKNVAEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAGHDNRMETIGMKGFAALAGDSLR 417
Cdd:TIGR00273 320 YPGPIGAVWSPLL-GGYTDYKHLPYLSSLCGACREVCPVKIPLPELIREHRSDKVEKGRHSGMEKLAMKMFAKMASDGAL 398

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 384093350  418 MKTALKLGklgqKLVARDGGIRIKIGPLKGWNTYRVTP 455
Cdd:TIGR00273 399 WKFGLKMA----QFFSPLGKLLAPIGPVKEWASVRDLP 432
LUD_dom pfam02589
LUD domain; This entry represents a domain found in lactate utilization proteins B (LutB) and ...
 70-294 2.22e-57

LUD domain; This entry represents a domain found in lactate utilization proteins B (LutB) and C (LutC), as well as several uncharacterized proteins. LutB and LutC are encoded by th conserved LutABC operon in bacteria. They are involved in lactate utilization and is implicated in the oxidative conversion of L-lactate into pyruvate


Pssm-ID: 426855  Cd Length: 188  Bit Score: 188.59  E-value: 2.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350   70 LNLFADNARANGVHVHFADTGEEAVKIALQIAENKsaksvvksksmvteelhlnhaleGIGVEAVETDLGEYIIqlaget 149
Cdd:pfam02589   1 LEEFKENLEANGAEVYYAKTAEEALEYILELIKEG-----------------------GVVSEGGSTDLGELGL------ 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  150 pshiiIPAIHKNRHQIAELLSKEagetlppdtsiLAGFVRKKLREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVS 229
Cdd:pfam02589  52 -----APALHSGRYEVLDLFEEK-----------LTAEAREELREKALTADVGITGANFAIAETGTLVLVDGEGNRRLLS 115

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384093350  230 TVPKTQITLMGMERIIPSWTDLEVMATLLPRSATGQKLTVYMSGITGPRRSKDAD--------GPEEMHIIIV 294
Cdd:pfam02589 116 FLPKVHIAVVGINKIVPDLEDAVKRLRLAPRNATRQKLTPYITFISGPSRTADIElvlvvgvhGPGELHVILV 188
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 312-378 8.48e-17

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: 74.65  E-value: 8.48e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384093350  312 NCIRCGACLNACPVYRHIGGHAYGGTYSGPIGAVLtpaLKKNVAEWDDIANASSLCGACYEACPVKI 378
Cdd:pfam13183   1 RCIRCGACLAACPVYLVTGGRFPGDPRGGAAALLG---RLEALEGLAEGLWLCTLCGACTEVCPVGI 64
LutC COG1556
L-lactate utilization protein LutC, contains LUD domain [Energy production and conversion];
72-295 2.92e-14

L-lactate utilization protein LutC, contains LUD domain [Energy production and conversion];


Pssm-ID: 441165  Cd Length: 206  Bit Score: 71.43  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  72 LFADNARANGVHVHFADTGEEAVKIALQIAENKSAKSVVksksMVTEELHLNHALEGIGVEAVETdlgeyiiqlagetps 151
Cdd:COG1556   41 LFVERLEAVGGEVVRVTTEAELPAALAELLAEAGLKRIV----VPEPGLPAALQLAWDPLEELED--------------- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 152 hiiipaihknrhqiaellskeagetlppdtsilagfvrkklREKFLEADIGMTGCNFAIAETGSMVLFENEGNARMVSTV 231
Cdd:COG1556  102 -----------------------------------------PAALEDADVGITGAEFGIAETGTIVLDSGPDQGRALSLL 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384093350 232 PKTQITLMGMERIIPSwtdlevMATLLPRSATGQKLTVYMSGITGPrrSKDAD----------GPEEMHIIIVD 295
Cdd:COG1556  141 PEHHIVVVPASQIVPT------MHEAYARLREKAGLPRNITFISGP--SKTADieqtlvlgahGPRRLHVILVE 206
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 281-395 1.49e-11

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 66.25  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 281 KDADGPEEMHIIIVDNGRSLQLGDPEFQELL----NCIRCGACLNACPVYRHIG-------GHAYGgtysgpIGAVLTPA 349
Cdd:COG0247   44 KIGLLNPGVELLGDGDLHDKNLKTLPWKELLdaldACVGCGFCRAMCPSYKATGdekdsprGRINL------LREVLEGE 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 384093350 350 LKKNV-AEWDDIANASSLCGACYEACPVKIPLHDMLVSLRRRKVEAG 395
Cdd:COG0247  118 LPLDLsEEVYEVLDLCLTCKACETACPSGVDIADLIAEARAQLVERG 164
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 312-379 9.96e-08

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: 48.61  E-value: 9.96e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384093350  312 NCIRCGACLNACPVYRHIGGHAYGGTYSgpigavLTPALKKNVaEWDDIANASSLCGACYEACPVKIP 379
Cdd:pfam13534   1 RCIQCGCCVDECPRYLLNGDEPKKLMRA------AYLGDLEEL-QANKVANLCSECGLCEYACPMGLD 61
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 313-375 1.35e-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: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 48.40  E-value: 1.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384093350  313 CIRCGACLNACPVYRHIGGHAYGGTYSGPIgavltpalkkNVAEWDDIAnasslCGACYEACP 375
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRVGAIVERLEGEAV----------RIGVWKCIG-----CGACVEACP 56
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 313-378 1.18e-06

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: 45.60  E-value: 1.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384093350  313 CIRCGACLNACPVYrhigghayggtysgpigaVLTPALKKNVAEWDDIANASS---LCGACYEACPVKI 378
Cdd:pfam12838   1 CIGCGACVAACPVG------------------AITLDEVGEKKGTKTVVIDPErcvGCGACVAVCPTGA 51
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 306-394 1.92e-06

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 48.97  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 306 EFQELLNCIRCGACLNACPVYrhigghAYGGTYSGPigAVLTPALK-------KNVAE-WDDIANASSL-----CGACYE 372
Cdd:COG0479  137 KADDLAECILCGACVAACPNV------WANPDFLGP--AALAQAYRfaldprdEETEErLEALEDEEGVwrcttCGNCTE 208

                         90       100
                 ....*....|....*....|..
gi 384093350 373 ACPVKIPLHDMLVSLRRRKVEA 394
Cdd:COG0479  209 VCPKGIPPTKAIAKLKREALKR 230
LutB_C pfam11870
Lactate utilization protein B, C-terminal; This domain is functionally uncharacterized. This ...
 387-466 9.44e-06

Lactate utilization protein B, C-terminal; This domain is functionally uncharacterized. This domain is found at the C-terminal of a family of 4Fe-4S, iron-sulphur cluster binding proteins, including Lactate utilization protein B (LutB). These proteins have a perfect 4Fe-4S binding motif C-x(2)-C-x(2)-C-x(3)-CP followed by either a perfect or imperfect (the first Cys replaced by Ser) second copy. Members probably bind two 4Fe-4S iron-sulphur clusters. This domain is found in LutB proteins in association with the LUD domain (pfam02589) and usually Fer4_8 (pfam13183). The LutABC operon is involved in lactate-utilization and is essential.


Pssm-ID: 432147 [Multi-domain]  Cd Length: 86  Bit Score: 43.81  E-value: 9.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  387 LRRRKVEAGHD---------NRMETIGMKGFAALAgdslrmkTALKLGKLGQKLVARDGGIrikiGP--LKGWNTYRVTP 455
Cdd:pfam11870   2 LRHEPVGQGPGvikgqgakrSAAERLAWKGFALAA-------SSPGLYRLGTWLATRFRGL----LPskLKAWTRVRTFP 70

                          90
                  ....*....|.
gi 384093350  456 TLPKQSFREQW 466
Cdd:pfam11870  71 KPAARSLHDLA 81
Fer4_9 pfam13187
4Fe-4S dicluster domain;
312-378 3.13e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.39  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384093350  312 NCIRCGACLNACPVYRHIGghayggtYSGPIGAVLtpalkknvaewdDIANAS-SLCGACYEACPVKI 378
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVP-------DLVGQTIRG------------DIAGLAcIGCGACVDACPRGA 49
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 312-380 8.46e-05

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: 45.13  E-value: 8.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384093350 312 NCIRCGACLNACPV-------YRHIGGHAYGGtysgpigavltpALKKNVAewDDIAnasslCGACYEACPVKIPL 380
Cdd:COG4656  365 PCIRCGRCVDACPMgllpqqlYWYARAGDFDK------------AEEYNLM--DCIE-----CGCCSYVCPSKIPL 421
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 312-376 1.18e-04

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.08  E-value: 1.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384093350 312 NCIRCGACLNACPVyrhigghayggtysgpigAVLTPALKKNVAEWDDiANASSLCGACYEACPV 376
Cdd:COG1146    9 KCIGCGACVEVCPV------------------DVLELDEEGKKALVIN-PEECIGCGACELVCPV 54
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
313-375 1.80e-04

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 39.78  E-value: 1.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384093350  313 CIRCGACLNACPVYrHIggHAYGGTY-SGPIGAVLTPALKK--NVAEWDDIANASSLCGACYEACP 375
Cdd:pfam13484   1 CGSCGKCIDACPTG-AI--VGPEGVLdARRCISYLTIEKKGliPDELRCLLGNRCYGCDICQDVCP 63
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 297-383 1.97e-04

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: 43.94  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 297 GRSLQLGDPEFQELLN-CIRCGACLNACPvyrhigghayggtYSGPIGAVLTPALKKNVAEWDDIANASSLCGACYEACP 375
Cdd:cd01916  350 GEKKLPTDEEFQELAAkCTDCGWCTRACP-------------NSLRIKEAMEAAKEGDFSGLADLFDQCVGCGRCEQECP 416


                 ....*...
gi 384093350 376 VKIPLHDM 383
Cdd:cd01916  417 KEIPIINM 424
rnfC TIGR01945
electron transport complex, RnfABCDGE type, C subunit; The six subunit complex RnfABCDGE in ...
 313-380 2.25e-04

electron transport complex, RnfABCDGE type, C 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 C subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273888 [Multi-domain]  Cd Length: 435  Bit Score: 43.49  E-value: 2.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384093350  313 CIRCGACLNACPVyrhigghayggtysgpigaVLTPALKKNVAEWDDIANASSL-------CGACYEACPVKIPL 380
Cdd:TIGR01945 365 CIRCGKCVQVCPM-------------------NLLPQQLNWLALADEFDEAEEHnlmdcieCGCCSYVCPSNIPL 420
NapF COG1145
Ferredoxin [Energy production and conversion];
120-377 2.38e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 42.79  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 120 LHLNHALEGIGVEAVETDLGEYIIQLAGETPSHIIIPAIHKNRHQIAELLSKEAGETLPPDTSILAGFVRKKLREKFLEA 199
Cdd:COG1145    5 LDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 200 DIGMTGCNFAIAETGSMVLFENEGNARMVSTVPKTQITLMGMERIIPSWTDLEVMATLLPRSATGQKLTVYMSGITGPRR 279
Cdd:COG1145   85 GIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 280 SKDADGPEEMHIIIVDNGRslqlgdpefqellnCIRCGACLNACPVyrhigghayggtysgpigAVLTPALKKNVAEWDD 359
Cdd:COG1145  165 EEELKIAIKKAKAVIDAEK--------------CIGCGLCVKVCPT------------------GAIRLKDGKPQIVVDP 212

                        250
                 ....*....|....*...
gi 384093350 360 iaNASSLCGACYEACPVK 377
Cdd:COG1145  213 --DKCIGCGACVKVCPVG 228
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 302-377 3.04e-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: 41.09  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 302 LGDPEFqeLLNCIRCGACLNACPvYR--HIGGHAYGgtysgpIGAVLTP-----------------------ALKKNVAE 356
Cdd:cd16373    7 LDEEEF--LALCIRCGLCVEACP-TGviQPAGLEDG------LEGGRTPyldpregpcdlccdacvevcptgALRPLDLE 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 384093350 357 WDD-------------IANASSL-CGACYEACPVK 377
Cdd:cd16373   78 EQKvkmgvavidkdrcLAWQGGTdCGVCVEACPTE 112
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 312-377 4.59e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.49  E-value: 4.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384093350 312 NCIRCGACLNACPVyrhigghayggtysgpiGAVltpALKKNVAEWDDiaNASSLCGACYEACPVK 377
Cdd:COG2221   16 KCIGCGLCVAVCPT-----------------GAI---SLDDGKLVIDE--EKCIGCGACIRVCPTG 59
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 312-377 9.30e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.10  E-value: 9.30e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384093350 312 NCIRCGACLNACPvyrhigghayggtysgpigaVLTPALKKNVAEWDDianasSLC---GACYEACPVK 377
Cdd:COG4231   23 KCTGCGACVKVCP--------------------ADAIEEGDGKAVIDP-----DLCigcGSCVQVCPVD 66
Fer4_2 pfam12797
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 309-325 2.72e-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: 463711 [Multi-domain]  Cd Length: 22  Bit Score: 35.07  E-value: 2.72e-03
                          10
                  ....*....|....*..
gi 384093350  309 ELLNCIRCGACLNACPV 325
Cdd:pfam12797   6 DADKCIGCGACVSACPA 22
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 306-388 3.41e-03

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 38.95  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350  306 EFQELLNCIRCGACLNACPVYrhigghAYGGTYSGPigAVLTPALKKNVAEWD-------DIANAS------SLCGACYE 372
Cdd:TIGR00384 133 KLDQLSGCILCGCCYSSCPAF------WWNPEFLGP--AALTAAYRFLIDSRDhatkdrlEGLNDKngvwrcTTCMNCSE 204

                          90
                  ....*....|....*.
gi 384093350  373 ACPVKIPLHDMLVSLR 388
Cdd:TIGR00384 205 VCPKGVNPARAIEKLK 220
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 313-325 7.31e-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: 34.15  E-value: 7.31e-03
                          10
                  ....*....|...
gi 384093350  313 CIRCGACLNACPV 325
Cdd:pfam00037   8 CIGCGACVEVCPV 20
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 281-377 9.30e-03

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: 37.51  E-value: 9.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384093350 281 KDADGpeemhIIIVDNGRslqlgdpefqellnCIRCGACLNACPvY--RHIgghayggTYSGPIGAVLTPALKKNVAE-- 356
Cdd:cd10551   72 KREDG-----IVLVDYDK--------------CIGCRYCMAACP-YgaRYF-------NPEEPHEFGEVPVRPKGVVEkc 124

                         90       100
                 ....*....|....*....|....*..
gi 384093350 357 ---WDDIANasslcG---ACYEACPVK 377
Cdd:cd10551  125 tfcYHRLDE-----GllpACVEACPTG 146
Fer4_4 pfam12800
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 312-326 9.65e-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: 463714  Cd Length: 17  Bit Score: 33.48  E-value: 9.65e-03
                          10
                  ....*....|....*
gi 384093350  312 NCIRCGACLNACPVY 326
Cdd:pfam12800   3 KCIGCGACVDACPYG 17
 
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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