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Conserved domains on  [gi|681105299|emb|CDZ75558|]
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Activator of (R)-2-hydroxyglutaryl-CoA dehydratase [Peptoniphilus sp. ING2-D1G]

Protein Classification

YjiL family protein( domain architecture ID 10004942)

YjiL family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 7-261 2.73e-157

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24103:

Pssm-ID: 483947  Cd Length: 255  Bit Score: 437.61  E-value: 2.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELSC 86
Cdd:cd24103    1 TMGIDIGSTASKCVILKDGKEIVAQSVISVGTGTSGPARALEEVLEKAGLAKEDIAYTVATGYGRNSFEGADKQISELSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  87 HAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTISS 166
Cdd:cd24103   81 HARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQSTNPVSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 167 TCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQL 246
Cdd:cd24103  161 TCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNPQL 240

                        250
                 ....*....|....*
gi 681105299 247 NGALGAAIFAHQKIM 261
Cdd:cd24103  241 TGALGAALYAYEKAK 255
 
Name Accession Description Interval E-value
ASKHA_NBD_HgdC_HadI-like cd24103
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
 7-261 2.73e-157

nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.


Pssm-ID: 466953  Cd Length: 255  Bit Score: 437.61  E-value: 2.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELSC 86
Cdd:cd24103    1 TMGIDIGSTASKCVILKDGKEIVAQSVISVGTGTSGPARALEEVLEKAGLAKEDIAYTVATGYGRNSFEGADKQISELSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  87 HAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTISS 166
Cdd:cd24103   81 HARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQSTNPVSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 167 TCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQL 246
Cdd:cd24103  161 TCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNPQL 240

                        250
                 ....*....|....*
gi 681105299 247 NGALGAAIFAHQKIM 261
Cdd:cd24103  241 TGALGAALYAYEKAK 255
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 6-264 1.17e-123

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 352.87  E-value: 1.17e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   6 YTMGVDVGSTASKGLILKNGKEIMASSVIDVGAGT-SGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEE--ADFQMS 82
Cdd:COG1924    4 IYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPlEAAKEALKELLEEAGLKREDIAGVVATGYGRVLIGAafADKVVT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  83 ELSCHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVlENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDV 162
Cdd:COG1924   84 EITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVV-VDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAKNPV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 163 TISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSE 242
Cdd:COG1924  163 DISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIVPP 242

                        250       260
                 ....*....|....*....|..
gi 681105299 243 YCQLNGALGAAIFAHQKIMQNK 264
Cdd:COG1924  243 IPQLMGALGAALLAREKVKKGK 264
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 6-254 4.30e-84

CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.


Pssm-ID: 129344  Cd Length: 248  Bit Score: 252.02  E-value: 4.30e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299    6 YTMGVDVGSTASKGLILKNGKeIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGK-VIGYKWLDTTPVIEETARAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   86 CHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGgVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTIS 165
Cdd:TIGR00241  80 CHGKGANYLAPEARGVIDIGGQDSKVIKIDDG-KVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAKIS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  166 STCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQ 245
Cdd:TIGR00241 159 SMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQ 238


                  ....*....
gi 681105299  246 LNGALGAAI 254
Cdd:TIGR00241 239 IVGAVGAAL 247
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 9-256 1.40e-65

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 205.67  E-value: 1.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299    9 GVDVGSTASKGLILKNGKEIMAS--------SVIDVGAGTSGPSRAINAVLEKANLTLDDIDFI--TATGYGRNSLE--- 75
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRaiagsanfESVGVEAAERNLKDAITEALEEAGLKLDDIEYMflGLTGYGRAGVDghf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   76 EADFQMSELSCHAKGAYFLFPRV---HTIIDIGGQDAKALKIgDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELD 152
Cdd:pfam01869  82 GKDIVREEITVHADGAVALAPGTrgeDGVIDIGGTGSKVIGL-DGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  153 DLDKKSTL-DVTISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGI-KDDVVMTGGVALNKGMVRAL 230
Cdd:pfam01869 161 GLAPKTTLnKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFvPDEVVLTGGVAKNAGLVKAL 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 681105299  231 -----EENVGHKIYTSEYCQLNGALGAAIFA 256
Cdd:pfam01869 241 rdylkENILGVKVNVHPDPQYAGAIGAALLA 271
PRK05790 PRK05790
putative acyltransferase; Provisional
 41-64 1.59e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 39.37  E-value: 1.59e-03
                         10        20
                 ....*....|....*....|....
gi 681105299  41 SGPSRAINAVLEKANLTLDDIDFI 64
Cdd:PRK05790 291 IGPVPAIRKALEKAGWSLADLDLI 314
 
Name Accession Description Interval E-value
ASKHA_NBD_HgdC_HadI-like cd24103
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
 7-261 2.73e-157

nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.


Pssm-ID: 466953  Cd Length: 255  Bit Score: 437.61  E-value: 2.73e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELSC 86
Cdd:cd24103    1 TMGIDIGSTASKCVILKDGKEIVAQSVISVGTGTSGPARALEEVLEKAGLAKEDIAYTVATGYGRNSFEGADKQISELSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  87 HAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTISS 166
Cdd:cd24103   81 HARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQSTNPVSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 167 TCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQL 246
Cdd:cd24103  161 TCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNPQL 240

                        250
                 ....*....|....*
gi 681105299 247 NGALGAAIFAHQKIM 261
Cdd:cd24103  241 TGALGAALYAYEKAK 255
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
 7-255 3.61e-127

nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.


Pssm-ID: 466886 [Multi-domain]  Cd Length: 250  Bit Score: 361.09  E-value: 3.61e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGA-GTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:cd24036    1 FAGIDVGSTTTKAVILDDKGKILGKAVIRTGTdPEKTAERALEEALEEAGLSREDIEYIVATGYGRNSVPFADKTITEIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  86 CHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTIS 165
Cdd:cd24036   81 CHARGAHFLFPEARTVIDIGGQDSKVIRLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELALKSTNPVEIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 166 STCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQ 245
Cdd:cd24036  161 STCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKRVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQ 240

                        250
                 ....*....|
gi 681105299 246 LNGALGAAIF 255
Cdd:cd24036  241 LVGALGAALL 250
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 6-264 1.17e-123

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 352.87  E-value: 1.17e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   6 YTMGVDVGSTASKGLILKNGKEIMASSVIDVGAGT-SGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEE--ADFQMS 82
Cdd:COG1924    4 IYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPlEAAKEALKELLEEAGLKREDIAGVVATGYGRVLIGAafADKVVT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  83 ELSCHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVlENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDV 162
Cdd:COG1924   84 EITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVV-VDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAKNPV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 163 TISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSE 242
Cdd:COG1924  163 DISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIVPP 242

                        250       260
                 ....*....|....*....|..
gi 681105299 243 YCQLNGALGAAIFAHQKIMQNK 264
Cdd:COG1924  243 IPQLMGALGAALLAREKVKKGK 264
ASKHA_NBD_benz_CoA_BcrA_BadF cd24104
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
 8-256 4.47e-98

nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.


Pssm-ID: 466954  Cd Length: 253  Bit Score: 287.65  E-value: 4.47e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   8 MGVDVGSTASKGLILKNGKEIMASSVIDVGAGTS-GPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELSC 86
Cdd:cd24104    2 AGVDVGSTQTKAVIIDEDGEIVGRGLTNTGANVVvAAERAFREAIEEAGIKEEEVEYVVGTGYGRYKVTFGNAQRTEISC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  87 HAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTISS 166
Cdd:cd24104   82 HARGAHHMFPNTRTVLDIGGQDTKAIRVDETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLALKSTKPVRISS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 167 TCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQL 246
Cdd:cd24104  162 TCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIRRVGIEPEFTFTGGVARNEAMVKALEELLGVKINVSPDSHF 241

                        250
                 ....*....|
gi 681105299 247 NGALGAAIFA 256
Cdd:cd24104  242 MGALGAALFA 251
ASKHA_NBD_benz_CoA_BzdP cd24107
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
 7-256 3.11e-93

nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.


Pssm-ID: 466957 [Multi-domain]  Cd Length: 250  Bit Score: 275.19  E-value: 3.11e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGkEIMASSVIDVGAGTSG-PSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:cd24107    1 TAGIDVGSKFTKAVILEDG-EILAKAIVPTGFDVAKaAERALDEALAAAGISRDDVKKIVATGAGRKLVSFADDTVTEVV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  86 CHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTIS 165
Cdd:cd24107   80 CAAKGAYFLFPSARTVIDVGAEEGRAIKLDENGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSLKSTKKIPMN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 166 STCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQ 245
Cdd:cd24107  160 AQCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVRRVGIEDDVALIGGVAKNPGFVESLKELLGKEVLVPEDPE 239

                        250
                 ....*....|.
gi 681105299 246 LNGALGAAIFA 256
Cdd:cd24107  240 YVGALGAALIA 250
ASKHA_NBD_benz_CoA_BcrD_BadG cd24105
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ...
 7-259 1.07e-91

nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.


Pssm-ID: 466955  Cd Length: 256  Bit Score: 271.38  E-value: 1.07e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGTSGPSR-AINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:cd24105    1 TAGIDVGSGYTKAVIMDDGEKILAKRVERTRQRDEEVAReAYNEALEEAGLKRDDIAYVATTGEGRYVVFFRDGHFTDLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  86 CHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTIS 165
Cdd:cd24105   81 THARGAIFLFPGTRTVLDIGAQHTRAIRIDEKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSLQADNPEPIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 166 STCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYC- 244
Cdd:cd24105  161 GVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLKRVGAEPEVTLTGGLARNEGMVEALEELLGAKVNVAEHDd 240

                        250
                 ....*....|....*.
gi 681105299 245 -QLNGALGAAIFAHQK 259
Cdd:cd24105  241 sIYAGALGAALLGAFR 256
ASKHA_NBD_BcrAD_BadFG-like cd24002
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ...
 7-255 5.86e-91

nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466852 [Multi-domain]  Cd Length: 255  Bit Score: 269.69  E-value: 5.86e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGTSGPSRAINAVLEKA----NLTLDDIDFITATGYGRNSLE-EADFQM 81
Cdd:cd24002    1 TLGLDIGSTTSKAVLLDEGKNIVATEYERSGTGTSGPIEAVKKTLEKFllekGVKEEDIACTGVTGYGRVELFiDGDKQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  82 SELSCHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLD 161
Cdd:cd24002   81 SEVSAHARGANHIYPDARTIIDVGGQDAKVIILDENGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKMNSKKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 162 VTISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGI-KDDVVMTGGVALNKGMVRALEENVGHKIYT 240
Cdd:cd24002  161 VSVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLGVpKKDVVLQGGVARNSAVVRALEEIINNEIIV 240

                        250
                 ....*....|....*
gi 681105299 241 SEYCQLNGALGAAIF 255
Cdd:cd24002  241 PEIAQVMGALGAALL 255
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 9-255 1.29e-88

nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466959 [Multi-domain]  Cd Length: 243  Bit Score: 263.29  E-value: 1.29e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   9 GVDVGSTASKGLILkNGKEIMASSVIDVGAgtSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELSCHA 88
Cdd:cd24109    3 GIDIGSRATKIALF-EDDKILEKFVIPTGW--FYKEYGRRIIKELLEDINYEDDKIVATGYGRNNLDFADKTITEITAHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  89 KGAYFLFPRVHTIIDIGGQDAKALKIgDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTlDVTISSTC 168
Cdd:cd24109   80 KGARYLTGKDFTVIDIGGQDTKVIKV-ENGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPE-PLSISSTC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 169 TVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIkDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQLNG 248
Cdd:cd24109  158 AVFAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLKS-PPIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAG 236


                 ....*..
gi 681105299 249 ALGAAIF 255
Cdd:cd24109  237 AIGAALI 243
ASKHA_NBD_benz_CoA_BzdQ cd24106
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ...
 7-256 5.33e-88

nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.


Pssm-ID: 466956  Cd Length: 253  Bit Score: 262.16  E-value: 5.33e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGkEIMASSVIDVGAGTSGPS-RAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:cd24106    1 TAGIDVGSVSSQAVIMVDG-ELYAYSNMRTGSDSPESAqKALNAALEKTGLKLEDIHYIVGTGYGRVNVPFANKAITEIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  86 CHAKGAYFLF-PRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDV-T 163
Cdd:cd24106   80 CHARGANYMYgPSVRTVLDMGGQDCKAIRCDEKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPIEEIGELSLEVDKEPpP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 164 ISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEY 243
Cdd:cd24106  160 VSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLLERVGVEKDFVITGGIAKNIGVVKRIEKELGIKALIPKE 239

                        250
                 ....*....|....
gi 681105299 244 C-QLNGALGAAIFA 256
Cdd:cd24106  240 DpQIAGALGAALFA 253
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 6-254 4.30e-84

CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.


Pssm-ID: 129344  Cd Length: 248  Bit Score: 252.02  E-value: 4.30e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299    6 YTMGVDVGSTASKGLILKNGKeIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEEADFQMSELS 85
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGK-VIGYKWLDTTPVIEETARAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   86 CHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGgVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVTIS 165
Cdd:TIGR00241  80 CHGKGANYLAPEARGVIDIGGQDSKVIKIDDG-KVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAKIS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  166 STCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKIYTSEYCQ 245
Cdd:TIGR00241 159 SMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQ 238


                  ....*....
gi 681105299  246 LNGALGAAI 254
Cdd:TIGR00241 239 IVGAVGAAL 247
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 9-256 1.40e-65

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 205.67  E-value: 1.40e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299    9 GVDVGSTASKGLILKNGKEIMAS--------SVIDVGAGTSGPSRAINAVLEKANLTLDDIDFI--TATGYGRNSLE--- 75
Cdd:pfam01869   2 GIDGGSTKTKAVLMDDDGEVLGRaiagsanfESVGVEAAERNLKDAITEALEEAGLKLDDIEYMflGLTGYGRAGVDghf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   76 EADFQMSELSCHAKGAYFLFPRV---HTIIDIGGQDAKALKIgDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELD 152
Cdd:pfam01869  82 GKDIVREEITVHADGAVALAPGTrgeDGVIDIGGTGSKVIGL-DGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  153 DLDKKSTL-DVTISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGI-KDDVVMTGGVALNKGMVRAL 230
Cdd:pfam01869 161 GLAPKTTLnKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFvPDEVVLTGGVAKNAGLVKAL 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 681105299  231 -----EENVGHKIYTSEYCQLNGALGAAIFA 256
Cdd:pfam01869 241 rdylkENILGVKVNVHPDPQYAGAIGAALLA 271
ASKHA_NBD_O66634-like_rpt2 cd24035
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ...
 8-260 1.40e-59

nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466885  Cd Length: 258  Bit Score: 189.67  E-value: 1.40e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   8 MGVDVGSTASKGLILKNGKEIMASSVIDvgagTSG-PSRAINAVLEKANLTLDDIDFIT---ATGYGRN---SLEEADFQ 80
Cdd:cd24035    2 LGIDVGSTTTKAVLIDEDGEILASVYLR----TKGnPIEAVKKGLKELREQLPEKVVIVgvgTTGSGREllkDALGADVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  81 MSELSCHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLEnFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTL 160
Cdd:cd24035   78 KVEITAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVVKD-FAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALKAKN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 161 DVTISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVgsLAKRVGIK---DDVVMTGGVALNKGMVRALEENVGHK 237
Cdd:cd24035  157 PPDLGSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNY--LNKVVGGRnlgKKIVFQGGTFLNKAVLAAFEQVTGKE 234

                        250       260
                 ....*....|....*....|...
gi 681105299 238 IYTSEYCQLNGALGAAIFAHQKI 260
Cdd:cd24035  235 IIVPPHPGLMGAYGAALLAKEEI 257
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
 7-256 1.06e-55

nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466884 [Multi-domain]  Cd Length: 258  Bit Score: 179.71  E-value: 1.06e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNGKEIMASSVIDVGAGtsgPSRAINAVLEKANLTLDD-IDFITATGYGRNSLEEAD--FQMSE 83
Cdd:cd24034    1 YLGIDIGSTTVKAVVLDEKGNIVFSDYERHFGN---PREALLELLEEIKERLGDeIARIAVTGSGGRGLAELLglPFVQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  84 LSCHAKGAYFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTLDVT 163
Cdd:cd24034   78 VVAIEAAVKHLHPDARTVIEIGGEDFKLIELDGDGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 164 ISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRV-GSLAKRVGIKDDVVMTGGVALNKGMVRALEENV--GHKIYT 240
Cdd:cd24034  158 IAGRCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNViATLAKGREIEGPVILVGGVATNNAVLREAFEELlgDEELIV 237

                        250
                 ....*....|....*.
gi 681105299 241 SEYCQLNGALGAAIFA 256
Cdd:cd24034  238 PEHAEYFEALGAALYA 253
benz_CoA_bzdQ TIGR03192
benzoyl-CoA reductase, bzd-type, Q subunit; Members of this family are the Q subunit of one of ...
 5-264 1.62e-48

benzoyl-CoA reductase, bzd-type, Q subunit; Members of this family are the Q subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene.


Pssm-ID: 132236  Cd Length: 293  Bit Score: 162.57  E-value: 1.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299    5 IYTMGVDVGSTASKGLILKNGKEIMASSVidvGAGTSGPSRAINA---VLEKANLTLDDIDFITATGYGRNSLEEADFQM 81
Cdd:TIGR03192  32 IITCGIDVGSVSSQAVLVCDGELYGYNSM---RTGNNSPDSAKNAlqgIMDKIGMKLEDINYVVGTGYGRVNVPFAHKAI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   82 SELSCHAKGA-YFLFPRVHTIIDIGGQDAKALKIGDGGVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDdldkKSTL 160
Cdd:TIGR03192 109 TEIACHARGAnYMGGNAVRTILDMGGQDCKAIHCDEKGKVTNFLMNDKCAAGTGRGMEVISDLMQIPIADLG----PRSF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  161 DV-----TISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRVGSLAKRVGIKDDVVMTGGVALNKGMVRALEENVG 235
Cdd:TIGR03192 185 DVetepeAVSSICVVFAKSEALGLLKAGYTKNMVIAAYCQAMAERVVSLLERIGVEEGFFITGGIAKNPGVVKRIERILG 264

                         250       260       270
                  ....*....|....*....|....*....|
gi 681105299  236 HK-IYTSEYCQLNGALGAAIFAHqKIMQNK 264
Cdd:TIGR03192 265 IKaVDTKIDSQIAGALGAALFGY-TLMQKQ 293
ASKHA_NBD_MJ0800-like cd24108
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ...
 7-256 3.03e-45

nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ0800, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466958  Cd Length: 259  Bit Score: 152.99  E-value: 3.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299   7 TMGVDVGSTASKGLILKNgKEIMASSVIDVGAGTSGPSRAINAVLEKANLTLDDIDFITATGYGRNSLEE---ADFQMSE 83
Cdd:cd24108    1 TAGIDSGSTTTKAVVMKD-NEIIGTGWMPTTDVIESAEKAFEEALEEAGIKLSDIEAIGTTGYGRYTIGKhfnADLVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  84 LSCHAKGAYFLFPRVH---TIIDIGGQDAKALKIGDGgVLENFVMNDKCAAGTGRFLDVIARVLEVDISELDDLDKKSTL 160
Cdd:cd24108   80 LTVNSKGAVYLADKQKgeaTVIDIGGMDNKAITVNDG-IPDNFTMGGICAGASGRFLEMTARRLGVDITELGELALKGDW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 161 D-VTISSTCTVFAESEVISQLAQGTKIEDIVKGIHKSIASRV-GSLAKRVGIKDDVVMTGGVALNKGMVRALEENVGHKI 238
Cdd:cd24108  159 RkIRMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVyEQQLQEIDVREPVIQVGGTSLIEGLVKALGEVLGIEV 238

                        250
                 ....*....|....*...
gi 681105299 239 YTSEYCQLNGALGAAIFA 256
Cdd:cd24108  239 IVPPYSQLIGAVGAALLA 256
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 132-252 2.86e-04

nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and similar proteins mainly from archaea and bacteria; Kae1 (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466981  Cd Length: 323  Bit Score: 41.49  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 132 GTGRFLDVIARvlEVDIS-----ELDDLDKKST-----------LDVTISSTCTvfaesEVISQLAQGTKIEDIVKGIHK 195
Cdd:cd24131  155 GIGNALDKFAR--EVGLGhpggpKIEKLAEKGKkyvelpytvkgMDLSFSGLLT-----AALRAYKSGARLEDVCYSLQE 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 681105299 196 SIASRVGSLAKR---VGIKDDVVMTGGVALNK---GMVRALEENVGHKIYT--SEYCQLNGALGA 252
Cdd:cd24131  228 TAFAMLVEVTERalaHTGKDEVLLVGGVAANNrlrEMLREMCEERGAKFYVppPELCGDNGAMIA 292
ASKHA_NBD_TobZ_N cd24098
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
 42-121 5.70e-04

N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.


Pssm-ID: 466948 [Multi-domain]  Cd Length: 243  Bit Score: 40.52  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  42 GPSRAINAVLEKANLTLDDIDFItATGYGRNSLEEADFQMSE--LsCHAKGAYFLFPRVHTII---D-IGGQDAKALKIG 115
Cdd:cd24098   41 LPVNAIRYCLKEAGITLDDVDAV-AFGWDPPLKFEPPIHFVEhhL-AHAASAFYPSGFDEAAIlvlDgVGEWASTSLGVG 118


                 ....*.
gi 681105299 116 DGGVLE 121
Cdd:cd24098  119 EGNKIE 124
PRK05790 PRK05790
putative acyltransferase; Provisional
 41-64 1.59e-03

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 39.37  E-value: 1.59e-03
                         10        20
                 ....*....|....*....|....
gi 681105299  41 SGPSRAINAVLEKANLTLDDIDFI 64
Cdd:PRK05790 291 IGPVPAIRKALEKAGWSLADLDLI 314
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 132-252 1.74e-03

nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called kinase-associated endopeptidase 1, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, kinase-associated endopeptidase 1 (Kae1), t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is the mammalian orthologue of kinase-associated endopeptidase Kae1. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466946  Cd Length: 301  Bit Score: 38.95  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 132 GTGRFLDVIARVLEVDIS---ELDDLDKKST----LDVTISSTCTVFAE--SEVISQLAQGTKIEDIVKGIHKSIASRVG 202
Cdd:cd24096  154 GIGNCLDQFARELGLPFPggpKIEKLAEKGKklidLPYTVKGMDVSFSGllTAAERAYKSGYRKEDLCYSLQETAFAMLV 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 681105299 203 SLAKR---VGIKDDVVMTGGVALNK---GMVRALEENVGHKIYTS--EYCQLNGALGA 252
Cdd:cd24096  234 EITERalaHTGKDEVLLVGGVAANNrlrEMLKAMCEDRGIKFFVPpkEYCGDNGAMIA 291
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 43-121 1.76e-03

N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466950 [Multi-domain]  Cd Length: 238  Bit Score: 38.99  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299  43 PSRAINAVLEKANLTLDDIDFIT-ATGYGRNSLEEADFQMselsCHAKGAYFL---FPRVHTI-IDiGGQDAKALK--IG 115
Cdd:cd24100   40 PYRAIEEVLKLAGISPSDIDAVAvAGLFSKAKIIFVDHHL----AHAASAYYTspgFDDALVItLD-GGGDGLSGTvsIG 114


                 ....*.
gi 681105299 116 DGGVLE 121
Cdd:cd24100  115 EGGKLE 120
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 185-265 1.77e-03

nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.


Pssm-ID: 466983  Cd Length: 328  Bit Score: 39.00  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 681105299 185 KIEDIVKGIHKSI----ASRVGSLAKRVGIKDdVVMTGGVALNKGMVRALEE---NVGHKIY--TSEYCQLNGALGAAiF 255
Cdd:cd24133  231 NKADIAASFQEAVvdvlVEKTLRAAKETGIKR-LVVAGGVAANSRLREKLEEaaeKRGLEVYipPPELCTDNAAMIAA-A 308

                         90
                 ....*....|
gi 681105299 256 AHQKIMQNKR 265
Cdd:cd24133  309 GYYRYKRGKF 318
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
 42-64 3.97e-03

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 38.12  E-value: 3.97e-03
                         10        20
                 ....*....|....*....|...
gi 681105299  42 GPSRAINAVLEKANLTLDDIDFI 64
Cdd:COG0183  290 GPVPATRKALARAGLTLDDIDLI 312
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
 42-64 8.13e-03

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 37.07  E-value: 8.13e-03
                         10        20
                 ....*....|....*....|...
gi 681105299  42 GPSRAINAVLEKANLTLDDIDFI 64
Cdd:cd00751  286 GPVPAIPKALKRAGLTLDDIDLI 308
 
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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