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Conserved domains on  [gi|544972738|ref|WP_021375396|]
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acyl-CoA dehydratase activase [Clostridioides difficile]

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
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-251 1.40e-108

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


:

Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 313.58  E-value: 1.40e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   1 MFSIGMDSGSVATKGVLFDGEKIIKKII-IPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMD--FADKKV 75
Cdd:COG1924    3 MIYLGIDIGSTTTKAVLLDEDGEILASAyLPTGGDPLEAAKEALKELLEEagLKREDIAGVVATGYGRVLIGaaFADKVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  76 TEITCHTRGVYFLNKNIRTILDVGGQDSKVINLdRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEP 154
Cdd:COG1924   83 TEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKL-EDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELAlKAKNP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 155 VNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIA 234
Cdd:COG1924  162 VDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIVP 241

                        250
                 ....*....|....*..
gi 544972738 235 EDTQIIGALGAAVIGFR 251
Cdd:COG1924  242 PIPQLMGALGAALLARE 258
 
Name Accession Description Interval E-value
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-251 1.40e-108

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


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 313.58  E-value: 1.40e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   1 MFSIGMDSGSVATKGVLFDGEKIIKKII-IPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMD--FADKKV 75
Cdd:COG1924    3 MIYLGIDIGSTTTKAVLLDEDGEILASAyLPTGGDPLEAAKEALKELLEEagLKREDIAGVVATGYGRVLIGaaFADKVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  76 TEITCHTRGVYFLNKNIRTILDVGGQDSKVINLdRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEP 154
Cdd:COG1924   83 TEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKL-EDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELAlKAKNP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 155 VNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIA 234
Cdd:COG1924  162 VDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIVP 241

                        250
                 ....*....|....*..
gi 544972738 235 EDTQIIGALGAAVIGFR 251
Cdd:COG1924  242 PIPQLMGALGAALLARE 258
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
 3-248 9.22e-100

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: 290.98  E-value: 9.22e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGVLFDGEKI-IKKIIIPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMDFADKKVTEIT 79
Cdd:cd24036    1 FAGIDVGSTTTKAVILDDKGKiLGKAVIRTGTDPEKTAERALEEALEEagLSREDIEYIVATGYGRNSVPFADKTITEIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  80 CHTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNIS 158
Cdd:cd24036   81 CHARGAHFLFPEARTVIDIGGQDSKVIRLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELAlKSTNPVEIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 159 SMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQ 238
Cdd:cd24036  161 STCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKRVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQ 240

                        250
                 ....*....|
gi 544972738 239 IIGALGAAVI 248
Cdd:cd24036  241 LVGALGAALL 250
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 2-248 2.02e-77

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: 234.30  E-value: 2.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738    2 FSIGMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYELLSS-EIDKKDIKKVVGTGYGRGVMDFADKKVTEITC 80
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGKVIGYKWLDTTPVIEETARAILEALKEaGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   81 HTRGVYFLNKNIRTILDVGGQDSKVINLDrDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNISS 159
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKID-DGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAeKADRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  160 MCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQI 239
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 544972738  240 IGALGAAVI 248
Cdd:TIGR00241 240 VGAVGAALL 248
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 4-249 6.82e-46

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: 154.43  E-value: 6.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738    4 IGMDSGSVATKGVLFD--GEKIIKKIIIPTGWSP-------KSTSKQVYELLS-SEIDKKDIK--KVVGTGYGR-GV-MD 69
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDddGEVLGRAIAGSANFESvgveaaeRNLKDAITEALEeAGLKLDDIEymFLGLTGYGRaGVdGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   70 FADKKVT-EITCHTRGVYFLNKNIR---TILDVGGQDSKVINLDrDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESI 145
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLD-GGKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  146 DTLA-KG-YEPVNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLAR-GEVLDEVAFTGGLAKSKELVKM 222
Cdd:pfam01869 160 DGLApKTtLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRlGFVPDEVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 544972738  223 I-----EEILGKKIFIAEDTQIIGALGAAVIG 249
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 211-247 4.03e-03

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 38.03  E-value: 4.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 544972738 211 GGLAKSKELVKMIEEILGKKIFIAEDTQIIgALGAAV 247
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVVPEMAETT-ALGAAL 449
 
Name Accession Description Interval E-value
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-251 1.40e-108

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


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 313.58  E-value: 1.40e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   1 MFSIGMDSGSVATKGVLFDGEKIIKKII-IPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMD--FADKKV 75
Cdd:COG1924    3 MIYLGIDIGSTTTKAVLLDEDGEILASAyLPTGGDPLEAAKEALKELLEEagLKREDIAGVVATGYGRVLIGaaFADKVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  76 TEITCHTRGVYFLNKNIRTILDVGGQDSKVINLdRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEP 154
Cdd:COG1924   83 TEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKL-EDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELAlKAKNP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 155 VNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIA 234
Cdd:COG1924  162 VDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIVP 241

                        250
                 ....*....|....*..
gi 544972738 235 EDTQIIGALGAAVIGFR 251
Cdd:COG1924  242 PIPQLMGALGAALLARE 258
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
 3-248 9.22e-100

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: 290.98  E-value: 9.22e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGVLFDGEKI-IKKIIIPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMDFADKKVTEIT 79
Cdd:cd24036    1 FAGIDVGSTTTKAVILDDKGKiLGKAVIRTGTDPEKTAERALEEALEEagLSREDIEYIVATGYGRNSVPFADKTITEIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  80 CHTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNIS 158
Cdd:cd24036   81 CHARGAHFLFPEARTVIDIGGQDSKVIRLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELAlKSTNPVEIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 159 SMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQ 238
Cdd:cd24036  161 STCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKRVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQ 240

                        250
                 ....*....|
gi 544972738 239 IIGALGAAVI 248
Cdd:cd24036  241 LVGALGAALL 250
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 3-248 9.84e-93

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: 272.92  E-value: 9.84e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYELLSSEIDKKDIKkVVGTGYGRGVMDFADKKVTEITCHT 82
Cdd:cd24109    1 YIGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINYEDDK-IVATGYGRNNLDFADKTITEITAHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  83 RGVYFLNKNIRTILDVGGQDSKVINLDrDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLAKGYEPVNISSMCT 162
Cdd:cd24109   80 KGARYLTGKDFTVIDIGGQDTKVIKVE-NGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPLSISSTCA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 163 VFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEvLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQIIGA 242
Cdd:cd24109  159 VFAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLK-SPPIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAGA 237


                 ....*.
gi 544972738 243 LGAAVI 248
Cdd:cd24109  238 IGAALI 243
ASKHA_NBD_HgdC_HadI-like cd24103
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
 3-250 6.72e-80

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: 240.78  E-value: 6.72e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGV-LFDGEKIIKKIIIP--TGWS-PKSTSKQVYEllSSEIDKKDIKKVVGTGYGRGVMDFADKKVTEI 78
Cdd:cd24103    1 TMGIDIGSTASKCViLKDGKEIVAQSVISvgTGTSgPARALEEVLE--KAGLAKEDIAYTVATGYGRNSFEGADKQISEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  79 TCHTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTL-AKGYEPVNI 157
Cdd:cd24103   79 SCHARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELdAQSTNPVSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 158 SSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDT 237
Cdd:cd24103  159 SSTCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNP 238

                        250
                 ....*....|...
gi 544972738 238 QIIGALGAAVIGF 250
Cdd:cd24103  239 QLTGALGAALYAY 251
ASKHA_NBD_benz_CoA_BzdP cd24107
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
 4-248 1.85e-79

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: 239.37  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   4 IGMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYE--LLSSEIDKKDIKKVVGTGYGRGVMDFADKKVTEITCH 81
Cdd:cd24107    2 AGIDVGSKFTKAVILEDGEILAKAIVPTGFDVAKAAERALDeaLAAAGISRDDVKKIVATGAGRKLVSFADDTVTEVVCA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  82 TRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNISSM 160
Cdd:cd24107   82 AKGAYFLFPSARTVIDVGAEEGRAIKLDENGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSlKSTKKIPMNAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 161 CTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQII 240
Cdd:cd24107  162 CAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVRRVGIEDDVALIGGVAKNPGFVESLKELLGKEVLVPEDPEYV 241


                 ....*...
gi 544972738 241 GALGAAVI 248
Cdd:cd24107  242 GALGAALI 249
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 2-248 2.02e-77

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: 234.30  E-value: 2.02e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738    2 FSIGMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYELLSS-EIDKKDIKKVVGTGYGRGVMDFADKKVTEITC 80
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGKVIGYKWLDTTPVIEETARAILEALKEaGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   81 HTRGVYFLNKNIRTILDVGGQDSKVINLDrDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNISS 159
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKID-DGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAeKADRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  160 MCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQI 239
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 544972738  240 IGALGAAVI 248
Cdd:TIGR00241 240 VGAVGAALL 248
ASKHA_NBD_benz_CoA_BzdQ cd24106
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ...
 5-249 8.39e-73

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: 222.48  E-value: 8.39e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   5 GMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYE--LLSSEIDKKDIKKVVGTGYGRGVMDFADKKVTEITCHT 82
Cdd:cd24106    3 GIDVGSVSSQAVIMVDGELYAYSNMRTGSDSPESAQKALNaaLEKTGLKLEDIHYIVGTGYGRVNVPFANKAITEIACHA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  83 RGV-YFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLAKGY--EPVNISS 159
Cdd:cd24106   83 RGAnYMYGPSVRTVLDMGGQDCKAIRCDEKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPIEEIGELSLEVdkEPPPVSS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 160 MCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIA-EDTQ 238
Cdd:cd24106  163 TCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLLERVGVEKDFVITGGIAKNIGVVKRIEKELGIKALIPkEDPQ 242

                        250
                 ....*....|.
gi 544972738 239 IIGALGAAVIG 249
Cdd:cd24106  243 IAGALGAALFA 253
ASKHA_NBD_benz_CoA_BcrA_BadF cd24104
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
 4-251 3.23e-70

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: 216.01  E-value: 3.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   4 IGMDSGSVATKGVLFDGEKIIKKII-IPTGWSPKSTSKQVYE--LLSSEIDKKDIKKVVGTGYGRGVMDFADKKVTEITC 80
Cdd:cd24104    2 AGVDVGSTQTKAVIIDEDGEIVGRGlTNTGANVVVAAERAFReaIEEAGIKEEEVEYVVGTGYGRYKVTFGNAQRTEISC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  81 HTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNISS 159
Cdd:cd24104   82 HARGAHHMFPNTRTVLDIGGQDTKAIRVDETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLAlKSTKPVRISS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 160 MCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQI 239
Cdd:cd24104  162 TCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIRRVGIEPEFTFTGGVARNEAMVKALEELLGVKINVSPDSHF 241

                        250
                 ....*....|..
gi 544972738 240 IGALGAAVIGFR 251
Cdd:cd24104  242 MGALGAALFALE 253
ASKHA_NBD_benz_CoA_BcrD_BadG cd24105
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ...
 4-251 1.81e-69

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: 213.99  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   4 IGMDSGSVATKGVLFD-GEKIIKKIIIPTGWSPKSTSKQVYELLSSE--IDKKDIKKVVGTGYGRGVMDFADKKVTEITC 80
Cdd:cd24105    2 AGIDVGSGYTKAVIMDdGEKILAKRVERTRQRDEEVAREAYNEALEEagLKRDDIAYVATTGEGRYVVFFRDGHFTDLTT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  81 HTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNISS 159
Cdd:cd24105   82 HARGAIFLFPGTRTVLDIGAQHTRAIRIDEKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSlQADNPEPISG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 160 MCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAE--DT 237
Cdd:cd24105  162 VCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLKRVGAEPEVTLTGGLARNEGMVEALEELLGAKVNVAEhdDS 241

                        250
                 ....*....|....
gi 544972738 238 QIIGALGAAVIGFR 251
Cdd:cd24105  242 IYAGALGAALLGAF 255
ASKHA_NBD_BcrAD_BadFG-like cd24002
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ...
 4-248 9.50e-58

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: 184.17  E-value: 9.50e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   4 IGMDSGSVATKGVLFDGEK----IIKKIIIPTGWSPKSTSKQVYE--LLSSEIDKKDIKKVVGTGYGRGVMDF-ADKKVT 76
Cdd:cd24002    2 LGLDIGSTTSKAVLLDEGKnivaTEYERSGTGTSGPIEAVKKTLEkfLLEKGVKEEDIACTGVTGYGRVELFIdGDKQIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  77 EITCHTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPV 155
Cdd:cd24002   82 EVSAHARGANHIYPDARTIIDVGGQDAKVIILDENGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKmNSKKEV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 156 NISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVL-DEVAFTGGLAKSKELVKMIEEILGKKIFIA 234
Cdd:cd24002  162 SVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLGVPkKDVVLQGGVARNSAVVRALEEIINNEIIVP 241

                        250
                 ....*....|....
gi 544972738 235 EDTQIIGALGAAVI 248
Cdd:cd24002  242 EIAQVMGALGAALL 255
ASKHA_NBD_O66634-like_rpt2 cd24035
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ...
 4-248 1.32e-57

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: 183.89  E-value: 1.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   4 IGMDSGSVATKGVLFDGEKIIKKII-IPTGWSPKSTSKQVYELLSSEIDKKDIKKVVG-TGYGR---GVMDFADKKVTEI 78
Cdd:cd24035    2 LGIDVGSTTTKAVLIDEDGEILASVyLRTKGNPIEAVKKGLKELREQLPEKVVIVGVGtTGSGRellKDALGADVVKVEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  79 TCHTRGVYFLNKNIRTILDVGGQDSKVINLdRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KGYEPVNI 157
Cdd:cd24035   82 TAHATAALHFDPDVDTIFEIGGQDSKYISL-KNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELAlKAKNPPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 158 SSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDE-VAFTGGLAKSKELVKMIEEILGKKIFIAED 236
Cdd:cd24035  161 GSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRNLGKkIVFQGGTFLNKAVLAAFEQVTGKEIIVPPH 240

                        250
                 ....*....|..
gi 544972738 237 TQIIGALGAAVI 248
Cdd:cd24035  241 PGLMGAYGAALL 252
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
 3-249 1.27e-50

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: 165.84  E-value: 1.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGVLFDGEKI-IKKIIIPTGWSPKSTSKQVYEllssEIDKKDIKKVVGTGY-GRGVMDFAD----KKVT 76
Cdd:cd24034    1 YLGIDIGSTTVKAVVLDEKGNiVFSDYERHFGNPREALLELLE----EIKERLGDEIARIAVtGSGGRGLAEllglPFVQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  77 EITCHTRGVYFLNKNIRTILDVGGQDSKVINLDRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLAKGYEPV- 155
Cdd:cd24034   77 EVVAIEAAVKHLHPDARTVIEIGGEDFKLIELDGDGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPa 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 156 NISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLARGEVLDE-VAFTGGLA-KSKELVKMIEEILGKK-IF 232
Cdd:cd24034  157 PIAGRCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIEGpVILVGGVAtNNAVLREAFEELLGDEeLI 236

                        250
                 ....*....|....*..
gi 544972738 233 IAEDTQIIGALGAAVIG 249
Cdd:cd24034  237 VPEHAEYFEALGAALYA 253
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 4-249 6.82e-46

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: 154.43  E-value: 6.82e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738    4 IGMDSGSVATKGVLFD--GEKIIKKIIIPTGWSP-------KSTSKQVYELLS-SEIDKKDIK--KVVGTGYGR-GV-MD 69
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDddGEVLGRAIAGSANFESvgveaaeRNLKDAITEALEeAGLKLDDIEymFLGLTGYGRaGVdGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   70 FADKKVT-EITCHTRGVYFLNKNIR---TILDVGGQDSKVINLDrDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESI 145
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLD-GGKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  146 DTLA-KG-YEPVNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKSTSMLAR-GEVLDEVAFTGGLAKSKELVKM 222
Cdd:pfam01869 160 DGLApKTtLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRlGFVPDEVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 544972738  223 I-----EEILGKKIFIAEDTQIIGALGAAVIG 249
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
ASKHA_NBD_MJ0800-like cd24108
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ...
 3-248 3.17e-35

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: 126.41  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738   3 SIGMDSGSVATKGVLFDGEKIIKKIIIPTGWSPKSTSKQVYELLS-SEIDKKDIKKVVGTGYGR---GVMDFADKKVTEI 78
Cdd:cd24108    1 TAGIDSGSTTTKAVVMKDNEIIGTGWMPTTDVIESAEKAFEEALEeAGIKLSDIEAIGTTGYGRytiGKHFNADLVQEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738  79 TCHTRGVYFL---NKNIRTILDVGGQDSKVINLdRDGNVFNFIMNDKCAAGTGRFLEITSNLLGSDIESIDTLA-KG-YE 153
Cdd:cd24108   81 TVNSKGAVYLadkQKGEATVIDIGGMDNKAITV-NDGIPDNFTMGGICAGASGRFLEMTARRLGVDITELGELAlKGdWR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 154 PVNISSMCTVFAESEIVSLLAQNISTGEVAAGILKSIANKS-TSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIF 232
Cdd:cd24108  160 KIRMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVyEQQLQEIDVREPVIQVGGTSLIEGLVKALGEVLGIEVI 239

                        250
                 ....*....|....*.
gi 544972738 233 IAEDTQIIGALGAAVI 248
Cdd:cd24108  240 VPPYSQLIGAVGAALL 255
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
 196-250 6.98e-05

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 43.66  E-value: 6.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 544972738 196 SMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQIIGALGAAVIGF 250
Cdd:cd07805  391 ALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENPQEAGALGAALLAA 445
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
 178-248 7.10e-05

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 43.36  E-value: 7.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544972738 178 STGEVAAGILKSIANKSTSMLAR-----GEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQiiGALGAAVI 248
Cdd:cd07783  351 DRAEFLRALLEGIAFIERLGYERleelgAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEE--AALGAALL 424
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
 172-251 3.42e-04

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 41.44  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 172 LLAQNISTGEVAAGILKSIAnksTSMLARGEVLDEVA--------FTGGLAKSKELVKMIEEILGKKIFIAEDTQiIGAL 243
Cdd:cd07798  362 LSASELTRGDFARAILENIA---FAIRANLEQLEEVSgreipyiiLCGGGSRSALLCQILADVLGKPVLVPEGRE-ASAL 437


                 ....*...
gi 544972738 244 GAAVIGFR 251
Cdd:cd07798  438 GAAICAAV 445
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
 112-246 4.17e-04

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 41.05  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544972738 112 GNVFNFIMndkcaagtgRFLEITSNLLGSDI------ESIDTLA--KGYEPVNISsmCTVFAE-------SEIVSLLAQN 176
Cdd:cd07777  291 GRALAVLV---------DFLREWLRELGGSLsddeiwEKLDELAesEESSDLSVD--PTFFGErhdpegrGSITNIGESN 359

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544972738 177 ISTGEVAAGILKSIANKSTSMLAR----GEVLDEVAFTGG-LAKSKELVKMIEEILGKKIFIA---EDTqiigALGAA 246
Cdd:cd07777  360 FTLGNLFRALCRGIAENLHEMLPRldldLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSegsEEA----AVGAA 433
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 204-251 5.06e-04

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 40.00  E-value: 5.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 544972738  204 LDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQiIGALGAAVIGFR 251
Cdd:pfam02782 149 IDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDE-ATALGAALLAAV 195
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 197-249 1.04e-03

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 39.82  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544972738 197 MLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEdTQIIGALGAAVIG 249
Cdd:COG1070  389 LEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPE-AEEGGALGAALLA 440
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 187-251 1.31e-03

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 39.46  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544972738 187 LKSIANkstSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQiIGALGAAVIGFR 251
Cdd:cd07770  377 LKSIYE---ALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEE-ASALGAALLALE 437
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
 205-249 2.50e-03

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 38.67  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 544972738 205 DEVAFTGGLA-KSKELVKMIEEILGKKIFIAEDTQiIGALGAAVIG 249
Cdd:cd07781  410 NRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQ-APALGAAILA 454
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 211-247 4.03e-03

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 38.03  E-value: 4.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 544972738 211 GGLAKSKELVKMIEEILGKKIFIAEDTQIIgALGAAV 247
Cdd:PTZ00294 414 GGLTKNKLLMQFQADILGKDIVVPEMAETT-ALGAAL 449
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 197-249 4.40e-03

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY 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: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 37.93  E-value: 4.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544972738 197 MLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQiIGALGAAVIG 249
Cdd:cd00366  341 LEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAE-GAALGAAILA 392
ASKHA_NBD_BK cd24011
nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC ...
 186-234 6.25e-03

nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC 2.7.2.7) catalyzes the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate. Butyrate kinases exist in many fermentative species of the bacterial and archaeal families. They belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466861  Cd Length: 345  Bit Score: 37.13  E-value: 6.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544972738 186 ILKSIAnkstSMLA--RGEVlDEVAFTGGLAKSKELVKMIEEILGkkiFIA 234
Cdd:cd24011  279 IAKEIG----ALAAvlKGKV-DAIILTGGLAYSKRLVDRIKERVG---FIA 321
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
 180-250 8.86e-03

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 37.11  E-value: 8.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544972738 180 GEVAAGILKSIA----NKSTSMLARGEVLDEVAFTGGLAKSKELVKMIEEILGKKIFIAEDTQiIGALGAAVIGF 250
Cdd:cd07779  327 AHLARAILEGIAfelrDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSE-ATALGAAILAA 400
 
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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