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Conserved domains on  [gi|496097821|ref|WP_008822328|]
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ADP-forming succinate--CoA ligase subunit beta [Prevotella histicola]

Protein Classification

succinate--CoA ligase subunit beta( domain architecture ID 11414565)

ADP/GDP-forming succinate--CoA ligase subunit beta provides nucleotide specificity and binds the succinate substrate for the succinate--CoA ligase enzyme, which functions in the citric acid cycle (TCA) by coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-378 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


:

Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 616.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:COG0045    1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:COG0045   81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:COG0045  161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:COG0045  241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSKN 378
Cdd:COG0045  321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAesGLNIIAADTLEEAAKKAVELAKG 387
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-378 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 616.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:COG0045    1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:COG0045   81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:COG0045  161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:COG0045  241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSKN 378
Cdd:COG0045  321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAesGLNIIAADTLEEAAKKAVELAKG 387
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-377 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 578.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:PRK00696  81 LvthqtgpKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSK 377
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAesGLNIIAADTLDDAAQKAVEAAK 386
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-377 1.15e-180

succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]


Pssm-ID: 273396 [Multi-domain]  Cd Length: 386  Bit Score: 506.53  E-value: 1.15e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   81 IKGF-------TVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:TIGR01016  81 LVTNqtdplgqPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496097821  314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSK 377
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAesGLNIIFATSMEEAAEKAVEAAE 386
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-195 5.72e-84

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 254.11  E-value: 5.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    2 KVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMNI 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   82 K-------GFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLAR 154
Cdd:pfam08442  81 VtkqtgpdGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 496097821  155 EAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLV 195
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLV 201
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-378 0e+00

Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439815 [Multi-domain]  Cd Length: 388  Bit Score: 616.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:COG0045    1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:COG0045   81 LvthqtgpKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:COG0045  161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:COG0045  241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSKN 378
Cdd:COG0045  321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAesGLNIIAADTLEEAAKKAVELAKG 387
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-377 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 578.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:PRK00696  81 LvthqtgpKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSK 377
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAesGLNIIAADTLDDAAQKAVEAAK 386
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-377 1.15e-180

succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not discriminate the ADP-forming enzyme ((EC 6.2.1.5) from the GDP_forming (EC 6.2.1.4) enzyme. The N-terminal half is described by the CoA-ligases model (pfam00549). The C-terminal half is described by the ATP-grasp model (pfam02222). This family contains a split seen both in a maximum parsimony tree (which ignores gaps) and in the gap pattern near position 85 of the seed alignment. Eukaryotic and most bacterial sequences are longer and contain a region similar to TXQTXXXG. Sequences from Deinococcus radiodurans, Mycobacterium tuberculosis, Streptomyces coelicolor, and the Archaea are 6 amino acids shorter in that region and contain a motif resembling [KR]G [Energy metabolism, TCA cycle]


Pssm-ID: 273396 [Multi-domain]  Cd Length: 386  Bit Score: 506.53  E-value: 1.15e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   81 IKGF-------TVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:TIGR01016  81 LVTNqtdplgqPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496097821  314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSK 377
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAesGLNIIFATSMEEAAEKAVEAAE 386
PRK14046 PRK14046
malate--CoA ligase subunit beta; Provisional
 1-378 1.44e-157

malate--CoA ligase subunit beta; Provisional


Pssm-ID: 237594 [Multi-domain]  Cd Length: 392  Bit Score: 448.39  E-value: 1.44e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   1 MKVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMN 80
Cdd:PRK14046   1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  81 I-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLA 153
Cdd:PRK14046  81 LvthqtgpEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 154 REAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELFEPTPEER 233
Cdd:PRK14046 161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 234 KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKVVLINIFG 313
Cdd:PRK14046 241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496097821 314 GITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILE--GTQFTVGTSMSDAGHKAVELSKN 378
Cdd:PRK14046 321 GINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAesGLPIITADTLAEAAEKAVEAWKG 387
PLN00124 PLN00124
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
 3-373 1.47e-108

succinyl-CoA ligase [GDP-forming] subunit beta; Provisional


Pssm-ID: 177736 [Multi-domain]  Cd Length: 422  Bit Score: 324.78  E-value: 1.47e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   3 VHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKA--VVKAQVHTGGRGKA-------GGVKLgSNETEIRQHA 73
Cdd:PLN00124  30 IHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMFPDEGevVVKSQILAGGRGLGtfknglkGGVHI-VKKDKAEELA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  74 EAILGMNI-------KGFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVI 146
Cdd:PLN00124 109 GKMLGQILvtkqtgpAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDIFK 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 147 GMSDYLAREAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLVMLKDGSLKAIDAKMTFDDNALYRHPDVAELF 226
Cdd:PLN00124 189 GITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFALR 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 227 EPTPEERKEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKLYGGEPANFLDIGGSSNPEKIVEAMRLLLGDKHVKV 306
Cdd:PLN00124 269 DTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKVKA 348

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496097821 307 VLINIFGGITRCDDVAKGLIEAFKILKTDIPIVIRLTGTNEAEGRSILEGTQFTVGTS--MSDAGHKAV 373
Cdd:PLN00124 349 ILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAedLDDAAEKAV 417
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-195 5.72e-84

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 254.11  E-value: 5.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    2 KVHEYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQHAEAILGMNI 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   82 K-------GFTVDRVLVSEAVDIASEYYMSILVDRKSKCPMLMLSRAGGMDIEQVAKETPEKIEKIIIDPVIGMSDYLAR 154
Cdd:pfam08442  81 VtkqtgpdGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 496097821  155 EAAFKLFDDMAQVKQAVPIFKNIYKLFTEKDASLAEINPLV 195
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLV 201
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 255-346 8.57e-26

CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, malate CoA ligase and ATP-citrate lyase. Some members of the family utilize ATP others use GTP.


Pssm-ID: 395434 [Multi-domain]  Cd Length: 128  Bit Score: 100.41  E-value: 8.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  255 MVNGAGLAMATMDMIKLYGGEPANFLDIGG-SSNPEKIVEAMRLLLGDKHVKVVLINIFGGITRCDDVAKGLIEAFK-IL 332
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGdAFTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKeAR 80

                          90
                  ....*....|....
gi 496097821  333 KTDIPIVIRLTGTN 346
Cdd:pfam00549  81 ARELPVVARVCGTE 94
PLN02235 PLN02235
ATP citrate (pro-S)-lyase
 2-330 4.42e-14

ATP citrate (pro-S)-lyase


Pssm-ID: 177879 [Multi-domain]  Cd Length: 423  Bit Score: 73.26  E-value: 4.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   2 KVHEYQAKQFF-------ASYGLPVDRNIICRTPD--EAVEAYKKLGLEKAVVKAQVHTGGRGKAGGVKLGSNETEIRQH 72
Cdd:PLN02235   5 KIREYDSKRLLkehlkrlAGIDLPIRSAQVTESTDfnELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQVATF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821  73 AEAILGMNI-----KGfTVDRVLVSEAVDIASEYYMSILVDRKSKcpMLMLSRAGGMDIEqvakETPEKIEKIIIDpvig 147
Cdd:PLN02235  85 VKERLGKEVemggcKG-PITTFIVEPFVPHDQEFYLSIVSDRLGC--SISFSECGGIEIE----ENWDKVKTIFLP---- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 148 MSDYLAREAAFKLFDDMA-QVKQAVPIF-KNIYKLFTEKDASLAEINPLVMLkDGSLKAIDAKMTFDDNALYRH-PDVAE 224
Cdd:PLN02235 154 TEAPLTSEICAPLIATLPlEIRGKIEEFiKGVFAVFQDLDFTFLEMNPFTLV-DGEPYPLDMRGELDDTAAFKNfKKWGN 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821 225 LFEPTPEER------------KEREAKDKGFSYVNLGGSIGCMVNGAGLAMATMDMIKL--YGGEPANFLDIGGSSNPEK 290
Cdd:PLN02235 233 IEFPLPFGRvmsptesfihglDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDlgYASELGNYAEYSGAPNEEE 312

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 496097821 291 IVEAMRLLLG------DKHVKVVLINifGGITRCDDVA---KGLIEAFK 330
Cdd:PLN02235 313 VLQYARVVIDcatanpDGRKRALLIG--GGIANFTDVAatfNGIIRALR 359
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 5-86 1.92e-09

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 463918 [Multi-domain]  Cd Length: 221  Bit Score: 57.10  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    5 EYQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLeKAVVKAQ----VHtggRGKAGGVKLG-SNETEIRQHAEAIL-- 77
Cdd:pfam13549  12 EPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGY-PVVLKIVspdiLH---KSDVGGVRLNlRSAEAVRAAYEEILer 87

                          90
                  ....*....|....*
gi 496097821   78 ------GMNIKGFTV 86
Cdd:pfam13549  88 vrryrpDARIEGVLV 102
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 8-146 1.11e-05

Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).


Pssm-ID: 395851 [Multi-domain]  Cd Length: 194  Bit Score: 45.74  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    8 AKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLEKAVVKAQVHTGGRgkagGVKLGSNETEIRQHAEAILGMNIKGFTVD 87
Cdd:pfam01071   6 AKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK----GVIVASSNEEAIKAVDEILEQKKFGEAGE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496097821   88 RVLVSEAVDiASEYYMSILVDRKSKCPMLMLS---RA---------GGMD----IEQVAKETPEKIEKIIIDPVI 146
Cdd:pfam01071  82 TVVIEEFLE-GEEVSVLAFVDGKTVKPLPPAQdhkRAgegdtgpntGGMGayspAPVITPELLERIKETIVEPTV 155
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 6-96 6.44e-05

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 44.09  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821   6 YQAKQFFASYGLPVDRNIICRTPDEAVEAYKKLGLeKAVVKAQVHTGGRgkagGVKLGSNETEIRQHAEAILGMNIKGFT 85
Cdd:COG0439   56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-PVVVKPADGAGSR----GVRVVRDEEELEAALAEARAEAKAGSP 130

                         90
                 ....*....|.
gi 496097821  86 VDRVLVSEAVD 96
Cdd:COG0439  131 NGEVLVEEFLE 141
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 16-113 7.36e-03

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 38.44  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496097821    16 GLPVDRNIICRTPDEAVEAYKKLGLeKAVVKAQVHTGGRGkaGGVklGSNETEIRQHAEAILGMNikgfTVDRVLVSEAV 95
Cdd:TIGR01369  139 GEPVPESEIAHSVEEALAAAKEIGY-PVIVRPAFTLGGTG--GGI--AYNREELKEIAERALSAS----PINQVLVEKSL 209

                           90
                   ....*....|....*...
gi 496097821    96 DIASEYYMSILVDRKSKC 113
Cdd:TIGR01369  210 AGWKEIEYEVMRDSNDNC 227
 
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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