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Conserved domains on  [gi|16128703|ref|NP_415256|]
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succinyl-CoA synthetase subunit beta [Escherichia coli str. K-12 substr. MG1655]

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

CATH:  3.40.50.261
EC:  6.2.1.-
Gene Ontology:  GO:0004774|GO:0000287|GO:0000166|GO:0006099|GO:0042709
PubMed:  3332988

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 ...
 1-388 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: 700.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:COG0045   1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:COG0045  81 LVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703 321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK 388
Cdd:COG0045 321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKGA 388
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-388 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: 700.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:COG0045   1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:COG0045  81 LVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703 321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK 388
Cdd:COG0045 321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKGA 388
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-388 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 699.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK00696  81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703  321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK 388
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKGK 388
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-386 0e+00

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: 639.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:TIGR01016  81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128703   321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVE 386
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-203 3.69e-112

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 326.14  E-value: 3.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     2 NLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRL 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    82 VTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGR 161
Cdd:pfam08442  81 VTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 16128703   162 ELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVI 203
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
 
Name Accession Description Interval E-value
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 1-388 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: 700.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:COG0045   1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:COG0045  81 LVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703 321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK 388
Cdd:COG0045 321 GITRCDVVAEGIVAALKEVGLKVPVVVRLEGTNVEEGRKILAESGLNIIAADTLEEAAKKAVELAKGA 388
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
1-388 0e+00

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 699.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK00696   1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK00696  81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703  321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEGK 388
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKGK 388
sucCoAbeta TIGR01016
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ...
 1-386 0e+00

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: 639.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:TIGR01016   1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:TIGR01016  81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128703   321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVE 386
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAAE 386
PRK14046 PRK14046
malate--CoA ligase subunit beta; Provisional
 1-387 3.92e-174

malate--CoA ligase subunit beta; Provisional


Pssm-ID: 237594 [Multi-domain]  Cd Length: 392  Bit Score: 490.76  E-value: 3.92e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKR 80
Cdd:PRK14046   1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   81 LVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQG 160
Cdd:PRK14046  81 LVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  161 RELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLREMRDQSQEDP 240
Cdd:PRK14046 161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVLVNIFG 320
Cdd:PRK14046 241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128703  321 GIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEG 387
Cdd:PRK14046 321 GINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAVEAWKG 387
PLN00124 PLN00124
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
 1-387 2.08e-134

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


Pssm-ID: 177736 [Multi-domain]  Cd Length: 422  Bit Score: 391.03  E-value: 2.08e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    1 MNLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKI--GAGPWVVKCQVHAGGRGKA-------GGVKVVnSKEDIRA 71
Cdd:PLN00124  28 LNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpDEGEVVVKSQILAGGRGLGtfknglkGGVHIV-KKDKAEE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   72 FAENWLGKRLVTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDP 151
Cdd:PLN00124 107 LAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDI 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  152 LTGPMPYQGRELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVITKQGDLICLDGKLGADGNALFRQPDLRE 231
Cdd:PLN00124 187 FKGITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  232 MRDQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKV 311
Cdd:PLN00124 267 LRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKV 346

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128703  312 KAVLVNIFGGIVRCDLIADGIIGAVAEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAAKGLTDAAQQVVAAVEG 387
Cdd:PLN00124 347 KAILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKALAI 422
ATP-grasp_2 pfam08442
ATP-grasp domain;
2-203 3.69e-112

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 326.14  E-value: 3.69e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     2 NLHEYQAKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKVVNSKEDIRAFAENWLGKRL 81
Cdd:pfam08442   1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    82 VTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFMASTEGGVEIEKVAEETPHLIHKVALDPLTGPMPYQGR 161
Cdd:pfam08442  81 VTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 16128703   162 ELAFKLGLEGKLVQQFTKIFMGLATIFLERDLALIEINPLVI 203
Cdd:pfam08442 161 EIAFKLGLPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
Ligase_CoA pfam00549
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ...
 262-382 2.68e-29

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: 110.04  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   262 MVNGAGLAMGTMDIVKLHGGEPANFLDVGGGA-TKERVTEAFKIILSDDKVKAVLVNIFGGIVRCDLIADGIIGAVAEVG 340
Cdd:pfam00549   1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 16128703   341 VNVPVV-VRLEGNNAEL-----GAKKLADSGLNIIAAKGLTDAAQQVV 382
Cdd:pfam00549  81 ARELPVvARVCGTEADPqgrsgQAKALAESGVLIASSNNQALRAAGAV 128
PLN02235 PLN02235
ATP citrate (pro-S)-lyase
 3-338 1.39e-06

ATP citrate (pro-S)-lyase


Pssm-ID: 177879 [Multi-domain]  Cd Length: 423  Bit Score: 50.15  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    3 LHEYQAKQLFARY-----GLPAPVGYACTTprEAEEAASKIGAGPW------VVKCQVHAGGRGKAGGVKVVNSKEDIRA 71
Cdd:PLN02235   6 IREYDSKRLLKEHlkrlaGIDLPIRSAQVT--ESTDFNELANKEPWlsstklVVKPDMLFGKRGKSGLVALNLDLAQVAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703   72 FAENWLGKrlvTYQTDANGQPVNQILVEAATDIAKELYLGAVVDRSSRRVVFmaSTEGGVEIEK-------VAEETPHLI 144
Cdd:PLN02235  84 FVKERLGK---EVEMGGCKGPITTFIVEPFVPHDQEFYLSIVSDRLGCSISF--SECGGIEIEEnwdkvktIFLPTEAPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  145 HKVALDPLTGPMPyqgrelafkLGLEGKLvQQFTKifmGLATIFLERDLALIEINPLVITkQGDLICLDGKLGADGNALF 224
Cdd:PLN02235 159 TSEICAPLIATLP---------LEIRGKI-EEFIK---GVFAVFQDLDFTFLEMNPFTLV-DGEPYPLDMRGELDDTAAF 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703  225 RQ-----------PDLREMR--DQSQEDPREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHG--GEPANFLDV 289
Cdd:PLN02235 225 KNfkkwgniefplPFGRVMSptESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGyaSELGNYAEY 304

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703  290 GGGATKERVTEAFKIILS------DDKVKAVLvnIFGGIVR-CDLIA--DGIIGAVAE 338
Cdd:PLN02235 305 SGAPNEEEVLQYARVVIDcatanpDGRKRALL--IGGGIANfTDVAAtfNGIIRALRE 360
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 6-74 4.35e-06

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: 47.56  E-value: 4.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128703   6 YQAKQLFARYGLPAPVGYACTTPREAEEAASKIGaGPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAE 74
Cdd:COG0439  56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIG-YPVVVKPADGAGSR----GVRVVRDEEELEAALA 119
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 8-74 1.07e-03

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 40.77  E-value: 1.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128703   8 AKQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAE 74
Cdd:COG0151 106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGA-PIVVKADGLAAGK----GVVVAETLEEALAAVD 167
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 9-99 1.50e-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: 40.75  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703      9 KQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGvkVVNSKEDIRAFAENWLgkrlvtyqtda 88
Cdd:TIGR01369  132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGY-PVIVRPAFTLGGTG--GG--IAYNREELKEIAERAL----------- 195

                           90
                   ....*....|.
gi 16128703     89 NGQPVNQILVE 99
Cdd:TIGR01369  196 SASPINQVLVE 206
GARS_A pfam01071
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ...
 8-99 1.66e-03

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: 39.19  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     8 AKQLFARYGLPAPVGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRgkagGVKVVNSKEDIRAFAENWLgkrlvtyQTD 87
Cdd:pfam01071   6 AKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK----GVIVASSNEEAIKAVDEIL-------EQK 74

                          90
                  ....*....|..
gi 16128703    88 ANGQPVNQILVE 99
Cdd:pfam01071  75 KFGEAGETVVIE 86
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 9-74 2.93e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 39.75  E-value: 2.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128703    9 KQLFARYGLPAPVGYACTTPREAEEAASKIGaGPWVVKCQvhAGGRGKagGVKV-VNSKEDIR-AFAE 74
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIG-YPVVVKPL--DGNHGR--GVTVnITTREEIEaAYAV 281
RTC pfam01137
RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are ...
 29-145 3.51e-03

RNA 3'-terminal phosphate cyclase; RNA cyclases are a family of RNA-modifying enzymes that are conserved in all cellular organizms. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. The structure of RTC demonstrates that RTCs are comprised two domain. The larger domain contains an insert domain of approximately 100 amino acids.


Pssm-ID: 460079 [Multi-domain]  Cd Length: 324  Bit Score: 39.03  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703    29 REAEEAAS-KIGAGPWVVKCQVHA-----GGRGKAGGVKVVNSKEDIRAFAENwLGKRlvtyqtdanGQPVNQILVEAAT 102
Cdd:pfam01137 196 RMVAAAAGlLLRFLPDVYIITDVEkgeesGKGGGGGIVLVAETTEGCILGASA-LGER---------GKPAEDVGEEAAE 265

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 16128703   103 DIAKELYLGAVVDRSSRR--VVFMASTEGGVEIeKVAEETPHLIH 145
Cdd:pfam01137 266 ELLEELESGGCVDEHLQDqlILFMALAGGESVF-RTGPLTLHTIT 309
carB PRK05294
carbamoyl-phosphate synthase large subunit;
9-99 5.71e-03

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 38.92  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128703     9 KQLFARYGLPAPVGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGvkVVNSKEDIRAFAENWLgkrlvtyqtDA 88
Cdd:PRK05294  133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGY-PVIIRPSFTLGGTG--GG--IAYNEEELEEIVERGL---------DL 198

                          90
                  ....*....|.
gi 16128703    89 NgqPVNQILVE 99
Cdd:PRK05294  199 S--PVTEVLIE 207
 
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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