|
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: 702.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:COG0045 1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:COG0045 81 LVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGAK 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: 697.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:PRK00696 1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:PRK00696 81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGAK 388
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKGK 388
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
1-385 |
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: 625.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:TIGR01016 1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:TIGR01016 81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAV 385
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAA 385
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
2-203 |
3.73e-110 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 321.13 E-value: 3.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 2 NLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKKL 81
Cdd:pfam08442 1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 82 VTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQGR 161
Cdd:pfam08442 81 VTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 189030227 162 ELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVI 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: 702.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:COG0045 1 MNLHEYQAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRGKAGGVKLAKSPEEAREAAEEILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:COG0045 81 LVTHQTGPKGKPVNKVLVEEGVDIAKELYLSILLDRATRRPVIMASTEGGMDIEEVAEETPEKIIKVPIDPLVGLQPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:COG0045 161 RELAFALGLPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTKDGRLVALDAKVNFDDNALFRHPELAALRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:COG0045 241 LEVEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLAGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGAK 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: 697.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:PRK00696 1 MNLHEYQAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRGKAGGVKLAKSPEEAREFAKQILGMT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:PRK00696 81 LVTHQTGPKGQPVNKVLVEEGADIAKEYYLSIVLDRATRRVVFMASTEGGMDIEEVAEETPEKIHKVAIDPLTGLQPFQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:PRK00696 161 REIAFKLGLPGEQVKQFAKILMGLYKAFVEKDASLVEINPLVVTKDGDLIALDAKINFDDNALFRHPDLAELRDLSEEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:PRK00696 241 LEAEASKYGLNYVKLDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGATAERVAEAFKIILSDPNVKAILVNIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGAK 388
Cdd:PRK00696 321 GITRCDVIAEGIIAAVKEVGVTVPLVVRLEGTNVELGKKILAESGLNIIAADTLDDAAQKAVEAAKGK 388
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
1-385 |
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: 625.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:TIGR01016 1 MNLHEYQAKQIFAKYGIPVPRGYVATSVEEAEEIAAKLGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:TIGR01016 81 LVTNQTDPLGQPVNKILIEEATDIDKEYYLSIVIDRSARCPVIMASTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:TIGR01016 161 REIAKKLGLEGELVKQVADIIKKLYQIFLEYDASLVEINPLVITKDGNLIALDAKLTIDDNALFRHPDLEEMRDYSQEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:TIGR01016 241 REVLAKQWGLNYVALDGNIGCMVNGAGLAMATMDIIKLYGGEPANFLDVGGGASAERVREALKLVLSDKSVKVVFINIFG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAV 385
Cdd:TIGR01016 321 GITRCDLVAKGLVEALKEVGVNVPVVVRLEGTNVEEGKKILAESGLNIIFATSMEEAAEKAVEAA 385
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
1-387 |
4.02e-176 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 495.77 E-value: 4.02e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKK 80
Cdd:PRK14046 1 MDIHEYQAKELLASFGVAVPRGALAYSPEQAVYRARELGGWHWVVKAQIHSGARGKAGGIKLCRTYNEVRDAAEDLLGKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 81 LVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQG 160
Cdd:PRK14046 81 LVTHQTGPEGKPVQRVYVETADPIERELYLGFVLDRKSERVRVIASARGGMEIEEIAAKEPEAIIQVVVEPAVGLQQFQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 161 RELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELREMRDKSQEDE 240
Cdd:PRK14046 161 REIAFGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDDRVLALDAKMSFDDNALFRRPNIAEMRDPSQEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 241 REAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKVKAVFVNIFG 320
Cdd:PRK14046 241 REAQAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGGEPANFLDVGGGASPERVAKAFRLVLSDRNVKAILVNIFA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189030227 321 GIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGA 387
Cdd:PRK14046 321 GINRCDWVAEGVVQAAREVGIDVPLVVRLAGTNVEEGRKILAESGLPIITADTLAEAAEKAVEAWKG 387
|
|
| PLN00124 |
PLN00124 |
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional |
1-387 |
1.96e-133 |
|
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
Pssm-ID: 177736 [Multi-domain] Cd Length: 422 Bit Score: 388.34 E-value: 1.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 1 MNLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKI--GAGPWVVKCQVHAGGRGKA-------GGVKLVnSKEDIRA 71
Cdd:PLN00124 28 LNIHEYQGAELMSKYGVNVPKGAAASSLDEVKKALEKMfpDEGEVVVKSQILAGGRGLGtfknglkGGVHIV-KKDKAEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 72 FAEQWLGKKLVTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDP 151
Cdd:PLN00124 107 LAGKMLGQILVTKQTGPAGKPVNKVYLCEKMSLVNEMYFAILLDRASAGPLIIACSKGGTSIEDLAEKFPEKIIKVPIDI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 152 LTGPQPYQGRELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVITKQGDLVCLDGKLGADGNALFRQPELRE 231
Cdd:PLN00124 187 FKGITDEDAAKVVDGLAPKVADRNDAIEQVKKLYKLFCKCDCTMVEINPLAETADGQLVAADAKLNFDDNAAFRQKEIFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 232 MRDKSQEDEREAQAAQWELNYVALDGNIGCMVNGAGLAMGTMDIVKLHGGEPANFLDVGGGATKERVTEAFKIILSDDKV 311
Cdd:PLN00124 267 LRDTSQEDPREVAAAKADLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSPANFLDVGGNASEQQVVEAFKILTSDDKV 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189030227 312 KAVFVNIFGGIVRCDLIADGIIGAVEEVGVNVPVVVRLEGNNAELGAKKLADSGLNIIAATSLTDAAQQVVAAVGA 387
Cdd:PLN00124 347 KAILVNIFGGIMKCDVIASGIVNAAKQVGLKVPLVVRLEGTNVDQGKRILKESGMTLITAEDLDDAAEKAVKALAI 422
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
2-203 |
3.73e-110 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 321.13 E-value: 3.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 2 NLHEYQAKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRGKAGGVKLVNSKEDIRAFAEQWLGKKL 81
Cdd:pfam08442 1 NLHEYQAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 82 VTYQTDVHGQPVHQILVEAATDIDKELYLGAVIDRSSRRVVFMASTEGGVEIEKVAEETPELIHKVALDPLTGPQPYQGR 161
Cdd:pfam08442 81 VTKQTGPDGQPVNKVLVEEALDIKKEYYLSIVLDRASKGPVIIASTEGGVDIEEVAAKNPEKIHKFPIDPLKGLTPYQAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 189030227 162 ELAFKLGLTGKQVAQFTKIFMGLATLFLERDLAMVEINPLVI 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 |
7.45e-27 |
|
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: 103.49 E-value: 7.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 262 MVNGAGLAMGTMDIVKLHGGEPANFLDVGGGA-TKERVTEAFKIILSDDKVKAVFVNIFGGIVRCDLIADGIIGAVEEVG 340
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAfTPTTRIDALKLEAADPEVKVILLDIVLGYGACEDPAGGLLKAIKEAR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 189030227 341 VNVPVV-VRLEGNNAEL-----GAKKLADSGLNIIAATSLTDAAQQVV 382
Cdd:pfam00549 81 ARELPVvARVCGTEADPqgrsgQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
6-99 |
1.39e-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: 46.02 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 6 YQAKQLFARYGMPAPTGYACTTPREAEEAASKIGaGPWVVKCQVHAGGRgkagGVKLVNSKEDIRAFAEQwlgkklvTYQ 85
Cdd:COG0439 56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIG-YPVVVKPADGAGSR----GVRVVRDEEELEAALAE-------ARA 123
|
90
....*....|....
gi 189030227 86 TDVHGQPVHQILVE 99
Cdd:COG0439 124 EAKAGSPNGEVLVE 137
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
3-225 |
1.77e-05 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 46.69 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 3 LHEYQAKQLFARY-----GMPAPTGYACTTprEAEEAASKIGAGPW------VVKCQVHAGGRGKAGGVKLVNSKEDIRA 71
Cdd:PLN02235 6 IREYDSKRLLKEHlkrlaGIDLPIRSAQVT--ESTDFNELANKEPWlsstklVVKPDMLFGKRGKSGLVALNLDLAQVAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 72 FAEQWLGKklvtyQTDVHG--QPVHQILVEAATDIDKELYLGAVIDRSSRRVVFmaSTEGGVEIEK-------VAEETPE 142
Cdd:PLN02235 84 FVKERLGK-----EVEMGGckGPITTFIVEPFVPHDQEFYLSIVSDRLGCSISF--SECGGIEIEEnwdkvktIFLPTEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 143 LIHKVALDPLTGPQPyqgrelafkLGLTGKqVAQFTKifmGLATLFLERDLAMVEINPLVITkQGDLVCLDGKLGADGNA 222
Cdd:PLN02235 157 PLTSEICAPLIATLP---------LEIRGK-IEEFIK---GVFAVFQDLDFTFLEMNPFTLV-DGEPYPLDMRGELDDTA 222
|
...
gi 189030227 223 LFR 225
Cdd:PLN02235 223 AFK 225
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
9-99 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 9 KQLFARYGMPAPTGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGVklVNSKEDIRAFAEQWLGKklvtyqtdv 88
Cdd:TIGR01369 132 REAMKEIGEPVPESEIAHSVEEALAAAKEIGY-PVIVRPAFTLGGTG--GGI--AYNREELKEIAERALSA--------- 197
|
90
....*....|.
gi 189030227 89 hgQPVHQILVE 99
Cdd:TIGR01369 198 --SPINQVLVE 206
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
8-99 |
3.50e-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: 38.42 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 8 AKQLFARYGMPAPTGYACTTPREAEEAASKIGAGPWVVKCQVHAGGRgkagGVKLVNSKEDIRAFAEQWLGKKlvtyqtd 87
Cdd:pfam01071 6 AKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGK----GVIVASSNEEAIKAVDEILEQK------- 74
|
90
....*....|..
gi 189030227 88 VHGQPVHQILVE 99
Cdd:pfam01071 75 KFGEAGETVVIE 86
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
8-74 |
4.58e-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: 38.84 E-value: 4.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189030227 8 AKQLFARYGMPAPTGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRgkagGVKLVNSKEDIRAFAE 74
Cdd:COG0151 106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGA-PIVVKADGLAAGK----GVVVAETLEEALAAVD 167
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
9-74 |
4.89e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 38.98 E-value: 4.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189030227 9 KQLFARYGMPAPTGYACTTPREAEEAASKIGaGPWVVKCQvhAGGRGKagGVKL-VNSKEDIR-AFAE 74
Cdd:PRK14016 219 KRLLAAAGVPVPEGRVVTSAEDAWEAAEEIG-YPVVVKPL--DGNHGR--GVTVnITTREEIEaAYAV 281
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
9-99 |
7.08e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 38.54 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189030227 9 KQLFARYGMPAPTGYACTTPREAEEAASKIGAgPWVVKCQVHAGGRGkaGGVklVNSKEDIRAFAEQWLgkklvtyqtdv 88
Cdd:PRK05294 133 KEAMKKIGLPVPRSGIAHSMEEALEVAEEIGY-PVIIRPSFTLGGTG--GGI--AYNEEELEEIVERGL----------- 196
|
90
....*....|.
gi 189030227 89 HGQPVHQILVE 99
Cdd:PRK05294 197 DLSPVTEVLIE 207
|
|
|