|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
1-608 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 1293.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 1 MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHAAIEAACAAHPTAD 80
Cdd:PLN02522 1 MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 81 VFINFASFRSAAASSMAALKQPTIKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTIDNII 160
Cdd:PLN02522 81 VFINFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 161 QCKLYRPGSVGFVSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSL 240
Cdd:PLN02522 161 QCKLYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 241 VEALKEGKVNKPVVAWVSGTCARLFKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFEKLVEE 320
Cdd:PLN02522 241 VEALKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 321 GKVSPIKEVIPPQIPEDLNSAIKSGKVRAPTHIISTISDDRGEEPCYAGVPMSSIIEQGYGVGDVISLLWFKRSLPRYCT 400
Cdd:PLN02522 321 GKIIPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 401 KFIEICIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKKKG 480
Cdd:PLN02522 401 KFIEMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 481 IRVPGIGHRIKSRDNRDKRVELLQKFARSNFPSVKYMEYAVTVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQE 560
Cdd:PLN02522 481 IRVPGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQE 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15239897 561 IDEIVQIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK 608
Cdd:PLN02522 561 IDEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK 608
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
369-606 |
4.43e-90 |
|
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 277.91 E-value: 4.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 369 GVPMSSIIEQgYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSGAHNTIVTARAG-KDLVSSLVSGLLTIGPR 447
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 448 FGGAIDDAARYFKDACDRN----LTPYEFVEGMKKKGIRVPGIGHRIKSrdNRDKRVELLQKFARSNFPSVKYMEYAVTV 523
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 524 ETYTLSKAN-NLVLNVDGAIGSLFLDLlagsGMFTkqeideivqiGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWE 602
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 15239897 603 DVLY 606
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
104-312 |
3.66e-43 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 156.37 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 104 IKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGdtagtidnIIQCKLYRPGSVGFVSKSGGMSNEM 183
Cdd:COG0074 89 IKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 184 YNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEgKVNKPVVAWVSGTCAr 263
Cdd:COG0074 161 VWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKE-NMTKPVVAYIAGRTA- 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15239897 264 lfKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKE 312
Cdd:COG0074 239 --PPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKK 285
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
173-298 |
7.89e-18 |
|
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: 80.00 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 173 VSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELG-GRDEY---SLVEALKEGK 248
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDpagGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15239897 249 VNK-PVVAWVSGTCARLFKsevQFGHAGAKSGGEMESAQAKNQALIDAGAI 298
Cdd:pfam00549 81 ARElPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
1-608 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 1293.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 1 MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHAAIEAACAAHPTAD 80
Cdd:PLN02522 1 MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 81 VFINFASFRSAAASSMAALKQPTIKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTIDNII 160
Cdd:PLN02522 81 VFINFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 161 QCKLYRPGSVGFVSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSL 240
Cdd:PLN02522 161 QCKLYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 241 VEALKEGKVNKPVVAWVSGTCARLFKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFEKLVEE 320
Cdd:PLN02522 241 VEALKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 321 GKVSPIKEVIPPQIPEDLNSAIKSGKVRAPTHIISTISDDRGEEPCYAGVPMSSIIEQGYGVGDVISLLWFKRSLPRYCT 400
Cdd:PLN02522 321 GKIIPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 401 KFIEICIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKKKG 480
Cdd:PLN02522 401 KFIEMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 481 IRVPGIGHRIKSRDNRDKRVELLQKFARSNFPSVKYMEYAVTVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQE 560
Cdd:PLN02522 481 IRVPGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQE 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15239897 561 IDEIVQIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK 608
Cdd:PLN02522 561 IDEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK 608
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
369-606 |
4.43e-90 |
|
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CCL cleaves citryl-CoA (CiCoA) to acetyl-CoA (AcCoA) and oxaloacetate (OAA). ACL catalyzes an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. ACL may be required for fruiting body maturation in the filamentous fungus Sordaria macrospore. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL; the first enzyme is citryl-CoA synthetase (CCS) which is not included in this group. Chlorobium limicola ACL is an example of a two-subunit type ACL. It is comprised of a large and a small subunit; it has been speculated that the large subunit arose from a fusion of the small subunit of the two subunit CCS with CCL. The small ACL subunit is a homolog of the larger CCS subunit. Mammalian ACL is of the single-subunit type and may have arisen from the two-subunit ACL by another gene fusion. Mammalian ACLs are homotetramers; the ACLs of C. limicola and Arabidopsis are a heterooctomers (alpha4beta4). In cancer cells there is a shift in energy metabolism to aerobic glycolysis, the glycolytic end product pyruvate enters a truncated TCA cycle generating citrate which is cleaved in the cytosol by ACL. Inhibiting ACL limits the in-vitro proliferation and survival of these cancer cells, reduces in vivo tumor growth, and induces differentiation.
Pssm-ID: 99854 [Multi-domain] Cd Length: 227 Bit Score: 277.91 E-value: 4.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 369 GVPMSSIIEQgYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSGAHNTIVTARAG-KDLVSSLVSGLLTIGPR 447
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 448 FGGAIDDAARYFKDACDRN----LTPYEFVEGMKKKGIRVPGIGHRIKSrdNRDKRVELLQKFARSNFPSVKYMEYAVTV 523
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 524 ETYTLSKAN-NLVLNVDGAIGSLFLDLlagsGMFTkqeideivqiGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWE 602
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 15239897 603 DVLY 606
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
104-312 |
3.66e-43 |
|
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439844 [Multi-domain] Cd Length: 288 Bit Score: 156.37 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 104 IKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGdtagtidnIIQCKLYRPGSVGFVSKSGGMSNEM 183
Cdd:COG0074 89 IKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 184 YNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEgKVNKPVVAWVSGTCAr 263
Cdd:COG0074 161 VWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIKE-NMTKPVVAYIAGRTA- 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15239897 264 lfKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKE 312
Cdd:COG0074 239 --PPGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAESPSEIGELLKK 285
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
104-318 |
1.64e-30 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 121.75 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 104 IKVVAIIAEGVPESDTKQLIAYARANNKV-VIGPATVGGIQAGAFKIGDTAGTIdniiqcklYRPGSVGFVSKSGGMSNE 182
Cdd:PTZ00187 113 IPLVVCITEGIPQHDMVKVKHALLSQNKTrLIGPNCPGIIKPGECKIGIMPGHI--------HKKGKIGIVSRSGTLTYE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 183 MYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEGKVNKPVVAWVSGTCA 262
Cdd:PTZ00187 185 AVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITA 264
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15239897 263 rlfKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFEKLV 318
Cdd:PTZ00187 265 ---PPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVVKSPAQLGKTMLEVMKKKG 317
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
104-299 |
9.87e-29 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 116.04 E-value: 9.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 104 IKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTIdniiqcklYRPGSVGFVSKSGGMSNEM 183
Cdd:PRK05678 90 IDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGIITPGECKIGIMPGHI--------HKKGRVGVVSRSGTLTYEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 184 yntVARVTD---GIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEgKVNKPVVAWVSGT 260
Cdd:PRK05678 162 ---VAQLTDlgfGQSTCVGIGGDPINGTNFIDVLEAFEEDPETEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGV 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 15239897 261 CARLFKsevQFGHAGAKSGGEMESAQAKNQALIDAGAIV 299
Cdd:PRK05678 238 TAPPGK---RMGHAGAIISGGKGTAEEKKEALEAAGVKV 273
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
104-315 |
1.22e-24 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 104.66 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 104 IKVVAIIAEGVPESDTKQLIAYARANNKV-VIGPATVGGIQAGAFKIGDTAGTIdniiqcklYRPGSVGFVSKSGGMSNE 182
Cdd:PLN00125 94 LDLVVCITEGIPQHDMVRVKAALNRQSKTrLIGPNCPGIIKPGECKIGIMPGYI--------HKPGRIGIVSRSGTLTYE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 183 MYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEGKVNKPVVAWVSGTCA 262
Cdd:PLN00125 166 AVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15239897 263 RLFKsevQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFE 315
Cdd:PLN00125 246 PPGR---RMGHAGAIVSGGKGTAQDKIKALREAGVTVVESPAKIGVAMLEVFK 295
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
349-591 |
2.30e-22 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 96.86 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 349 APTHIISTISDDRGEEPCYAGVPMSSIIEQgYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSgahntIVTAR 428
Cdd:PRK06224 5 KTKWWRTSISDVTPEEIYVRGYDLEDLIGK-LSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPS-----AAAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 429 ----AGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDA---CDRNLTPYE----FVEGMKKKGIRVPGIGHRIksRDNRD 497
Cdd:PRK06224 79 mtasGGESLQGAVAAGLLALGSVHGGAGEQAAELLQEIaaaADAGADLDAaaraIVAEYRAAGKRVPGFGHPL--HKPVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 498 KRVELLQKFARSNFPSVKYMEYAVTVETYTLSKANN-LVLNVDGAIGSLFLDLlagsgmftkqeideivqiGY----LNG 572
Cdd:PRK06224 157 PRAPRLLALAREAGVAGRHCRLAEALEAALAAAKGKpLPLNVDGAIAAILADL------------------GFppalARG 218
|
250
....*....|....*....
gi 15239897 573 LFVLARSIGLIGHTFDQKR 591
Cdd:PRK06224 219 LFVISRAAGLVAHVWEELQ 237
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
400-598 |
4.30e-18 |
|
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase (ACL) and the C-terminal portion of the large subunit of the two-subunit type ACL. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) from citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. Some CS proteins function as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. CCL cleaves citryl-CoA (CiCoA) to AcCoA and OAA. ACLs catalyze an ATP- and a CoA- dependant cleavage of citrate to form AcCoA and OAA; they do this in a multistep reaction, the final step of which is likely to involve the cleavage of CiCoA to generate AcCoA and OAA. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate CiCoA, and c) the hydrolysis of CiCoA to produce citrate and CoA. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. In fungi, yeast, plants, and animals ACL is cytosolic and generates AcCoA for lipogenesis. In several groups of autotrophic prokaryotes and archaea, ACL carries out the citrate-cleavage reaction of the reductive tricarboxylic acid (rTCA) cycle. In the family Aquificaceae this latter reaction in the rTCA cycle is carried out via a two enzyme system the second enzyme of which is CCL.
Pssm-ID: 99853 [Multi-domain] Cd Length: 213 Bit Score: 83.16 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 400 TKFIEICIMLCADHGPCVSgAHNTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDA---CDRNLTPYeFVEG 475
Cdd:cd06099 20 ARAMDLALILHADHEGNAS-TFTARVVGSTGSDPYSAIAAAIGALkGPLHGGANEAVLKMLEEIgtpKNEPAEAY-IRKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 476 MKKKGiRVPGIGHRIKSrdNRDKRVELLQKFARSNFPSVK-------YMEYAVTVETYTLSKanNLVLNVDGAIGSLFLD 548
Cdd:cd06099 98 LESKR-VIMGFGHRVYK--KYDPRATVLKKFAEELLKEDGddpmfelAAELEKIAEEVLYEK--KLYPNVDFYSGVLYKA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15239897 549 LLAGSGMFTkqeideivqigylnGLFVLARSIGLIGHTFDQKRLKQPLYR 598
Cdd:cd06099 173 MGFPTELFT--------------PLFAVARAVGWLAHLIEQLEDNFKIIR 208
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
173-298 |
7.89e-18 |
|
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: 80.00 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 173 VSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELG-GRDEY---SLVEALKEGK 248
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDpagGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15239897 249 VNK-PVVAWVSGTCARLFKsevQFGHAGAKSGGEMESAQAKNQALIDAGAI 298
Cdd:pfam00549 81 ARElPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
389-585 |
1.63e-16 |
|
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
Pssm-ID: 459747 [Multi-domain] Cd Length: 357 Bit Score: 81.40 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 389 LWFKRSLPRYCTKFIEICIMLCADHGPCVSgAHNTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDACDRNl 467
Cdd:pfam00285 156 MLFGYEPDPEEARALDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPD- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 468 TPYEFVEGMKKKGI-RVPGIGHRI-KsrdNRDKRVELLQKFAR---SNFPSVKYMEYAVTVETYTLS----KANNLVLNV 538
Cdd:pfam00285 234 EVEEYIRKVLNKGKeRIMGFGHRVyK---NYDPRAKILKEFAEelaEEGGDDPLLELAEELEEVAPEdlyfVEKNLYPNV 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15239897 539 DGAIGSLFLDLlaG--SGMFTkqeideivqigylnGLFVLARSIGLIGH 585
Cdd:pfam00285 311 DFYSGVLYHAL--GipTDMFT--------------PLFAISRTAGWLAH 343
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
404-598 |
1.72e-10 |
|
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440141 [Multi-domain] Cd Length: 387 Bit Score: 63.19 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 404 EICIMLCADHGPCVSgAHNTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDACDRNLTPyEFVEGMKKKGIR 482
Cdd:COG0372 185 DLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDNVE-EYIRKALDKKER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 483 VPGIGHRI-KsrdNRDKRVELLQKFARSNFPSV---KYMEYAVTVETYTLS----KANNLVLNVD---GAIgslfLDLLa 551
Cdd:COG0372 263 IMGFGHRVyK---NYDPRAKILKEAAEELLEELgddPLLEIAEELEEVALEdeyfIEKKLYPNVDfysGIV----YHAL- 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15239897 552 gsG----MFTkqeideivqigylnGLFVLARSIGLIGHTFDQkRLKQPLYR 598
Cdd:COG0372 335 --GiptdMFT--------------PIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
396-585 |
6.81e-10 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 61.58 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 396 PRyCTKFIEICIMLCADH-GPCVSgAHNTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDACDRNLTPyEFV 473
Cdd:PLN02456 242 PR-LARLLDLYFIIHADHeGGCST-AAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEIGTVENIP-EYV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 474 EGMKKKGIRVPGIGHRIKSrdNRDKRVELLQKFARSNFpsvKYM------EYAVTVETYTLS----KANNLVLNVDGAIG 543
Cdd:PLN02456 319 EGVKNSKKVLPGFGHRVYK--NYDPRAKCIREFALEVF---KHVgddplfKVASALEEVALLdeyfKVRKLYPNVDFYSG 393
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15239897 544 SLFLDLLAGSGMFTKqeideivqigylngLFVLARSIGLIGH 585
Cdd:PLN02456 394 VLLRALGFPEEFFTV--------------LFAVSRAAGYLSQ 421
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
401-600 |
8.79e-05 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 45.12 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 401 KFIEICIMLCADHG-PCVSGAhnTIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKK 478
Cdd:PRK14037 171 KAMDAALILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIIN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 479 KGIRVPGIGHRI-KSRDNRDKRV-ELLQKFARSNFPSVKYMEYAVTVETYTLSK--ANNLVLNVDGAIGSLFLDLLAGSG 554
Cdd:PRK14037 249 GKKRLMGFGHRVyKTYDPRAKIFkELAETLIERNSEAKKYFEIAQKLEELGIKQfgSKGIYPNTDFYSGIVFYALGFPVY 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15239897 555 MFTkqeideivqigylnGLFVLARSIGLIGHTF----DQKRLKQP--LYRHP 600
Cdd:PRK14037 329 MFT--------------ALFALSRTLGWLAHIIeyveEQHRLIRPraLYVGP 366
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
401-509 |
5.16e-03 |
|
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the oxidative citric acid cycle (TCA or Krebs cycle). Peroxisomal CS is involved in the glyoxylate cycle. This group also includes CS proteins which functions as a 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-CoA (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) a carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) hydrolysis of citryl-CoA to produce citrate and CoA. CSs are found in two structural types: type I (homodimeric) and type II CSs (homohexameric). Type II CSs are unique to gram-negative bacteria. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria. Type I CS is active as a homodimer, both subunits participating in the active site. Type II CS is a hexamer of identical subunits (approximated as a trimer of dimers). Some type II CSs are strongly and specifically inhibited by NADH through an allosteric mechanism. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99866 Cd Length: 406 Bit Score: 39.56 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 401 KFIEICIMLCADHGpcvsGAHN----TIVTARAGKDLVSSLVSGLLTI-GPRFGGAIDDAARYF-------KDACDRNLT 468
Cdd:cd06113 196 KLLDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLedikenvKDWTDEDEV 271
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15239897 469 PyEFVEGM------KKKGIrVPGIGHRIKSRDnrDKRVELLQKFARS 509
Cdd:cd06113 272 R-AYLRKIlnkeafDKSGL-IYGMGHAVYTLS--DPRAVVLKKYARS 314
|
|
| Succ_CoA_lig |
pfam13607 |
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ... |
167-306 |
6.90e-03 |
|
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer.
Pssm-ID: 433345 [Multi-domain] Cd Length: 138 Bit Score: 37.06 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239897 167 PGSVGFVSKSGGMSNEMYNTVARVTDGIYEGIAIGG--DVfpgsTLSDHILRFNNIPQIKmmVVLGELGG-RDEYSLVEA 243
Cdd:pfam13607 1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNeaDV----DFADLLEYLADDPETR--VILLYLEGiRDGRRFLRA 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239897 244 LKEGKVNKPVVAWVSGtcarlfKSEvqfghAGAKSGGEMESAQAKNQALIDA-----GAIVPTSFEAL 306
Cdd:pfam13607 75 ARRAARRKPVVVLKAG------RSE-----AGARAAASHTGALAGSDAVYDAafrqaGVIRVDDLEEL 131
|
|
| |
