|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
503-1106 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 924.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 503 KFFSNTTKAIVWGMQQRAVQSMLDFDFICRRDEPSVVAMVYPfTGDHKQKYYWGHKEILIPVYKKMSDAIHKHKEVDVMV 582
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 583 NFASMRSAYESTLEVLEFPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGPATVGGVKPGCFKIGNTGGMLDNILHSK 662
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 663 LYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPETKLIVLLGEVGGTEEYDVCAA 742
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 743 LKDGRITKPLVAWCIGTCASMFTSEVQFGHAGSCANSDRETATAKNKGLRDAGAYVPDSFDTLGELIHHVYGELVKTGRV 822
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 823 VPKEEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPISEVLSKDVGIGGVISLLWFQRCLPSYVCKFF 902
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 903 EMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSVVSGLLTIGDRFGGALDGSARQFSEAYDTNLHPMEFVNKMRKEGKLI 982
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 983 LGIGHRVKSINNPDVRVKIIKEFVLENFPACPLLKYALEVEKITTNKKPNLILNVDGVIATAFVDMLRNSGSFTSEEAQE 1062
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 281363475 1063 YINVGAINSLFVLGRSIGFIGHYMDQKRLKQGLYRHPWDDISYV 1106
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-421 |
5.07e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 413.01 E-value: 5.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1 MSAKAITEASGKDILNRHLNTHGAGAATCRFSTVNSTTDWSKLAVDHPWLLTTPLVCKPDQLIKRRGKLGLIGVKKNFEQ 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 81 VKQWIGERLNKDQKIGNAVGKLRNFIIEPFVPHTdaEEMYVCIYSHRAADTILFYHQGGVDIGDVDAKAVKLDVPVNSSL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHD--QEFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 161 S---LADVKSKLLKEVKDAgtkerIAKFVSALYTTYVDLYFTYLEINPLVVTADNLYILDLAAKLDSTADFICRPKWGEI 237
Cdd:PLN02235 159 TseiCAPLIATLPLEIRGK-----IEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 238 DYPPPFGRDAYPEEAYIADLDAKSGASLKLTILNRNGRIWTMVAGGGASVIYSDTICDLGGASELANYGEYSGAPSEQQT 317
Cdd:PLN02235 234 EFPLPFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 318 YEYAKTILNLMTSspkHPDGK--VLITGGGIANFTNVAATFQGIITALREFQPKLVEHNVSIFVRRAGPNYQEGLRKMRD 395
Cdd:PLN02235 314 LQYARVVIDCATA---NPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRA 390
|
410 420
....*....|....*....|....*.
gi 281363475 396 FGSTLGIPLHVFGPETHMTAICGMAL 421
Cdd:PLN02235 391 LGEEIGVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
245-423 |
2.82e-121 |
|
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. This domain has a Rossmann fold.
Pssm-ID: 465025 Cd Length: 178 Bit Score: 369.67 E-value: 2.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 245 RDAYPEEAYIADLDAKSGASLKLTILNRNGRIWTMVAGGGASVIYSDTICDLGGASELANYGEYSGAPSEQQTYEYAKTI 324
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 325 LNLMTSSPkHPDGKVLITGGGIANFTNVAATFQGIITALREFQPKLVEHNVSIFVRRAGPNYQEGLRKMRDFGSTLGIPL 404
Cdd:pfam16114 81 LDLMTREP-HPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPI 159
|
170
....*....|....*....
gi 281363475 405 HVFGPETHMTAICGMALGK 423
Cdd:pfam16114 160 HVYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
868-1105 |
3.73e-88 |
|
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: 283.30 E-value: 3.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 868 GMPISEVLsKDVGIGGVISLLWFQRCLPSYVCKFFEMCLMVTADHGPAVSGAHNTIVCARAG-KDLVSSVVSGLLTIGDR 946
Cdd:cd06100 1 GYDLSDLI-GKISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 947 FGGALDGSARQFSEAYDTN----LHPMEFVNKMRKEGKLILGIGHRVKSinNPDVRVKIIKEFVLENFPACPLLKYALEV 1022
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1023 EKITTNKKP-NLILNVDGVIATAFVDMlrnsgsftseeaqeYINVGAINSLFVLGRSIGFIGHYMDQKRLKQGLYRHPWD 1101
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL--------------GFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 281363475 1102 DISY 1105
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
562-814 |
6.92e-44 |
|
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: 161.00 E-value: 6.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 562 IPVYKKMSDAIHKHkEVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGPATVGGV 641
Cdd:COG0074 50 VPVFDTVAEAVEET-GADASVIFVPPPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 642 KPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPE 721
Cdd:COG0074 128 TPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 722 TKLIVLLGEVGGTEEYDVCAALKDGrITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDAGAYVPDS 801
Cdd:COG0074 200 TEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTAP---PGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAES 275
|
250
....*....|...
gi 281363475 802 FDTLGELIHHVYG 814
Cdd:COG0074 276 PSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
556-809 |
1.43e-34 |
|
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]
Pssm-ID: 130091 [Multi-domain] Cd Length: 286 Bit Score: 134.08 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 556 GHKEILIPVYKKMSDAIHKhKEVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGP 635
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 636 ATVGGVKPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILR 715
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYEAVHQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 716 YQADPETKLIVLLGEVGGTEEYDVCAALKDgRITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDAG 795
Cdd:TIGR01019 193 FEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAP---PGKRMGHAGAIISGGKGTAESKIEALEAAG 268
|
250
....*....|....
gi 281363475 796 AYVPDSFDTLGELI 809
Cdd:TIGR01019 269 VTVVKSPSDIGELL 282
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
672-796 |
8.27e-24 |
|
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: 97.71 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 672 VSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPETKLIVLLGEVG-GTEEY---DVCAALKDGR 747
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDpagGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 281363475 748 -ITKPLVAWCIGTCASMFTsevQFGHAGSCANSDRETATAKNKGLRDAGA 796
Cdd:pfam00549 81 aRELPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGA 127
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
8-397 |
3.48e-22 |
|
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: 100.15 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 8 EASGKDILNRHlnthgaGAATCRFSTVNSTTDWSKLAVDhpwLLTTPLVCKPDQLIKRRGKLGLIGVKKNFEQVKQ---- 83
Cdd:TIGR01016 5 EYQAKQIFAKY------GIPVPRGYVATSVEEAEEIAAK---LGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAaaek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 84 WIGERLNKDQkiGNAVGKLRNFI-IEPFVPhtDAEEMYVCIYSHRAAD--TILFYHQGGVDIGDVDAKAVK--LDVPVNS 158
Cdd:TIGR01016 76 LLGKELVTNQ--TDPLGQPVNKIlIEEATD--IDKEYYLSIVIDRSARcpVIMASTEGGVDIEEVAEKSPEkiIKYAIDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 159 SLSLADVKSK-LLKEVKDAGTK-ERIAKFVSALYTTYVDLYFTYLEINPLVVTAD-NLYILDlaAKLDSTADFICR-PKW 234
Cdd:TIGR01016 152 LTGLLPYQAReIAKKLGLEGELvKQVADIIKKLYQIFLEYDASLVEINPLVITKDgNLIALD--AKLTIDDNALFRhPDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 235 GEI-DYPPPFGRDAYPEE---AYIAdLDaksgaslkltilnrnGRIWTMVAGGGASVIYSDTICDLGGasELANYGEYSG 310
Cdd:TIGR01016 230 EEMrDYSQEDPREVLAKQwglNYVA-LD---------------GNIGCMVNGAGLAMATMDIIKLYGG--EPANFLDVGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 311 APSEQQTYEYAKTILNlmtsspkHPDGKVLITG--GGIANFTNVAatfQGIITALREfqpklVEHNVSIFVRRAGPNYQE 388
Cdd:TIGR01016 292 GASAERVREALKLVLS-------DKSVKVVFINifGGITRCDLVA---KGLVEALKE-----VGVNVPVVVRLEGTNVEE 356
|
....*....
gi 281363475 389 GLRKMRDFG 397
Cdd:TIGR01016 357 GKKILAESG 365
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-397 |
9.11e-16 |
|
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: 80.48 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 66 RGKLGliGVK--KNFEQVKQ----WIGERLNKDQ--KIGNAVGKLrnfIIEPFVPHtdAEEMYVCIYSHRAA--DTILFY 135
Cdd:COG0045 54 RGKAG--GVKlaKSPEEAREaaeeILGMTLVTHQtgPKGKPVNKV---LVEEGVDI--AKELYLSILLDRATrrPVIMAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 136 HQGGVDIGDVDA----KAVKLDVPVNSSLSLADVKsKLLKEVK-DAGTKERIAKFVSALYTTYVDLYFTYLEINPLVVTA 210
Cdd:COG0045 127 TEGGMDIEEVAEetpeKIIKVPIDPLVGLQPYQAR-ELAFALGlPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 211 DN-LYILDlaAK--LDSTADFicR-PKWGEIdypppfgRDAYPE-----EAYIADLdaksgASLKLtilnrNGRIWTMVA 281
Cdd:COG0045 206 DGrLVALD--AKvnFDDNALF--RhPELAAL-------RDLSEEdplevEASKYGL-----NYVKL-----DGNIGCMVN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 282 GGG---ASViysDTICDLGGasELANYGEYSGAPSEQQTYEYAKTILnlmtsspKHPDGK-VLITG-GGIANFTNVAatf 356
Cdd:COG0045 265 GAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIIL-------SDPNVKaILVNIfGGITRCDVVA--- 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 281363475 357 QGIITALREfqpklVEHNVSIFVRRAGPNYQEGLRKMRDFG 397
Cdd:COG0045 330 EGIVAALKE-----VGLKVPVVVRLEGTNVEEGRKILAESG 365
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
503-1106 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 924.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 503 KFFSNTTKAIVWGMQQRAVQSMLDFDFICRRDEPSVVAMVYPfTGDHKQKYYWGHKEILIPVYKKMSDAIHKHKEVDVMV 582
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 583 NFASMRSAYESTLEVLEFPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGPATVGGVKPGCFKIGNTGGMLDNILHSK 662
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 663 LYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPETKLIVLLGEVGGTEEYDVCAA 742
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 743 LKDGRITKPLVAWCIGTCASMFTSEVQFGHAGSCANSDRETATAKNKGLRDAGAYVPDSFDTLGELIHHVYGELVKTGRV 822
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 823 VPKEEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPISEVLSKDVGIGGVISLLWFQRCLPSYVCKFF 902
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 903 EMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSVVSGLLTIGDRFGGALDGSARQFSEAYDTNLHPMEFVNKMRKEGKLI 982
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 983 LGIGHRVKSINNPDVRVKIIKEFVLENFPACPLLKYALEVEKITTNKKPNLILNVDGVIATAFVDMLRNSGSFTSEEAQE 1062
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 281363475 1063 YINVGAINSLFVLGRSIGFIGHYMDQKRLKQGLYRHPWDDISYV 1106
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-421 |
5.07e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 413.01 E-value: 5.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1 MSAKAITEASGKDILNRHLNTHGAGAATCRFSTVNSTTDWSKLAVDHPWLLTTPLVCKPDQLIKRRGKLGLIGVKKNFEQ 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 81 VKQWIGERLNKDQKIGNAVGKLRNFIIEPFVPHTdaEEMYVCIYSHRAADTILFYHQGGVDIGDVDAKAVKLDVPVNSSL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHD--QEFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 161 S---LADVKSKLLKEVKDAgtkerIAKFVSALYTTYVDLYFTYLEINPLVVTADNLYILDLAAKLDSTADFICRPKWGEI 237
Cdd:PLN02235 159 TseiCAPLIATLPLEIRGK-----IEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 238 DYPPPFGRDAYPEEAYIADLDAKSGASLKLTILNRNGRIWTMVAGGGASVIYSDTICDLGGASELANYGEYSGAPSEQQT 317
Cdd:PLN02235 234 EFPLPFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 318 YEYAKTILNLMTSspkHPDGK--VLITGGGIANFTNVAATFQGIITALREFQPKLVEHNVSIFVRRAGPNYQEGLRKMRD 395
Cdd:PLN02235 314 LQYARVVIDCATA---NPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRA 390
|
410 420
....*....|....*....|....*.
gi 281363475 396 FGSTLGIPLHVFGPETHMTAICGMAL 421
Cdd:PLN02235 391 LGEEIGVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
245-423 |
2.82e-121 |
|
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. This domain has a Rossmann fold.
Pssm-ID: 465025 Cd Length: 178 Bit Score: 369.67 E-value: 2.82e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 245 RDAYPEEAYIADLDAKSGASLKLTILNRNGRIWTMVAGGGASVIYSDTICDLGGASELANYGEYSGAPSEQQTYEYAKTI 324
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 325 LNLMTSSPkHPDGKVLITGGGIANFTNVAATFQGIITALREFQPKLVEHNVSIFVRRAGPNYQEGLRKMRDFGSTLGIPL 404
Cdd:pfam16114 81 LDLMTREP-HPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPI 159
|
170
....*....|....*....
gi 281363475 405 HVFGPETHMTAICGMALGK 423
Cdd:pfam16114 160 HVYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
868-1105 |
3.73e-88 |
|
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: 283.30 E-value: 3.73e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 868 GMPISEVLsKDVGIGGVISLLWFQRCLPSYVCKFFEMCLMVTADHGPAVSGAHNTIVCARAG-KDLVSSVVSGLLTIGDR 946
Cdd:cd06100 1 GYDLSDLI-GKISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 947 FGGALDGSARQFSEAYDTN----LHPMEFVNKMRKEGKLILGIGHRVKSinNPDVRVKIIKEFVLENFPACPLLKYALEV 1022
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1023 EKITTNKKP-NLILNVDGVIATAFVDMlrnsgsftseeaqeYINVGAINSLFVLGRSIGFIGHYMDQKRLKQGLYRHPWD 1101
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL--------------GFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 281363475 1102 DISY 1105
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
562-814 |
6.92e-44 |
|
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: 161.00 E-value: 6.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 562 IPVYKKMSDAIHKHkEVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGPATVGGV 641
Cdd:COG0074 50 VPVFDTVAEAVEET-GADASVIFVPPPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPNCPGII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 642 KPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPE 721
Cdd:COG0074 128 TPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELFEEDPE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 722 TKLIVLLGEVGGTEEYDVCAALKDGrITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDAGAYVPDS 801
Cdd:COG0074 200 TEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTAP---PGKRMGHAGAIISGGKGTAESKIEALEAAGVPVAES 275
|
250
....*....|...
gi 281363475 802 FDTLGELIHHVYG 814
Cdd:COG0074 276 PSEIGELLKKALK 288
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
557-813 |
5.99e-35 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 136.00 E-value: 5.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 557 HKEILIPVYKKMSDAIHKHKeVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPE-NMTR-KLIIEADKKgVAIIG 634
Cdd:PTZ00187 69 HLKHGLPVFATVKEAKKATG-ADASVIYVPPPHAASAIIEAIE-AEIPLVVCITEGIPQhDMVKvKHALLSQNK-TRLIG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 635 PATVGGVKPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHIL 714
Cdd:PTZ00187 146 PNCPGIIKPGECKIG--------IMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 715 RYQADPETKLIVLLGEVGGTEEYDVCAALKDGRITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDA 794
Cdd:PTZ00187 218 LFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITAP---PGRRMGHAGAIISGGKGTAPGKIEALEAA 294
|
250
....*....|....*....
gi 281363475 795 GAYVPDSFDTLGELIHHVY 813
Cdd:PTZ00187 295 GVRVVKSPAQLGKTMLEVM 313
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
556-809 |
1.43e-34 |
|
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha subunits but does not discriminate between GTP-specific and ATP-specific reactions. The model is designated as subfamily rather than equivalog for that reason. ATP citrate lyases appear to form an outgroup. [Energy metabolism, TCA cycle]
Pssm-ID: 130091 [Multi-domain] Cd Length: 286 Bit Score: 134.08 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 556 GHKEILIPVYKKMSDAIHKhKEVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGP 635
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 636 ATVGGVKPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILR 715
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYEAVHQLTKAGFGQSTCVGIGGDPVNGTSFIDVLEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 716 YQADPETKLIVLLGEVGGTEEYDVCAALKDgRITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDAG 795
Cdd:TIGR01019 193 FEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAP---PGKRMGHAGAIISGGKGTAESKIEALEAAG 268
|
250
....*....|....
gi 281363475 796 AYVPDSFDTLGELI 809
Cdd:TIGR01019 269 VTVVKSPSDIGELL 282
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
562-816 |
2.59e-30 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 121.82 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 562 IPVYKKMSDAIHKHkEVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPENMTRKLIIEADKKGVAIIGPATVGGV 641
Cdd:PRK05678 51 LPVFNTVAEAVEAT-GANASVIYVPPPFAADAILEAID-AGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGII 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 642 KPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPE 721
Cdd:PRK05678 129 TPGECKIG--------IMPGHIHKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLEAFEEDPE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 722 TKLIVLLGEVGGTEEYDVCAALKDgRITKPLVAWCIGTCA----SMftsevqfGHAGSCANSDRETATAKNKGLRDAGAY 797
Cdd:PRK05678 201 TEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGVTAppgkRM-------GHAGAIISGGKGTAEEKKEALEAAGVK 272
|
250
....*....|....*....
gi 281363475 798 VPDSFDTLGELIHHVYGEL 816
Cdd:PRK05678 273 VARTPSEIGELLKEVLKGL 291
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
556-815 |
1.97e-28 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 116.61 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 556 GHKEILIPVYKKMSDAIHKHKeVDVMVNFASMRSAYESTLEVLEfPQIRTVAIIAEGIPE-NMTRKLIIEADKKGVAIIG 634
Cdd:PLN00125 49 GTEHLGLPVFNTVAEAKAETK-ANASVIYVPPPFAAAAILEAME-AELDLVVCITEGIPQhDMVRVKAALNRQSKTRLIG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 635 PATVGGVKPGCFKIGntggmldnILHSKLYRPGSVAYVSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHIL 714
Cdd:PLN00125 127 PNCPGIIKPGECKIG--------IMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 715 RYQADPETKLIVLLGEVGGTEEYDVCAALKDGRITKPLVAWCIGTCASmftSEVQFGHAGSCANSDRETATAKNKGLRDA 794
Cdd:PLN00125 199 KFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTAP---PGRRMGHAGAIVSGGKGTAQDKIKALREA 275
|
250 260
....*....|....*....|.
gi 281363475 795 GAYVPDSFDTLGELIHHVYGE 815
Cdd:PLN00125 276 GVTVVESPAKIGVAMLEVFKE 296
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
672-796 |
8.27e-24 |
|
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: 97.71 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 672 VSRSGGMSNELNNIISKATDGVIEGIAIGGDRYPGSTFMDHILRYQADPETKLIVLLGEVG-GTEEY---DVCAALKDGR 747
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDpagGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 281363475 748 -ITKPLVAWCIGTCASMFTsevQFGHAGSCANSDRETATAKNKGLRDAGA 796
Cdd:pfam00549 81 aRELPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGA 127
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
8-397 |
3.48e-22 |
|
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: 100.15 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 8 EASGKDILNRHlnthgaGAATCRFSTVNSTTDWSKLAVDhpwLLTTPLVCKPDQLIKRRGKLGLIGVKKNFEQVKQ---- 83
Cdd:TIGR01016 5 EYQAKQIFAKY------GIPVPRGYVATSVEEAEEIAAK---LGAGPVVVKAQVHAGGRGKAGGVKVAKSKEEARAaaek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 84 WIGERLNKDQkiGNAVGKLRNFI-IEPFVPhtDAEEMYVCIYSHRAAD--TILFYHQGGVDIGDVDAKAVK--LDVPVNS 158
Cdd:TIGR01016 76 LLGKELVTNQ--TDPLGQPVNKIlIEEATD--IDKEYYLSIVIDRSARcpVIMASTEGGVDIEEVAEKSPEkiIKYAIDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 159 SLSLADVKSK-LLKEVKDAGTK-ERIAKFVSALYTTYVDLYFTYLEINPLVVTAD-NLYILDlaAKLDSTADFICR-PKW 234
Cdd:TIGR01016 152 LTGLLPYQAReIAKKLGLEGELvKQVADIIKKLYQIFLEYDASLVEINPLVITKDgNLIALD--AKLTIDDNALFRhPDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 235 GEI-DYPPPFGRDAYPEE---AYIAdLDaksgaslkltilnrnGRIWTMVAGGGASVIYSDTICDLGGasELANYGEYSG 310
Cdd:TIGR01016 230 EEMrDYSQEDPREVLAKQwglNYVA-LD---------------GNIGCMVNGAGLAMATMDIIKLYGG--EPANFLDVGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 311 APSEQQTYEYAKTILNlmtsspkHPDGKVLITG--GGIANFTNVAatfQGIITALREfqpklVEHNVSIFVRRAGPNYQE 388
Cdd:TIGR01016 292 GASAERVREALKLVLS-------DKSVKVVFINifGGITRCDLVA---KGLVEALKE-----VGVNVPVVVRLEGTNVEE 356
|
....*....
gi 281363475 389 GLRKMRDFG 397
Cdd:TIGR01016 357 GKKILAESG 365
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
854-1110 |
1.12e-20 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 93.01 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 854 TSICDERGQELIYAGMPISEVLSKdVGIGGVISLLWFQRcLPSYVC-KFFEMCLMVTADHGPAVSgahntIVCAR----A 928
Cdd:PRK06224 11 TSISDVTPEEIYVRGYDLEDLIGK-LSFTDMIFLLLRGR-LPTPNEaRLLDAVLVALVDHGLTPS-----AAAARmtasG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 929 GKDLVSSVVSGLLTIGDRFGGALDGSARQFSEA---YDTNLHPME----FVNKMRKEGKLILGIGHRVKSINNPdvRVKI 1001
Cdd:PRK06224 84 GESLQGAVAAGLLALGSVHGGAGEQAAELLQEIaaaADAGADLDAaaraIVAEYRAAGKRVPGFGHPLHKPVDP--RAPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1002 IKEFVLENFPACPLLKYALEVEK-ITTNKKPNLILNVDGVIATAFVDMlrnsgSFTSEEAQeyinvgainSLFVLGRSIG 1080
Cdd:PRK06224 162 LLALAREAGVAGRHCRLAEALEAaLAAAKGKPLPLNVDGAIAAILADL-----GFPPALAR---------GLFVISRAAG 227
|
250 260 270
....*....|....*....|....*....|..
gi 281363475 1081 FIGHYMDQKRLKQG--LYRHPWDDISYVIPEQ 1110
Cdd:PRK06224 228 LVAHVWEELQQPIGfrIWDPAEEAVEYTGPPP 259
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
900-1090 |
6.10e-17 |
|
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: 83.71 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 900 KFFEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSVVSGLLTI-GDRFGGALDGSARQFSEAYDTNlHPMEFVNKM-RK 977
Cdd:pfam00285 168 RALDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPD-EVEEYIRKVlNK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 978 EGKLILGIGHRV-KsinNPDVRVKIIKEF---VLENFPACPLLKYALEVEKIT----TNKKPNLILNVD---GVIATAF- 1045
Cdd:pfam00285 246 GKERIMGFGHRVyK---NYDPRAKILKEFaeeLAEEGGDDPLLELAEELEEVApedlYFVEKNLYPNVDfysGVLYHALg 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 281363475 1046 --VDMlrnsgsFTSeeaqeyinvgainsLFVLGRSIGFIGHYMDQKR 1090
Cdd:pfam00285 323 ipTDM------FTP--------------LFAISRTAGWLAHWIEQLA 349
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-397 |
9.11e-16 |
|
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: 80.48 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 66 RGKLGliGVK--KNFEQVKQ----WIGERLNKDQ--KIGNAVGKLrnfIIEPFVPHtdAEEMYVCIYSHRAA--DTILFY 135
Cdd:COG0045 54 RGKAG--GVKlaKSPEEAREaaeeILGMTLVTHQtgPKGKPVNKV---LVEEGVDI--AKELYLSILLDRATrrPVIMAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 136 HQGGVDIGDVDA----KAVKLDVPVNSSLSLADVKsKLLKEVK-DAGTKERIAKFVSALYTTYVDLYFTYLEINPLVVTA 210
Cdd:COG0045 127 TEGGMDIEEVAEetpeKIIKVPIDPLVGLQPYQAR-ELAFALGlPGKQVKQFAKILKKLYRAFVEKDASLVEINPLVVTK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 211 DN-LYILDlaAK--LDSTADFicR-PKWGEIdypppfgRDAYPE-----EAYIADLdaksgASLKLtilnrNGRIWTMVA 281
Cdd:COG0045 206 DGrLVALD--AKvnFDDNALF--RhPELAAL-------RDLSEEdplevEASKYGL-----NYVKL-----DGNIGCMVN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 282 GGG---ASViysDTICDLGGasELANYGEYSGAPSEQQTYEYAKTILnlmtsspKHPDGK-VLITG-GGIANFTNVAatf 356
Cdd:COG0045 265 GAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIIL-------SDPNVKaILVNIfGGITRCDVVA--- 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 281363475 357 QGIITALREfqpklVEHNVSIFVRRAGPNYQEGLRKMRDFG 397
Cdd:COG0045 330 EGIVAALKE-----VGLKVPVVVRLEGTNVEEGRKILAESG 365
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
900-1097 |
1.56e-12 |
|
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: 70.51 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 900 KFFEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSVVSGLltigdrfgGALDGSA---------RQFsEAYDTNLHPME 970
Cdd:COG0372 182 RALDLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAI--------GALKGPLhgganeavlEML-EEIGSPDNVEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 971 FVNKMRKEGKLILGIGHRV-KsinNPDVRVKIIKEF---VLENFPACPLLKYALEVEKITTNKKP----NLILNVD---G 1039
Cdd:COG0372 252 YIRKALDKKERIMGFGHRVyK---NYDPRAKILKEAaeeLLEELGDDPLLEIAEELEEVALEDEYfiekKLYPNVDfysG 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281363475 1040 VIATAF---VDMlrnsgsFTseeaqeyinvgainSLFVLGRSIGFIGHYMDQkRLKQGLYR 1097
Cdd:COG0372 329 IVYHALgipTDM------FT--------------PIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
66-397 |
7.34e-12 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 68.58 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 66 RGKLGliGVK--KNFEQVK----QWIGERLNKDQKIGNA--VGKLrnfIIEPFVPhtDAEEMYVCIYSHRAADTILFY-- 135
Cdd:PRK00696 54 RGKAG--GVKlaKSPEEARefakQILGMTLVTHQTGPKGqpVNKV---LVEEGAD--IAKEYYLSIVLDRATRRVVFMas 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 136 HQGGVDIGDVDA----KAVKldVPVNSSLSLADVKSKLLkeVKDAGTK----ERIAKFVSALYTTYVDLYFTYLEINPLV 207
Cdd:PRK00696 127 TEGGMDIEEVAEetpeKIHK--VAIDPLTGLQPFQAREI--AFKLGLPgeqvKQFAKILMGLYKAFVEKDASLVEINPLV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 208 VTAD-NLYILDlaAK--LDSTADFicR-PKWGEIdypppfgRDAYPE-----EA------YIAdLDaksgaslkltilnr 272
Cdd:PRK00696 203 VTKDgDLIALD--AKinFDDNALF--RhPDLAEL-------RDLSEEdpleaEAskyglnYVK-LD-------------- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 273 nGRIWTMVAGGGASVIYSDTIcDLGGAsELANYGEYSGAPSEQQTYEYAKTILnlmtsspKHPDGK-VLIT-GGGIANFT 350
Cdd:PRK00696 257 -GNIGCMVNGAGLAMATMDII-KLYGG-EPANFLDVGGGATAERVAEAFKIIL-------SDPNVKaILVNiFGGITRCD 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 281363475 351 NVAatfQGIITALREfqpklVEHNVSIFVRRAGPNYQEGLRKMRDFG 397
Cdd:PRK00696 327 VIA---EGIIAAVKE-----VGVTVPLVVRLEGTNVELGKKILAESG 365
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
66-397 |
1.55e-11 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 67.43 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 66 RGKLGLIGVKKNFEQV----KQWIGERLNKDQKigNAVGKLRNFI-IEPFVPHtdAEEMYVCIYSHRAADTILFY--HQG 138
Cdd:PRK14046 54 RGKAGGIKLCRTYNEVrdaaEDLLGKKLVTHQT--GPEGKPVQRVyVETADPI--ERELYLGFVLDRKSERVRVIasARG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 139 GVDIGDVDAKAVK--LDVPVNSSLSLADVKSKLL--KEVKDAGTKERIAKFVSALYTTYVDLYFTYLEINPLVVTADNlY 214
Cdd:PRK14046 130 GMEIEEIAAKEPEaiIQVVVEPAVGLQQFQAREIafGLGLDIKQVSRAVKTIMGCYRAFRDLDATMLEINPLVVTKDD-R 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 215 ILDLAAKL--DSTADFIcRPKWGEIdypppfgRDAY---PEEAYIADLDaksgaslkLTILNRNGRIWTMVAGGGASVIY 289
Cdd:PRK14046 209 VLALDAKMsfDDNALFR-RPNIAEM-------RDPSqedPREAQAAEHG--------LSYVGLDGDIGCIVNGAGLAMAT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 290 SDTICDLGGasELANYGEYSGAPSEQQTYEYAKTILnlmtsSPKHPDGKVLITGGGIANFTNVAatfQGIITALREfqpk 369
Cdd:PRK14046 273 MDMIKLAGG--EPANFLDVGGGASPERVAKAFRLVL-----SDRNVKAILVNIFAGINRCDWVA---EGVVQAARE---- 338
|
330 340
....*....|....*....|....*...
gi 281363475 370 lVEHNVSIFVRRAGPNYQEGLRKMRDFG 397
Cdd:PRK14046 339 -VGIDVPLVVRLAGTNVEEGRKILAESG 365
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
898-1085 |
3.41e-10 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 63.50 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 898 VCKFFEMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSVVSGLLTI-GDRFGGALDGSARQFSEAYDTNLHPmEFVNKMR 976
Cdd:PLN02456 244 LARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEIGTVENIP-EYVEGVK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 977 KEGKLILGIGHRVksINNPDVRVKIIKEFVLENF---PACPLLKYALEVEKIT----TNKKPNLILNVD---GVIatafv 1046
Cdd:PLN02456 323 NSKKVLPGFGHRV--YKNYDPRAKCIREFALEVFkhvGDDPLFKVASALEEVAlldeYFKVRKLYPNVDfysGVL----- 395
|
170 180 190
....*....|....*....|....*....|....*....
gi 281363475 1047 dmLRNSGsFTseeaQEYINVgainsLFVLGRSIGFIGHY 1085
Cdd:PLN02456 396 --LRALG-FP----EEFFTV-----LFAVSRAAGYLSQW 422
|
|
| PLN00124 |
PLN00124 |
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional |
118-400 |
1.25e-08 |
|
succinyl-CoA ligase [GDP-forming] subunit beta; Provisional
Pssm-ID: 177736 [Multi-domain] Cd Length: 422 Bit Score: 58.60 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 118 EMYVCIYSHR--AADTILFYHQGGVDIGDVDAK----AVKLDVPVNSSLSLADVkSKLLK--EVKDAGTKERIAKfVSAL 189
Cdd:PLN00124 142 EMYFAILLDRasAGPLIIACSKGGTSIEDLAEKfpekIIKVPIDIFKGITDEDA-AKVVDglAPKVADRNDAIEQ-VKKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 190 YTTYVDLYFTYLEINPLVVTADNLYILdLAAKL--DSTADFicRPKwgEIdypppFG-RDAYPEeayiadlDAKSGASLK 266
Cdd:PLN00124 220 YKLFCKCDCTMVEINPLAETADGQLVA-ADAKLnfDDNAAF--RQK--EI-----FAlRDTSQE-------DPREVAAAK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 267 --LTILNRNGRIWTMVAGGGASVIYSDTICDLGGASelANYGEYSGAPSEQQTYEYAKtilnLMTSSPKHPDGKVLITGG 344
Cdd:PLN00124 283 adLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGSP--ANFLDVGGNASEQQVVEAFK----ILTSDDKVKAILVNIFGG 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 281363475 345 GIAnfTNVAATfqGIITALREfqpklVEHNVSIFVRRAGPNYQEGLRKMRDFGSTL 400
Cdd:PLN00124 357 IMK--CDVIAS--GIVNAAKQ-----VGLKVPLVVRLEGTNVDQGKRILKESGMTL 403
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
924-1089 |
1.20e-06 |
|
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxalacetate (OAA) to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and OAA to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). This group contains proteins similar to the E. coli 2MCS, EcPrpC. EcPrpC is one of two CS isozymes in the gram-negative E. coli. EcPrpC is a dimeric (type I ) CS; it is induced during growth on propionate and prefers PrCoA as a substrate though it has partial CS activity with AcCoA. This group also includes Salmonella typhimurium PrpC and Ralstonia eutropha (Re) 2-MCS1 which are also induced during growth on propionate and prefer PrCoA as substrate, but can also use AcCoA. Re 2-MCS1 can use butyryl-CoA and valeryl-CoA at a lower rate. A second Ralstonia eutropha 2MCS, Re 2-MCS2, which is induced on propionate is also found in this group. This group may include proteins which may function exclusively as a CS, those which may function exclusively as a 2MCS, or those with dual specificity which functions as both a CS and a 2MCS.
Pssm-ID: 99861 [Multi-domain] Cd Length: 363 Bit Score: 51.92 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 924 VCARAGKDLVSSVVSGLLTI-GDRFGGAlDGSARQFSEAYDTNLHPMEFVNKMRKEGKLILGIGHRVKSINNPdvRVKII 1002
Cdd:cd06108 189 VTASTLSDFYSAITGAIGTLrGPLHGGA-NEAAMELIERFKSPEEAEQGLLEKLERKELIMGFGHRVYKEGDP--RSDII 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 1003 KEFVL---ENFPACPLLKYALEVEKITTNKKpNLILNVDGVIATAFVDMLRNSGSFTSeeaqeyinvgainsLFVLGRSI 1079
Cdd:cd06108 266 KKWSKklsEEGGDPLLYQISERIEEVMWEEK-KLFPNLDFYSASAYHFCGIPTELFTP--------------IFVMSRVT 330
|
170
....*....|
gi 281363475 1080 GFIGHYMDQK 1089
Cdd:cd06108 331 GWAAHIMEQR 340
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
8-208 |
2.19e-06 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 8 EASGKDILNRHlnthgaGAATCRFSTVNSTTDWSKLAVDhpwLLTTPLVCKPDQLIKRRGKLGliGVKKNF------EQV 81
Cdd:pfam08442 4 EYQAKEIFAKY------GIPVPRGEVATSPEEAEEIAKK---LGGKVYVVKAQVLAGGRGKAG--GVKLAKspeeakEVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 82 KQWIGERLNKDQ--KIGNAVGKLrnFIIEPfvphTD-AEEMYVCIYSHRAADTILFY--HQGGVDIGDVDAKA----VKl 152
Cdd:pfam08442 73 KEMLGKNLVTKQtgPDGQPVNKV--LVEEA----LDiKKEYYLSIVLDRASKGPVIIasTEGGVDIEEVAAKNpekiHK- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281363475 153 dVPVNSSLSLAD-------VKSKLLKEVKDAGtkeriAKFVSALYTTYVDLYFTYLEINPLVV 208
Cdd:pfam08442 146 -FPIDPLKGLTPyqareiaFKLGLPGELIKQA-----ADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
| gltA |
PRK05614 |
citrate synthase; |
970-1088 |
7.46e-05 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 46.41 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 970 EFVNKMR-KEG--KLiLGIGHRVksINNPDVRVKIIKEfvlenfpAC-----------PLLKYALEVEKITTN------K 1029
Cdd:PRK05614 289 EFIARAKdKNDgfRL-MGFGHRV--YKNYDPRAKIMRE-------TChevlkelglndPLLEVAMELEEIALNdeyfieR 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363475 1030 KpnLILNVD---GVIATAF---VDMlrnsgsFTseeaqeyinvgainSLFVLGRSIGFIGHYMDQ 1088
Cdd:PRK05614 359 K--LYPNVDfysGIILKALgipTSM------FT--------------VIFALARTVGWIAHWNEM 401
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
900-1008 |
2.93e-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: 41.48 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 900 KFFEMCLMVTADHGpavsGAHN----TIVCARAGKDLVSSVVSGLLTI-GDRFGGALDGSARQFS------EAYDTNLHP 968
Cdd:cd06113 196 KLLDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLEdikenvKDWTDEDEV 271
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 281363475 969 MEFVNK-MRKE----GKLILGIGHRVKSINNPdvRVKIIKEFVLE 1008
Cdd:cd06113 272 RAYLRKiLNKEafdkSGLIYGMGHAVYTLSDP--RAVVLKKYARS 314
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
906-1091 |
4.06e-03 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 40.89 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 906 LMVTADHG-PAVSGAhnTIVCARAGKDLVSSVVSGLLTI-GDRFGGALDGSARQFSEAYDTNLHPMEFVNKMRKEGKLIL 983
Cdd:PRK14037 177 LILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIINGKKRLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363475 984 GIGHRVKSINNPdvRVKIIKEFVLE----NFPACPLLKYALEVEK--ITTNKKPNLILNVD---GVIATAF---VDMlrn 1051
Cdd:PRK14037 255 GFGHRVYKTYDP--RAKIFKELAETlierNSEAKKYFEIAQKLEElgIKQFGSKGIYPNTDfysGIVFYALgfpVYM--- 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 281363475 1052 sgsFTseeaqeyinvgainSLFVLGRSIGFIGHYM----DQKRL 1091
Cdd:PRK14037 330 ---FT--------------ALFALSRTLGWLAHIIeyveEQHRL 356
|
|
| |
