|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
491-1094 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 954.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 491 TLFSRHTKAIIWGMQTRAVQGMLDFDYICSRDEPSVSAMVYPfTGDHRQKFYWGHKEILIPVYKNMSDAMRKHPEVDVLI 570
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 571 NFASLRSAYDSTVETMNYPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK 650
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 651 LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYEDTPGVKMIVVLGEIGGTEEYKICRG 730
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 731 IKEGRITKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEVIQSVYQDLVAKGVI 810
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 811 EPAEEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYACQFI 890
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 891 EMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLI 970
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 971 MGIGHRVKSINNPDMRVQILKDYVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDALRNCGSFTREEADE 1050
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 694627642 1051 YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1094
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-419 |
1.08e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 414.55 E-value: 1.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 1 MSAKAISEQTGKEFLYKYICTSSAIQNRFKYARVTPDTDWAWLIQEHPWLLSERLVVKPDQLIKRRGKLGLVGINLTLDQ 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 81 VKVWLKQRLGQETVIANAKGILKNFLIEPFVPHKQEeeFYVCIYAAREGDYVLFHHEGGVDVGDVDAKAQKLLVAVDENL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQE--FYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 161 SgSDVKKHLLQHAPANKKDILASFICGLFNFYEDLYFTYLEINPLVVTNDGVYILDLAAKIDATADYICKVKWGDVEFPP 240
Cdd:PLN02235 159 T-SEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 241 PFGREAYPEEAYIADLDAKSGASLKLTILNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 320
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 321 KTILSLMTreKHPEGK--ILIIGGSIANFTNVAATFKGIVRAIKDYQGPLKDHEVRIFVRRGGPNYQEGLRVMGEVGKTT 398
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 694627642 399 GIPIHVFGTETHMTAIVGMAL 419
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
244-421 |
5.31e-123 |
|
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: 373.91 E-value: 5.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 244 REAYPEEAYIADLDAKSGASLKLTILNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 323
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 324 LSLMTREKHPEGKILIIGGSIANFTNVAATFKGIVRAIKDYQGPLKDHEVRIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 403
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 694627642 404 VFGTETHMTAIVGMALGH 421
Cdd:pfam16114 161 VYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1093 |
2.73e-92 |
|
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: 294.47 E-value: 2.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 856 GMPITEVFKEeMGIGGVLGLLWFQRRLPKYACQFIEMCLMVTADHGPAVSGAHNTIVCARAG-KDLVSSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 935 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDYVKQHFPATPLLDYALEV 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 1011 EKITTSKKP-NLILNVDGFIGVAFVDalrnCGSFTreeadeyidiGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1089
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLD----LGFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 694627642 1090 DISY 1093
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
550-802 |
1.21e-48 |
|
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: 174.86 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 550 IPVYKNMSDAMRKHPevdvlINfASL-----RSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGPA 624
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 625 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 704
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 705 EDTPGVKMIVVLGEIGGTEEYKICRGIKEGrITKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 784
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 694627642 785 FVPRSFDELGEVIQSVYQ 802
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
544-800 |
1.83e-36 |
|
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: 139.47 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 544 GHKEILIPVYKNMSDAMRKhPEVDVLINFASLRSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGP 623
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 624 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 700
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 701 VLRYEDTPGVKMIVVLGEIGGTEEYKICRGIKEgRITKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 776
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 694627642 777 QALKEAGVFVPRSFDELGEVIQSV 800
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
876-1078 |
2.83e-22 |
|
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: 99.89 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 876 LWFQRRLPKYACQFIEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGI 954
Cdd:pfam00285 156 MLFGYEPDPEEARALDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 955 IPmEFVNKMK-KEGKLIMGIGHRV-KsinNPDMRVQILKDYVKQHFPAT---PLLDYALEVEKIT----TSKKPNLILNV 1025
Cdd:pfam00285 235 VE-EYIRKVLnKGKERIMGFGHRVyK---NYDPRAKILKEFAEELAEEGgddPLLELAEELEEVApedlYFVEKNLYPNV 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694627642 1026 DGFIGVAFvDALRncgsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:pfam00285 311 DFYSGVLY-HALG-------------IPTDMFTPLFAISRTAGWLAHWIEQLA 349
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
55-403 |
1.61e-13 |
|
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: 73.57 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 55 LVVKPDQLIKRRGKLGLVGINLTLDQVKVWLKQRLGQETVIANAKG---ILKNFLIEPFVPhkQEEEFYVCIYAAREGDY 131
Cdd:TIGR01016 43 VVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKELVTNQTDPlgqPVNKILIEEATD--IDKEYYLSIVIDRSARC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 132 VLF--HHEGGVDVGDVDAKAQKLLVAVDENLSGSDVKKHLLQHA-----PANKKDILASFICGLFNFYEDLYFTYLEINP 204
Cdd:TIGR01016 121 PVImaSTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQAREIAkklglEGELVKQVADIIKKLYQIFLEYDASLVEINP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 205 LVVTNDG-VYILDlaAKIDATADYIckvkwgdveFPPPFGREAY-PEEAYIADLDAKsgaSLKLTILNPKGRIWTMVAGG 282
Cdd:TIGR01016 201 LVITKDGnLIALD--AKLTIDDNAL---------FRHPDLEEMRdYSQEDPREVLAK---QWGLNYVALDGNIGCMVNGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 283 GASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGKILIIG--GSIANFTNVAatfKGIVRA 360
Cdd:TIGR01016 267 GLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KGLVEA 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 694627642 361 IKDyqgplKDHEVRIFVRRGGPNYQEGLRVMGEvgktTGIPIH 403
Cdd:TIGR01016 336 LKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
2.02e-06 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 47.12 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 492 LFSRHTKAIIWGMQTRAVQgMLDFDYICSRDEPSVsaMVYPFTGDHRQKFYWGhkeilIPVYKNMSDAMRKHpEVDVLIN 571
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 694627642 572 FASLRSAYDSTVETMNYPqIRTIAIIAEGI 601
Cdd:smart00881 72 FVPAEAAPDAIDEAIEAG-IKGIVVITEGI 100
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-407 |
7.07e-06 |
|
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: 49.66 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 66 RGKLGlvGINL--TLDQVKVWLKQRLGQE--TVIANAKGILKNF-LIEPFVPHKQEeeFYVCIYAARE-GDYV-LFHHEG 138
Cdd:COG0045 54 RGKAG--GVKLakSPEEAREAAEEILGMTlvTHQTGPKGKPVNKvLVEEGVDIAKE--LYLSILLDRAtRRPViMASTEG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 139 GVDVGDVdAKAQ--KLL-VAVD--ENLSGSDVKKHL----LQHAPANKkdiLASFICGLFNFYEDLYFTYLEINPLVVTN 209
Cdd:COG0045 130 GMDIEEV-AEETpeKIIkVPIDplVGLQPYQARELAfalgLPGKQVKQ---FAKILKKLYRAFVEKDASLVEINPLVVTK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 210 DG-VYILDlaAKI--DATADY----IckVKWGDVEFPPPFGREAYPEE-AYIAdLDaksgaslkltilnpkGRIWTMVAG 281
Cdd:COG0045 206 DGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEEDPLEVEASKYGlNYVK-LD---------------GNIGCMVNG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 282 GG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGK-ILI-IGGSIANFTNVAatfKG 356
Cdd:COG0045 266 AGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS------DPNVKaILVnIFGGITRCDVVA---EG 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 694627642 357 IVRAIKDYQGPLKdhevrIFVRRGGPNYQEGLRVMGEvgktTGIPIHVFGT 407
Cdd:COG0045 332 IVAALKEVGLKVP-----VVVRLEGTNVEEGRKILAE----SGLNIIAADT 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
491-1094 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 954.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 491 TLFSRHTKAIIWGMQTRAVQGMLDFDYICSRDEPSVSAMVYPfTGDHRQKFYWGHKEILIPVYKNMSDAMRKHPEVDVLI 570
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 571 NFASLRSAYDSTVETMNYPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK 650
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 651 LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYEDTPGVKMIVVLGEIGGTEEYKICRG 730
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 731 IKEGRITKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEVIQSVYQDLVAKGVI 810
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 811 EPAEEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYACQFI 890
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 891 EMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLI 970
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 971 MGIGHRVKSINNPDMRVQILKDYVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDALRNCGSFTREEADE 1050
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 694627642 1051 YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1094
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-419 |
1.08e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 414.55 E-value: 1.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 1 MSAKAISEQTGKEFLYKYICTSSAIQNRFKYARVTPDTDWAWLIQEHPWLLSERLVVKPDQLIKRRGKLGLVGINLTLDQ 80
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 81 VKVWLKQRLGQETVIANAKGILKNFLIEPFVPHKQEeeFYVCIYAAREGDYVLFHHEGGVDVGDVDAKAQKLLVAVDENL 160
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQE--FYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 161 SgSDVKKHLLQHAPANKKDILASFICGLFNFYEDLYFTYLEINPLVVTNDGVYILDLAAKIDATADYICKVKWGDVEFPP 240
Cdd:PLN02235 159 T-SEICAPLIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 241 PFGREAYPEEAYIADLDAKSGASLKLTILNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 320
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 321 KTILSLMTreKHPEGK--ILIIGGSIANFTNVAATFKGIVRAIKDYQGPLKDHEVRIFVRRGGPNYQEGLRVMGEVGKTT 398
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 694627642 399 GIPIHVFGTETHMTAIVGMAL 419
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
244-421 |
5.31e-123 |
|
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: 373.91 E-value: 5.31e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 244 REAYPEEAYIADLDAKSGASLKLTILNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 323
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 324 LSLMTREKHPEGKILIIGGSIANFTNVAATFKGIVRAIKDYQGPLKDHEVRIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 403
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 694627642 404 VFGTETHMTAIVGMALGH 421
Cdd:pfam16114 161 VYGPETHMTGIVPMALGY 178
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1093 |
2.73e-92 |
|
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: 294.47 E-value: 2.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 856 GMPITEVFKEeMGIGGVLGLLWFQRRLPKYACQFIEMCLMVTADHGPAVSGAHNTIVCARAG-KDLVSSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 935 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDYVKQHFPATPLLDYALEV 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 1011 EKITTSKKP-NLILNVDGFIGVAFVDalrnCGSFTreeadeyidiGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1089
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLD----LGFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 694627642 1090 DISY 1093
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
550-802 |
1.21e-48 |
|
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: 174.86 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 550 IPVYKNMSDAMRKHPevdvlINfASL-----RSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGPA 624
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 625 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 704
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 705 EDTPGVKMIVVLGEIGGTEEYKICRGIKEGrITKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 784
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 694627642 785 FVPRSFDELGEVIQSVYQ 802
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
544-800 |
1.83e-36 |
|
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: 139.47 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 544 GHKEILIPVYKNMSDAMRKhPEVDVLINFASLRSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGP 623
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 624 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 700
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 701 VLRYEDTPGVKMIVVLGEIGGTEEYKICRGIKEgRITKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 776
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 694627642 777 QALKEAGVFVPRSFDELGEVIQSV 800
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
550-804 |
6.99e-35 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 135.30 E-value: 6.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 550 IPVYKNMSDAMRKHpEVDVLINFASLRSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVTIIGPATVGGI 629
Cdd:PRK05678 51 LPVFNTVAEAVEAT-GANASVIYVPPPFAADAILEAID-AGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGII 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 630 KPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDHVLRYED 706
Cdd:PRK05678 129 TPGECKIG--------IMPGHIHKKGRVGVVSRSGTLTYE---AVAQLTDlgfGQSTCVGIGGDPINGTNFIDVLEAFEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 707 TPGVKMIVVLGEIGGTEEYKICRGIKEgRITKPVVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKNQALKEA 782
Cdd:PRK05678 198 DPETEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGVTAppgkRM-------GHAGAIISGGKGTAEEKKEALEAA 269
|
250 260
....*....|....*....|..
gi 694627642 783 GVFVPRSFDELGEVIQSVYQDL 804
Cdd:PRK05678 270 GVKVARTPSEIGELLKEVLKGL 291
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
545-805 |
1.07e-31 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 126.75 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 545 HKEILIPVYKNMSDAmRKHPEVDVLINFASLRSAYDSTVETMNyPQIRTIAIIAEGIPEA---LTRKLIKTADKkgVTII 621
Cdd:PTZ00187 69 HLKHGLPVFATVKEA-KKATGADASVIYVPPPHAASAIIEAIE-AEIPLVVCITEGIPQHdmvKVKHALLSQNK--TRLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 622 GPATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHV 701
Cdd:PTZ00187 145 GPNCPGIIKPGECKIG--------IMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 702 LRYEDTPGVKMIVVLGEIGGTEEYKICRGIKEGRITKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKE 781
Cdd:PTZ00187 217 KLFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITA---PPGRRMGHAGAIISGGKGTAPGKIEALEA 293
|
250 260
....*....|....*....|....
gi 694627642 782 AGVFVPRSFDELGEVIQSVYQDLV 805
Cdd:PTZ00187 294 AGVRVVKSPAQLGKTMLEVMKKKG 317
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
544-803 |
5.67e-26 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 109.67 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 544 GHKEILIPVYKNMSDAmRKHPEVDVLINFASLRSAYDSTVETMNyPQIRTIAIIAEGIPEALTRKLIKTADKKGVT-IIG 622
Cdd:PLN00125 49 GTEHLGLPVFNTVAEA-KAETKANASVIYVPPPFAAAAILEAME-AELDLVVCITEGIPQHDMVRVKAALNRQSKTrLIG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 623 PATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVL 702
Cdd:PLN00125 127 PNCPGIIKPGECKIG--------IMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 703 RYEDTPGVKMIVVLGEIGGTEEYKICRGIKEGRITKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEA 782
Cdd:PLN00125 199 KFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA---PPGRRMGHAGAIVSGGKGTAQDKIKALREA 275
|
250 260
....*....|....*....|.
gi 694627642 783 GVFVPRSFDELGEVIQSVYQD 803
Cdd:PLN00125 276 GVTVVESPAKIGVAMLEVFKE 296
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
890-1085 |
1.57e-22 |
|
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: 97.02 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 890 IEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEG 967
Cdd:cd06099 23 MDLALILHADHEGNAS-TFTARVVGSTGSDPYSAIAAAIGALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLESK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 968 KLIMGIGHRVKSinNPDMRVQILKDYVKQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGFIGVAFvDALRncgs 1042
Cdd:cd06099 102 RVIMGFGHRVYK--KYDPRATVLKKFAEELLKEDgddPMFELAAELEKIAEEVLYekKLYPNVDFYSGVLY-KAMG---- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694627642 1043 ftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06099 175 ---------FPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIR 208
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
842-1085 |
2.53e-22 |
|
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) 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 citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. 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 form 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. This subgroup includes both gram-positive and gram-negative bacteria.
Pssm-ID: 99855 [Multi-domain] Cd Length: 265 Bit Score: 97.77 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 842 TSICDERGQE--LIYAGMPITEVfKEEMGIGGVLGLLWFqRRLPKYACQFIEM----------------CLMVTADHGPA 903
Cdd:cd06101 11 SEISVIDGDEggLRYRGYPIEEL-AENSSFEEVAYLLLT-GELPSYAENFLYMlggeepdpefakamdlALILHADHEGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 904 VSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEGKLIMGIGHRVKSin 981
Cdd:cd06101 89 AS-TFTARVVGSTLSDPYSAIAAAIAALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLNSKRVLMGFGHRVYK-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 982 NPDMRVQILKDYVKQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGFIGVAFvdalRNCGsftreeadeyIDIGA 1056
Cdd:cd06101 166 KYDPRATVLKKFAEKLLKEKgldPMFELAAELEKIAPEVLYekKLYPNVDFYSGVLY----KAMG----------FPTEL 231
|
250 260
....*....|....*....|....*....
gi 694627642 1057 LNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06101 232 FTPLFAVSRAVGWLAHLIEQREDGQRIIR 260
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
876-1078 |
2.83e-22 |
|
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: 99.89 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 876 LWFQRRLPKYACQFIEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGI 954
Cdd:pfam00285 156 MLFGYEPDPEEARALDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 955 IPmEFVNKMK-KEGKLIMGIGHRV-KsinNPDMRVQILKDYVKQHFPAT---PLLDYALEVEKIT----TSKKPNLILNV 1025
Cdd:pfam00285 235 VE-EYIRKVLnKGKERIMGFGHRVyK---NYDPRAKILKEFAEELAEEGgddPLLELAEELEEVApedlYFVEKNLYPNV 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694627642 1026 DGFIGVAFvDALRncgsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:pfam00285 311 DFYSGVLY-HALG-------------IPTDMFTPLFAISRTAGWLAHWIEQLA 349
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
660-785 |
3.93e-20 |
|
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: 87.31 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 660 VSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYEDTPGVKMIVVLGEIG-GTEEYK---ICRGIKEGR 735
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPaggLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 694627642 736 -ITKPVVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGVF 785
Cdd:pfam00549 81 aRELPVVARVCGTEA---DPQGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
842-1097 |
1.53e-19 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 89.54 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 842 TSICDERGQELIYAGMPITEVFkEEMGIGGVLGLLWFQRRLPKYACQFIEMCLMVTADHGPAVSgahntIVCAR----AG 917
Cdd:PRK06224 11 TSISDVTPEEIYVRGYDLEDLI-GKLSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPS-----AAAARmtasGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 918 KDLVSSLTSGLLTIGDRFGGALDAAAKMFS---KAFDSGIIPME----FVNKMKKEGKLIMGIGHRVKSINNPdmRVQIL 990
Cdd:PRK06224 85 ESLQGAVAAGLLALGSVHGGAGEQAAELLQeiaAAADAGADLDAaaraIVAEYRAAGKRVPGFGHPLHKPVDP--RAPRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 991 KDYVKQHFPATPLLDYALEVEKI--TTSKKPnLILNVDGFIGVAFVDAlrncGsftreeadeyIDIGALNGIFVLGRSMG 1068
Cdd:PRK06224 163 LALAREAGVAGRHCRLAEALEAAlaAAKGKP-LPLNVDGAIAAILADL----G----------FPPALARGLFVISRAAG 227
|
250 260 270
....*....|....*....|....*....|.
gi 694627642 1069 FIGHYLDQKRLKQG--LYRHPWDDISYVLPE 1097
Cdd:PRK06224 228 LVAHVWEELQQPIGfrIWDPAEEAVEYTGPP 258
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
891-1085 |
4.25e-17 |
|
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: 84.76 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 891 EMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 969
Cdd:COG0372 185 DLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDNVE-EYIRKALDKKER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 970 IMGIGHRV-KsinNPDMRVQILKDYVKQHFPAT---PLLDYALEVEKITTSKKP----NLILNVDGFIGVafvdALRNCG 1041
Cdd:COG0372 263 IMGFGHRVyK---NYDPRAKILKEAAEELLEELgddPLLEIAEELEEVALEDEYfiekKLYPNVDFYSGI----VYHALG 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 694627642 1042 sftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQkRLKQGLYR 1085
Cdd:COG0372 336 ----------IPTDMFTPIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
890-1085 |
1.18e-16 |
|
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) 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 citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. 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.
Pssm-ID: 99871 [Multi-domain] Cd Length: 358 Bit Score: 83.03 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 890 IEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF------SKAFdsgiipmEFVNK 962
Cdd:cd06118 170 MDLALILHADHEGNAS-TFTARVVASTLSDMYSAIAAAIAALkGPLHGGANEAVLKMLleigtpENVE-------AYIWK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 963 MKKEGKLIMGIGHRVKSinNPDMRVQILKDYVKQHFP---ATPLLDYALEVEKITTSKKP--NLILNVDGFIGVAFvDAL 1037
Cdd:cd06118 242 KLANKRRIMGFGHRVYK--TYDPRAKILKELAEELAEekgDDKLFEIAEELEEIALEVLGekGIYPNVDFYSGVVY-KAL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694627642 1038 RncgsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1085
Cdd:cd06118 319 G-------------FPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIR 353
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
55-403 |
1.61e-13 |
|
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: 73.57 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 55 LVVKPDQLIKRRGKLGLVGINLTLDQVKVWLKQRLGQETVIANAKG---ILKNFLIEPFVPhkQEEEFYVCIYAAREGDY 131
Cdd:TIGR01016 43 VVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKELVTNQTDPlgqPVNKILIEEATD--IDKEYYLSIVIDRSARC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 132 VLF--HHEGGVDVGDVDAKAQKLLVAVDENLSGSDVKKHLLQHA-----PANKKDILASFICGLFNFYEDLYFTYLEINP 204
Cdd:TIGR01016 121 PVImaSTEGGVDIEEVAEKSPEKIIKYAIDPLTGLLPYQAREIAkklglEGELVKQVADIIKKLYQIFLEYDASLVEINP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 205 LVVTNDG-VYILDlaAKIDATADYIckvkwgdveFPPPFGREAY-PEEAYIADLDAKsgaSLKLTILNPKGRIWTMVAGG 282
Cdd:TIGR01016 201 LVITKDGnLIALD--AKLTIDDNAL---------FRHPDLEEMRdYSQEDPREVLAK---QWGLNYVALDGNIGCMVNGA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 283 GASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGKILIIG--GSIANFTNVAatfKGIVRA 360
Cdd:TIGR01016 267 GLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KGLVEA 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 694627642 361 IKDyqgplKDHEVRIFVRRGGPNYQEGLRVMGEvgktTGIPIH 403
Cdd:TIGR01016 336 LKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
807-1076 |
2.07e-11 |
|
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with activity as 2-methylcitrate synthase, citrate synthase, or both. Many Gram-negative species have a hexameric citrate synthase, termed citrate synthase I (TIGR01798). Members of this family (TIGR01800) appear as a second citrate synthase isozyme but typically are associated with propionate metabolism and synthesize 2-methylcitrate from propionyl-CoA; citrate synthase activity may be incidental. A number of species, including Thermoplasma acidophilum, Pyrococcus furiosus, and the Antarctic bacterium DS2-3R have a bifunctional member of this family as the only citrate synthase isozyme.
Pssm-ID: 130859 Cd Length: 368 Bit Score: 67.00 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 807 KGVIEPAEEVPPPTVPMDY--SWARELGLIRKPASFMTSICDERGQELIYAGMP-ITEVF------------KEEMGIGG 871
Cdd:TIGR01800 72 DEVIELIEALPAESHPMDVlrTAVSYLGALDPEKFGHTPEEARDIAIRLLAKLPtIVAYWyrirhggeiiapKDDDSIAG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 872 VLGLLWFQRRLPKYACQFIEMCLMVTADHG-PAVSGAhnTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFsKA 949
Cdd:TIGR01800 152 NFLYMLHGEEPTKEWEKAMDIALILYAEHEfNASTFA--ARVIASTLSDMYSAITAAIGALkGPLHGGANEAVMAML-DE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 950 FDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPdmRVQILKDYVKQHFPATPLLDY---ALEVEKITTSKKpNLILNVD 1026
Cdd:TIGR01800 229 IGDPDKAEAWIRKALENKERIMGFGHRVYKTYDP--RAKILKEYAKKLSAKEGSSKWyeiAERLEDVMEEEK-GIYPNVD 305
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 694627642 1027 GFIGVAFvdalrncgsftreeADEYIDIGALNGIFVLGRSMGFIGHYLDQ 1076
Cdd:TIGR01800 306 FFSASVY--------------YMMGIPTDLFTPIFAMSRVTGWTAHIIEQ 341
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
891-1073 |
1.72e-10 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 64.66 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 891 EMCLMVTADHGPAVSGAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 969
Cdd:PLN02456 249 DLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEIGTVENIP-EYVEGVKNSKKV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 970 IMGIGHRVksINNPDMRVQILKDY---VKQHFPATPLLDYALEVEKITTS----KKPNLILNVDGFIGVAFvdalRNCGs 1042
Cdd:PLN02456 328 LPGFGHRV--YKNYDPRAKCIREFaleVFKHVGDDPLFKVASALEEVALLdeyfKVRKLYPNVDFYSGVLL----RALG- 400
|
170 180 190
....*....|....*....|....*....|.
gi 694627642 1043 FTReeadEYIDIgalngIFVLGRSMGFIGHY 1073
Cdd:PLN02456 401 FPE----EFFTV-----LFAVSRAAGYLSQW 422
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
890-1078 |
5.97e-08 |
|
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. 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 citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-I, one of two CS isozymes in the gram-positive B. subtilis. The majority of CS activity in B. subtilis is provided by the other isozyme, BsCS-II (not included in this group). BsCS-I has a lower catalytic activity than BsCS-II, and has a Glu in place of a key catalytic Asp residue. This change is conserved in other members of this group. For E. coli CS (not included in this group), site directed mutagenesis of the key Asp residue to a Glu converts the enzyme into citryl-CoA lyase which cleaves citryl-CoA to AcCoA and OAA. A null mutation in the gene encoding BsCS-I (citA) had little effect on B. subtilis CS activity or on sporulation. However, disruption of the citA gene in a strain null for the gene encoding BsCS-II resulted in a sporulation deficiency, a characteristic of strains defective in the Krebs cycle. 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. Many of the gram-negative species represented in this group have a second CS isozyme which is in another group.
Pssm-ID: 99862 [Multi-domain] Cd Length: 349 Bit Score: 56.16 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 890 IEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKeGK 968
Cdd:cd06109 159 LDAYLVTVADHGMNAS-TFTARVIASTEADLTSAVLGAIGALkGPLHGGAPGPVLDMLDAIGTPENAEAWLREALAR-GE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 969 LIMGIGHRVKSINNPdmRVQILKDYVKQHFPATPLLDYALEVEKITTS----KKPN--LILNVDgFIGVAFVDALRncgs 1042
Cdd:cd06109 237 RLMGFGHRVYRVRDP--RADVLKAAAERLGAPDERLEFAEAVEQAALAllreYKPGrpLETNVE-FYTALLLEALG---- 309
|
170 180 190
....*....|....*....|....*....|....*.
gi 694627642 1043 ftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:cd06109 310 ---------LPREAFTPTFAAGRTAGWTAHVLEQAR 336
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
912-1077 |
1.93e-07 |
|
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: 54.62 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 912 VCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPdmRVQIL 990
Cdd:cd06108 189 VTASTLSDFYSAITGAIGTLrGPLHGGANEAAMELIER-FKSPEEAEQGLLEKLERKELIMGFGHRVYKEGDP--RSDII 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 991 KDYVKQHFPATP---LLDYALEVEKITTSKKpNLILNVDGFIGVAFvdalRNCGsftreeadeyIDIGALNGIFVLGRSM 1067
Cdd:cd06108 266 KKWSKKLSEEGGdplLYQISERIEEVMWEEK-KLFPNLDFYSASAY----HFCG----------IPTELFTPIFVMSRVT 330
|
170
....*....|
gi 694627642 1068 GFIGHYLDQK 1077
Cdd:cd06108 331 GWAAHIMEQR 340
|
|
| gltA |
PRK05614 |
citrate synthase; |
905-1076 |
6.43e-07 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 52.96 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 905 SGAhNTIVCARAGkdlVSSLTsglltiGDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG--KLiMGIGHRVksIN 981
Cdd:PRK05614 247 SGA-NPFACIAAG---IAALW------GPAHGGANEAVLKMLEEIGSVDNIP-EFIARAKdKNDgfRL-MGFGHRV--YK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 982 NPDMRVQILK---DYVKQHFPA-TPLLDYALEVEKITT------SKKpnLILNVDGFIGVafvdALRNCG----SFTree 1047
Cdd:PRK05614 313 NYDPRAKIMRetcHEVLKELGLnDPLLEVAMELEEIALndeyfiERK--LYPNVDFYSGI----ILKALGiptsMFT--- 383
|
170 180
....*....|....*....|....*....
gi 694627642 1048 adeyidigalnGIFVLGRSMGFIGHYLDQ 1076
Cdd:PRK05614 384 -----------VIFALARTVGWIAHWNEM 401
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
886-1078 |
1.34e-06 |
|
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions: 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 citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-II, the major CS of the gram-positive bacterium Bacillus subtilis. A mutation in the gene which encodes BsCS-II (citZ gene) has been described which resulted in a significant loss of CS activity, partial glutamate auxotrophy, and a sporulation deficiency, all of which are characteristic of strains defective in the Krebs cycle. Streptococcus mutans CS, found in this group, may participate in a pathway for the anaerobic biosynthesis of glutamate. This group also contains functionally uncharacterized CSs of various gram-negative bacteria. Some of the gram-negative species represented in this group have a second CS isozyme found in another group. 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.
Pssm-ID: 99863 [Multi-domain] Cd Length: 356 Bit Score: 51.89 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 886 ACQFIEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMK 964
Cdd:cd06110 166 AARAFDVALILHADHELNAS-TFAARVVASTLSDMYSAVTAAIGALkGPLHGGANERVMKMLLE-IGSVDNVAAYVKDKL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 965 KEGKLIMGIGHRVksINNPDMRVQILKDYVKQ---HFPATPLLDYALEVEKITTSKKpNLILNVDGFIGVAFvdalrncg 1041
Cdd:cd06110 244 ANKEKIMGFGHRV--YKTGDPRAKHLREMSRRlgkETGEPKWYEMSEAIEQAMRDEK-GLNPNVDFYSASVY-------- 312
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 694627642 1042 sftreeadeY---IDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:cd06110 313 ---------YmlgIPVDLFTPIFAISRVSGWCAHILEQYF 343
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
2.02e-06 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 214881 [Multi-domain] Cd Length: 100 Bit Score: 47.12 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 492 LFSRHTKAIIWGMQTRAVQgMLDFDYICSRDEPSVsaMVYPFTGDHRQKFYWGhkeilIPVYKNMSDAMRKHpEVDVLIN 571
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 694627642 572 FASLRSAYDSTVETMNYPqIRTIAIIAEGI 601
Cdd:smart00881 72 FVPAEAAPDAIDEAIEAG-IKGIVVITEGI 100
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
497-600 |
5.72e-06 |
|
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Pssm-ID: 396961 [Multi-domain] Cd Length: 97 Bit Score: 46.05 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 497 TKAIIWGMQTRAVQGM-LDFDYICSRDepsvSAMVYPFTGDHrqkfywGHKEIL-IPVYKNMSDAMRKHpEVDVLINFAS 574
Cdd:pfam02629 4 TKVIVIGAGGLGIQGLnYHFIQMLGYG----IKMVFGVNPGK------GGTEILgIPVYNSVDELEEKT-GVDVAVITVP 72
|
90 100
....*....|....*....|....*.
gi 694627642 575 LRSAYDSTVETMNyPQIRTIAIIAEG 600
Cdd:pfam02629 73 APFAQEAIDELVD-AGIKGIVNITPG 97
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-407 |
7.07e-06 |
|
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: 49.66 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 66 RGKLGlvGINL--TLDQVKVWLKQRLGQE--TVIANAKGILKNF-LIEPFVPHKQEeeFYVCIYAARE-GDYV-LFHHEG 138
Cdd:COG0045 54 RGKAG--GVKLakSPEEAREAAEEILGMTlvTHQTGPKGKPVNKvLVEEGVDIAKE--LYLSILLDRAtRRPViMASTEG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 139 GVDVGDVdAKAQ--KLL-VAVD--ENLSGSDVKKHL----LQHAPANKkdiLASFICGLFNFYEDLYFTYLEINPLVVTN 209
Cdd:COG0045 130 GMDIEEV-AEETpeKIIkVPIDplVGLQPYQARELAfalgLPGKQVKQ---FAKILKKLYRAFVEKDASLVEINPLVVTK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 210 DG-VYILDlaAKI--DATADY----IckVKWGDVEFPPPFGREAYPEE-AYIAdLDaksgaslkltilnpkGRIWTMVAG 281
Cdd:COG0045 206 DGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEEDPLEVEASKYGlNYVK-LD---------------GNIGCMVNG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 282 GG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPEGK-ILI-IGGSIANFTNVAatfKG 356
Cdd:COG0045 266 AGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS------DPNVKaILVnIFGGITRCDVVA---EG 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 694627642 357 IVRAIKDYQGPLKdhevrIFVRRGGPNYQEGLRVMGEvgktTGIPIHVFGT 407
Cdd:COG0045 332 IVAALKEVGLKVP-----VVVRLEGTNVEEGRKILAE----SGLNIIAADT 373
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
894-1078 |
1.37e-05 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 48.60 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 894 LMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKlIMG 972
Cdd:PRK14035 177 LVLHADHELNAS-TFTARCAVSSLSDMYSGVVAAVGSLkGPLHGGANERVMDMLSEIRSIGDVDAYLDEKFANKEK-IMG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 973 IGHRVKSINNPdmRVQILKDYVKQHFPAT---PLLDYALEVEKITTSKKpNLILNVDGFigvafvdalrncgsftreEAD 1049
Cdd:PRK14035 255 FGHRVYKDGDP--RAKYLREMSRKITKGTgreELFEMSVKIEKRMKEEK-GLIPNVDFY------------------SAT 313
|
170 180 190
....*....|....*....|....*....|...
gi 694627642 1050 EY----IDIGALNGIFVLGRSMGFIGHYLDQKR 1078
Cdd:PRK14035 314 VYhvmgIPHDLFTPIFAVSRVAGWIAHILEQYK 346
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
890-996 |
2.18e-05 |
|
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: 48.03 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 890 IEMCLMVTADHGpavsGAHN----TIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF-------SKAFDSGIIPm 957
Cdd:cd06113 198 LDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLedikenvKDWTDEDEVR- 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 694627642 958 EFVNKM--KKEGK---LIMGIGHRVKSINNPdmRVQILKDYVKQ 996
Cdd:cd06113 273 AYLRKIlnKEAFDksgLIYGMGHAVYTLSDP--RAVVLKKYARS 314
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
66-227 |
3.44e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 47.39 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 66 RGKLGLVGINLTLDQVKVWLKQRLGQE--TVIANAKG-ILKNFLIEPFVPhkQEEEFYVCIYAAREGDYVLF--HHEGGV 140
Cdd:PRK00696 54 RGKAGGVKLAKSPEEAREFAKQILGMTlvTHQTGPKGqPVNKVLVEEGAD--IAKEYYLSIVLDRATRRVVFmaSTEGGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 141 DVGDVDAKA-QKLL-VAVDE----------------NLSGSDVKKhllqhapankkdiLASFICGLFNFYEDLYFTYLEI 202
Cdd:PRK00696 132 DIEEVAEETpEKIHkVAIDPltglqpfqareiafklGLPGEQVKQ-------------FAKILMGLYKAFVEKDASLVEI 198
|
170 180
....*....|....*....|....*...
gi 694627642 203 NPLVVTNDG-VYILDlaAKI--DATADY 227
Cdd:PRK00696 199 NPLVVTKDGdLIALD--AKInfDDNALF 224
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
894-1079 |
3.78e-05 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 47.44 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 894 LMVTADHG-PAVSGAhnTIVCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIM 971
Cdd:PRK14037 177 LILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIINGKKRLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 972 GIGHRVKSINNPdmRVQILKDYVKQHFPATP----LLDYALEVEK--ITTSKKPNLILNVDGFIGVAFVDALRNCGSFTr 1045
Cdd:PRK14037 255 GFGHRVYKTYDP--RAKIFKELAETLIERNSeakkYFEIAQKLEElgIKQFGSKGIYPNTDFYSGIVFYALGFPVYMFT- 331
|
170 180 190
....*....|....*....|....*....|....*...
gi 694627642 1046 eeadeyidigalnGIFVLGRSMGFIGHYL----DQKRL 1079
Cdd:PRK14037 332 -------------ALFALSRTLGWLAHIIeyveEQHRL 356
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
890-1079 |
4.21e-04 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 43.80 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 890 IEMCLMVTADHGPAVSgAHNTIVCARAGKDLVSSLTSGL-LTIGDRFGGA-------LDA------AAKMFSKAFDsgii 955
Cdd:PRK12350 158 LDAYWVSAAEHGMNAS-TFTARVIASTGADVAAALSGAIgALSGPLHGGAparvlpmLDAvertgdARGWVKGALD---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 956 pmefvnkmkkEGKLIMGIGHRVKSINNPDMRVqiLKDYVKQhfPATPLLDYALEVEK----ITTSKKPNLIL--NVDGFI 1029
Cdd:PRK12350 233 ----------RGERLMGFGHRVYRAEDPRARV--LRATAKR--LGAPRYEVAEAVEQaalaELRERRPDRPLetNVEFWA 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 694627642 1030 GVaFVDALRncgsFTREeadeyidigALNGIFVLGRSMGFIGHYLDQKRL 1079
Cdd:PRK12350 299 AV-LLDFAG----VPAH---------MFTAMFTCGRTAGWSAHILEQKRT 334
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
959-1076 |
5.51e-04 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 43.79 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 959 FVNKMKKEGKLIMGIGHRVKSINNPdmRVQILKDYVKQ---HFPATPLLDYALEVEKITTSK-KPNLIL-NVDGFIGVAF 1033
Cdd:PRK14036 243 YLDERLANKQKIMGFGHREYKVKDP--RATILQKLAEElfaRFGHDEYYEIALELERVAEERlGPKGIYpNVDFYSGLVY 320
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 694627642 1034 vdalRNCGsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQ 1076
Cdd:PRK14036 321 ----RKLG----------IPRDLFTPIFAIARVAGWLAHWREQ 349
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
55-207 |
9.51e-04 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.86 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 55 LVVKPDQLIKRRGKLGLVGINLTLDQVKVWLKQRLGQE--TVIANAKG-ILKNFLIEPFVPHKqeEEFYVCIYAARE--G 129
Cdd:pfam08442 42 YVVKAQVLAGGRGKAGGVKLAKSPEEAKEVAKEMLGKNlvTKQTGPDGqPVNKVLVEEALDIK--KEYYLSIVLDRAskG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 130 DYVLFHHEGGVDVGDVDAKAQKLL--VAVD--ENLSGSDVKKHLLQ-HAPANKKDILASFICGLFNFYEDLYFTYLEINP 204
Cdd:pfam08442 120 PVIIASTEGGVDIEEVAAKNPEKIhkFPIDplKGLTPYQAREIAFKlGLPGELIKQAADIIKKLYKLFVEYDATLVEINP 199
|
...
gi 694627642 205 LVV 207
Cdd:pfam08442 200 LVE 202
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
912-1076 |
1.47e-03 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 42.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 912 VCARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKlIMGIGHRVksINNPDMRVQIL 990
Cdd:PRK14034 194 VCVATLSDVYSGITAAIGALkGPLHGGANENVMKMLTEIGEEENVESYIHNKLQNKEK-IMGFGHRV--YRQGDPRAKHL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694627642 991 KDYVKQhfpATPLL------DYALEVEKITTSKKpNLILNVDgFIGVAFVDALRncgsftreeadeyIDIGALNGIFVLG 1064
Cdd:PRK14034 271 REMSKR---LTVLLgeekwyNMSIKIEEIVTKEK-GLPPNVD-FYSASVYHCLG-------------IDHDLFTPIFAIS 332
|
170
....*....|..
gi 694627642 1065 RSMGFIGHYLDQ 1076
Cdd:PRK14034 333 RMSGWLAHILEQ 344
|
|
| |
