|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
545-1148 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 952.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 545 TLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPfTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLI 624
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 625 NFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK 704
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 705 LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRG 784
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 785 IKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVI 864
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 865 VPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFI 944
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 945 EMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLI 1024
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1025 MGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADE 1104
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 740086846 1105 YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1148
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
55-473 |
8.89e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 413.40 E-value: 8.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 55 MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDG 134
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 135 VKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQaeEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKL 214
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQ--EFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 215 NPEDIKKhLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP 294
Cdd:PLN02235 159 TSEICAP-LIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 295 PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 374
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 375 KTILSLMTreKHPDGK--ILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTT 452
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 740086846 453 GIPIHVFGTETHMTAIVGMAL 473
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
298-475 |
3.10e-122 |
|
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: 373.14 E-value: 3.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 298 REAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 377
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 378 LSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 457
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 740086846 458 VFGTETHMTAIVGMALGH 475
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 ... |
910-1147 |
6.35e-91 |
|
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: 291.39 E-value: 6.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 910 GMPITEVFKEeMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG-KDLVSSLTSGLLTIGDR 988
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 989 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDYVRQHFPATPLLDYALEV 1064
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1065 EKITTSKKP-NLILNVDGLIGVAFVDMlrncgsftreeadeYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1143
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL--------------GFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 740086846 1144 DISY 1147
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
604-856 |
8.44e-51 |
|
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: 181.03 E-value: 8.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 604 IPVFKNMADAMRKHPevdvlINfASL-----RSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPA 678
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 679 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 758
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 759 QDTPGVKMIVVLGEIGGTEEYKICRGIKEGrLTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 838
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 740086846 839 FVPRSFDELGEIIQSVYE 856
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
598-854 |
2.01e-37 |
|
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: 142.56 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 598 GHKEILIPVFKNMADAMRKhPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGP 677
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 678 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 754
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 755 VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPIVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 830
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 740086846 831 QALKEAGVFVPRSFDELGEIIQSV 854
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
714-839 |
1.46e-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: 88.47 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 714 VSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG-GTEEYK---ICRGIKEGR 789
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPaggLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 740086846 790 -LTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGVF 839
Cdd:pfam00549 81 aRELPVVARVCGTEA---DPQGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
109-457 |
1.93e-14 |
|
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: 76.65 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 109 LVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQE-ATVGKATGFLK--NFLIEPFVPhsQAEEFYVCIYATREGDY 185
Cdd:TIGR01016 43 VVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKElVTNQTDPLGQPvnKILIEEATD--IDKEYYLSIVIDRSARC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 186 VLF--HHEGGVDVGDVDAKAQKLLVGVdeKLNPED---------IKKHLLVHAPEDKKeiLASFISGLFNFYEDLYFTYL 254
Cdd:TIGR01016 121 PVImaSTEGGVDIEEVAEKSPEKIIKY--AIDPLTgllpyqareIAKKLGLEGELVKQ--VADIIKKLYQIFLEYDASLV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 255 EINPLVVTKDG-VYVLDLAAKVDATADYickvKWGDIEfpppfgrEAY-PEEAYIADLDAKsgaSLKLTLLNPKGRIWTM 332
Cdd:TIGR01016 197 EINPLVITKDGnLIALDAKLTIDDNALF----RHPDLE-------EMRdYSQEDPREVLAK---QWGLNYVALDGNIGCM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 333 VAGGGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPDGKILIIG--GSIANFTNVAatfKG 410
Cdd:TIGR01016 263 VNGAGLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KG 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 740086846 411 IVRAIRDyqgplKEHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPIH 457
Cdd:TIGR01016 332 LVEALKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
546-655 |
2.46e-08 |
|
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: 52.90 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 546 LFSRHTKAIVWGMQTRAVQgMLDFDYVCSRDEPSVaaMVYPFTGDHKQKFYWGhkeilIPVFKNMADAMRKHpEVDVLIN 625
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 740086846 626 FASLRSAYDSTMETMNyAQIRTIAIIAEGI 655
Cdd:smart00881 72 FVPAEAAPDAIDEAIE-AGIKGIVVITEGI 100
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
160-461 |
2.19e-07 |
|
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: 54.67 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 160 LIEPFVPHsqAEEFYVCIYATRE-GDYV-LFHHEGGVDVGDVDAKaqkllvgvdeklNPEDIKK---HLLV-----HAPE 229
Cdd:COG0045 97 LVEEGVDI--AKELYLSILLDRAtRRPViMASTEGGMDIEEVAEE------------TPEKIIKvpiDPLVglqpyQARE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 230 -------DKKEI--LASFISGLFNFYEDLYFTYLEINPLVVTKDG-VYVLDlaAKV--DATADY----IckVKWGDIEFP 293
Cdd:COG0045 163 lafalglPGKQVkqFAKILKKLYRAFVEKDASLVEINPLVVTKDGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 294 PPFGREAYPEE-AYIAdLDaksgaslkltllnpkGRIWTMVAGGG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQ 369
Cdd:COG0045 239 DPLEVEASKYGlNYVK-LD---------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 370 TYDYAKTILSlmtrekHPDGK-ILI-IGGSIANFTNVAatfKGIVRAirdyqgpLKEHEVT--IFVRRGGPNYQEGLRVM 445
Cdd:COG0045 298 VAEAFKIILS------DPNVKaILVnIFGGITRCDVVA---EGIVAA-------LKEVGLKvpVVVRLEGTNVEEGRKIL 361
|
330
....*....|....*.
gi 740086846 446 GEvgktTGIPIHVFGT 461
Cdd:COG0045 362 AE----SGLNIIAADT 373
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
545-1148 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 952.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 545 TLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPfTGDHKQKFYWGHKEILIPVFKNMADAMRKHPEVDVLI 624
Cdd:PLN02522 5 QLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 625 NFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASK 704
Cdd:PLN02522 84 NFASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 705 LYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRG 784
Cdd:PLN02522 164 LYRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 785 IKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVANGVI 864
Cdd:PLN02522 244 LKQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 865 VPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFI 944
Cdd:PLN02522 324 IPVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 945 EMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLI 1024
Cdd:PLN02522 404 EMCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1025 MGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTREEADE 1104
Cdd:PLN02522 484 PGIGHRIKSRDNRDKRVELLQKYARTHFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 740086846 1105 YIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYV 1148
Cdd:PLN02522 564 IVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
55-473 |
8.89e-134 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 413.40 E-value: 8.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 55 MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDG 134
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRLAGIDLPIRSAQVTESTDFNELANKEPWLSSTKLVVKPDMLFGKRGKSGLVALNLDLAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 135 VKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQaeEFYVCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKL 214
Cdd:PLN02235 81 VATFVKERLGKEVEMGGCKGPITTFIVEPFVPHDQ--EFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPTEAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 215 NPEDIKKhLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP 294
Cdd:PLN02235 159 TSEICAP-LIATLPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKWGNIEFPL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 295 PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYA 374
Cdd:PLN02235 238 PFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPNEEEVLQYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 375 KTILSLMTreKHPDGK--ILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTT 452
Cdd:PLN02235 318 RVVIDCAT--ANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGGPNYQKGLAKMRALGEEI 395
|
410 420
....*....|....*....|.
gi 740086846 453 GIPIHVFGTETHMTAIVGMAL 473
Cdd:PLN02235 396 GVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
298-475 |
3.10e-122 |
|
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: 373.14 E-value: 3.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 298 REAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTI 377
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 378 LSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIH 457
Cdd:pfam16114 81 LDLMTREPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPIH 160
|
170
....*....|....*...
gi 740086846 458 VFGTETHMTAIVGMALGH 475
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 ... |
910-1147 |
6.35e-91 |
|
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: 291.39 E-value: 6.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 910 GMPITEVFKEeMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAG-KDLVSSLTSGLLTIGDR 988
Cdd:cd06100 1 GYDLSDLIGK-ISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 989 FGGALDAAAKMFSKAFDSGI----IPMEFVNKMKKEGKLIMGIGHRVKSinNPDMRVQILKDYVRQHFPATPLLDYALEV 1064
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGDaldaAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELARELGPAGPHLDYALAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1065 EKITTSKKP-NLILNVDGLIGVAFVDMlrncgsftreeadeYIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYRHPWD 1143
Cdd:cd06100 158 EKALTAAKGkPLPLNVDGAIAAILLDL--------------GFPPGALRGLFVLGRSPGLIAHALEEKRLGQPLYRHPWD 223
|
....
gi 740086846 1144 DISY 1147
Cdd:cd06100 224 DIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
604-856 |
8.44e-51 |
|
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: 181.03 E-value: 8.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 604 IPVFKNMADAMRKHPevdvlINfASL-----RSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPA 678
Cdd:COG0074 50 VPVFDTVAEAVEETG-----AD-ASVifvppPFAADAILEAID-AGIKLIVCITEGIPVLDMVRVKRYAKAKGTRLIGPN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 679 TVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRY 758
Cdd:COG0074 123 CPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGDPIIGTSFIDVLELF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 759 QDTPGVKMIVVLGEIGGTEEYKICRGIKEGrLTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGV 838
Cdd:COG0074 195 EEDPETEAIVMIGEIGGSAEEEAAEYIKEN-MTKPVVAYIAGRTA---PPGKRMGHAGAIISGGKGTAESKIEALEAAGV 270
|
250
....*....|....*...
gi 740086846 839 FVPRSFDELGEIIQSVYE 856
Cdd:COG0074 271 PVAESPSEIGELLKKALK 288
|
|
| sucCoAalpha |
TIGR01019 |
succinyl-CoA synthetase, alpha subunit; This model describes succinyl-CoA synthetase alpha ... |
598-854 |
2.01e-37 |
|
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: 142.56 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 598 GHKEILIPVFKNMADAMRKhPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGP 677
Cdd:TIGR01019 43 GTTVLGLPVFDSVKEAVEE-TGANASVIFVPAPFAADAIFEAID-AGIELIVCITEGIPVHDMLKVKRYMEESGTRLIGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 678 ATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDH 754
Cdd:TIGR01019 121 NCPGIITPGECKIG--------IMPGHIHKPGNVGIVSRSGTLTYE---AVHQLTKagfGQSTCVGIGGDPVNGTSFIDV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 755 VLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPIVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKN 830
Cdd:TIGR01019 190 LEAFEKDPETEAIVMIGEIGGSAEEEAADFIKQ-NMSKPVVGFIAGATAppgkRM-------GHAGAIISGGKGTAESKI 261
|
250 260
....*....|....*....|....
gi 740086846 831 QALKEAGVFVPRSFDELGEIIQSV 854
Cdd:TIGR01019 262 EALEAAGVTVVKSPSDIGELLAEI 285
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
604-858 |
6.49e-37 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 141.08 E-value: 6.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 604 IPVFKNMADAMRKHpEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGI 683
Cdd:PRK05678 51 LPVFNTVAEAVEAT-GANASVIYVPPPFAADAILEAID-AGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIGPNCPGII 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 684 KPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNElnnIISRTTD---GVYEGVAIGGDRYPGSTFMDHVLRYQD 760
Cdd:PRK05678 129 TPGECKIG--------IMPGHIHKKGRVGVVSRSGTLTYE---AVAQLTDlgfGQSTCVGIGGDPINGTNFIDVLEAFEE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 761 TPGVKMIVVLGEIGGTEEYKICRGIKEgRLTKPIVCWCIGTCA----TMfssevqfGHAGACANQASETAVAKNQALKEA 836
Cdd:PRK05678 198 DPETEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGVTAppgkRM-------GHAGAIISGGKGTAEEKKEALEAA 269
|
250 260
....*....|....*....|..
gi 740086846 837 GVFVPRSFDELGEIIQSVYEDL 858
Cdd:PRK05678 270 GVKVARTPSEIGELLKEVLKGL 291
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
599-859 |
3.65e-33 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 130.99 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 599 HKEILIPVFKNMADAmRKHPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKlIKKA--DQKGVTIIG 676
Cdd:PTZ00187 69 HLKHGLPVFATVKEA-KKATGADASVIYVPPPHAASAIIEAIE-AEIPLVVCITEGIPQHDMVK-VKHAllSQNKTRLIG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 677 PATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVL 756
Cdd:PTZ00187 146 PNCPGIIKPGECKIG--------IMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 757 RYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEA 836
Cdd:PTZ00187 218 LFLNDPETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITA---PPGRRMGHAGAIISGGKGTAPGKIEALEAA 294
|
250 260
....*....|....*....|...
gi 740086846 837 GVFVPRSFDELGEIIQSVYEDLV 859
Cdd:PTZ00187 295 GVRVVKSPAQLGKTMLEVMKKKG 317
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
598-857 |
3.20e-27 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 113.14 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 598 GHKEILIPVFKNMADAmRKHPEVDVLINFASLRSAYDSTMETMNyAQIRTIAIIAEGIPEALTRKlIKKA--DQKGVTII 675
Cdd:PLN00125 49 GTEHLGLPVFNTVAEA-KAETKANASVIYVPPPFAAAAILEAME-AELDLVVCITEGIPQHDMVR-VKAAlnRQSKTRLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 676 GPATVGGIKPGCFKIGntggmldnILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHV 755
Cdd:PLN00125 126 GPNCPGIIKPGECKIG--------IMPGYIHKPGRIGIVSRSGTLTYEAVFQTTAVGLGQSTCVGIGGDPFNGTNFVDCL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 756 LRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKE 835
Cdd:PLN00125 198 EKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA---PPGRRMGHAGAIVSGGKGTAQDKIKALRE 274
|
250 260
....*....|....*....|..
gi 740086846 836 AGVFVPRSFDELGEIIQSVYED 857
Cdd:PLN00125 275 AGVTVVESPAKIGVAMLEVFKE 296
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
944-1139 |
4.00e-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: 95.87 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 944 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEG 1021
Cdd:cd06099 23 MDLALILHADHEGNAS-TFTARVVGSTGSDPYSAIAAAIGALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLESK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1022 KLIMGIGHRVKSinNPDMRVQILKDYVRQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGLIGVAFVDMlrncGs 1096
Cdd:cd06099 102 RVIMGFGHRVYK--KYDPRATVLKKFAEELLKEDgddPMFELAAELEKIAEEVLYekKLYPNVDFYSGVLYKAM----G- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740086846 1097 ftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1139
Cdd:cd06099 175 ---------FPTELFTPLFAVARAVGWLAHLIEQLEDNFKIIR 208
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
896-1139 |
2.81e-21 |
|
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: 95.07 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 896 TSICDERGQE--LIYAGMPITEVfKEEMGIGGVLGLLWFQKrLPKYSCQFIEM----------------CLMVTADHGPA 957
Cdd:cd06101 11 SEISVIDGDEggLRYRGYPIEEL-AENSSFEEVAYLLLTGE-LPSYAENFLYMlggeepdpefakamdlALILHADHEGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 958 VSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEF-VNKMKKEGKLIMGIGHRVKSin 1035
Cdd:cd06101 89 AS-TFTARVVGSTLSDPYSAIAAAIAALkGPLHGGANEAVLKMLEEIGTPKNEPAEAyIRKKLNSKRVLMGFGHRVYK-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1036 NPDMRVQILKDYVRQHFPAT---PLLDYALEVEKITTSKKP--NLILNVDGLIGVAFVDMlrncGsftreeadeyIDIGA 1110
Cdd:cd06101 166 KYDPRATVLKKFAEKLLKEKgldPMFELAAELEKIAPEVLYekKLYPNVDFYSGVLYKAM----G----------FPTEL 231
|
250 260
....*....|....*....|....*....
gi 740086846 1111 LNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1139
Cdd:cd06101 232 FTPLFAVSRAVGWLAHLIEQREDGQRIIR 260
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
714-839 |
1.46e-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: 88.47 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 714 VSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG-GTEEYK---ICRGIKEGR 789
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPaggLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 740086846 790 -LTKPIVCWCIGTCAtmfSSEVQFGHAGACANQASETAVAKNQALKEAGVF 839
Cdd:pfam00549 81 aRELPVVARVCGTEA---DPQGRSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
896-1151 |
1.58e-20 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 92.63 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 896 TSICDERGQELIYAGMPITEVfkeemgIGGV--LGLLWFQ--KRLPKYSC-QFIEMCLMVTADHGPAVSgahntIICAR- 969
Cdd:PRK06224 11 TSISDVTPEEIYVRGYDLEDL------IGKLsfTDMIFLLlrGRLPTPNEaRLLDAVLVALVDHGLTPS-----AAAARm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 970 ---AGKDLVSSLTSGLLTIGDRFGGALDAAAKMFS---KAFDSGIIPME----FVNKMKKEGKLIMGIGHRVKSINNPdm 1039
Cdd:PRK06224 80 tasGGESLQGAVAAGLLALGSVHGGAGEQAAELLQeiaAAADAGADLDAaaraIVAEYRAAGKRVPGFGHPLHKPVDP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1040 RVQILKDYVRQHFPATPLLDYALEVEKI--TTSKKPnLILNVDGLIGVAFVDMlrncGsftreeadeyIDIGALNGIFVL 1117
Cdd:PRK06224 158 RAPRLLALAREAGVAGRHCRLAEALEAAlaAAKGKP-LPLNVDGAIAAILADL----G----------FPPALARGLFVI 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 740086846 1118 GRSMGFIGHYLDQKRLKQG--LYRHPWDDISYVLPE 1151
Cdd:PRK06224 223 SRAAGLVAHVWEELQQPIGfrIWDPAEEAVEYTGPP 258
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
944-1132 |
2.09e-20 |
|
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: 94.50 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 944 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG 1021
Cdd:pfam00285 170 LDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDEVE-EYIRKVLnKGK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1022 KLIMGIGHRV-KsinNPDMRVQILKDYVRQHFPAT---PLLDYALEVEKIT----TSKKPNLILNVDGLIGVAFvDMLRn 1093
Cdd:pfam00285 248 ERIMGFGHRVyK---NYDPRAKILKEFAEELAEEGgddPLLELAEELEEVApedlYFVEKNLYPNVDFYSGVLY-HALG- 322
|
170 180 190
....*....|....*....|....*....|....*....
gi 740086846 1094 cgsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1132
Cdd:pfam00285 323 ------------IPTDMFTPLFAISRTAGWLAHWIEQLA 349
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
945-1139 |
5.02e-16 |
|
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: 81.29 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 945 EMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 1023
Cdd:COG0372 185 DLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPDNVE-EYIRKALDKKER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1024 IMGIGHRV-KsinNPDMRVQILKDYVRQHFPAT---PLLDYALEVEKITTSKKP----NLILNVD---GLIgvafvdmLR 1092
Cdd:COG0372 263 IMGFGHRVyK---NYDPRAKILKEAAEELLEELgddPLLEIAEELEEVALEDEYfiekKLYPNVDfysGIV-------YH 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740086846 1093 NCGsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQkRLKQGLYR 1139
Cdd:COG0372 333 ALG----------IPTDMFTPIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
944-1139 |
9.71e-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: 80.34 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 944 IEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF------SKAFdsgiipmEFVNK 1016
Cdd:cd06118 170 MDLALILHADHEGNAS-TFTARVVASTLSDMYSAIAAAIAALkGPLHGGANEAVLKMLleigtpENVE-------AYIWK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1017 MKKEGKLIMGIGHRVKSinNPDMRVQILKDYVRQHFP---ATPLLDYALEVEKITTSKKP--NLILNVDGLIGVAFVDMl 1091
Cdd:cd06118 242 KLANKRRIMGFGHRVYK--TYDPRAKILKELAEELAEekgDDKLFEIAEELEEIALEVLGekGIYPNVDFYSGVVYKAL- 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740086846 1092 rncGsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKRLKQGLYR 1139
Cdd:cd06118 319 ---G----------FPTELFTPLFAVSRAVGWLAHIIEYRENNQRLIR 353
|
|
| sucCoAbeta |
TIGR01016 |
succinyl-CoA synthetase, beta subunit; This model is designated subfamily because it does not ... |
109-457 |
1.93e-14 |
|
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: 76.65 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 109 LVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQE-ATVGKATGFLK--NFLIEPFVPhsQAEEFYVCIYATREGDY 185
Cdd:TIGR01016 43 VVVKAQVHAGGRGKAGGVKVAKSKEEARAAAEKLLGKElVTNQTDPLGQPvnKILIEEATD--IDKEYYLSIVIDRSARC 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 186 VLF--HHEGGVDVGDVDAKAQKLLVGVdeKLNPED---------IKKHLLVHAPEDKKeiLASFISGLFNFYEDLYFTYL 254
Cdd:TIGR01016 121 PVImaSTEGGVDIEEVAEKSPEKIIKY--AIDPLTgllpyqareIAKKLGLEGELVKQ--VADIIKKLYQIFLEYDASLV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 255 EINPLVVTKDG-VYVLDLAAKVDATADYickvKWGDIEfpppfgrEAY-PEEAYIADLDAKsgaSLKLTLLNPKGRIWTM 332
Cdd:TIGR01016 197 EINPLVITKDGnLIALDAKLTIDDNALF----RHPDLE-------EMRdYSQEDPREVLAK---QWGLNYVALDGNIGCM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 333 VAGGGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrekHPDGKILIIG--GSIANFTNVAatfKG 410
Cdd:TIGR01016 263 VNGAGLAMATMDIIKLYGG--EPANFLDVGGGASAERVREALKLVLS------DKSVKVVFINifGGITRCDLVA---KG 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 740086846 411 IVRAIRDyqgplKEHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPIH 457
Cdd:TIGR01016 332 LVEALKE-----VGVNVPVVVRLEGTNVEEGKKILAE----SGLNII 369
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
945-1130 |
1.15e-10 |
|
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: 64.69 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 945 EMCLMVTADHG-PAVSGAhnTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFsKAFDSGIIPMEFVNKMKKEGK 1022
Cdd:TIGR01800 171 DIALILYAEHEfNASTFA--ARVIASTLSDMYSAITAAIGALkGPLHGGANEAVMAML-DEIGDPDKAEAWIRKALENKE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1023 LIMGIGHRVKSINNPdmRVQILKDYVRQHFPATPLLDY---ALEVEKITTSKKpNLILNVDGLIGVAFVDMlrncGsftr 1099
Cdd:TIGR01800 248 RIMGFGHRVYKTYDP--RAKILKEYAKKLSAKEGSSKWyeiAERLEDVMEEEK-GIYPNVDFFSASVYYMM----G---- 316
|
170 180 190
....*....|....*....|....*....|.
gi 740086846 1100 eeadeyIDIGALNGIFVLGRSMGFIGHYLDQ 1130
Cdd:TIGR01800 317 ------IPTDLFTPIFAMSRVTGWTAHIIEQ 341
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
945-1127 |
4.64e-10 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 63.50 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 945 EMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPmEFVNKMKKEGKL 1023
Cdd:PLN02456 249 DLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEIGTVENIP-EYVEGVKNSKKV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1024 IMGIGHRVksINNPDMRVQILKDY---VRQHFPATPLLDYALEVEKITTS----KKPNLILNVDGLIGVafvdMLRNCGs 1096
Cdd:PLN02456 328 LPGFGHRV--YKNYDPRAKCIREFaleVFKHVGDDPLFKVASALEEVALLdeyfKVRKLYPNVDFYSGV----LLRALG- 400
|
170 180 190
....*....|....*....|....*....|.
gi 740086846 1097 FTReeadEYIDIgalngIFVLGRSMGFIGHY 1127
Cdd:PLN02456 401 FPE----EFFTV-----LFAVSRAAGYLSQW 422
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
546-655 |
2.46e-08 |
|
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: 52.90 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 546 LFSRHTKAIVWGMQTRAVQgMLDFDYVCSRDEPSVaaMVYPFTGDHKQKFYWGhkeilIPVFKNMADAMRKHpEVDVLIN 625
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTK--FVGGVYPGKVGPKVDG-----VPVYDSVAEAPEET-GVDVAVI 71
|
90 100 110
....*....|....*....|....*....|
gi 740086846 626 FASLRSAYDSTMETMNyAQIRTIAIIAEGI 655
Cdd:smart00881 72 FVPAEAAPDAIDEAIE-AGIKGIVVITEGI 100
|
|
| gltA |
PRK05614 |
citrate synthase; |
990-1130 |
1.05e-07 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 55.65 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 990 GGALDAAAKMFSKAFDSGIIPmEFVNKMK-KEG--KLiMGIGHRVksINNPDMRVQILK---DYVRQHFPA-TPLLDYAL 1062
Cdd:PRK05614 268 GGANEAVLKMLEEIGSVDNIP-EFIARAKdKNDgfRL-MGFGHRV--YKNYDPRAKIMRetcHEVLKELGLnDPLLEVAM 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1063 EVEKITT------SKKpnLILNVD---GLIGVAF---VDMlrncgsFTreeadeyidigalnGIFVLGRSMGFIGHYLDQ 1130
Cdd:PRK05614 344 ELEEIALndeyfiERK--LYPNVDfysGIILKALgipTSM------FT--------------VIFALARTVGWIAHWNEM 401
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
160-461 |
2.19e-07 |
|
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: 54.67 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 160 LIEPFVPHsqAEEFYVCIYATRE-GDYV-LFHHEGGVDVGDVDAKaqkllvgvdeklNPEDIKK---HLLV-----HAPE 229
Cdd:COG0045 97 LVEEGVDI--AKELYLSILLDRAtRRPViMASTEGGMDIEEVAEE------------TPEKIIKvpiDPLVglqpyQARE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 230 -------DKKEI--LASFISGLFNFYEDLYFTYLEINPLVVTKDG-VYVLDlaAKV--DATADY----IckVKWGDIEFP 293
Cdd:COG0045 163 lafalglPGKQVkqFAKILKKLYRAFVEKDASLVEINPLVVTKDGrLVALD--AKVnfDDNALFrhpeL--AALRDLSEE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 294 PPFGREAYPEE-AYIAdLDaksgaslkltllnpkGRIWTMVAGGG---ASVvysDTICDLGGvnELANYGEYSGAPSEQQ 369
Cdd:COG0045 239 DPLEVEASKYGlNYVK-LD---------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAER 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 370 TYDYAKTILSlmtrekHPDGK-ILI-IGGSIANFTNVAatfKGIVRAirdyqgpLKEHEVT--IFVRRGGPNYQEGLRVM 445
Cdd:COG0045 298 VAEAFKIILS------DPNVKaILVnIFGGITRCDVVA---EGIVAA-------LKEVGLKvpVVVRLEGTNVEEGRKIL 361
|
330
....*....|....*.
gi 740086846 446 GEvgktTGIPIHVFGT 461
Cdd:COG0045 362 AE----SGLNIIAADT 373
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
551-654 |
3.59e-07 |
|
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: 49.51 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 551 TKAIVWGMQTRAVQGM-LDFDYVCSRDEPSVAAMVYPFTGDhkqkfywghkEIL-IPVFKNMADAMRKHpEVDVLINFAS 628
Cdd:pfam02629 4 TKVIVIGAGGLGIQGLnYHFIQMLGYGIKMVFGVNPGKGGT----------EILgIPVYNSVDELEEKT-GVDVAVITVP 72
|
90 100
....*....|....*....|....*.
gi 740086846 629 LRSAYDSTMETMNyAQIRTIAIIAEG 654
Cdd:pfam02629 73 APFAQEAIDELVD-AGIKGIVNITPG 97
|
|
| PRK14046 |
PRK14046 |
malate--CoA ligase subunit beta; Provisional |
239-456 |
2.06e-06 |
|
malate--CoA ligase subunit beta; Provisional
Pssm-ID: 237594 [Multi-domain] Cd Length: 392 Bit Score: 51.64 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 239 ISGLFNFYEDLYFTYLEINPLVVTKDGvYVLDLAAKVDatadyickvkwgdiefpppFGREAYPEEAYIADLDAKS---- 314
Cdd:PRK14046 181 IMGCYRAFRDLDATMLEINPLVVTKDD-RVLALDAKMS-------------------FDDNALFRRPNIAEMRDPSqedp 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 315 ----GASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGvnELANYGEYSGAPSEQQTYDYAKTILSlmtrEKHPDGK 390
Cdd:PRK14046 241 reaqAAEHGLSYVGLDGDIGCIVNGAGLAMATMDMIKLAGG--EPANFLDVGGGASPERVAKAFRLVLS----DRNVKAI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740086846 391 ILIIGGSIANFTNVAatfKGIVRAIRDYQgplkeHEVTIFVRRGGPNYQEGLRVMGEvgktTGIPI 456
Cdd:PRK14046 315 LVNIFAGINRCDWVA---EGVVQAAREVG-----IDVPLVVRLAGTNVEEGRKILAE----SGLPI 368
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
944-1132 |
2.35e-06 |
|
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: 51.15 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 944 IEMCLMVTADHGPAVSGAHNTIIcARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKeGK 1022
Cdd:cd06109 159 LDAYLVTVADHGMNASTFTARVI-ASTEADLTSAVLGAIGALkGPLHGGAPGPVLDMLDAIGTPENAEAWLREALAR-GE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1023 LIMGIGHRVKSINNPdmRVQILKDYVRQHFPATPLLDYALEVEKITTS----KKPN--LILNVDGLIGVafvdMLRNCGs 1096
Cdd:cd06109 237 RLMGFGHRVYRVRDP--RADVLKAAAERLGAPDERLEFAEAVEQAALAllreYKPGrpLETNVEFYTAL----LLEALG- 309
|
170 180 190
....*....|....*....|....*....|....*.
gi 740086846 1097 ftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1132
Cdd:cd06109 310 ---------LPREAFTPTFAAGRTAGWTAHVLEQAR 336
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
942-1132 |
4.39e-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: 50.35 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 942 QFIEMCLMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMKKE 1020
Cdd:cd06110 168 RAFDVALILHADHELNAS-TFAARVVASTLSDMYSAVTAAIGALkGPLHGGANERVMKMLLE-IGSVDNVAAYVKDKLAN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1021 GKLIMGIGHRVksINNPDMRVQILKDYVRQ---HFPATPLLDYALEVEKITTSKKpNLILNVDGLIGVAFVDMlrncGsf 1097
Cdd:cd06110 246 KEKIMGFGHRV--YKTGDPRAKHLREMSRRlgkETGEPKWYEMSEAIEQAMRDEK-GLNPNVDFYSASVYYML----G-- 316
|
170 180 190
....*....|....*....|....*....|....*
gi 740086846 1098 treeadeyIDIGALNGIFVLGRSMGFIGHYLDQKR 1132
Cdd:cd06110 317 --------IPVDLFTPIFAISRVSGWCAHILEQYF 343
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
966-1131 |
6.71e-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: 49.61 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 966 ICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKaFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPdmRVQIL 1044
Cdd:cd06108 189 VTASTLSDFYSAITGAIGTLrGPLHGGANEAAMELIER-FKSPEEAEQGLLEKLERKELIMGFGHRVYKEGDP--RSDII 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1045 KDYVRQHFPATP---LLDYALEVEKITTSKKpNLILNVDGLIGVAFvdmlRNCGsftreeadeyIDIGALNGIFVLGRSM 1121
Cdd:cd06108 266 KKWSKKLSEEGGdplLYQISERIEEVMWEEK-KLFPNLDFYSASAY----HFCG----------IPTELFTPIFVMSRVT 330
|
170
....*....|
gi 740086846 1122 GFIGHYLDQK 1131
Cdd:cd06108 331 GWAAHIMEQR 340
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
948-1132 |
3.52e-05 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 47.45 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 948 LMVTADHGPAVSgAHNTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKlIMG 1026
Cdd:PRK14035 177 LVLHADHELNAS-TFTARCAVSSLSDMYSGVVAAVGSLkGPLHGGANERVMDMLSEIRSIGDVDAYLDEKFANKEK-IMG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1027 IGHRVKSINNPdmRVQILKDYVRQHFPAT---PLLDYALEVEKITTSKKpNLILNVDGLIGVAFVDMlrncgsftreead 1103
Cdd:PRK14035 255 FGHRVYKDGDP--RAKYLREMSRKITKGTgreELFEMSVKIEKRMKEEK-GLIPNVDFYSATVYHVM------------- 318
|
170 180
....*....|....*....|....*....
gi 740086846 1104 eYIDIGALNGIFVLGRSMGFIGHYLDQKR 1132
Cdd:PRK14035 319 -GIPHDLFTPIFAVSRVAGWIAHILEQYK 346
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
170-281 |
5.25e-05 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 47.01 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 170 AEEFYVCIYATREGDYVLF--HHEGGVDVGDVDAKA-QKL-------LVGVDE----------KLNPEDIKKhllvhape 229
Cdd:PRK00696 105 AKEYYLSIVLDRATRRVVFmaSTEGGMDIEEVAEETpEKIhkvaidpLTGLQPfqareiafklGLPGEQVKQ-------- 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 740086846 230 dkkeiLASFISGLFNFYEDLYFTYLEINPLVVTKDG-VYVLDlaAKV--DATADY 281
Cdd:PRK00696 177 -----FAKILMGLYKAFVEKDASLVEINPLVVTKDGdLIALD--AKInfDDNALF 224
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
944-1050 |
7.76e-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: 46.49 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 944 IEMCLMVTADHGpavsGAHN----TIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMF-------SKAFDSGIIPm 1011
Cdd:cd06113 198 LDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLedikenvKDWTDEDEVR- 272
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 740086846 1012 EFVNKM--KKEGK---LIMGIGHRVKSINNPdmRVQILKDYVRQ 1050
Cdd:cd06113 273 AYLRKIlnKEAFDksgLIYGMGHAVYTLSDP--RAVVLKKYARS 314
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
948-1133 |
3.31e-04 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 44.35 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 948 LMVTADHG-PAVSGAhnTIICARAGKDLVSSLTSGLLTI-GDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIM 1025
Cdd:PRK14037 177 LILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIINGKKRLM 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1026 GIGHRVKSINNPdmRVQILKDYVRQHFPATP----LLDYALEVEK--ITTSKKPNLILNVDGLIGVAFVDMLRNCGSFTr 1099
Cdd:PRK14037 255 GFGHRVYKTYDP--RAKIFKELAETLIERNSeakkYFEIAQKLEElgIKQFGSKGIYPNTDFYSGIVFYALGFPVYMFT- 331
|
170 180 190
....*....|....*....|....*....|....*...
gi 740086846 1100 eeadeyidigalnGIFVLGRSMGFIGHYL----DQKRL 1133
Cdd:PRK14037 332 -------------ALFALSRTLGWLAHIIeyveEQHRL 356
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
1013-1130 |
2.54e-03 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 41.48 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 1013 FVNKMKKEGKLIMGIGHRVKSINNPdmRVQILKDYVRQ---HFPATPLLDYALEVEKITTSK-KPNLIL-NVDGLIGVAF 1087
Cdd:PRK14036 243 YLDERLANKQKIMGFGHREYKVKDP--RATILQKLAEElfaRFGHDEYYEIALELERVAEERlGPKGIYpNVDFYSGLVY 320
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 740086846 1088 vdmlRNCGsftreeadeyIDIGALNGIFVLGRSMGFIGHYLDQ 1130
Cdd:PRK14036 321 ----RKLG----------IPRDLFTPIFAIARVAGWLAHWREQ 349
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
60-261 |
4.24e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.94 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 60 ISEQTGKELLYKFICTTSaiqnRFKYARvTPDT--DWARLLQDHPWllsqnlVVKPDQLIKRRGKLGLVGVNLTLDGVKS 137
Cdd:pfam08442 2 LHEYQAKEIFAKYGIPVP----RGEVAT-SPEEaeEIAKKLGGKVY------VVKAQVLAGGRGKAGGVKLAKSPEEAKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740086846 138 WLKPRLGQEaTVGKATGFL----KNFLIEPFVPhsQAEEFYVCIYATRE--GDYVLFHHEGGVDVGDVDAKaqkllvgvd 211
Cdd:pfam08442 71 VAKEMLGKN-LVTKQTGPDgqpvNKVLVEEALD--IKKEYYLSIVLDRAskGPVIIASTEGGVDIEEVAAK--------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740086846 212 eklNPEDIKK-HLLVH---APEDKKEIL-------------ASFISGLFNFYEDLYFTYLEINPLVV 261
Cdd:pfam08442 139 ---NPEKIHKfPIDPLkglTPYQAREIAfklglpgelikqaADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
| |
