|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
492-1097 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 904.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 492 LFEDDTKAIIWGQQAKAIQGMLDFDYVCRRSSPSVVASTYPfTGDNKQKYYFGQKEILIPAYKSMAKAFATHPDASIMVT 571
Cdd:PLN02522 6 LFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 572 FASMRSVFETVLEALEFPQIKVIAIIAEGVPENQTRKLLKIAHDRGVTLVGPATVGGIKPGCFKIGNTGGMMDNILASKL 651
Cdd:PLN02522 85 FASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 652 YRPGSVAYVSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVGGVEEYKIVDLL 731
Cdd:PLN02522 165 YRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 732 KQKKVTKPLVAWCIGTCADHITSEVQFGHAGASANALGETAACKNAALRASGALVPESFDDLGNKIRQTYDELVSQQIIV 811
Cdd:PLN02522 245 KQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKII 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 812 PQPEVPPPAVPMDYAWARELGLIRKPASFMTSICDERGEELNYAGVPITKVLESDMGIGGVLGLLWFQKRLPPHANKFIE 891
Cdd:PLN02522 325 PVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFIE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 892 ICLMLTADHGPAVSGAHNTIVCARAGKDLISSLTSGLLTIGDRFGGALDGAARQFSEAFDQGWSANQFVSEMRKKGKHIM 971
Cdd:PLN02522 405 MCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRVP 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 972 GIGHRVKSINNPDKRVEILKRFAMDkkeFAQETPLFEYALEVEKITTAKKPNLILNVDGAIAILFVDILRHSGMFTKQEA 1051
Cdd:PLN02522 485 GIGHRIKSRDNRDKRVELLQKYART---HFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17551266 1052 EETIEIGSLNGLFVLGRSIGFIGHYLDQSRLKQGLYRHPWDDISYI 1097
Cdd:PLN02522 562 DEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-431 |
4.85e-118 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 370.64 E-value: 4.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 1 MSAKAVSELSGKEVLYKYFEP-SGLLSAPHAFHVKAGENFDEIANKYEWLArDNKGVIKPDQLIKRRGKLGLVKIGTPQE 79
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRlAGIDLPIRSAQVTESTDFNELANKEPWLS-STKLVVKPDMLFGKRGKSGLVALNLDLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 80 LKAWF--EKTGDSyVRVGQTEGRLHTFIVEPFCAHteKDEMYIAIYSERFRDVIMFYEQGGVDIGDVEEKARTVSVPVql 157
Cdd:PLN02235 80 QVATFvkERLGKE-VEMGGCKGPITTFIVEPFVPH--DQEFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPT-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 158 nENAMTPsdEELTTLLG--PLKDSDIVRRFVVELYKAYKDLHFTYLEINPFVLLNNQIHVLDLAARLDETANFLCADKWk 235
Cdd:PLN02235 155 -EAPLTS--EICAPLIAtlPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKW- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 236 srltpyggpNHVEFPAPFGRDLTSEEQYISEMDAKTGASLKLTILNRKGRVWTMVAGGGASVVFTDTVCDLGGASELANY 315
Cdd:PLN02235 231 ---------GNIEFPLPFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 316 GEYSGDPSESQTYEYAKTLLSVmteGTPRPDGK--VLIIGGSIANFTNVAKTFGGIVRAFETFVSKLKEHKVTIFVRRGG 393
Cdd:PLN02235 302 AEYSGAPNEEEVLQYARVVIDC---ATANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGG 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 17551266 394 PNYQEGLRRIKDAATKLELPIHVFGPETHMTAIVGAAL 431
Cdd:PLN02235 379 PNYQKGLAKMRALGEEIGVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
255-432 |
8.34e-114 |
|
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: 350.02 E-value: 8.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 255 RDLTSEEQYISEMDAKTGASLKLTILNRKGRVWTMVAGGGASVVFTDTVCDLGGASELANYGEYSGDPSESQTYEYAKTL 334
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 335 LSVMTEgTPRPDGKVLIIGGSIANFTNVAKTFGGIVRAFETFVSKLKEHKVTIFVRRGGPNYQEGLRRIKDAATKLELPI 414
Cdd:pfam16114 81 LDLMTR-EPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPI 159
|
170
....*....|....*...
gi 17551266 415 HVFGPETHMTAIVGAALG 432
Cdd:pfam16114 160 HVYGPETHMTGIVPMALG 177
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1096 |
2.00e-87 |
|
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: 281.38 E-value: 2.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 856 GVPITKVLEsDMGIGGVLGLLWFQKRLPPHANKFIEICLMLTADHGPAVSGAHNTIVCARAG-KDLISSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIG-KISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 935 FGGALDGAARQFSEAFDQG----WSANQFVSEMRKKGKHIMGIGHRVKSinNPDKRVEILKRFAmdkKEFAQETPLFEYA 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELA---RELGPAGPHLDYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 1011 LEVEKITTAKKP-NLILNVDGAIAILFVDIlrhsGMFTkqeaeetieiGSLNGLFVLGRSIGFIGHYLDQSRLKQGLYRH 1089
Cdd:cd06100 155 LAVEKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRH 220
|
....*..
gi 17551266 1090 PWDDISY 1096
Cdd:cd06100 221 PWDDIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
526-801 |
4.13e-45 |
|
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: 164.46 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 526 VVASTYPFTGdnkqkyyfGQKEILIPAYKSMAKAF-ATHPDASIMvtFASMRSVFETVLEALEfPQIKVIAIIAEGVPEN 604
Cdd:COG0074 34 VVAGVTPGKG--------GQTVLGVPVFDTVAEAVeETGADASVI--FVPPPFAADAILEAID-AGIKLIVCITEGIPVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 605 QTRKLLKIAHDRGVTLVGPATVGGIKPGCFKIGntggmmdnILASKLYRPGSVAYVSRSGGMSNELNNIISQNTNGVYEG 684
Cdd:COG0074 103 DMVRVKRYAKAKGTRLIGPNCPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 685 IAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVGGVEEYKIVDLLKqKKVTKPLVAWCIGTCAdhiTSEVQFGHAGAS 764
Cdd:COG0074 175 VGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIK-ENMTKPVVAYIAGRTA---PPGKRMGHAGAI 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 17551266 765 ANALGETAACKNAALRASGALVPESFDDLGNKIRQTY 801
Cdd:COG0074 251 ISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
660-785 |
1.46e-35 |
|
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: 131.23 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 660 VSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVG-GVEEYKIVDLLKQKKVTK 738
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17551266 739 ----PLVAWCIGTCADHITsevQFGHAGASANALGETAACKNAALRASGAL 785
Cdd:pfam00549 81 arelPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
883-1080 |
2.01e-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: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 883 PPHANKFIEICLMLTADHG-PAVSGAhnTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEaFDQGWSANQFV 960
Cdd:TIGR01800 163 TKEWEKAMDIALILYAEHEfNASTFA--ARVIASTLSDMYSAITAAIGALkGPLHGGANEAVMAMLDE-IGDPDKAEAWI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 961 SEMRKKGKHIMGIGHRVksINNPDKRVEILKRFAmdkKEFAQETP---LFEYALEVEKITTAKKpNLILNVDGAIAILFV 1037
Cdd:TIGR01800 240 RKALENKERIMGFGHRV--YKTYDPRAKILKEYA---KKLSAKEGsskWYEIAERLEDVMEEEK-GIYPNVDFFSASVYY 313
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17551266 1038 DILRHSGMFTKqeaeetieigslngLFVLGRSIGFIGHYLDQS 1080
Cdd:TIGR01800 314 MMGIPTDLFTP--------------IFAMSRVTGWTAHIIEQV 342
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-416 |
3.74e-11 |
|
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: 66.23 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 66 RGKLGLVKI-GTPQELKA----WFEKTgdsyVRVGQT--EGRL-HTFIVEPFCAHteKDEMYIAI----YSERFrdVIMF 133
Cdd:COG0045 54 RGKAGGVKLaKSPEEAREaaeeILGMT----LVTHQTgpKGKPvNKVLVEEGVDI--AKELYLSIlldrATRRP--VIMA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 134 YEQGGVDIgdvEEKART-----VSVPVqlnENAMTPSDEELTTLLGPLK-DSDIVRRFV---VELYKAYKDLHFTYLEIN 204
Cdd:COG0045 126 STEGGMDI---EEVAEEtpekiIKVPI---DPLVGLQPYQARELAFALGlPGKQVKQFAkilKKLYRAFVEKDASLVEIN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 205 PFVLL-NNQIHVLDlaAR--LDETANFlcadkwksRLtpyggPNHVEFpapfgRDLTSEEQ-----------YIsEMDak 270
Cdd:COG0045 200 PLVVTkDGRLVALD--AKvnFDDNALF--------RH-----PELAAL-----RDLSEEDPleveaskyglnYV-KLD-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 271 tgaslkltilnrkGRVWTMVAGGG---ASVvftDTVCDLGGasELANYGEYSGDPSESQTYEYAKTLLSvmtegtprpDG 347
Cdd:COG0045 257 -------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS---------DP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551266 348 KVLIIggsianFTNVaktFGGIVR----AfETFVSKLKEHKVT--IFVRRGGPNYQEGLRRIKDAAtkleLPIHV 416
Cdd:COG0045 310 NVKAI------LVNI---FGGITRcdvvA-EGIVAALKEVGLKvpVVVRLEGTNVEEGRKILAESG----LNIIA 370
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
9.62e-05 |
|
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: 42.50 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 492 LFEDDTKAIIWGQQAKAIQgMLDFDYVCRRSSPSVVAstYPFTGDNKQKYYFGqkeilIPAYKSMAKA-FATHPDASIMv 570
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTKFV--GGVYPGKVGPKVDG-----VPVYDSVAEApEETGVDVAVI- 71
|
90 100 110
....*....|....*....|....*....|.
gi 17551266 571 tFASMRSVFETVLEALEFPqIKVIAIIAEGV 601
Cdd:smart00881 72 -FVPAEAAPDAIDEAIEAG-IKGIVVITEGI 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02522 |
PLN02522 |
ATP citrate (pro-S)-lyase |
492-1097 |
0e+00 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 178137 [Multi-domain] Cd Length: 608 Bit Score: 904.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 492 LFEDDTKAIIWGQQAKAIQGMLDFDYVCRRSSPSVVASTYPfTGDNKQKYYFGQKEILIPAYKSMAKAFATHPDASIMVT 571
Cdd:PLN02522 6 LFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINP-GSEGFQKLFFGQEEIAIPVHGSIEAACKAHPTADVFIN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 572 FASMRSVFETVLEALEFPQIKVIAIIAEGVPENQTRKLLKIAHDRGVTLVGPATVGGIKPGCFKIGNTGGMMDNILASKL 651
Cdd:PLN02522 85 FASFRSAAASSMEALKQPTIRVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTLDNIIQCKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 652 YRPGSVAYVSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVGGVEEYKIVDLL 731
Cdd:PLN02522 165 YRPGSVGFVSKSGGMSNEMYNVIARVTDGIYEGIAIGGDVFPGSTLSDHVLRFNNIPQIKMIVVLGELGGRDEYSLVEAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 732 KQKKVTKPLVAWCIGTCADHITSEVQFGHAGASANALGETAACKNAALRASGALVPESFDDLGNKIRQTYDELVSQQIIV 811
Cdd:PLN02522 245 KQGKVSKPVVAWVSGTCARLFKSEVQFGHAGAKSGGDMESAQAKNKALKDAGAIVPTSFEALEAAIKETFEKLVEEGKII 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 812 PQPEVPPPAVPMDYAWARELGLIRKPASFMTSICDERGEELNYAGVPITKVLESDMGIGGVLGLLWFQKRLPPHANKFIE 891
Cdd:PLN02522 325 PVKEVTPPQIPEDLNSAIKSGKVRAPTHIVSTISDDRGEEPCYAGVPMSSIIEKDYGVGDVISLLWFKRSLPRYCTKFIE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 892 ICLMLTADHGPAVSGAHNTIVCARAGKDLISSLTSGLLTIGDRFGGALDGAARQFSEAFDQGWSANQFVSEMRKKGKHIM 971
Cdd:PLN02522 405 MCIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDAYDRGLTPYEFVEGMKKKGIRVP 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 972 GIGHRVKSINNPDKRVEILKRFAMDkkeFAQETPLFEYALEVEKITTAKKPNLILNVDGAIAILFVDILRHSGMFTKQEA 1051
Cdd:PLN02522 485 GIGHRIKSRDNRDKRVELLQKYART---HFPSVKYMEYAVQVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEI 561
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17551266 1052 EETIEIGSLNGLFVLGRSIGFIGHYLDQSRLKQGLYRHPWDDISYI 1097
Cdd:PLN02522 562 DEIVEIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYT 607
|
|
| PLN02235 |
PLN02235 |
ATP citrate (pro-S)-lyase |
1-431 |
4.85e-118 |
|
ATP citrate (pro-S)-lyase
Pssm-ID: 177879 [Multi-domain] Cd Length: 423 Bit Score: 370.64 E-value: 4.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 1 MSAKAVSELSGKEVLYKYFEP-SGLLSAPHAFHVKAGENFDEIANKYEWLArDNKGVIKPDQLIKRRGKLGLVKIGTPQE 79
Cdd:PLN02235 1 MARKKIREYDSKRLLKEHLKRlAGIDLPIRSAQVTESTDFNELANKEPWLS-STKLVVKPDMLFGKRGKSGLVALNLDLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 80 LKAWF--EKTGDSyVRVGQTEGRLHTFIVEPFCAHteKDEMYIAIYSERFRDVIMFYEQGGVDIGDVEEKARTVSVPVql 157
Cdd:PLN02235 80 QVATFvkERLGKE-VEMGGCKGPITTFIVEPFVPH--DQEFYLSIVSDRLGCSISFSECGGIEIEENWDKVKTIFLPT-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 158 nENAMTPsdEELTTLLG--PLKDSDIVRRFVVELYKAYKDLHFTYLEINPFVLLNNQIHVLDLAARLDETANFLCADKWk 235
Cdd:PLN02235 155 -EAPLTS--EICAPLIAtlPLEIRGKIEEFIKGVFAVFQDLDFTFLEMNPFTLVDGEPYPLDMRGELDDTAAFKNFKKW- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 236 srltpyggpNHVEFPAPFGRDLTSEEQYISEMDAKTGASLKLTILNRKGRVWTMVAGGGASVVFTDTVCDLGGASELANY 315
Cdd:PLN02235 231 ---------GNIEFPLPFGRVMSPTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 316 GEYSGDPSESQTYEYAKTLLSVmteGTPRPDGK--VLIIGGSIANFTNVAKTFGGIVRAFETFVSKLKEHKVTIFVRRGG 393
Cdd:PLN02235 302 AEYSGAPNEEEVLQYARVVIDC---ATANPDGRkrALLIGGGIANFTDVAATFNGIIRALREKESKLKAARMHIFVRRGG 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 17551266 394 PNYQEGLRRIKDAATKLELPIHVFGPETHMTAIVGAAL 431
Cdd:PLN02235 379 PNYQKGLAKMRALGEEIGVPIEVYGPEATMTGICKQAI 416
|
|
| Citrate_bind |
pfam16114 |
ATP citrate lyase citrate-binding; This is the citrate-binding domain of ATP citrate lyase. ... |
255-432 |
8.34e-114 |
|
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: 350.02 E-value: 8.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 255 RDLTSEEQYISEMDAKTGASLKLTILNRKGRVWTMVAGGGASVVFTDTVCDLGGASELANYGEYSGDPSESQTYEYAKTL 334
Cdd:pfam16114 1 RELSPEEAYIAELDAKTGASLKLTILNPKGRIWTMVAGGGASVVYADTIADLGGASELANYGEYSGAPSETQTYEYAKTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 335 LSVMTEgTPRPDGKVLIIGGSIANFTNVAKTFGGIVRAFETFVSKLKEHKVTIFVRRGGPNYQEGLRRIKDAATKLELPI 414
Cdd:pfam16114 81 LDLMTR-EPHPDGKVLIIGGGIANFTDVAATFKGIIRALREYKSKLKEHKVKIWVRRGGPNYQEGLRAMRALGEELGLPI 159
|
170
....*....|....*...
gi 17551266 415 HVFGPETHMTAIVGAALG 432
Cdd:pfam16114 160 HVYGPETHMTGIVPMALG 177
|
|
| CCL_ACL-C |
cd06100 |
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ... |
856-1096 |
2.00e-87 |
|
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: 281.38 E-value: 2.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 856 GVPITKVLEsDMGIGGVLGLLWFQKRLPPHANKFIEICLMLTADHGPAVSGAHNTIVCARAG-KDLISSLTSGLLTIGDR 934
Cdd:cd06100 1 GYDLSDLIG-KISFGDVLYLLLKGRLPTPYEARLLEALLVALADHGPATPSAHAARLTASAGpEDLQSAVAAGLLGIGDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 935 FGGALDGAARQFSEAFDQG----WSANQFVSEMRKKGKHIMGIGHRVKSinNPDKRVEILKRFAmdkKEFAQETPLFEYA 1010
Cdd:cd06100 80 FGGAGEGAARLFKEAVDSGdaldAAAAEFVAEYRAAKKRIPGFGHPVHK--NPDPRVPRLLELA---RELGPAGPHLDYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 1011 LEVEKITTAKKP-NLILNVDGAIAILFVDIlrhsGMFTkqeaeetieiGSLNGLFVLGRSIGFIGHYLDQSRLKQGLYRH 1089
Cdd:cd06100 155 LAVEKALTAAKGkPLPLNVDGAIAAILLDL----GFPP----------GALRGLFVLGRSPGLIAHALEEKRLGQPLYRH 220
|
....*..
gi 17551266 1090 PWDDISY 1096
Cdd:cd06100 221 PWDDIEY 227
|
|
| SucD |
COG0074 |
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ... |
526-801 |
4.13e-45 |
|
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: 164.46 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 526 VVASTYPFTGdnkqkyyfGQKEILIPAYKSMAKAF-ATHPDASIMvtFASMRSVFETVLEALEfPQIKVIAIIAEGVPEN 604
Cdd:COG0074 34 VVAGVTPGKG--------GQTVLGVPVFDTVAEAVeETGADASVI--FVPPPFAADAILEAID-AGIKLIVCITEGIPVL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 605 QTRKLLKIAHDRGVTLVGPATVGGIKPGCFKIGntggmmdnILASKLYRPGSVAYVSRSGGMSNELNNIISQNTNGVYEG 684
Cdd:COG0074 103 DMVRVKRYAKAKGTRLIGPNCPGIITPGECKLG--------IMPGHIFKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTC 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 685 IAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVGGVEEYKIVDLLKqKKVTKPLVAWCIGTCAdhiTSEVQFGHAGAS 764
Cdd:COG0074 175 VGIGGDPIIGTSFIDVLELFEEDPETEAIVMIGEIGGSAEEEAAEYIK-ENMTKPVVAYIAGRTA---PPGKRMGHAGAI 250
|
250 260 270
....*....|....*....|....*....|....*..
gi 17551266 765 ANALGETAACKNAALRASGALVPESFDDLGNKIRQTY 801
Cdd:COG0074 251 ISGGKGTAESKIEALEAAGVPVAESPSEIGELLKKAL 287
|
|
| Ligase_CoA |
pfam00549 |
CoA-ligase; This family includes the CoA ligases Succinyl-CoA synthetase alpha and beta chains, ... |
660-785 |
1.46e-35 |
|
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: 131.23 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 660 VSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVIRYQNDDRVKMIVLLGEVG-GVEEYKIVDLLKQKKVTK 738
Cdd:pfam00549 1 LVNGGTLAMEAMDLIKLAGGGPHNFIDLGGDAFTPTTRIDALKLEAADPEVKVILLDIVLGyGACEDPAGGLLKAIKEAR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 17551266 739 ----PLVAWCIGTCADHITsevQFGHAGASANALGETAACKNAALRASGAL 785
Cdd:pfam00549 81 arelPVVARVCGTEADPQG---RSGQAKALAESGVLIASSNNQALRAAGAV 128
|
|
| PTZ00187 |
PTZ00187 |
succinyl-CoA synthetase alpha subunit; Provisional |
550-805 |
7.07e-32 |
|
succinyl-CoA synthetase alpha subunit; Provisional
Pssm-ID: 240307 [Multi-domain] Cd Length: 317 Bit Score: 127.14 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 550 IPAYKSMAKAF-ATHPDASimVTFASMRSVFETVLEALEfPQIKVIAIIAEGVPENQTRKLLKIAHDRGVT-LVGPATVG 627
Cdd:PTZ00187 74 LPVFATVKEAKkATGADAS--VIYVPPPHAASAIIEAIE-AEIPLVVCITEGIPQHDMVKVKHALLSQNKTrLIGPNCPG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 628 GIKPGCFKIGntggmmdnILASKLYRPGSVAYVSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVIRYQND 707
Cdd:PTZ00187 151 IIKPGECKIG--------IMPGHIHKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPFNGTNFIDCLKLFLND 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 708 DRVKMIVLLGEVGGVEEYKIVDLLKQKKVTKPLVAWCIGTCAdhiTSEVQFGHAGASANALGETAACKNAALRASGALVP 787
Cdd:PTZ00187 223 PETEGIILIGEIGGTAEEEAAEWIKNNPIKKPVVSFIAGITA---PPGRRMGHAGAIISGGKGTAPGKIEALEAAGVRVV 299
|
250
....*....|....*...
gi 17551266 788 ESFDDLGNKIRQTYDELV 805
Cdd:PTZ00187 300 KSPAQLGKTMLEVMKKKG 317
|
|
| PRK05678 |
PRK05678 |
succinyl-CoA synthetase subunit alpha; Validated |
544-804 |
9.11e-29 |
|
succinyl-CoA synthetase subunit alpha; Validated
Pssm-ID: 180194 [Multi-domain] Cd Length: 291 Bit Score: 117.20 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 544 GQKEILIPAYKSMAKAF-ATHPDASimVTFASMRSVFETVLEALEfPQIKVIAIIAEGVPENQTRKLLKIAHDRGVTLVG 622
Cdd:PRK05678 45 GTTVLGLPVFNTVAEAVeATGANAS--VIYVPPPFAADAILEAID-AGIDLIVCITEGIPVLDMLEVKAYLERKKTRLIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 623 PATVGGIKPGCFKIGntggmmdnILASKLYRPGSVAYVSRSGGMSNELNNIISQNTNGVYEGIAIGGDRYPGSTYTDHVI 702
Cdd:PRK05678 122 PNCPGIITPGECKIG--------IMPGHIHKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTCVGIGGDPINGTNFIDVLE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 703 RYQNDDRVKMIVLLGEVGGVEEYKIVDLLKQkKVTKPLVAWCIGTCAdhiTSEVQFGHAGASANALGETAACKNAALRAS 782
Cdd:PRK05678 194 AFEEDPETEAIVMIGEIGGSAEEEAAEYIKA-NVTKPVVGYIAGVTA---PPGKRMGHAGAIISGGKGTAEEKKEALEAA 269
|
250 260
....*....|....*....|..
gi 17551266 783 GALVPESFDDLGNKIRQTYDEL 804
Cdd:PRK05678 270 GVKVARTPSEIGELLKEVLKGL 291
|
|
| PLN00125 |
PLN00125 |
Succinyl-CoA ligase [GDP-forming] subunit alpha |
544-803 |
8.68e-25 |
|
Succinyl-CoA ligase [GDP-forming] subunit alpha
Pssm-ID: 215066 [Multi-domain] Cd Length: 300 Bit Score: 106.20 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 544 GQKEILIPAYKSMAKAFA-THPDASIMVTFASMRSvfETVLEALEfPQIKVIAIIAEGVPENQTRKLLKIAHDRGVT-LV 621
Cdd:PLN00125 49 GTEHLGLPVFNTVAEAKAeTKANASVIYVPPPFAA--AAILEAME-AELDLVVCITEGIPQHDMVRVKAALNRQSKTrLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 622 GPATVGGIKPGCFKIGntggmmdnILASKLYRPGSVAYVSRSGGMSNELnniISQNTN---GVYEGIAIGGDRYPGSTYT 698
Cdd:PLN00125 126 GPNCPGIIKPGECKIG--------IMPGYIHKPGRIGIVSRSGTLTYEA---VFQTTAvglGQSTCVGIGGDPFNGTNFV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 699 DHVIRYQNDDRVKMIVLLGEVGGVEEYKIVDLLKQKKVTKPLVAWCIGTCAdhiTSEVQFGHAGASANALGETAACKNAA 778
Cdd:PLN00125 195 DCLEKFVKDPQTEGIILIGEIGGTAEEDAAAFIKESGTEKPVVAFIAGLTA---PPGRRMGHAGAIVSGGKGTAQDKIKA 271
|
250 260
....*....|....*....|....*
gi 17551266 779 LRASGALVPESFDDLGNKIRQTYDE 803
Cdd:PLN00125 272 LREAGVTVVESPAKIGVAMLEVFKE 296
|
|
| Citrate_synt |
pfam00285 |
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme. |
876-1079 |
8.99e-23 |
|
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: 101.43 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 876 LWFQKRLPPHANKFIEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEAFDQGw 954
Cdd:pfam00285 156 MLFGYEPDPEEARALDLYLILHADHEGNAS-TFTARVVASTLADPYSAIAAAIGALkGPLHGGANEAVLEMLEEIGSPD- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 955 SANQFVSEMRKKGK-HIMGIGHRV-KsinNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKIT----TAKKPNLILNV 1028
Cdd:pfam00285 234 EVEEYIRKVLNKGKeRIMGFGHRVyK---NYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVApedlYFVEKNLYPNV 310
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17551266 1029 DGAIAIlfvdILRHSG----MFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQ 1079
Cdd:pfam00285 311 DFYSGV----LYHALGiptdMFT--------------PLFAISRTAGWLAHWIEQ 347
|
|
| CS_ACL-C_CCL |
cd06099 |
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ... |
888-1079 |
2.52e-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: 96.25 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 888 KFIEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSE-AFDQGWSANQFVSEMRK 965
Cdd:cd06099 21 RAMDLALILHADHEGNAS-TFTARVVGSTGSDPYSAIAAAIGALkGPLHGGANEAVLKMLEEiGTPKNEPAEAYIRKKLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 966 KGKHIMGIGHRVKSinNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKP--NLILNVDGAIAILFVDILRHS 1043
Cdd:cd06099 100 SKRVIMGFGHRVYK--KYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVLYekKLYPNVDFYSGVLYKAMGFPT 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 17551266 1044 GMFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQ 1079
Cdd:cd06099 178 ELFT--------------PLFAVARAVGWLAHLIEQ 199
|
|
| citrate_synt |
cd06101 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
842-1088 |
6.88e-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: 96.61 E-value: 6.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 842 TSICDERGEE--LNYAGVPItKVLESDMGIGGVLGLLWFQKrLPPHANKF----------------IEICLMLTADHGPA 903
Cdd:cd06101 11 SEISVIDGDEggLRYRGYPI-EELAENSSFEEVAYLLLTGE-LPSYAENFlymlggeepdpefakaMDLALILHADHEGN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 904 VSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSE--------AFDQGWSAnqfvsemRKKGKHIMGIG 974
Cdd:cd06101 89 AS-TFTARVVGSTLSDPYSAIAAAIAALkGPLHGGANEAVLKMLEEigtpknepAEAYIRKK-------LNSKRVLMGFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 975 HRVKSinNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKP--NLILNVDGAIAILFVDILRHSGMFTKqeae 1052
Cdd:cd06101 161 HRVYK--KYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYekKLYPNVDFYSGVLYKAMGFPTELFTP---- 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 17551266 1053 etieigslngLFVLGRSIGFIGHYLDQSRLKQGLYR 1088
Cdd:cd06101 235 ----------LFAVSRAVGWLAHLIEQREDGQRIIR 260
|
|
| PRK06224 |
PRK06224 |
citryl-CoA lyase; |
842-1081 |
1.30e-19 |
|
citryl-CoA lyase;
Pssm-ID: 235748 [Multi-domain] Cd Length: 263 Bit Score: 89.93 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 842 TSICDERGEELNYAGVPITKVLESdMGIGGVLGLLWFQKRLPPHANKFIEICLMLTADHGPAVSgahntIVCAR----AG 917
Cdd:PRK06224 11 TSISDVTPEEIYVRGYDLEDLIGK-LSFTDMIFLLLRGRLPTPNEARLLDAVLVALVDHGLTPS-----AAAARmtasGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 918 KDLISSLTSGLLTIGDRFGGALDGAARQFSEAFDQGWS-------ANQFVSEMRKKGKHIMGIGHRVKSINNPdkRVEIL 990
Cdd:PRK06224 85 ESLQGAVAAGLLALGSVHGGAGEQAAELLQEIAAAADAgadldaaARAIVAEYRAAGKRVPGFGHPLHKPVDP--RAPRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 991 krfamdkKEFAQETPLF----EYALEVEK-ITTAKKPNLILNVDGAIAILFVDIlrhsGmftkqeaeetIEIGSLNGLFV 1065
Cdd:PRK06224 163 -------LALAREAGVAgrhcRLAEALEAaLAAAKGKPLPLNVDGAIAAILADL----G----------FPPALARGLFV 221
|
250
....*....|....*.
gi 17551266 1066 LGRSIGFIGHYLDQSR 1081
Cdd:PRK06224 222 ISRAAGLVAHVWEELQ 237
|
|
| citrate_synt_like_1 |
cd06118 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
888-1088 |
1.70e-17 |
|
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: 85.35 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 888 KFIEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEAFDQGwSANQFVSEMRKK 966
Cdd:cd06118 168 KAMDLALILHADHEGNAS-TFTARVVASTLSDMYSAIAAAIAALkGPLHGGANEAVLKMLLEIGTPE-NVEAYIWKKLAN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 967 GKHIMGIGHRVKSinNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKP--NLILNVDGAIAILFVDILRHSG 1044
Cdd:cd06118 246 KRRIMGFGHRVYK--TYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVLGekGIYPNVDFYSGVVYKALGFPTE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17551266 1045 MFTKqeaeetieigslngLFVLGRSIGFIGHYLDQSRLKQGLYR 1088
Cdd:cd06118 324 LFTP--------------LFAVSRAVGWLAHIIEYRENNQRLIR 353
|
|
| GltA |
COG0372 |
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ... |
891-1088 |
4.45e-15 |
|
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: 78.60 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 891 EICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFsEAFDQGWSANQFVSEMRKKGKH 969
Cdd:COG0372 185 DLLLILHADHEQNAS-TFTARVVASTLADLYSAIAAAIGALkGPLHGGANEAVLEML-EEIGSPDNVEEYIRKALDKKER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 970 IMGIGHRV-KsinNPDKRVEILKRFAmdkKEFAQET---PLFEYALEVEKITTAKKP----NLILNVDGAIAIlfvdILR 1041
Cdd:COG0372 263 IMGFGHRVyK---NYDPRAKILKEAA---EELLEELgddPLLEIAEELEEVALEDEYfiekKLYPNVDFYSGI----VYH 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17551266 1042 HSG----MFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQsRLKQGLYR 1088
Cdd:COG0372 333 ALGiptdMFT--------------PIFAISRVAGWIAHWLEQ-RADNRIIR 368
|
|
| CoA_binding |
pfam02629 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
496-600 |
1.13e-11 |
|
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: 62.22 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 496 DTKAIIWGQQAKAIQGM-LDFDYVCRRSSPSVVASTYPFTGDNKQkyyfgqkeiLIPAYKSMAKAFATHpDASIMVTFAS 574
Cdd:pfam02629 3 DTKVIVIGAGGLGIQGLnYHFIQMLGYGIKMVFGVNPGKGGTEIL---------GIPVYNSVDELEEKT-GVDVAVITVP 72
|
90 100
....*....|....*....|....*.
gi 17551266 575 MRSVFETVLEALEfPQIKVIAIIAEG 600
Cdd:pfam02629 73 APFAQEAIDELVD-AGIKGIVNITPG 97
|
|
| cit_synth_II |
TIGR01800 |
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ... |
883-1080 |
2.01e-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: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 883 PPHANKFIEICLMLTADHG-PAVSGAhnTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEaFDQGWSANQFV 960
Cdd:TIGR01800 163 TKEWEKAMDIALILYAEHEfNASTFA--ARVIASTLSDMYSAITAAIGALkGPLHGGANEAVMAMLDE-IGDPDKAEAWI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 961 SEMRKKGKHIMGIGHRVksINNPDKRVEILKRFAmdkKEFAQETP---LFEYALEVEKITTAKKpNLILNVDGAIAILFV 1037
Cdd:TIGR01800 240 RKALENKERIMGFGHRV--YKTYDPRAKILKEYA---KKLSAKEGsskWYEIAERLEDVMEEEK-GIYPNVDFFSASVYY 313
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17551266 1038 DILRHSGMFTKqeaeetieigslngLFVLGRSIGFIGHYLDQS 1080
Cdd:TIGR01800 314 MMGIPTDLFTP--------------IFAMSRVTGWTAHIIEQV 342
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
66-416 |
3.74e-11 |
|
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: 66.23 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 66 RGKLGLVKI-GTPQELKA----WFEKTgdsyVRVGQT--EGRL-HTFIVEPFCAHteKDEMYIAI----YSERFrdVIMF 133
Cdd:COG0045 54 RGKAGGVKLaKSPEEAREaaeeILGMT----LVTHQTgpKGKPvNKVLVEEGVDI--AKELYLSIlldrATRRP--VIMA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 134 YEQGGVDIgdvEEKART-----VSVPVqlnENAMTPSDEELTTLLGPLK-DSDIVRRFV---VELYKAYKDLHFTYLEIN 204
Cdd:COG0045 126 STEGGMDI---EEVAEEtpekiIKVPI---DPLVGLQPYQARELAFALGlPGKQVKQFAkilKKLYRAFVEKDASLVEIN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 205 PFVLL-NNQIHVLDlaAR--LDETANFlcadkwksRLtpyggPNHVEFpapfgRDLTSEEQ-----------YIsEMDak 270
Cdd:COG0045 200 PLVVTkDGRLVALD--AKvnFDDNALF--------RH-----PELAAL-----RDLSEEDPleveaskyglnYV-KLD-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 271 tgaslkltilnrkGRVWTMVAGGG---ASVvftDTVCDLGGasELANYGEYSGDPSESQTYEYAKTLLSvmtegtprpDG 347
Cdd:COG0045 257 -------------GNIGCMVNGAGlamATM---DIIKLAGG--EPANFLDVGGGATAERVAEAFKIILS---------DP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551266 348 KVLIIggsianFTNVaktFGGIVR----AfETFVSKLKEHKVT--IFVRRGGPNYQEGLRRIKDAAtkleLPIHV 416
Cdd:COG0045 310 NVKAI------LVNI---FGGITRcdvvA-EGIVAALKEVGLKvpVVVRLEGTNVEEGRKILAESG----LNIIA 370
|
|
| Ec2MCS_like |
cd06108 |
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ... |
888-1079 |
3.13e-10 |
|
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: 63.09 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 888 KFIEICLMLTADHGPAVSgahnTI---VCARAGKDLISSLTSGLLTI-GDRFGGAlDGAARQFSEAFDQGWSANQFVSEM 963
Cdd:cd06108 166 KAMDVSLILYAEHEFNAS----TFaarVTASTLSDFYSAITGAIGTLrGPLHGGA-NEAAMELIERFKSPEEAEQGLLEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 964 RKKGKHIMGIGHRVKSINNPdkRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKpNLILNVD--GAIAILFVDILR 1041
Cdd:cd06108 241 LERKELIMGFGHRVYKEGDP--RSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWEEK-KLFPNLDfySASAYHFCGIPT 317
|
170 180 190
....*....|....*....|....*....|....*...
gi 17551266 1042 HsgMFTKqeaeetieigslngLFVLGRSIGFIGHYLDQ 1079
Cdd:cd06108 318 E--LFTP--------------IFVMSRVTGWAAHIMEQ 339
|
|
| PLN02456 |
PLN02456 |
citrate synthase |
879-1076 |
1.01e-09 |
|
citrate synthase
Pssm-ID: 215250 [Multi-domain] Cd Length: 455 Bit Score: 62.35 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 879 QKRLPPHANKFIEICLMLTADHGPAVSGAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEAfdqGWSAN 957
Cdd:PLN02456 237 SYKPDPRLARLLDLYFIIHADHEGGCSTAAARHLVGSSGVDPYTSVAAGVNALaGPLHGGANEAVLKMLKEI---GTVEN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 958 --QFVSEMRKKGKHIMGIGHRVksINNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKIT----TAKKPNLILNVDGA 1031
Cdd:PLN02456 314 ipEYVEGVKNSKKVLPGFGHRV--YKNYDPRAKCIREFALEVFKHVGDDPLFKVASALEEVAlldeYFKVRKLYPNVDFY 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17551266 1032 IAIlfvdILRHSG----MFTKqeaeetieigslngLFVLGRSIGFIGHY 1076
Cdd:PLN02456 392 SGV----LLRALGfpeeFFTV--------------LFAVSRAAGYLSQW 422
|
|
| BsCS-I_like |
cd06109 |
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ... |
802-1081 |
1.32e-09 |
|
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: 61.17 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 802 DELVSQQIIVP-QPEVPPPAVPMDYAWARELG---------------LIRKPASFMTSICD-ERGEElnyagvPItkvlE 864
Cdd:cd06109 62 AALAAARALPDvVAALLPALAGLDPMDALRALlallpdspdlatalrLLAAAPVITAALLRlSRGKQ------PI----A 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 865 SDMGIGGVLGLLWFQKRLPPHANKF--IEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDG 941
Cdd:cd06109 132 PDPSLSHAADYLRMLTGEPPSEAHVraLDAYLVTVADHGMNAS-TFTARVIASTEADLTSAVLGAIGALkGPLHGGAPGP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 942 AARQFSEAFDQGwSANQFVSEMRKKGKHIMGIGHRVKSINNPdkRVEILKRFAmdkKEFAQETPLFEYALEVEKITTA-- 1019
Cdd:cd06109 211 VLDMLDAIGTPE-NAEAWLREALARGERLMGFGHRVYRVRDP--RADVLKAAA---ERLGAPDERLEFAEAVEQAALAll 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17551266 1020 --KKPN--LILNVDGAIAIL--FVDILRhsGMFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQSR 1081
Cdd:cd06109 285 reYKPGrpLETNVEFYTALLleALGLPR--EAFT--------------PTFAAGRTAGWTAHVLEQAR 336
|
|
| BSuCS-II_like |
cd06110 |
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ... |
884-1079 |
5.36e-09 |
|
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: 59.21 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 884 PHANKFIEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEaFDQGWSANQFVSE 962
Cdd:cd06110 164 EEAARAFDVALILHADHELNAS-TFAARVVASTLSDMYSAVTAAIGALkGPLHGGANERVMKMLLE-IGSVDNVAAYVKD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 963 MRKKGKHIMGIGHRVksINNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKpNLILNVDGAIAILF------ 1036
Cdd:cd06110 242 KLANKEKIMGFGHRV--YKTGDPRAKHLREMSRRLGKETGEPKWYEMSEAIEQAMRDEK-GLNPNVDFYSASVYymlgip 318
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17551266 1037 VDIlrhsgmFTKqeaeetieigslngLFVLGRSIGFIGHYLDQ 1079
Cdd:cd06110 319 VDL------FTP--------------IFAISRVSGWCAHILEQ 341
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
8-208 |
3.94e-08 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 54.57 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 8 ELSGKEVLYKYfepsGLlSAPHAFHVKAGENFDEIANKYEwlarDNKGVIKPDQLIKRRGKLGLVKI-GTPQELKAWFEK 86
Cdd:pfam08442 4 EYQAKEIFAKY----GI-PVPRGEVATSPEEAEEIAKKLG----GKVYVVKAQVLAGGRGKAGGVKLaKSPEEAKEVAKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 87 TGDSYVRVGQTEGRLHTFIVEPFCAHTE-KDEMYIAIYSERF--RDVIMFYEQGGVDIGDVEEKA--RTVSVPVQLNENA 161
Cdd:pfam08442 75 MLGKNLVTKQTGPDGQPVNKVLVEEALDiKKEYYLSIVLDRAskGPVIIASTEGGVDIEEVAAKNpeKIHKFPIDPLKGL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17551266 162 MTPSDEELTTLLG-PLKDSDIVRRFVVELYKAYKDLHFTYLEINPFVL 208
Cdd:pfam08442 155 TPYQAREIAFKLGlPGELIKQAADIIKKLYKLFVEYDATLVEINPLVE 202
|
|
| PRK12350 |
PRK12350 |
citrate synthase 2; Provisional |
883-1082 |
7.67e-08 |
|
citrate synthase 2; Provisional
Pssm-ID: 237070 [Multi-domain] Cd Length: 353 Bit Score: 55.74 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 883 PPHAnKFIEICLMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLltigdrfgGALDG------AARQFS--EAFDQGW 954
Cdd:PRK12350 152 PAHV-AALDAYWVSAAEHGMNAS-TFTARVIASTGADVAAALSGAI--------GALSGplhggaPARVLPmlDAVERTG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 955 SANQFVSEMRKKGKHIMGIGHRVKSINNPdkRVEILKRFAmdkKEFAQetPLFEYALEVEKITTA----KKPNLIL--NV 1028
Cdd:PRK12350 222 DARGWVKGALDRGERLMGFGHRVYRAEDP--RARVLRATA---KRLGA--PRYEVAEAVEQAALAelreRRPDRPLetNV 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17551266 1029 DGAIAIL--FVDILRHsgMFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQSRL 1082
Cdd:PRK12350 295 EFWAAVLldFAGVPAH--MFT--------------AMFTCGRTAGWSAHILEQKRT 334
|
|
| PRK14037 |
PRK14037 |
citrate synthase; Provisional |
888-1082 |
8.31e-08 |
|
citrate synthase; Provisional
Pssm-ID: 184470 Cd Length: 377 Bit Score: 55.91 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 888 KFIEICLMLTADHG-PAVSGAhnTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEAFDQGWSANQFVSEMRK 965
Cdd:PRK14037 171 KAMDAALILYTDHEvPASTTA--ALVAASTLSDMYSCITAALAALkGPLHGGAAEEAFKQFVEIGDPNNVEMWFNDKIIN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 966 KGKHIMGIGHRVKSINNPdkRVEILKRFAmdkKEFAQETP----LFEYALEVEK--ITTAKKPNLILNVDGAIAILFVDI 1039
Cdd:PRK14037 249 GKKRLMGFGHRVYKTYDP--RAKIFKELA---ETLIERNSeakkYFEIAQKLEElgIKQFGSKGIYPNTDFYSGIVFYAL 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17551266 1040 LRHSGMFTkqeaeetieigslnGLFVLGRSIGFIGHYL----DQSRL 1082
Cdd:PRK14037 324 GFPVYMFT--------------ALFALSRTLGWLAHIIeyveEQHRL 356
|
|
| PRK14035 |
PRK14035 |
citrate synthase; Provisional |
894-1081 |
7.42e-07 |
|
citrate synthase; Provisional
Pssm-ID: 184468 [Multi-domain] Cd Length: 371 Bit Score: 52.84 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 894 LMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEAFDQGwSANQFVSEMRKKGKHIMG 972
Cdd:PRK14035 177 LVLHADHELNAS-TFTARCAVSSLSDMYSGVVAAVGSLkGPLHGGANERVMDMLSEIRSIG-DVDAYLDEKFANKEKIMG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 973 IGHRVksINNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKpNLILNVDGAIAILFVDILRHSGMFTKqeae 1052
Cdd:PRK14035 255 FGHRV--YKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEK-GLIPNVDFYSATVYHVMGIPHDLFTP---- 327
|
170 180
....*....|....*....|....*....
gi 17551266 1053 etieigslngLFVLGRSIGFIGHYLDQSR 1081
Cdd:PRK14035 328 ----------IFAVSRVAGWIAHILEQYK 346
|
|
| gltA |
PRK05614 |
citrate synthase; |
894-1079 |
1.79e-06 |
|
citrate synthase;
Pssm-ID: 180164 Cd Length: 419 Bit Score: 51.80 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 894 LMLTADHGP----------AVSGAhNTIVCARAGkdlISSLTsglltiGDRFGGALDGAARQFSEaFDQGWSANQFVSEM 963
Cdd:PRK05614 226 FILHADHEQnaststvrlaGSSGA-NPFACIAAG---IAALW------GPAHGGANEAVLKMLEE-IGSVDNIPEFIARA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 964 RKK--GKHIMGIGHRVksINNPDKRVEILKRFAMD-KKEFAQETPLFEYALEVEKITTA------KKpnLILNVDGAIAI 1034
Cdd:PRK05614 295 KDKndGFRLMGFGHRV--YKNYDPRAKIMRETCHEvLKELGLNDPLLEVAMELEEIALNdeyfieRK--LYPNVDFYSGI 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17551266 1035 lfvdILRHSG----MFTkqeaeetieigslnGLFVLGRSIGFIGHYLDQ 1079
Cdd:PRK05614 371 ----ILKALGiptsMFT--------------VIFALARTVGWIAHWNEM 401
|
|
| PRK14036 |
PRK14036 |
citrate synthase; Provisional |
884-1079 |
5.74e-06 |
|
citrate synthase; Provisional
Pssm-ID: 237591 [Multi-domain] Cd Length: 377 Bit Score: 49.96 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 884 PHANKFIEICLMLTADHGPAVSgAHNTIVCAragkdliSSLTSGLLTIGDRFG---GALDGAARQ-FSEAFDQGWSANQ- 958
Cdd:PRK14036 169 PLAARIFDRCLILHAEHTINAS-TFSARVTA-------STLTDPYAVIASAVGtlaGPLHGGANEdVLAMLEEIGSVENv 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 959 --FVSEMRKKGKHIMGIGHRVKSINNPdkRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAK-KPNLIL-NVDGAIAI 1034
Cdd:PRK14036 241 rpYLDERLANKQKIMGFGHREYKVKDP--RATILQKLAEELFARFGHDEYYEIALELERVAEERlGPKGIYpNVDFYSGL 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17551266 1035 LFVDILRHSGMFTKqeaeetieigslngLFVLGRSIGFIGHYLDQ 1079
Cdd:PRK14036 319 VYRKLGIPRDLFTP--------------IFAIARVAGWLAHWREQ 349
|
|
| citrate_synt_like_1_2 |
cd06113 |
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ... |
888-1017 |
1.58e-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: 48.80 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 888 KFIEICLMLTADHGpavsGAHN----TIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFS--EAFDQGWSANQFV 960
Cdd:cd06113 196 KLLDLCLVLHAEHG----GGNNstftTRVVSSSGTDTYSAIAAAIGSLkGPRHGGANIKVMEMLEdiKENVKDWTDEDEV 271
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551266 961 SE-----MRKK-GKH---IMGIGHRVKSINNPdkRVEILKRFAMD---KKEFAQETPLFEyalEVEKIT 1017
Cdd:cd06113 272 RAylrkiLNKEaFDKsglIYGMGHAVYTLSDP--RAVVLKKYARSlakEKGREEEFALYE---RIERLA 335
|
|
| CoA_binding |
smart00881 |
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ... |
492-601 |
9.62e-05 |
|
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: 42.50 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 492 LFEDDTKAIIWGQQAKAIQgMLDFDYVCRRSSPSVVAstYPFTGDNKQKYYFGqkeilIPAYKSMAKA-FATHPDASIMv 570
Cdd:smart00881 1 LLNPNTSVAVVGASGNLGS-FGLAVMRNLLEYGTKFV--GGVYPGKVGPKVDG-----VPVYDSVAEApEETGVDVAVI- 71
|
90 100 110
....*....|....*....|....*....|.
gi 17551266 571 tFASMRSVFETVLEALEFPqIKVIAIIAEGV 601
Cdd:smart00881 72 -FVPAEAAPDAIDEAIEAG-IKGIVVITEGI 100
|
|
| PRK12351 |
PRK12351 |
methylcitrate synthase; Provisional |
912-1079 |
1.38e-03 |
|
methylcitrate synthase; Provisional
Pssm-ID: 183463 [Multi-domain] Cd Length: 378 Bit Score: 42.22 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 912 VCARAGKDLISSLTSGLLTI-GDRFGGAlDGAARQFSEAFDQGWSANQFVSEMRKKGKHIMGIGHRVKSINNPdkRVEIL 990
Cdd:PRK12351 201 VIAGTGSDMYSAITGAIGALrGPKHGGA-NEVAFEIQQRYDTPDEAEADIRRRVENKEVVIGFGHPVYTISDP--RNKVI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 991 KRFAMDKKEFAQETPLFEYALEVEKITTAKKpNLILNVD--GAIAILFVDIlrHSGMFTKqeaeetieigslngLFVLGR 1068
Cdd:PRK12351 278 KEVAKKLSKEAGDTKLYDIAERLETVMWEEK-KMFPNLDwfSAVSYHMMGV--PTAMFTP--------------LFVISR 340
|
170
....*....|.
gi 17551266 1069 SIGFIGHYLDQ 1079
Cdd:PRK12351 341 TTGWAAHVIEQ 351
|
|
| PRK14034 |
PRK14034 |
citrate synthase; Provisional |
894-1079 |
2.89e-03 |
|
citrate synthase; Provisional
Pssm-ID: 184467 [Multi-domain] Cd Length: 372 Bit Score: 41.29 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 894 LMLTADHGPAVSgAHNTIVCARAGKDLISSLTSGLLTI-GDRFGGALDGAARQFSEaFDQGWSANQFVSEMRKKGKHIMG 972
Cdd:PRK14034 177 LVLHADHELNAS-TFTARVCVATLSDVYSGITAAIGALkGPLHGGANENVMKMLTE-IGEEENVESYIHNKLQNKEKIMG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551266 973 IGHRVksINNPDKRVEILKRFAMDKKEFAQETPLFEYALEVEKITTAKKpNLILNVDGAIAILFVDILRHSGMFTKqeae 1052
Cdd:PRK14034 255 FGHRV--YRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKEK-GLPPNVDFYSASVYHCLGIDHDLFTP---- 327
|
170 180
....*....|....*....|....*..
gi 17551266 1053 etieigslngLFVLGRSIGFIGHYLDQ 1079
Cdd:PRK14034 328 ----------IFAISRMSGWLAHILEQ 344
|
|
| |
