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Conserved domains on  [gi|381382448|dbj|BAL99264|]
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citrate synthase [Caldilinea aerophila DSM 14535 = NBRC 104270]

Protein Classification

citrate synthase family protein( domain architecture ID 475)

citrate synthase family protein similar to citrate synthase that 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

CATH:  1.10.580.10
EC:  2.3.-.-
Gene Ontology:  GO:0016746
PubMed:  3013232
SCOP:  3001050

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CS_ACL-C_CCL super family cl00416
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
42-425 0e+00

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.


The actual alignment was detected with superfamily member cd06116:

Pssm-ID: 469765  Cd Length: 384  Bit Score: 644.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  42 GTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENM 121
Cdd:cd06116    1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 122 TELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENF 201
Cdd:cd06116   81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 202 LYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTE 281
Cdd:cd06116  161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 282 IGDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPN 361
Cdd:cd06116  241 IGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDEYFISRKLYPN 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 362 VDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06116  321 VDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
 
Name Accession Description Interval E-value
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
42-425 0e+00

Chloroflexus aurantiacus (Ca) citrate synthase (CS)_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). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. 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. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.


Pssm-ID: 99869  Cd Length: 384  Bit Score: 644.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  42 GTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENM 121
Cdd:cd06116    1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 122 TELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENF 201
Cdd:cd06116   81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 202 LYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTE 281
Cdd:cd06116  161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 282 IGDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPN 361
Cdd:cd06116  241 IGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDEYFISRKLYPN 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 362 VDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06116  321 VDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
gltA PRK05614
citrate synthase;
1-417 0e+00

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 626.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   1 MSKNTFTIIDNRTGKSYEIPVeYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQL 80
Cdd:PRK05614   1 MADKKATLTLNGGEASVELPI-LKGTLGPDVIDIRKLYGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  81 AEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDV 160
Cdd:PRK05614  80 AEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 161 RLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTS 240
Cdd:PRK05614 160 REIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 241 VMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKKGE--FRLMGFGHRVYKNYDPRAK 318
Cdd:PRK05614 240 TVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNdgFRLMGFGHRVYKNYDPRAK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 319 IIKRIAYEVFEVTGMN-PLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWV 397
Cdd:PRK05614 320 IMRETCHEVLKELGLNdPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWN 399
                        410       420
                 ....*....|....*....|
gi 381382448 398 ELITDPEQKIARPRQIYLGY 417
Cdd:PRK05614 400 EMHSDPEQKIGRPRQLYTGY 419
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
46-428 0e+00

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: 591.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  46 YDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELF 125
Cdd:COG0372   13 VDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 126 HAFRYDAHPMGMMISALAFMSTLHKEASRVDdPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYML 205
Cdd:COG0372   93 DGFPRDAHPMDVLRTAVSALGAFDPDADDID-PEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAENFLYML 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 206 dymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDV 285
Cdd:COG0372  172 -----FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 286 KNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPNVDFY 365
Cdd:COG0372  247 DNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEDEYFIEKKLYPNVDFY 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381382448 366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:COG0372  327 SGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRAD--NRIIRPRQIYVGPEDRDYVPIEER 387
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
14-422 0e+00

citrate synthase I (hexameric type); This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes. [Energy metabolism, TCA cycle]


Pssm-ID: 273811  Cd Length: 412  Bit Score: 541.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   14 GKSYEIPVeYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLL 93
Cdd:TIGR01798   1 NKSVELPI-YSGTLGPDVIDIRKLYKQTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   94 IFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLP 173
Cdd:TIGR01798  80 LYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  174 TVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPY 253
Cdd:TIGR01798 160 TLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  254 SAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVK--KGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVT 331
Cdd:TIGR01798 240 ACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKdkNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  332 GM--NPLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIAR 409
Cdd:TIGR01798 320 GLhdDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGR 399
                         410
                  ....*....|...
gi 381382448  410 PRQIYLGYDYRDY 422
Cdd:TIGR01798 400 PRQLYTGETQRDY 412
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
49-411 0e+00

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: 518.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   49 GYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAF 128
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  129 RYDAHPMGMMISALAFMSTLHKEAsrVDDPDVRLKQIYR--ILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLd 206
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEA--ISDKADYWENALRddLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYML- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  207 ymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVK 286
Cdd:pfam00285 158 ----FGYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  287 NVPAYIERVK-KGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPNVDFY 365
Cdd:pfam00285 234 EVEEYIRKVLnKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 381382448  366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPR 411
Cdd:pfam00285 314 SGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLAD--NRIIRPR 357
Cit_synThplmales NF041157
citrate synthase;
47-429 9.98e-113

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 335.44  E-value: 9.98e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  47 DPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFH 126
Cdd:NF041157   4 SKGLENVFIKYTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 127 AFRYDAHPMGMMISALAFMSTlhKEASRVDDPDVRLKQIyRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLD 206
Cdd:NF041157  84 SLPRDSDALAMMETAFSALAS--IENYKWNKENDREKAL-KIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 207 YMHQTKYEVnpvlaKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVK 286
Cdd:NF041157 161 GRKPSEEEI-----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 287 NVPAYI-ERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALedEYFISRKLYPNVDFY 365
Cdd:NF041157 236 NVEKWFnENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPNTDFY 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpEQKIARPRQIYLGYDYRDYVPIEQRG 429
Cdd:NF041157 314 SGIVFYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEE-QHRLIRPRALYVGPEKRDFVPIDERK 376
 
Name Accession Description Interval E-value
CaCS_like cd06116
Chloroflexus aurantiacus (Ca) citrate synthase (CS)_like. CS catalyzes the condensation of ...
42-425 0e+00

Chloroflexus aurantiacus (Ca) citrate synthase (CS)_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). This group is similar to gram-negative Escherichia coli (Ec) CS (type II, gltA) and Arabidopsis thaliana (Ath) peroxisomal (Per) CS. However EcCS and AthPerCS are not found in this group. 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. C. aurantiacus is a gram-negative thermophilic green gliding bacterium, its CS belonging to this group may be a type I CS; it is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group.


Pssm-ID: 99869  Cd Length: 384  Bit Score: 644.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  42 GTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENM 121
Cdd:cd06116    1 GLMTYDPAYLNTASCKSAITYIDGEKGILRYRGYPIEQLAEQSSYLEVAYLLLHGELPTKERLAQWVYDITRHTMTHENL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 122 TELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENF 201
Cdd:cd06116   81 KKFMDGFRYDAHPMGILISSVAALSTFYPEAKNIGDEEQRNKQIIRLIGKMPTIAAFAYRHRLGLPYVLPDNDLSYTGNF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 202 LYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTE 281
Cdd:cd06116  161 LSMLFKMTEPKYEPNPVLAKALDVLFILHADHEQNCSTSAMRSVGSSRADPYTAVAAAVAALYGPLHGGANEAVLRMLQQ 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 282 IGDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPN 361
Cdd:cd06116  241 IGSPKNIPDFIETVKQGKERLMGFGHRVYKNYDPRARIIKKIADEVFEATGRNPLLDIAVELEKIALEDEYFISRKLYPN 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 362 VDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06116  321 VDFYSGLIYQALGFPTEAFTVLFAIPRTSGWLAQWIEMLRDPEQKIARPRQVYTGPRDRDYVPI 384
gltA PRK05614
citrate synthase;
1-417 0e+00

citrate synthase;


Pssm-ID: 180164  Cd Length: 419  Bit Score: 626.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   1 MSKNTFTIIDNRTGKSYEIPVeYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQL 80
Cdd:PRK05614   1 MADKKATLTLNGGEASVELPI-LKGTLGPDVIDIRKLYGSTGYFTYDPGFTSTASCESKITYIDGDKGILLYRGYPIEQL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  81 AEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDV 160
Cdd:PRK05614  80 AEKSDFLEVCYLLLYGELPTAEQKAEFDTTVTRHTMVHEQLKRFFRGFRRDAHPMAVLCGVVGALSAFYHDSLDINDPEH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 161 RLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTS 240
Cdd:PRK05614 160 REIAAIRLIAKMPTLAAMAYKYSIGQPFVYPRNDLSYAENFLRMMFATPCEEYEVNPVLVRALDRIFILHADHEQNASTS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 241 VMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKKGE--FRLMGFGHRVYKNYDPRAK 318
Cdd:PRK05614 240 TVRLAGSSGANPFACIAAGIAALWGPAHGGANEAVLKMLEEIGSVDNIPEFIARAKDKNdgFRLMGFGHRVYKNYDPRAK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 319 IIKRIAYEVFEVTGMN-PLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWV 397
Cdd:PRK05614 320 IMRETCHEVLKELGLNdPLLEVAMELEEIALNDEYFIERKLYPNVDFYSGIILKALGIPTSMFTVIFALARTVGWIAHWN 399
                        410       420
                 ....*....|....*....|
gi 381382448 398 ELITDPEQKIARPRQIYLGY 417
Cdd:PRK05614 400 EMHSDPEQKIGRPRQLYTGY 419
EcCS_like cd06114
Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl ...
24-416 0e+00

Escherichia coli (Ec) citrate synthase (CS) GltA_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). 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 including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding.


Pssm-ID: 99867  Cd Length: 400  Bit Score: 617.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  24 SAIRARDLRQikvhpdEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQ 103
Cdd:cd06114   11 KVIDISSLRK------KTGVFTYDPGFMNTASCESAITYIDGEKGILRYRGYPIEQLAEKSSFLEVCYLLLYGELPTAEQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 104 LAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHR 183
Cdd:cd06114   85 LQEFREEITRHTLVHEQMKRFFNGFPRDAHPMAILSAMVNALSAFYPDSLDVNDPEQRELAAIRLIAKVPTIAAMAYRYS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 184 IGRPFNYPNADMGYTENFLYML-DYMHQtKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAA 262
Cdd:cd06114  165 IGQPFIYPDNDLSYVENFLHMMfAVPYE-PYEVDPVVVKALDTILILHADHEQNASTSTVRMVGSSGANLFASISAGIAA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 263 LFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVK--KGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMN-PLIDI 339
Cdd:cd06114  244 LWGPLHGGANEAVLEMLEEIGSVGNVDKYIAKAKdkNDPFRLMGFGHRVYKNYDPRAKILKKTCDEVLAELGKDdPLLEI 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 381382448 340 AVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIYLG 416
Cdd:cd06114  324 AMELEEIALKDDYFIERKLYPNVDFYSGIILRALGIPTEMFTVLFALGRTPGWIAQWREMHEDPELKIGRPRQLYTG 400
AthCS_per_like cd06115
Arabidopsis thaliana (Ath) peroxisomal (Per) CS_like. CS catalyzes the condensation of acetyl ...
22-424 0e+00

Arabidopsis thaliana (Ath) peroxisomal (Per) CS_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). 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 three Arabidopsis peroxisomal CS proteins, CYS1, -2, and -3 which are involved in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and is thought to be located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99868  Cd Length: 410  Bit Score: 612.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  22 EYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTK 101
Cdd:cd06115    1 DHGTVKATDFKKIKAGKDDKGLRLYDPGYLNTAVVRSKISYIDGDKGILRYRGYPIEELAEKSTFLEVAYLLIYGNLPTK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 102 QQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRV-------DDPDVRLKQIYRILGKLPT 174
Cdd:cd06115   81 SQLSDWEFAVSQHTAVPTGVLDMIKSFPHDAHPMGMLVSAISALSAFHPEANPAlagqdiyKNKQVRDKQIVRILGKAPT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 175 VAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYS 254
Cdd:cd06115  161 IAAAAYRRRAGRPPNLPSQDLSYTENFLYMLDSLGERKYKPNPRLARALDILFILHAEHEMNCSTAAVRHLASSGVDVYT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 255 AMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMN 334
Cdd:cd06115  241 AVAGAVGALYGPLHGGANEAVLRMLAEIGTVENIPAFIEGVKNRKRKLSGFGHRVYKNYDPRAKIIKKLADEVFEIVGKD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 335 PLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIY 414
Cdd:cd06115  321 PLIEIAVALEKAALSDEYFVKRKLYPNVDFYSGLIYRAMGFPTDFFPVLFAIPRMAGYLAHWRESLDDPDTKIMRPQQLY 400
                        410
                 ....*....|
gi 381382448 415 LGYDYRDYVP 424
Cdd:cd06115  401 TGVWLRHYVP 410
GltA COG0372
Citrate synthase [Energy production and conversion]; Citrate synthase is part of the Pathway ...
46-428 0e+00

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: 591.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  46 YDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELF 125
Cdd:COG0372   13 VDPGLEGVVAGETAISYIDGEKGILRYRGYPIEDLAEKSSFEEVAYLLLYGELPTKEELAEFKAELARHRELPEEVKEFL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 126 HAFRYDAHPMGMMISALAFMSTLHKEASRVDdPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYML 205
Cdd:COG0372   93 DGFPRDAHPMDVLRTAVSALGAFDPDADDID-PEARLEKAIRLIAKLPTIAAYAYRYRRGLPPVYPDPDLSYAENFLYML 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 206 dymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDV 285
Cdd:COG0372  172 -----FGEEPDPEEARALDLLLILHADHEQNASTFTARVVASTLADLYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSP 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 286 KNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPNVDFY 365
Cdd:COG0372  247 DNVEEYIRKALDKKERIMGFGHRVYKNYDPRAKILKEAAEELLEELGDDPLLEIAEELEEVALEDEYFIEKKLYPNVDFY 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381382448 366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:COG0372  327 SGIVYHALGIPTDMFTPIFAISRVAGWIAHWLEQRAD--NRIIRPRQIYVGPEDRDYVPIEER 387
EcCS_AthCS-per_like cd06107
Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal ...
42-416 0e+00

Escherichia coli (Ec) citrate synthase (CS) gltA and Arabidopsis thaliana (Ath) peroxisomal (Per) CS_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). 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, including EcCS, are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding. C. aurantiacus is a gram-negative thermophilic green gliding bacterium; its CS belonging to this group may be a type I CS. It is not inhibited by NADH or 2-oxoglutarate and is inhibited by ATP. Both gram-positive and gram-negative bacteria are found in this group. This group also contains three Arabidopsis peroxisomal CS proteins, CYS-1, -2, and -3 which participate in the glyoxylate cycle. AthCYS1, in addition to a peroxisomal targeting sequence, has a predicted secretory signal peptide; it may be targeted to both the secretory pathway and the peroxisomes and perhaps is located in the extracellular matrix. AthCSY1 is expressed only in siliques and specifically in developing seeds. AthCSY2 and 3 are active during seed germination and seedling development and are thought to participate in the beta-oxidation of fatty acids.


Pssm-ID: 99860  Cd Length: 382  Bit Score: 584.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  42 GTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENM 121
Cdd:cd06107    1 GLRVYDPGYLNTAVCESSITYIDGDKGILLYRGYPIEQLAESSTYEEVAYLLLWGELPTQEQYDEFQRRLSEHMMVPESV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 122 TELFHAFRYDAHPMGMMISALAFMSTLHKEASRVD-------DPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNAD 194
Cdd:cd06107   81 HRLIQTFPRDAHPMGILCAGLSALSAFYPEAIPAHtgdlyqnNPEVRDKQIIRTLAKMPTIAAAAYCHRIGRPFVYPRAN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 195 MGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEA 274
Cdd:cd06107  161 LSYIENFLYMMGYVDQEPYEPNPRLARALDRLWILHADHEMNCSTSAARHTGSSLADPISCMAAAIAALYGPLHGGANEA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 275 VIRMLTEIGDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFI 354
Cdd:cd06107  241 ALKMLREIGTPENVPAFIERVKNGKRRLMGFGHRVYKNYDPRAKVIREILHEVLTEVEKDPLLKVAMELERIALEDEYFV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 381382448 355 SRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIARPRQIYLG 416
Cdd:cd06107  321 SRKLYPNVDFYSGFIYKALGFPPEFFTVLFAVARTSGWMAHWREMMEDPLQRIWRPRQVYTG 382
PLN02456 PLN02456
citrate synthase
3-428 0e+00

citrate synthase


Pssm-ID: 215250 [Multi-domain]  Cd Length: 455  Bit Score: 556.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   3 KNTFTIIDNRTGKSYEIPV-EYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLA 81
Cdd:PLN02456  20 SGSLTIVDNRTGKDYESPLsELGPVQAERLKKIKAGKDDLGLKTVDPGYRNTAPVLSEISLIDGDEGILRFRGYPIEELA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  82 EKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEAS-------R 154
Cdd:PLN02456 100 EKSPFEEVAYLLLYGNLPTKEQLADWEAELRQHSAVPEHVLDVIDALPHDAHPMTQLVSGVMALSTFSPDANaylrgqhK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 155 VDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHE 234
Cdd:PLN02456 180 YKSWEVRDEDIVRLIGKLPTLAAAIYRRMYGRGPVIPDNSLDYAENFLYMLGSLGDRSYKPDPRLARLLDLYFIIHADHE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 235 QNASTSVMR-AIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKKGEFRLMGFGHRVYKNY 313
Cdd:PLN02456 260 GGCSTAAARhLVGSSGVDPYTSVAAGVNALAGPLHGGANEAVLKMLKEIGTVENIPEYVEGVKNSKKVLPGFGHRVYKNY 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 314 DPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWL 393
Cdd:PLN02456 340 DPRAKCIREFALEVFKHVGDDPLFKVASALEEVALLDEYFKVRKLYPNVDFYSGVLLRALGFPEEFFTVLFAVSRAAGYL 419
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 381382448 394 AQWVELITDPEQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:PLN02456 420 SQWDEALGLPDERIMRPKQVYTGEWLRHYCPKAER 454
cit_synth_I TIGR01798
citrate synthase I (hexameric type); This model describes one of several distinct but closely ...
14-422 0e+00

citrate synthase I (hexameric type); This model describes one of several distinct but closely homologous classes of citrate synthase, the protein that brings carbon (from acetyl-CoA) into the TCA cycle. This form, class I, is known to be hexameric and allosterically inhibited by NADH in Escherichia coli, Acinetobacter anitratum, Azotobacter vinelandii, Pseudomonas aeruginosa, etc. In most species with a class I citrate synthase, a dimeric class II isozyme is found. The class II enzyme may act primarily on propionyl-CoA to make 2-methylcitrate or be bifunctional, may be found among propionate utilization enzymes, and may be constitutive or induced by propionate. Some members of this model group as class I enzymes, and may be hexameric, but have shown regulatory properties more like class II enzymes. [Energy metabolism, TCA cycle]


Pssm-ID: 273811  Cd Length: 412  Bit Score: 541.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   14 GKSYEIPVeYSAIRARDLRQIKVHPDEFGTLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLL 93
Cdd:TIGR01798   1 NKSVELPI-YSGTLGPDVIDIRKLYKQTGLFTFDPGFTSTASCESKITFIDGDKGILLYRGYPIDQLAEKSDYLEVCYLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   94 IFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVRLKQIYRILGKLP 173
Cdd:TIGR01798  80 LYGELPTAEQKDEFDDTVTRHTMVHEQVTRFFNGFRRDAHPMAVMVGVVGALSAFYHDALDINDPRHREISAIRLIAKIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  174 TVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPY 253
Cdd:TIGR01798 160 TLAAMSYKYSIGQPFVYPRNNLSYAENFLHMMFATPCEDYKVNPVLARAMDRIFILHADHEQNASTSTVRLAGSSGANPF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  254 SAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVK--KGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVT 331
Cdd:TIGR01798 240 ACIAAGIAALWGPAHGGANEAALKMLEEIGSVKNIDEFIKKVKdkNDPFRLMGFGHRVYKNYDPRAKVMRETCHEVLKEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  332 GM--NPLIDIAVELERVALEDEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEQKIAR 409
Cdd:TIGR01798 320 GLhdDPLFKLAMELEKIALNDPYFIERKLYPNVDFYSGIILKAMGIPTSMFTVIFALARTVGWISHWSEMISDPGQKIGR 399
                         410
                  ....*....|...
gi 381382448  410 PRQIYLGYDYRDY 422
Cdd:TIGR01798 400 PRQLYTGETQRDY 412
Citrate_synt pfam00285
Citrate synthase, C-terminal domain; This is the long, C-terminal part of the enzyme.
49-411 0e+00

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: 518.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   49 GYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAF 128
Cdd:pfam00285   1 GLRGVAAGETEISYIDGEKGILRYRGYDIEELAERSSFEEVAYLLLTGELPTKEELEEFSAELAAHRELPEDVLELLRAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  129 RYDAHPMGMMISALAFMSTLHKEAsrVDDPDVRLKQIYR--ILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLd 206
Cdd:pfam00285  81 PRDAHPMAVLRAAVSALAAFDPEA--ISDKADYWENALRddLIAKLPTIAAYIYRHRRGLPPIYPDPDLSYAENFLYML- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  207 ymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVK 286
Cdd:pfam00285 158 ----FGYEPDPEEARALDLYLILHADHEGNASTFTARVVASTLADPYSAIAAAIGALKGPLHGGANEAVLEMLEEIGSPD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  287 NVPAYIERVK-KGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFISRKLYPNVDFY 365
Cdd:pfam00285 234 EVEEYIRKVLnKGKERIMGFGHRVYKNYDPRAKILKEFAEELAEEGGDDPLLELAEELEEVAPEDLYFVEKNLYPNVDFY 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 381382448  366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPR 411
Cdd:pfam00285 314 SGVLYHALGIPTDMFTPLFAISRTAGWLAHWIEQLAD--NRIIRPR 357
citrate_synt_like_1 cd06118
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
48-414 1.69e-172

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: 486.72  E-value: 1.69e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  48 PGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHA 127
Cdd:cd06118    1 PGLEGVKAKETSISYIDGDEGILRYRGYDIEELAEKSSFEEVAYLLLYGKLPTKEELAEFKKKLASHRALPEHVVEILDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 128 FRYDAHPMGMMISALAFMSTLHKEAsRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDY 207
Cdd:cd06118   81 LPKNAHPMDVLRTAVSALGSFDPFA-RDKSPEARYEKAIRLIAKLPTIAANIYRNREGLEIIAPDPDLSYAENFLYMLFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 208 MhqtkyEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKN 287
Cdd:cd06118  160 E-----EPDPEEAKAMDLALILHADHEGNASTFTARVVASTLSDMYSAIAAAIAALKGPLHGGANEAVLKMLLEIGTPEN 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 288 VPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFisRKLYPNVDFYSG 367
Cdd:cd06118  235 VEAYIWKKLANKRRIMGFGHRVYKTYDPRAKILKELAEELAEEKGDDKLFEIAEELEEIALEVLGE--KGIYPNVDFYSG 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 381382448 368 IIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPeQKIARPRQIY 414
Cdd:cd06118  313 VVYKALGFPTELFTPLFAVSRAVGWLAHIIEYRENN-QRLIRPRAEY 358
PRK14036 PRK14036
citrate synthase; Provisional
46-429 5.26e-131

citrate synthase; Provisional


Pssm-ID: 237591 [Multi-domain]  Cd Length: 377  Bit Score: 382.38  E-value: 5.26e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  46 YDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELF 125
Cdd:PRK14036   4 YRPGLEGVPATQSSISYVDGQKGILEYRGYPIEELAEKSSFLETAYLLIWGELPTAEELEEFEQEVRMHRRVKYRIRDMM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 126 HAFRYDAHPMGMMISALAFMSTLHKEASrVDDPDVRLKQIYRILGKLPT-VAAFcyrHRIGRPFN--YPNADMGYTENFL 202
Cdd:PRK14036  84 KCFPETGHPMDALQASAAALGLFYSRRA-LDDPEYIRDAVVRLIAKIPTmVAAF---QLIRKGNDpiQPRDDLDYAANFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 203 YMLdymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEI 282
Cdd:PRK14036 160 YML-----TEREPDPLAARIFDRCLILHAEHTINASTFSARVTASTLTDPYAVIASAVGTLAGPLHGGANEDVLAMLEEI 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 283 GDVKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVAleDEYFISRKLYPNV 362
Cdd:PRK14036 235 GSVENVRPYLDERLANKQKIMGFGHREYKVKDPRATILQKLAEELFARFGHDEYYEIALELERVA--EERLGPKGIYPNV 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 381382448 363 DFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQRG 429
Cdd:PRK14036 313 DFYSGLVYRKLGIPRDLFTPIFAIARVAGWLAHWREQLGA--NRIFRPTQIYTGSHNRRYIPLEERS 377
citrate_synt_like_1_1 cd06112
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
46-425 6.69e-130

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: 99865  Cd Length: 373  Bit Score: 379.46  E-value: 6.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  46 YDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELF 125
Cdd:cd06112    1 YIPGLAGVPAAESSISYIDGKNGILEYRGYDIEELAEYSSFEEVALLLLDGDLPTAAELEEFDKELRQHRRVKYNIRDMM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 126 HAFRYDAHPMGMMISALAFMSTLH-KEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYM 204
Cdd:cd06112   81 KCFPETGHPMDMLQATVAALGMFYpKPEVLKPNPDYIDAATVKLIAKMPTLVAMWARIRNGDDPIEPRPDLDYAENFLYM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 205 LdymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGD 284
Cdd:cd06112  161 L-----FGEEPDPATAKILDACLILHAEHTMNASTFSALVTGSTLADPYAVISSAIGTLSGPLHGGANEDVLEMLEEIGS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 285 VKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTG-MNPLIDIAVELERVALedEYFISRKLYPNVD 363
Cdd:cd06112  236 PENVKAYLDKKLANKQKIWGFGHRVYKTKDPRATILQKLAEDLFAKMGeLSKLYEIALEVERLCE--ELLGHKGVYPNVD 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 381382448 364 FYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06112  314 FYSGIVYKELGIPADLFTPIFAVARVAGWLAHWKEQLGD--NRIFRPTQIYIGEIDRKYVPL 373
cit_synth_II TIGR01800
2-methylcitrate synthase/citrate synthase II; Members of this family are dimeric enzymes with ...
55-428 2.51e-120

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: 354.75  E-value: 2.51e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448   55 SCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHP 134
Cdd:TIGR01800   8 AGETALSTIDGSGGILTYRGYDIEDLAEHASFEEVAYLLLHGKLPTRSELRKFKTELAKLRGLPDEVIELIEALPAESHP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  135 MGMMISALAFMSTLHKEASRVDDPDVRLKQIyRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLdymhqTKYE 214
Cdd:TIGR01800  88 MDVLRTAVSYLGALDPEKFGHTPEEARDIAI-RLLAKLPTIVAYWYRIRHGGEIIAPKDDDSIAGNFLYML-----HGEE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  215 VNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIER 294
Cdd:TIGR01800 162 PTKEWEKAMDIALILYAEHEFNASTFAARVIASTLSDMYSAITAAIGALKGPLHGGANEAVMAMLDEIGDPDKAEAWIRK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  295 -VKKGEfRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEdeyfiSRKLYPNVDFYSGIIYQAM 373
Cdd:TIGR01800 242 aLENKE-RIMGFGHRVYKTYDPRAKILKEYAKKLSAKEGSSKWYEIAERLEDVMEE-----EKGIYPNVDFFSASVYYMM 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 381382448  374 RFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:TIGR01800 316 GIPTDLFTPIFAMSRVTGWTAHIIEQVEN--NRLIRPRADYVGPEERKYVPIEER 368
citrate_synt cd06101
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
48-414 3.65e-116

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: 340.06  E-value: 3.65e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  48 PGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTkqqlaeweykimhhtflhenmtelfha 127
Cdd:cd06101    1 PGLRGVAALESEISVIDGDEGGLRYRGYPIEELAENSSFEEVAYLLLTGELPS--------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 128 frydahpmgmmisalafmstlhkeasrvddpdvrlkqiyrilgklptvaafcyrhrigrpfnypnadmgYTENFLYMLDY 207
Cdd:cd06101   54 ---------------------------------------------------------------------YAENFLYMLGG 64
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 208 MhqtkyEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKN 287
Cdd:cd06101   65 E-----EPDPEFAKAMDLALILHADHEGNASTFTARVVGSTLSDPYSAIAAAIAALKGPLHGGANEAVLKMLEEIGTPKN 139
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 288 VPAYIERVKKGE--FRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFisRKLYPNVDFY 365
Cdd:cd06101  140 EPAEAYIRKKLNskRVLMGFGHRVYKKYDPRATVLKKFAEKLLKEKGLDPMFELAAELEKIAPEVLYE--KKLYPNVDFY 217
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 381382448 366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPeQKIARPRQIY 414
Cdd:cd06101  218 SGVLYKAMGFPTELFTPLFAVSRAVGWLAHLIEQREDG-QRIIRPRAEY 265
Cit_synThplmales NF041157
citrate synthase;
47-429 9.98e-113

citrate synthase;


Pssm-ID: 469069  Cd Length: 376  Bit Score: 335.44  E-value: 9.98e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  47 DPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFH 126
Cdd:NF041157   4 SKGLENVFIKYTSLTYIDGEKGILRYRGYDINDLVNNASFEEVIYLMLYGELPNRKELEEFKEKINESYEVPDHVISIIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 127 AFRYDAHPMGMMISALAFMSTlhKEASRVDDPDVRLKQIyRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLD 206
Cdd:NF041157  84 SLPRDSDALAMMETAFSALAS--IENYKWNKENDREKAL-KIIGKASTIVANVYRHKEGLKPRIPEPSESYAESFLRATF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 207 YMHQTKYEVnpvlaKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVK 286
Cdd:NF041157 161 GRKPSEEEI-----KAMNAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEAAFKQFLEIGSPD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 287 NVPAYI-ERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALedEYFISRKLYPNVDFY 365
Cdd:NF041157 236 NVEKWFnENIINGKKRLMGFGHRVYKTYDPRAKIFKEYAEKLASTNEAKKYLEIAEKLEELGI--KHFGSKGIYPNTDFY 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 366 SGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpEQKIARPRQIYLGYDYRDYVPIEQRG 429
Cdd:NF041157 314 SGIVFYSLGFPVYMFTSLFALSRVLGWLAHIIEYVEE-QHRLIRPRALYVGPEKRDFVPIDERK 376
BSuCS-II_like cd06110
Bacillus subtilis (Bs) citrate synthase (CS)-II_like. CS catalyzes the condensation of acetyl ...
56-416 2.93e-105

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: 315.75  E-value: 2.93e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  56 CKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPM 135
Cdd:cd06110    9 ADSKISYIDGDAGILIYRGYDIHDLAENSTFEEVAYLLWNGELPTAEELDAFKAQLAAERELPAEIIDLLKLLPKDAHPM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 136 GMMISALAFMSTLHKEASrVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLdymhqTKYEV 215
Cdd:cd06110   89 DVLRTAVSALALYDPEAD-DMSREANLRKAIRLIAKMPTIVAAFHRIRNGLEPVAPDPDLSHAANFLYML-----TGEKP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 216 NPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERV 295
Cdd:cd06110  163 SEEAARAFDVALILHADHELNASTFAARVVASTLSDMYSAVTAAIGALKGPLHGGANERVMKMLLEIGSVDNVAAYVKDK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 296 KKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAvelerVALEDEYFISRKLYPNVDFYSGIIYQAMRF 375
Cdd:cd06110  243 LANKEKIMGFGHRVYKTGDPRAKHLREMSRRLGKETGEPKWYEMS-----EAIEQAMRDEKGLNPNVDFYSASVYYMLGI 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 381382448 376 PPDMFTVLFTLGRAPGWLAQWVELITDPeqKIARPRQIYLG 416
Cdd:cd06110  318 PVDLFTPIFAISRVSGWCAHILEQYFNN--RLIRPRAEYVG 356
CS_ACL-C_CCL cd06099
Citrate synthase (CS), citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit ...
196-414 4.71e-98

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: 291.93  E-value: 4.71e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 196 GYTENFLYMLDYMhqtkyEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAV 275
Cdd:cd06099    1 SYAENFLYMLGGE-----EPDPEFARAMDLALILHADHEGNASTFTARVVGSTGSDPYSAIAAAIGALKGPLHGGANEAV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 276 IRMLTEIGDVKNVPAYIERVKKGE--FRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYF 353
Cdd:cd06099   76 LKMLEEIGTPKNEPAEAYIRKKLEskRVIMGFGHRVYKKYDPRATVLKKFAEELLKEDGDDPMFELAAELEKIAEEVLYE 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 381382448 354 isRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPeQKIARPRQIY 414
Cdd:cd06099  156 --KKLYPNVDFYSGVLYKAMGFPTELFTPLFAVARAVGWLAHLIEQLEDN-FKIIRPRSEY 213
PRK14037 PRK14037
citrate synthase; Provisional
58-428 4.49e-92

citrate synthase; Provisional


Pssm-ID: 184470  Cd Length: 377  Bit Score: 282.79  E-value: 4.49e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  58 SRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGM 137
Cdd:PRK14037  16 TNLTFIDGEKGILRYRGYNIEDLVNYGSYEETIYLMLYGELPTKKELNDLKEKLNEEYEVPQEVIDSIYLMPRDSDAIGL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 138 MISALAFMSTLHKEASRVD-DPDVRLKqiyrILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDYMHQTKYEVn 216
Cdd:PRK14037  96 MEAAFAALASIDKNFKWKEnDKEKAIS----IIAKMATIVANVYRRKEGNKPRIPEPSDSFAESFLLASFAREPTAEEI- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 217 pvlaKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYI-ERV 295
Cdd:PRK14037 171 ----KAMDAALILYTDHEVPASTTAALVAASTLSDMYSCITAALAALKGPLHGGAAEEAFKQFVEIGDPNNVEMWFnDKI 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 296 KKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTG-MNPLIDIAVELERVALEDeyFISRKLYPNVDFYSGIIYQAMR 374
Cdd:PRK14037 247 INGKKRLMGFGHRVYKTYDPRAKIFKELAETLIERNSeAKKYFEIAQKLEELGIKQ--FGSKGIYPNTDFYSGIVFYALG 324
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 381382448 375 FPPDMFTVLFTLGRAPGWLAQWVELITDpEQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:PRK14037 325 FPVYMFTALFALSRTLGWLAHIIEYVEE-QHRLIRPRALYVGPEHREYVPIDKR 377
PRK14034 PRK14034
citrate synthase; Provisional
70-429 1.77e-85

citrate synthase; Provisional


Pssm-ID: 184467 [Multi-domain]  Cd Length: 372  Bit Score: 265.86  E-value: 1.77e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  70 LRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYD-AHPMGMMISALAFMSTL 148
Cdd:PRK14034  25 LTYVGYNIDDLAENASFEEVVYLLWHRKLPNKQELAEFKEQLSENAKVPGEIIEHLKQYDLKkVHPMSVLRTAISMLGLY 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 149 HKEASRVDDPDVRLKQIyRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLdymhqTKYEVNPVLAKALDVLFI 228
Cdd:PRK14034 105 DEEAEIMDEEANYRKAV-RLQAKVPTIVAAFSRIRKGLDPVEPRKDLSLAANFLYML-----NGEEPDEVEVEAFNKALV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 229 LHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKKGEFRLMGFGHR 308
Cdd:PRK14034 179 LHADHELNASTFTARVCVATLSDVYSGITAAIGALKGPLHGGANENVMKMLTEIGEEENVESYIHNKLQNKEKIMGFGHR 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 309 VYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDeyfisRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGR 388
Cdd:PRK14034 259 VYRQGDPRAKHLREMSKRLTVLLGEEKWYNMSIKIEEIVTKE-----KGLPPNVDFYSASVYHCLGIDHDLFTPIFAISR 333
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 381382448 389 APGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQRG 429
Cdd:PRK14034 334 MSGWLAHILEQYEN--NRLIRPRADYVGPTHQVYVPIEERI 372
DsCS_like cd06111
Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-like. CS ...
58-421 3.06e-85

Cold-active citrate synthase (CS) from an Antarctic bacterial strain DS2-3R (Ds)-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). 2-methylcitrate synthase (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: 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. DsCS, compared with CS from the hyperthermophile Pyrococcus furiosus (not included in this group), has an increase in the size of surface loops, a higher proline content in the loop regions, a more accessible active site, and a higher number of intramolecular ion pairs. 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. For example, included in this group are Corynebacterium glutamicum (Cg) PrpC1 and -2, which are only synthesized during growth on propionate-containing medium, can use PrCoA, AcCoA and butyryl-CoA as substrates, and have comparable catalytic activity with AcCoA as the major CgCS (GltA, not included in this group).


Pssm-ID: 99864 [Multi-domain]  Cd Length: 362  Bit Score: 264.66  E-value: 3.06e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  58 SRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGM 137
Cdd:cd06111   11 TAISKVMPETNSLTYRGYPVQDLAENCSFEEVAYLLWNGELPNAAQLAEFSQRERSYRRLDRNLLSLIASLPKNCHPMDV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 138 MISALAFMSTLHKEAsRVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLdymhqTKYEVNP 217
Cdd:cd06111   91 LRTAVSVLGAEDSET-DDSSPDANLAKAIRLLAQLPTVVAADIRRRKGLDPIPPDSDLGIAENFLHMC-----FGEVPSP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 218 VLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYIERVKK 297
Cdd:cd06111  165 EVVRAFDVSLILYAEHSFNASTFTARVITSTLSDIYSAITGAIGALKGPLHGGANEAVMHMMLEIDDPEKAAQWMLDALA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 298 GEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAvelerVALEDEYFISRKLYPNVDFYSGIIYQAMRFPP 377
Cdd:cd06111  245 RKEKVMGFGHRVYKSGDSRVPTMEKALRRVAAVHDGQKWLAMY-----DALEDAMVAAKGIKPNLDFPAGPAYYLMGFDI 319
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 381382448 378 DMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRD 421
Cdd:cd06111  320 DFFTPIFVMARITGWTAHIMEQRAD--NALIRPLSEYNGPEQRP 361
PRK14033 PRK14033
bifunctional 2-methylcitrate synthase/citrate synthase;
51-425 2.99e-82

bifunctional 2-methylcitrate synthase/citrate synthase;


Pssm-ID: 237590 [Multi-domain]  Cd Length: 375  Bit Score: 257.57  E-value: 2.99e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  51 DNTAscksrITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRY 130
Cdd:PRK14033  19 DTTA-----ISKVVPETNSLTYRGYPVQDLAARCSFEEVAYLLWNGELPTDAELALFSQRERAYRRLDRSVLSLIDKLPT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 131 DAHPMGMMISALAFMSTLHKEASrVDDPDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMldymhq 210
Cdd:PRK14033  94 TCHPMDVVRTAVSYLGAEDPEAD-DSSPEANLAKALRLFAVLPTIVAADQRRRRGLDPIAPRSDLGYAENFLHM------ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 211 TKYEV-NPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVP 289
Cdd:PRK14033 167 CFGEVpEPEVVRAFEVSLILYAEHSFNASTFTARVITSTLSDIYSAVTGAIGALKGPLHGGANEAVMHTMLEIGDPARAA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 290 AYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEdeyfiSRKLYPNVDFYSGII 369
Cdd:PRK14033 247 EWLRDALARKEKVMGFGHRVYKHGDSRVPTMKAALRRVAAVRDGQRWLDIYEALEKAMAE-----ATGIKPNLDFPAGPA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 381382448 370 YQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPI 425
Cdd:PRK14033 322 YYLMGFDIDFFTPIFVMSRITGWTAHIMEQRAS--NALIRPLSEYNGPEQREVPPI 375
PRK14035 PRK14035
citrate synthase; Provisional
49-428 6.12e-82

citrate synthase; Provisional


Pssm-ID: 184468 [Multi-domain]  Cd Length: 371  Bit Score: 256.61  E-value: 6.12e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  49 GYDNTASCKSRITYIDGEKgiLRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAF 128
Cdd:PRK14035   6 GLEGVIAAETKISSIIDSQ--LTYAGYDIDDLAENASFEEVIFLLWNYRLPTEEELAHLKGKLRKYMTLNDRVYQHFEEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 129 -RYDAHPMGMMISALAFMSTLHKEASRVDDpDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLDY 207
Cdd:PRK14035  84 sTDHVHPMTALRTSVSYLAHFDPDAEEESD-EARYERAIRIQAKVASLVTAFARVRQGKEPLKPRPDLSYAANFLYMLRG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 208 MHQTKYEVnpvlaKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKN 287
Cdd:PRK14035 163 ELPTDIEV-----EAFNKALVLHADHELNASTFTARCAVSSLSDMYSGVVAAVGSLKGPLHGGANERVMDMLSEIRSIGD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 288 VPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDEYFIsrklyPNVDFYSG 367
Cdd:PRK14035 238 VDAYLDEKFANKEKIMGFGHRVYKDGDPRAKYLREMSRKITKGTGREELFEMSVKIEKRMKEEKGLI-----PNVDFYSA 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 381382448 368 IIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:PRK14035 313 TVYHVMGIPHDLFTPIFAVSRVAGWIAHILEQYKD--NRIMRPRAKYIGETNRKYIPIEER 371
Ec2MCS_like cd06108
Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the condensation of ...
70-425 1.54e-78

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: 247.60  E-value: 1.54e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  70 LRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLH 149
Cdd:cd06108   23 LTYRGYDIEDLAENATFEEVAYLLLYGKLPTRKQLDAYKTKLVALRRLPAALKTVLELIPKDSHPMDVMRTGCSMLGCLE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 150 KEASRVDDPDVRLkqiyRILGKLPTVAAFCYR-HRIGRPFNYPNADMGYTENFLYMLdymHQTKYEVNPVlaKALDVLFI 228
Cdd:cd06108  103 PENEFSQQYEIAI----RLLAIFPSILLYWYHySHSGKRIETETDEDSIAGHFLHLL---HGKKPGELEI--KAMDVSLI 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 229 LHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYI-ERVKKGEfRLMGFGH 307
Cdd:cd06108  174 LYAEHEFNASTFAARVTASTLSDFYSAITGAIGTLRGPLHGGANEAAMELIERFKSPEEAEQGLlEKLERKE-LIMGFGH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 308 RVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEdeyfiSRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLG 387
Cdd:cd06108  253 RVYKEGDPRSDIIKKWSKKLSEEGGDPLLYQISERIEEVMWE-----EKKLFPNLDFYSASAYHFCGIPTELFTPIFVMS 327
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 381382448 388 RAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06108  328 RVTGWAAHIMEQRAN--NRLIRPSADYIGPEPRPFVPI 363
BsCS-I_like cd06109
Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl ...
48-416 1.24e-76

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: 242.21  E-value: 1.24e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  48 PGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHA 127
Cdd:cd06109    1 PGLEGVVAAETVLSDVDGEAGRLIIRGYSVEDLAGSASFEDVAALLWNGFFPDLPELEEFRAALAAARALPDVVAALLPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 128 frydAHPMGMMiSAL-AFMSTLHkeasrvDDPDvrLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGYTENFLYMLd 206
Cdd:cd06109   81 ----LAGLDPM-DALrALLALLP------DSPD--LATALRLLAAAPVITAALLRLSRGKQPIAPDPSLSHAADYLRML- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 207 ymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVK 286
Cdd:cd06109  147 ----TGEPPSEAHVRALDAYLVTVADHGMNASTFTARVIASTEADLTSAVLGAIGALKGPLHGGAPGPVLDMLDAIGTPE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 287 NVPAYI-ERVKKGEfRLMGFGHRVYKNYDPRAKIIKRIAYEVFevtGMNPLIDIAVELERVALE--DEYFISRKLYPNVD 363
Cdd:cd06109  223 NAEAWLrEALARGE-RLMGFGHRVYRVRDPRADVLKAAAERLG---APDERLEFAEAVEQAALAllREYKPGRPLETNVE 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 381382448 364 FYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLG 416
Cdd:cd06109  299 FYTALLLEALGLPREAFTPTFAAGRTAGWTAHVLEQART--GRLIRPQSRYVG 349
PRK12349 PRK12349
citrate synthase;
43-419 1.24e-67

citrate synthase;


Pssm-ID: 237069 [Multi-domain]  Cd Length: 369  Bit Score: 219.59  E-value: 1.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  43 TLSYDPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMT 122
Cdd:PRK12349   2 EEKFSPGLDGVIAAETKISFLDTVKGEIVIQGYDLIELSKTKEYLDIVHLLLEEHLPNEDEKATLEKKLKEEYAVPEGVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 123 ELFHAFRYDAHPMGMM---ISALAFMSTlhkeasRVDD--PDVRLKQIYRILGKLPTVAAFCYRHRIGRPFNYPNADMGY 197
Cdd:PRK12349  82 NILKALPKETHPMDGLrtgVSALAGYDN------DIEDrsLEVNKSRAYKLLSKVPNIVANSYHILNNEEPIEPLKELSY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 198 TENFLYMLdymhqTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIR 277
Cdd:PRK12349 156 SANFLYML-----TGKKPTELEEKIFDRSLVLYSEHEMPNSTFTARVIASTQSDLYGALTGAVASLKGSLHGGANEAVMY 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 278 MLTEIGDVKNVPAYIERVKKGEFRLMGFGHRVY-KNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEDeyfisR 356
Cdd:PRK12349 231 MLLEAGTVEKFEELLQKKLYNKEKIMGFGHRVYmKKMDPRALMMKEALKQLCDVKGDYTLYEMCEAGEKIMEKE-----K 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 381382448 357 KLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDY 419
Cdd:PRK12349 306 GLYPNLDYYAAPVYWMLGIPIQLYTPIFFSSRTVGLCAHVIEQHAN--NRLFRPRVNYIGERH 366
PRK12351 PRK12351
methylcitrate synthase; Provisional
70-428 3.54e-63

methylcitrate synthase; Provisional


Pssm-ID: 183463 [Multi-domain]  Cd Length: 378  Bit Score: 208.24  E-value: 3.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  70 LRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDAHPMGMMISALAFMSTLH 149
Cdd:PRK12351  32 LHYRGYDILDLAEHCEFEEVAHLLVHGKLPTQAELAAYKTKLKALRGLPAAVKTVLEAIPAAAHPMDVMRTGVSVLGCLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 150 KEASRVDDPDVRlKQIYRILGKLPtvAAFCYRHRI---GRPFNYPNADMGYTENFLYMLdymHQTKyeVNPVLAKALDVL 226
Cdd:PRK12351 112 PEKEDHNFSGAR-DIADRLLASLG--SILLYWYHYshnGRRIEVETDDDSIGGHFLHLL---HGKK--PSESWVKAMHTS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 227 FILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYI-ERVKKGEfRLMGF 305
Cdd:PRK12351 184 LILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYDTPDEAEADIrRRVENKE-VVIGF 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 306 GHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEdeyfiSRKLYPNVDFYSGIIYQAMRFPPDMFTVLFT 385
Cdd:PRK12351 263 GHPVYTISDPRNKVIKEVAKKLSKEAGDTKLYDIAERLETVMWE-----EKKMFPNLDWFSAVSYHMMGVPTAMFTPLFV 337
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 381382448 386 LGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPIEQR 428
Cdd:PRK12351 338 ISRTTGWAAHVIEQRQD--NKIIRPSANYTGPEDRKFVPIEKR 378
Ec2MCS_like_1 cd06117
Subgroup of Escherichia coli (Ec) 2-methylcitrate synthase (2MCS)_like. 2MCS catalyzes the ...
52-425 1.16e-62

Subgroup of 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, but has a 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, prefer PrCoA as substrate, but can also can use AcCoA. Re 2-MCS1 at a low rate can use butyryl-CoA and valeryl-CoA. A second Ralstonia eutropha 2MCS is also found in this group, Re 2-MCS2, which is induced on propionate. 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: 99870 [Multi-domain]  Cd Length: 366  Bit Score: 206.62  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  52 NTASCKSRITYIDgekgiLRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYD 131
Cdd:cd06117   10 NTALCTVGRSGND-----LHYRGYDILDLAEKCEFEEVAHLLVHGKLPTKSELAAYKTKLKSLRGLPANVKTALEQLPAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 132 AHPMGMMISALAFMSTLHKEasRVDDPDVRLKQIY-RILGKLPTVAAFCYRH-RIGRPFNYPNADMGYTENFLYMLdymH 209
Cdd:cd06117   85 AHPMDVMRTGVSVLGCVLPE--KEDHPVSGARDIAdRLMASLGSILLYWYHYsHNGKRIEVETDDDSIGGHFLHLL---H 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 210 QTKyeVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVP 289
Cdd:cd06117  160 GEK--PSESWEKAMHISLILYAEHEFNASTFTARVIAGTGSDMYSAITGAIGALRGPKHGGANEVAFEIQQRYESADEAE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 290 AYI-ERVKKGEFrLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALEdeyfiSRKLYPNVDFYSGI 368
Cdd:cd06117  238 ADIrRRVENKEV-VIGFGHPVYTIADPRNQVIKEVAKQLSKEGGDMKMFDIAERLETVMWE-----EKKMFPNLDWFSAV 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 381382448 369 IYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDpeQKIARPRQIYLGYDYRDYVPI 425
Cdd:cd06117  312 SYHMMGVPTAMFTPLFVIARTTGWSAHIIEQRQD--GKIIRPSANYTGPEDLKFVPI 366
PRK14032 PRK14032
citrate synthase; Provisional
62-428 2.44e-59

citrate synthase; Provisional


Pssm-ID: 184465 [Multi-domain]  Cd Length: 447  Bit Score: 200.13  E-value: 2.44e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  62 YIDGEK----GILRYRGYPIEQLAEKST------FLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYD 131
Cdd:PRK14032  56 IDDGEKipdeGKLYYRGYDIKDLVNGFLkekrfgFEEVAYLLLFGELPTKEELAEFTELLGDYRELPDGFTRDMILKAPS 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 132 AHPMGMMISALAFMSTLHKEASRVDDPDVrLKQIYRILGKLPTVAAFCY---RHRI-GRPFNYPNADMGYT--ENFLYML 205
Cdd:PRK14032 136 KDIMNSLARSVLALYSYDDNPDDTSIDNV-LRQSISLIARFPTLAVYAYqayRHYHdGKSLYIHPPKPELStaENILYML 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 206 dyMHQTKYEvnPVLAKALDVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEI-- 282
Cdd:PRK14032 215 --RPDNKYT--ELEARLLDLALVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPKHGGANIKVMEMFEDIke 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 283 -----GDVKNVPAYIERVKKGEF-----RLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVALE--- 349
Cdd:PRK14032 291 nvkdwEDEDEIADYLTKILNKEAfdksgLIYGMGHAVYTISDPRAVILKKFAEKLAKEKGREEEFNLYEKIEKLAPElia 370
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 381382448 350 DEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITDPEqKIARPRQIYLGyDYRDYVPIEQR 428
Cdd:PRK14032 371 EERGIYKGVSANVDFYSGFVYDMLGIPEELYTPLFAIARIVGWSAHRIEELVNGG-KIIRPAYKSVL-ERREYVPLEER 447
citrate_synt_like_1_2 cd06113
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
63-416 2.88e-58

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: 195.95  E-value: 2.88e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  63 IDGEK----GILRYRGYPIEQLAEKST------FLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYDA 132
Cdd:cd06113   27 IDGEKvpcpGKLYYRGYDVEDLVNGAQkenrfgFEETAYLLLFGYLPNKEELEEFCEILSSYRTLPDNFVEDVILKAPSK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 133 HPMGMMISALAFMSTLHKEASRVDDPDVRLKQIyRILGKLPTVAAFCY---RHRIGRP---FNYPNADMGYTENFLYML- 205
Cdd:cd06113  107 DIMNKLQRSVLALYSYDDKPDDISLENVLRQSI-QLIARLPTIAVYAYqakRHYYDGEslyIHHPQPELSTAENILSMLr 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 206 DYMHQTKYEvnpvlAKALDVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEI-- 282
Cdd:cd06113  186 PDKKYTELE-----AKLLDLCLVLHAEHGGgNNSTFTTRVVSSSGTDTYSAIAAAIGSLKGPRHGGANIKVMEMLEDIke 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 283 -----GDVKNVPAYIERVKKGEFR-----LMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLIDIAVELERVA---LE 349
Cdd:cd06113  261 nvkdwTDEDEVRAYLRKILNKEAFdksglIYGMGHAVYTLSDPRAVVLKKYARSLAKEKGREEEFALYERIERLApevIA 340
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 381382448 350 DEYFISRKLYPNVDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVE-LITDpeQKIARPRQIYLG 416
Cdd:cd06113  341 EERGIGKTVCANVDFYSGFVYKMLGIPQELYTPLFAVARIVGWCAHRIEeLLNS--GRIIRPAYKYVG 406
PRK12350 PRK12350
citrate synthase 2; Provisional
47-416 3.57e-52

citrate synthase 2; Provisional


Pssm-ID: 237070 [Multi-domain]  Cd Length: 353  Bit Score: 178.62  E-value: 3.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  47 DPGYDNTASCKSRITYIDGEKGILRYRGYPIEQLAEKSTFLEVAYLLIFGELPTKQQLAEwEYKIMHHTflhenmtelfH 126
Cdd:PRK12350   2 VPGLEGVVAFETEIAEPDGDGGALRYRGVDIEDLVGRVTFEDVWALLVDGRFGPGLPPAE-PFPLPVHL----------G 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 127 AFRYDAHpmgmmiSALAFMSTLHKEASRVDDPDVRLKQiyRILGKLPTVAAFCYRHR--IGRPFnYPNADMGYTENFLYM 204
Cdd:PRK12350  71 DARVDVQ------AALAMLAPVWGFRPLLDIDDLTARL--DLARASVMALSAVAQSArgIGQPA-VPQREIDHAATILER 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 205 LdyMHQTKYEVNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGD 284
Cdd:PRK12350 142 F--MGRWRGEPDPAHVAALDAYWVSAAEHGMNASTFTARVIASTGADVAAALSGAIGALSGPLHGGAPARVLPMLDAVER 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 285 VKNVPAYIERV-KKGEfRLMGFGHRVYKNYDPRAKIIKRIAYEVFEvtgmnPLIDIAVELERVALED--EYFISRKLYPN 361
Cdd:PRK12350 220 TGDARGWVKGAlDRGE-RLMGFGHRVYRAEDPRARVLRATAKRLGA-----PRYEVAEAVEQAALAElrERRPDRPLETN 293
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 381382448 362 VDFYSGIIYQAMRFPPDMFTVLFTLGRAPGWLAQWVELITdpEQKIARPRQIYLG 416
Cdd:PRK12350 294 VEFWAAVLLDFAGVPAHMFTAMFTCGRTAGWSAHILEQKR--TGRLVRPSARYVG 346
PRK09569 PRK09569
citrate (Si)-synthase;
60-416 4.89e-43

citrate (Si)-synthase;


Pssm-ID: 181961  Cd Length: 437  Bit Score: 156.45  E-value: 4.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  60 ITYIDGEKGIlRYRGYPIEQLAEK---------STFLEVAYLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRY 130
Cdd:PRK09569  52 ISYLDPQEGI-RFRGKTIPETFEAlpkapgseyPTVESFWYFLLTGEVPTQEQVQEVVAEWKKRQNVPQYVIDAIRALPR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 131 DAHPMGMMISALAFMSTLHKEASR--------VDDPDVRLKQIYRILGKLPTVAAFCYRHRI-GRPFNYPNADMGYTENF 201
Cdd:PRK09569 131 DSHPMVMLSVGILAMQRESKFAKFynegkfnkMDAWEYMYEDASDLVARIPVIAAYIYNLKYkGDKQIPSDPELDYGANF 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 202 LYMLDYMHQtkyevnpvLAKALDVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIR--- 277
Cdd:PRK09569 211 AHMIGQPKP--------YKDVARMYFILHSDHESgNVSAHTTHLVASALSDAYYSYSAGLNGLAGPLHGLANQEVLGwiq 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 278 -MLTEIGDV----KNVPAYI-ERVKKGEFrLMGFGHRVYKNYDPRAKIIKRIAYEVFEvtgMNPLIDIAVELERVA---L 348
Cdd:PRK09569 283 qFQEKLGGEeptkEQVEQALwDTLNAGQV-IPGYGHAVLRKTDPRYTAQREFCLKHLP---DDPLFKLVAMIFEVApgvL 358
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 381382448 349 EdEYFISRKLYPNVDFYSGIIYQAMRFP-PDMFTVLFTLGRAPGWLAQ--WVELITDPeqkIARPRQIYLG 416
Cdd:PRK09569 359 T-EHGKTKNPWPNVDAQSGVIQWYYGVKeWDFYTVLFGVGRALGVMANitWDRGLGYA---IERPKSVTTE 425
ScCS-like cd06103
Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of ...
60-413 5.57e-35

Saccharomyces cerevisiae (Sc) citrate synthase (CS)-like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 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 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). This group includes three S. cerevisiae CS proteins, ScCit1,-2,-3. ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA; in addition to having activity with AcCoA, it plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. ScCit3 is a mitochondrial CS and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the ScCIT1 gene and its expression is increased in the presence of a ScCIT1 deletion. Included in this group is the Tetrahymena 14 nm filament protein which functions as a CS in mitochondria and as a cytoskeletal component in cytoplasm and Geobacter sulfurreducens (GSu) CS. GSuCS is dimeric and eukaryotic-like; it lacks 2MCS activity and is inhibited by ATP. In contrast to eukaryotic and other prokaryotic CSs, GSuCIT is not stimulated by K+ ions. 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: 99857  Cd Length: 426  Bit Score: 134.35  E-value: 5.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  60 ITYIDGEKGIlRYRGYPIEQLAEKSTFLE---------VAYLLIFGELPTKQQL----AEWEY--KIMHHTFlhenmtEL 124
Cdd:cd06103   50 TSVLDPDEGI-RFRGKTIPECQELLPKADgggeplpegLFWLLLTGEVPTEEQVdelsKEWAKraEVPSHVV------KM 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 125 FHAFRYDAHPMGMMISALAFMSTLHKEASRVDDPDVR--------LKQIYRILGKLPTVAAFCYRHRIGR---PFNYpNA 193
Cdd:cd06103  123 IDNLPRNLHPMTQLSAAILALQSESKFAKAYAEGKINkttyweyvYEDAMDLIAKLPVVAAKIYRRKYRKggeIGAI-DS 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 194 DMGYTENFLYMLDYmhqTKYEVNPVLAkaldVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGAN 272
Cdd:cd06103  202 KLDWSANFAHMLGY---EDEEFTDLMR----LYLTLHSDHEGgNVSAHTSHLVGSALSDPYLSFSAALNGLAGPLHGLAN 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 273 EAVIRMLTEIGDVKNVPAYIERVKKGEFRLM-------GFGHRVYKNYDPRAKIIKRIAYEVFEvtgMNPLIDIAVELER 345
Cdd:cd06103  275 QEVLKWLLKMQKELGKDVSDEELEKYIWDTLnsgrvvpGYGHAVLRKTDPRFTCQREFALKHLP---DDPLFKLVAQCYK 351
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 346 VALE--DEYFISRKLYPNVDFYSGIIYQ--AMRfPPDMFTVLFTLGRAPGWLAQ--WVELITDPeqkIARPRQI 413
Cdd:cd06103  352 IIPGvlKEHGKVKNPYPNVDAHSGVLLQhyGMT-EPQYYTVLFGVSRALGVLAQlvWSRALGLP---IERPKSM 421
citrate_synt_like_2 cd06102
Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate ...
215-416 1.06e-26

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. This subgroup includes both gram-positive and gram-negative bacteria.


Pssm-ID: 99856 [Multi-domain]  Cd Length: 282  Bit Score: 108.12  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 215 VNPVLAKALDVLFILHADHEQNASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIRMLTEIGDVKNVPAYI-E 293
Cdd:cd06102   93 LDPAAADLLRRALVLLADHELNASTFAARVAASTGASLYAAVLAGLAALSGPRHGGATARVEALLDEALRAGDAEAAVrE 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 294 RVKKGEfRLMGFGHRVYKNYDPRAKIIkriaYEVFEVTGMNPLIDIAVELERVALEDEyfisrkLYPNVDFYSGIIYQAM 373
Cdd:cd06102  173 RLRRGE-ALPGFGHPLYPDGDPRAAAL----LAALRPLGPAAPPAARALIEAARALTG------ARPNIDFALAALTRAL 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 381382448 374 RFPPDMFTVLFTLGRAPGWLAQWVELITDPeqKIARPRQIYLG 416
Cdd:cd06102  242 GLPAGAAFALFALGRSAGWIAHALEQRAQG--KLIRPRARYVG 282
ScCit3_like cd06106
Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase ...
61-415 6.01e-26

Saccharomyces cerevisiae (Sc) 2-methylcitrate synthase Cit3-like. 2-methylcitrate synthase (2MCS) catalyzes the condensation of propionyl-coenzyme A (PrCoA) and oxaloacetate (OAA) to form 2-methylcitrate and CoA. Citrate synthase (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with OAA to form citrate and CoA, the first step in the citric acid cycle (TCA or Krebs cycle). 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). ScCit3 is mitochondrial and functions in the metabolism of PrCoA; it is a dual specificity CS and 2MCS, having similar catalytic efficiency with both AcCoA and PrCoA. The pattern of expression of the ScCIT3 gene follows that of the major mitochondrial CS gene (CIT1, not included in this group) and its expression is increased in the presence of a CIT1 deletion. This group also contains Aspergillus nidulans 2MCS; a deletion of the gene encoding this protein results in a strain unable to grow on propionate. 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: 99859  Cd Length: 428  Bit Score: 108.75  E-value: 6.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  61 TYIDGEKGIlRYRGYPIEQLAEK-------STFLEVA--YLLIFGELPTKQQLAEWEYKIMHHTFLHENMTELFHAFRYD 131
Cdd:cd06106   51 SVLDAEEGI-RFHGKTIPECQKElpkapigGEMLPESmlWLLLTGKVPTFEQARGLSKELAERGKLPHYIEKLLDSLPKT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 132 AHPM---GMMISAL----AFMSTLHKEASRVDDPDVRLKQIYRILGKLPTVAAFCYRHRI--GRPFNYPNADMGYTENFL 202
Cdd:cd06106  130 LHPMtqlSIGVAALnhdsKFAAAYEKGIKKTEYWEPTLEDSLNLIARLPALAARIYRNVYgeGHGLGKIDPEVDWSYNFT 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 203 YMLDYMHQTKyevnpvLAKALDVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVIR---- 277
Cdd:cd06106  210 SMLGYGDNLD------FVDLLRLYIALHGDHEGgNVSAHTTHLVGSALSDPYLSYSAGLMGLAGPLHGLAAQEVLRwile 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 278 MLTEIGDV---KNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGmNPLIDIAVELERVA--LEDEY 352
Cdd:cd06106  284 MQKNIGSKatdQDIRDYLWKTLKSGRVVPGYGHAVLRKPDPRFTALMEFAQTRPELEN-DPVVQLVQKLSEIApgVLTEH 362
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 381382448 353 FISRKLYPNVDFYSGIIYQAMRF-PPDMFTVLFTLGRAPGWLAQ--WVELITDPeqkIARPRQIYL 415
Cdd:cd06106  363 GKTKNPFPNVDAASGVLFYHYGIrEFLYYTVIFGVSRALGPLTQlvWDRILGLP---IERPKSLSL 425
ScCit1-2_like cd06105
Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes ...
63-397 3.43e-25

Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 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 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). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. 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: 99858  Cd Length: 427  Bit Score: 106.68  E-value: 3.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448  63 IDGEKGIlRYRGYPIEQLAEKstfLEVA------------YLLIFGELPTKQQLA----EWEYKimhhTFLHENMTELFH 126
Cdd:cd06105   53 LDPEEGI-RFRGLSIPECQKL---LPKApggeeplpeglfWLLLTGEVPTKEQVSalskEWAAR----AALPSHVVTMLD 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 127 AFRYDAHPM---GMMISALAFMSTLHKEASRVDDPDVRLKQIYR----ILGKLPTVAAFCYRhRIGRPFNYPNADMG--Y 197
Cdd:cd06105  125 NFPTNLHPMsqlSAAITALNSESKFAKAYAEGIHKSKYWEYVYEdsmdLIAKLPCVAAKIYR-NLYRGGKIIAIDSNldW 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 198 TENFLYMLDYmhqtkyeVNPVLAKALDVLFILHADHEQ-NASTSVMRAIGSAYADPYSAMAGAAAALFGPRHGGANEAVI 276
Cdd:cd06105  204 SANFANMLGY-------TDPQFTELMRLYLTIHSDHEGgNVSAHTTHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVL 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 277 RMLT----EIGD---VKNVPAYIERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVTGMNPLI--------DIAV 341
Cdd:cd06105  277 VWLTklqkEVGKdvsDEQLREYVWKTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPNDPLFKLVsqlykivpPVLT 356
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 381382448 342 ELERValedeyfisRKLYPNVDFYSGIIYQ-----AMRFppdmFTVLFTLGRAPGWLAQWV 397
Cdd:cd06105  357 EQGKA---------KNPWPNVDAHSGVLLQyygltEMNY----YTVLFGVSRALGVLSQLI 404
CCL_ACL-C cd06100
Citryl-CoA lyase (CCL), the C-terminal portion of the single-subunit type ATP-citrate lyase ...
220-398 3.23e-21

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: 91.47  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 220 AKALDVLFILHADHEQNAStSVMRAIGSAYADPYSAMAGAAAAL--FGPRHGGANEAVIRMLTEIGD-----VKNVPAYI 292
Cdd:cd06100   31 ARLLEALLVALADHGPATP-SAHAARLTASAGPEDLQSAVAAGLlgIGDRFGGAGEGAARLFKEAVDsgdalDAAAAEFV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 293 ERVKKGEFRLMGFGHRVYKNYDPRAKIIKRIAYEVFEVtgmNPLIDIAVELERVALEDEyfiSRKLYPNVDFYSGIIYQA 372
Cdd:cd06100  110 AEYRAAKKRIPGFGHPVHKNPDPRVPRLLELARELGPA---GPHLDYALAVEKALTAAK---GKPLPLNVDGAIAAILLD 183
                        170       180
                 ....*....|....*....|....*.
gi 381382448 373 MRFPPDMFTVLFTLGRAPGWLAQWVE 398
Cdd:cd06100  184 LGFPPGALRGLFVLGRSPGLIAHALE 209
PRK06224 PRK06224
citryl-CoA lyase;
216-418 5.79e-15

citryl-CoA lyase;


Pssm-ID: 235748 [Multi-domain]  Cd Length: 263  Bit Score: 74.52  E-value: 5.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 216 NPVLAKALDVLFILHADHEQNASTSVMRAIGSAyADPYSAMAGAAAALFGPRHGGANEAVIRMLTEI----GDVKNVPAY 291
Cdd:PRK06224  51 TPNEARLLDAVLVALVDHGLTPSAAAARMTASG-GESLQGAVAAGLLALGSVHGGAGEQAAELLQEIaaaaDAGADLDAA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 292 IERVKKgEFR-----LMGFGHRVYKNYDPRAKIIKRIAYEVfEVTGmnPLIDIAVELERVALEDEyfiSRKLYPNVDFYS 366
Cdd:PRK06224 130 ARAIVA-EYRaagkrVPGFGHPLHKPVDPRAPRLLALAREA-GVAG--RHCRLAEALEAALAAAK---GKPLPLNVDGAI 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 381382448 367 GIIYQAMRFPPDMFTVLFTLGRAPGWLAQ-WVELITDPEQKIARPRQIYLGYD 418
Cdd:PRK06224 203 AAILADLGFPPALARGLFVISRAAGLVAHvWEELQQPIGFRIWDPAEEAVEYT 255
PLN02522 PLN02522
ATP citrate (pro-S)-lyase
265-391 3.54e-06

ATP citrate (pro-S)-lyase


Pssm-ID: 178137 [Multi-domain]  Cd Length: 608  Bit Score: 49.05  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 381382448 265 GPRHGGANEAVIRMLTEIGDVKNVP-AYIERVKKGEFRLMGFGHRVYK--NYDPRAKIIKRIAYEVFEvtgMNPLIDIAV 341
Cdd:PLN02522 445 GPRFGGAIDDAARYFKDAYDRGLTPyEFVEGMKKKGIRVPGIGHRIKSrdNRDKRVELLQKYARTHFP---SVKYMEYAV 521
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 381382448 342 ELERVALEDeyfiSRKLYPNVDFYSGIIYQAMRFPPDMFTV--------------LFTLGRAPG 391
Cdd:PLN02522 522 QVETYTLSK----ANNLVLNVDGAIGSLFLDLLAGSGMFTKqeideiveigylngLFVLARSIG 581
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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