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Conserved domains on  [gi|1847328181|gb|QKF72989|]
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DRE-TIM metallolyase superfamily protein [Aliarcobacter faecis]

Protein Classification

aldolase catalytic domain-containing protein( domain architecture ID 10168244)

aldolase catalytic domain-containing protein adopts a triose-phosphate isomerase (TIM) barrel fold and contains three invariant catalytic residues, an aspartate (D), an arginine (R), and a glutamate (E), and thus belongs to the DRE-TIM metallolyase superfamily

CATH:  3.20.20.70
Gene Ontology:  GO:0003824|GO:0046872
PubMed:  26935545|12206759|11257493
SCOP:  2000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 17-283 4.25e-129

4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


:

Pssm-ID: 163682  Cd Length: 266  Bit Score: 368.81  E-value: 4.25e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  17 VFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVSPtlmSEDEYGPWNFCKEQDIRRIVGENNTNLKIAVM 96
Cdd:cd07944     1 ILDCTLRDGGYVNNWDFGDEFVKAIYRALAAAGIDYVEIGYRSSP---EKEFKGKSAFCDDEFLRRLLGDSKGNTKIAVM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  97 SDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMAISKSFDDELDEVLEQLAKTPVDVIYI 176
Cdd:cd07944    78 VDYGNDDIDLLEPASGSVVDMIRVAFHKHEFDEALPLIKAIKEKGYEVFFNLMAISGYSDEELLELLELVNEIKPDVFYI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 177 ADSFGSFYPEQIRKLTEKYLSFAEKsGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:cd07944   158 VDSFGSMYPEDIKRIISLLRSNLDK-DIKLGFHAHNNLQLALANTLEAIELGVEIIDATVYGMGRGAGNLPTELLLDYLN 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1847328181 257 N---PKYKQMPVLEFIENYIVDLEKKLDWG 283
Cdd:cd07944   237 NkfgKKYNLEPVLELIDEYIAPLKKKYEWG 266
 
Name Accession Description Interval E-value
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 17-283 4.25e-129

4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163682  Cd Length: 266  Bit Score: 368.81  E-value: 4.25e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  17 VFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVSPtlmSEDEYGPWNFCKEQDIRRIVGENNTNLKIAVM 96
Cdd:cd07944     1 ILDCTLRDGGYVNNWDFGDEFVKAIYRALAAAGIDYVEIGYRSSP---EKEFKGKSAFCDDEFLRRLLGDSKGNTKIAVM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  97 SDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMAISKSFDDELDEVLEQLAKTPVDVIYI 176
Cdd:cd07944    78 VDYGNDDIDLLEPASGSVVDMIRVAFHKHEFDEALPLIKAIKEKGYEVFFNLMAISGYSDEELLELLELVNEIKPDVFYI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 177 ADSFGSFYPEQIRKLTEKYLSFAEKsGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:cd07944   158 VDSFGSMYPEDIKRIISLLRSNLDK-DIKLGFHAHNNLQLALANTLEAIELGVEIIDATVYGMGRGAGNLPTELLLDYLN 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1847328181 257 N---PKYKQMPVLEFIENYIVDLEKKLDWG 283
Cdd:cd07944   237 NkfgKKYNLEPVLELIDEYIAPLKKKYEWG 266
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
 14-251 4.02e-26

4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 105.69  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  14 DLKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGK---------NVSPTLMSEDEYgpwnfckeqdIRrIV 84
Cdd:PRK08195    3 KIYISDVTLRDGMHAVRHQYTLEQVRAIARALDAAGVPVIEVTHgdglggssfNYGFGAHTDEEY----------IE-AA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  85 GENNTNLKIAV--MSDIGRslKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMaisKSFDDELDEV 162
Cdd:PRK08195   72 AEVVKQAKIAAllLPGIGT--VDDLKMAYDAGVRVVRVATHCTEADVSEQHIGLARELGMDTVGFLM---MSHMAPPEKL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 163 LEQlAKTPVD----VIYIADSFGSFYPEQIRKLTEKYLSfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSG 238
Cdd:PRK08195  147 AEQ-AKLMESygaqCVYVVDSAGALLPEDVRDRVRALRA-ALKPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSLAG 224

                         250
                  ....*....|...
gi 1847328181 239 LGRGAGNCPLELL 251
Cdd:PRK08195  225 LGAGAGNTPLEVL 237
4OH_2_O_val_ald TIGR03217
4-hydroxy-2-oxovalerate aldolase; Members of this protein family are 4-hydroxy-2-oxovalerate ...
 14-256 2.43e-25

4-hydroxy-2-oxovalerate aldolase; Members of this protein family are 4-hydroxy-2-oxovalerate aldolase, also called 4-hydroxy-2-ketovalerate aldolase and 2-oxo-4-hydroxypentanoate aldolase. This enzyme, part of the pathway for the meta-cleavage of catechol, produces pyruvate and acetaldehyde. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; EC 1.2.1.10) to acetyl-CoA. The two enzymes are tightly associated. [Energy metabolism, Other]


Pssm-ID: 274481 [Multi-domain]  Cd Length: 333  Bit Score: 103.58  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  14 DLKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEI--GKNVSPtlmSEDEYGpWNFCKEQDIRRIVGENNTNL 91
Cdd:TIGR03217   2 KLYITDVTLRDGMHAIRHQFTIEQVRAIAAALDEAGVDAIEVthGDGLGG---SSFNYG-FSAHTDLEYIEAAADVVKRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  92 KIAVMSDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMAISKSFDDELDEVLEQLAKTPV 171
Cdd:TIGR03217  78 KVAVLLLPGIGTVHDLKAAYDAGARTVRVATHCTEADVSEQHIGMARELGMDTVGFLMMSHMTPPEKLAEQAKLMESYGA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 172 DVIYIADSFGSFYPEQIRKLTEKYLSfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELL 251
Cdd:TIGR03217 158 DCVYIVDSAGAMLPDDVRDRVRALKA-VLKPETQVGFHAHHNLSLAVANSIAAIEAGATRIDASLRGLGAGAGNAPLEVF 236


                  ....*
gi 1847328181 252 LGFLK 256
Cdd:TIGR03217 237 VAVLD 241
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 15-251 5.78e-25

HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.


Pssm-ID: 459902 [Multi-domain]  Cd Length: 264  Bit Score: 101.26  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVsptlMSEDEygpWNFCKEqdIRRIVGENN-TNLKI 93
Cdd:pfam00682   2 VAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGFPA----ASEDD---FEVVRA--IAKVIPHARiLVLCR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  94 AVMSDIGRSLKEELRPKSESVVdmIRIATYIHQIPA------------AIELIEDAHAKGYETTVNIMAISKSFDDELDE 161
Cdd:pfam00682  73 AREHDIKAAVEALKGAGAVRVH--VFIATSDLHRKYklgkdreevakrAVAAVKAARSRGIDVEFSPEDASRTDPEFLAE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 162 VLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEkYLSFAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGR 241
Cdd:pfam00682 151 VVEAAIEAGATRINIPDTVGVLTPNEAAELIS-ALKARVPNKAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIGE 229

                         250
                  ....*....|
gi 1847328181 242 GAGNCPLELL 251
Cdd:pfam00682 230 RAGNAALEEV 239
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 12-256 9.87e-19

Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439889 [Multi-domain]  Cd Length: 452  Bit Score: 86.37  E-value: 9.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  12 REDLKVFDCTIRDG--GLVNNFHfTDEFVKAhYEMCVASGVDYMEIGknvSPtLMSEDEYgpwnfckeQDIRRIVgENNT 89
Cdd:COG0119     1 PDRIIIFDTTLRDGeqAPGVSFS-VEEKLRI-ARLLDELGVDEIEAG---FP-AASPGDF--------EAVRRIA-ELGL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  90 NLKI-----AVMSDIGRSLkEELRPKSESVVDMIrIATYIHQI--------PAAIELIEDA--HAKGYETTVNIMA--IS 152
Cdd:COG0119    66 DATIcalarARRKDIDAAL-EALKGAGVDRVHLF-IKTSDLHVeyklrktrEEVLEMAVEAvkYAKEHGLEVEFSAedAT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 153 KSFDDELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKylsFAEK-SGKKVGIHAHNNLQLAYANTLEAMIYGASF 231
Cdd:COG0119   144 RTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEE---LRERvPDVILSVHCHNDLGLAVANSLAAVEAGADQ 220

                         250       260
                  ....*....|....*....|....*
gi 1847328181 232 LDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:COG0119   221 VEGTINGIGERAGNAALEEVVMNLK 245
 
Name Accession Description Interval E-value
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 17-283 4.25e-129

4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of bacterial enzymes is sequence-similar to 4-hydroxy-2-oxovalerate aldolase (HOA) but its exact function is unknown. This family includes the Bacteroides vulgatus Bvu_2661 protein and belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163682  Cd Length: 266  Bit Score: 368.81  E-value: 4.25e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  17 VFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVSPtlmSEDEYGPWNFCKEQDIRRIVGENNTNLKIAVM 96
Cdd:cd07944     1 ILDCTLRDGGYVNNWDFGDEFVKAIYRALAAAGIDYVEIGYRSSP---EKEFKGKSAFCDDEFLRRLLGDSKGNTKIAVM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  97 SDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMAISKSFDDELDEVLEQLAKTPVDVIYI 176
Cdd:cd07944    78 VDYGNDDIDLLEPASGSVVDMIRVAFHKHEFDEALPLIKAIKEKGYEVFFNLMAISGYSDEELLELLELVNEIKPDVFYI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 177 ADSFGSFYPEQIRKLTEKYLSFAEKsGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:cd07944   158 VDSFGSMYPEDIKRIISLLRSNLDK-DIKLGFHAHNNLQLALANTLEAIELGVEIIDATVYGMGRGAGNLPTELLLDYLN 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1847328181 257 N---PKYKQMPVLEFIENYIVDLEKKLDWG 283
Cdd:cd07944   237 NkfgKKYNLEPVLELIDEYIAPLKKKYEWG 266
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 18-256 3.33e-50

DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163674 [Multi-domain]  Cd Length: 265  Bit Score: 167.63  E-value: 3.33e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  18 FDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVSPtlmsedEYGPWNFCKEQDIRRIVgENNTNLKIAVMs 97
Cdd:cd03174     1 TDTTLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASP------KAVPQMEDDWEVLRAIR-KLVPNVKLQAL- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  98 diGRSLKEELRPKSESVVDMIRI---ATYIHQ-----------IPAAIELIEDAHAKGYETTVNIMAIS--KSFDDELDE 161
Cdd:cd03174    73 --VRNREKGIERALEAGVDEVRIfdsASETHSrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDAFgcKTDPEYVLE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 162 VLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKYLSFAekSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGR 241
Cdd:cd03174   151 VAKALEEAGADEISLKDTVGLATPEEVAELVKALREAL--PDVPLGLHTHNTLGLAVANSLAALEAGADRVDGSVNGLGE 228

                         250
                  ....*....|....*
gi 1847328181 242 GAGNCPLELLLGFLK 256
Cdd:cd03174   229 RAGNAATEDLVAALE 243
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
 15-256 2.18e-33

4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163681  Cd Length: 263  Bit Score: 123.76  E-value: 2.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIG---------KNVSPTLMSEDEYgpwnfckeqdiRRIVG 85
Cdd:cd07943     1 VYIHDVTLRDGMHAVRHQFTLEQVRAIARALDAAGVPLIEVGhgdglggssLNYGFAAHTDEEY-----------LEAAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  86 ENNTNLKIAVMSDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMaisKSFDDELDEVLEQ 165
Cdd:cd07943    70 EALKQAKLGVLLLPGIGTVDDLKMAADLGVDVVRVATHCTEADVSEQHIGAARKLGMDVVGFLM---MSHMASPEELAEQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 166 lAKTPV----DVIYIADSFGSFYPEQIRkltEKYLSFAEKSG-KKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLG 240
Cdd:cd07943   147 -AKLMEsygaDCVYVTDSAGAMLPDDVR---ERVRALREALDpTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLG 222

                         250
                  ....*....|....*.
gi 1847328181 241 RGAGNCPLELLLGFLK 256
Cdd:cd07943   223 AGAGNTPLEVLVAVLE 238
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
 14-251 4.02e-26

4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 105.69  E-value: 4.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  14 DLKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGK---------NVSPTLMSEDEYgpwnfckeqdIRrIV 84
Cdd:PRK08195    3 KIYISDVTLRDGMHAVRHQYTLEQVRAIARALDAAGVPVIEVTHgdglggssfNYGFGAHTDEEY----------IE-AA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  85 GENNTNLKIAV--MSDIGRslKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMaisKSFDDELDEV 162
Cdd:PRK08195   72 AEVVKQAKIAAllLPGIGT--VDDLKMAYDAGVRVVRVATHCTEADVSEQHIGLARELGMDTVGFLM---MSHMAPPEKL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 163 LEQlAKTPVD----VIYIADSFGSFYPEQIRKLTEKYLSfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSG 238
Cdd:PRK08195  147 AEQ-AKLMESygaqCVYVVDSAGALLPEDVRDRVRALRA-ALKPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSLAG 224

                         250
                  ....*....|...
gi 1847328181 239 LGRGAGNCPLELL 251
Cdd:PRK08195  225 LGAGAGNTPLEVL 237
4OH_2_O_val_ald TIGR03217
4-hydroxy-2-oxovalerate aldolase; Members of this protein family are 4-hydroxy-2-oxovalerate ...
 14-256 2.43e-25

4-hydroxy-2-oxovalerate aldolase; Members of this protein family are 4-hydroxy-2-oxovalerate aldolase, also called 4-hydroxy-2-ketovalerate aldolase and 2-oxo-4-hydroxypentanoate aldolase. This enzyme, part of the pathway for the meta-cleavage of catechol, produces pyruvate and acetaldehyde. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; EC 1.2.1.10) to acetyl-CoA. The two enzymes are tightly associated. [Energy metabolism, Other]


Pssm-ID: 274481 [Multi-domain]  Cd Length: 333  Bit Score: 103.58  E-value: 2.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  14 DLKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEI--GKNVSPtlmSEDEYGpWNFCKEQDIRRIVGENNTNL 91
Cdd:TIGR03217   2 KLYITDVTLRDGMHAIRHQFTIEQVRAIAAALDEAGVDAIEVthGDGLGG---SSFNYG-FSAHTDLEYIEAAADVVKRA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  92 KIAVMSDIGRSLKEELRPKSESVVDMIRIATYIHQIPAAIELIEDAHAKGYETTVNIMAISKSFDDELDEVLEQLAKTPV 171
Cdd:TIGR03217  78 KVAVLLLPGIGTVHDLKAAYDAGARTVRVATHCTEADVSEQHIGMARELGMDTVGFLMMSHMTPPEKLAEQAKLMESYGA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 172 DVIYIADSFGSFYPEQIRKLTEKYLSfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELL 251
Cdd:TIGR03217 158 DCVYIVDSAGAMLPDDVRDRVRALKA-VLKPETQVGFHAHHNLSLAVANSIAAIEAGATRIDASLRGLGAGAGNAPLEVF 236


                  ....*
gi 1847328181 252 LGFLK 256
Cdd:TIGR03217 237 VAVLD 241
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 15-251 5.78e-25

HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.


Pssm-ID: 459902 [Multi-domain]  Cd Length: 264  Bit Score: 101.26  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVsptlMSEDEygpWNFCKEqdIRRIVGENN-TNLKI 93
Cdd:pfam00682   2 VAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGFPA----ASEDD---FEVVRA--IAKVIPHARiLVLCR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  94 AVMSDIGRSLKEELRPKSESVVdmIRIATYIHQIPA------------AIELIEDAHAKGYETTVNIMAISKSFDDELDE 161
Cdd:pfam00682  73 AREHDIKAAVEALKGAGAVRVH--VFIATSDLHRKYklgkdreevakrAVAAVKAARSRGIDVEFSPEDASRTDPEFLAE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 162 VLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEkYLSFAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGR 241
Cdd:pfam00682 151 VVEAAIEAGATRINIPDTVGVLTPNEAAELIS-ALKARVPNKAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIGE 229

                         250
                  ....*....|
gi 1847328181 242 GAGNCPLELL 251
Cdd:pfam00682 230 RAGNAALEEV 239
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 12-256 9.87e-19

Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439889 [Multi-domain]  Cd Length: 452  Bit Score: 86.37  E-value: 9.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  12 REDLKVFDCTIRDG--GLVNNFHfTDEFVKAhYEMCVASGVDYMEIGknvSPtLMSEDEYgpwnfckeQDIRRIVgENNT 89
Cdd:COG0119     1 PDRIIIFDTTLRDGeqAPGVSFS-VEEKLRI-ARLLDELGVDEIEAG---FP-AASPGDF--------EAVRRIA-ELGL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  90 NLKI-----AVMSDIGRSLkEELRPKSESVVDMIrIATYIHQI--------PAAIELIEDA--HAKGYETTVNIMA--IS 152
Cdd:COG0119    66 DATIcalarARRKDIDAAL-EALKGAGVDRVHLF-IKTSDLHVeyklrktrEEVLEMAVEAvkYAKEHGLEVEFSAedAT 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 153 KSFDDELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKylsFAEK-SGKKVGIHAHNNLQLAYANTLEAMIYGASF 231
Cdd:COG0119   144 RTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEE---LRERvPDVILSVHCHNDLGLAVANSLAAVEAGADQ 220

                         250       260
                  ....*....|....*....|....*
gi 1847328181 232 LDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:COG0119   221 VEGTINGIGERAGNAALEEVVMNLK 245
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
 19-249 6.49e-17

Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163677 [Multi-domain]  Cd Length: 259  Bit Score: 78.70  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  19 DCTIRDG----GLVnnfhFTDEFVKAHYEMCVASGVDYMEIGknvSPTlMSEDEygpwnfckEQDIRRIVGENntnLKIA 94
Cdd:cd07939     3 DTTLRDGeqapGVA----FSREEKLAIARALDEAGVDEIEVG---IPA-MGEEE--------REAIRAIVALG---LPAR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  95 VMSdIGRSLKEELRPKSESVVDMIRIATYIH--QIPAAI------------ELIEDAHAKGYETTVNIMAISKSFDDELD 160
Cdd:cd07939    64 LIV-WCRAVKEDIEAALRCGVTAVHISIPVSdiHLAHKLgkdrawvldqlrRLVGRAKDRGLFVSVGAEDASRADPDFLI 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 161 EVLEQLAKTPVDVIYIADSFGSFYP----EQIRKLtekylsfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTV 236
Cdd:cd07939   143 EFAEVAQEAGADRLRFADTVGILDPfttyELIRRL-------RAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTV 215

                         250
                  ....*....|...
gi 1847328181 237 SGLGRGAGNCPLE 249
Cdd:cd07939   216 NGLGERAGNAALE 228
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
 17-249 8.64e-14

2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163678  Cd Length: 268  Bit Score: 70.17  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  17 VFDCTIRDGGLVNNFHFT-DEFVK-AHyeMCVASGVDYMEIGKNVSptlmSEDEYgpwnfckeQDIRRIVGENnTNLKIA 94
Cdd:cd07940     1 IFDTTLRDGEQTPGVSLTpEEKLEiAR--QLDELGVDVIEAGFPAA----SPGDF--------EAVKRIAREV-LNAEIC 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  95 VMSdigRSLKEELRPKSESV----VDMIR--IATY-IH----------QIpaaIELIEDA--HAKGYETTVNIMA--ISK 153
Cdd:cd07940    66 GLA---RAVKKDIDAAAEALkpakVDRIHtfIATSdIHlkyklkktreEV---LERAVEAveYAKSHGLDVEFSAedATR 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 154 SFDDELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTeKYLSfAEKSGKKVGI--HAHNNLQLAYANTLEAMIYGASF 231
Cdd:cd07940   140 TDLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELI-KKLK-ENVPNIKVPIsvHCHNDLGLAVANSLAAVEAGARQ 217

                         250
                  ....*....|....*...
gi 1847328181 232 LDVTVSGLGRGAGNCPLE 249
Cdd:cd07940   218 VECTINGIGERAGNAALE 235
PRK00915 PRK00915
2-isopropylmalate synthase; Validated
 15-249 1.56e-13

2-isopropylmalate synthase; Validated


Pssm-ID: 234864 [Multi-domain]  Cd Length: 513  Bit Score: 70.91  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDG----GLVNNfhfTDEFV---KAHYEMcvasGVDYMEIGKNVSptlmSEDEYgpwnfckeQDIRRIVgEN 87
Cdd:PRK00915    5 VIIFDTTLRDGeqspGASLT---VEEKLqiaKQLERL----GVDVIEAGFPAS----SPGDF--------EAVKRIA-RT 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  88 NTNLKI-----AVMSDI---GRSLKEELRPksesvvdmiRIATYI--------HQI----PAAIELIEDA--HAKGYetT 145
Cdd:PRK00915   65 VKNSTVcglarAVKKDIdaaAEALKPAEAP---------RIHTFIatspihmeYKLkmsrEEVLEMAVEAvkYARSY--T 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 146 VNIMAiskSFDD----ELD---EVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTeKYLSFAEKSGKKVGI--HAHNNLQL 216
Cdd:PRK00915  134 DDVEF---SAEDatrtDLDflcRVVEAAIDAGATTINIPDTVGYTTPEEFGELI-KTLRERVPNIDKAIIsvHCHNDLGL 209

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1847328181 217 AYANTLEAMIYGASFLDVTVSGLGRGAGNCPLE 249
Cdd:PRK00915  210 AVANSLAAVEAGARQVECTINGIGERAGNAALE 242
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
 131-257 2.34e-12

Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163683 [Multi-domain]  Cd Length: 280  Bit Score: 66.25  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 131 IELIEDAHAKGYETTVNIMAISKSFDDELDEV---LEQLAKTPVDVIYIADSFGSFYPEQ----IRKLTEKYLSFaeksg 203
Cdd:cd07945   118 REVIEYAIKNGIEVNIYLEDWSNGMRDSPDYVfqlVDFLSDLPIKRIMLPDTLGILSPFEtytyISDMVKRYPNL----- 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1847328181 204 kKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELLLGFLKN 257
Cdd:cd07945   193 -HFDFHAHNDYDLAVANVLAAVKAGIKGLHTTVNGLGERAGNAPLASVIAVLKD 245
aksA PRK11858
trans-homoaconitate synthase; Reviewed
 14-256 1.41e-11

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 64.43  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  14 DLKVFDCTIRDG----GLVnnfhFTDEFVKAHYEMCVASGVDYMEIGknvSPTlMSEDEygpwnfcKEQdIRRIVGENnT 89
Cdd:PRK11858    4 DIEIVDTTLRDGeqtpGVV----FTNEEKLAIARMLDEIGVDQIEAG---FPA-VSEDE-------KEA-IKAIAKLG-L 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  90 NLKI-----AVMSDIGRSLKEElrpksesvVDM--IRIATY-IH-------QIPAAIELIEDA--HAKGYETTVNIMAIS 152
Cdd:PRK11858   67 NASIlalnrAVKSDIDASIDCG--------VDAvhIFIATSdIHikhklkkTREEVLERMVEAveYAKDHGLYVSFSAED 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 153 KSFDDEldEVLEQLAKTP----VDVIYIADSFGSFYPEQIRKLTeKYLSfaEKSGKKVGIHAHNNLQLAYANTLEAMIYG 228
Cdd:PRK11858  139 ASRTDL--DFLIEFAKAAeeagADRVRFCDTVGILDPFTMYELV-KELV--EAVDIPIEVHCHNDFGMATANALAGIEAG 213

                         250       260
                  ....*....|....*....|....*...
gi 1847328181 229 ASFLDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:PRK11858  214 AKQVHTTVNGLGERAGNAALEEVVMALK 241
PRK09389 PRK09389
(R)-citramalate synthase; Provisional
 13-249 1.02e-10

(R)-citramalate synthase; Provisional


Pssm-ID: 236493 [Multi-domain]  Cd Length: 488  Bit Score: 62.26  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  13 EDLKVFDCTIRDGGLVNNFHFTDEfVKAHYEMCV-ASGVDYMEIGKNVSptlmSEDEygpwnfckEQDIRRIVGENnTNL 91
Cdd:PRK09389    1 MMVRILDTTLRDGEQTPGVSLTPE-EKLEIARKLdELGVDVIEAGSAIT----SEGE--------REAIKAVTDEG-LNA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  92 KI-----AVMSDIGRSL------------------KEELRPKSESVVDMiriatyihqipaAIELIEdaHAKGYETTVNI 148
Cdd:PRK09389   67 EIcsfarAVKVDIDAALecdvdsvhlvvptsdlhiEYKLKKTREEVLET------------AVEAVE--YAKDHGLIVEL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 149 MAISKSFDDEldEVLEQLAKTPVDV----IYIADSFGSFYPEqirKLTEKYLSFAEKSGKKVGIHAHNNLQLAYANTLEA 224
Cdd:PRK09389  133 SGEDASRADL--DFLKELYKAGIEAgadrICFCDTVGILTPE---KTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAA 207

                         250       260
                  ....*....|....*....|....*
gi 1847328181 225 MIYGASFLDVTVSGLGRGAGNCPLE 249
Cdd:PRK09389  208 LAAGADQVHVTINGIGERAGNASLE 232
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
 15-275 3.79e-10

Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel domain; Homocitrate synthase (HCS) catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate, the first step in the lysine biosynthesis pathway. This family includes the Yarrowia lipolytica LYS1 protein as well as the Saccharomyces cerevisiae LYS20 and LYS21 proteins. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163685  Cd Length: 262  Bit Score: 59.65  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDGGLVNNFHFTDEFVKAHYEMCVASGVDYMEIGKNVSptlmSEDEygpwnfckEQDIRRIVgenNTNLKIA 94
Cdd:cd07948     1 FKIIDSTLREGEQFANAFFDTEDKIEIAKALDAFGVDYIELTSPAA----SPQS--------RADCEAIA---KLGLKAK 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  95 VMSDIgRSLKEELRPKSESVVDMIR--IAT--YIHQ----------IPAAIELIEDAHAKGYEttVNIMAiSKSFDDELD 160
Cdd:cd07948    66 ILTHI-RCHMDDARIAVETGVDGVDlvFGTspFLREashgksiteiIESAVEVIEFVKSKGIE--VRFSS-EDSFRSDLV 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 161 EVL---EQLAKTPVDVIYIADSFGSFYPEQI-------RKLTEKYLSFaeksgkkvgiHAHNNLQLAYANTLEAMIYGAS 230
Cdd:cd07948   142 DLLrvyRAVDKLGVNRVGIADTVGIATPRQVyelvrtlRGVVSCDIEF----------HGHNDTGCAIANAYAALEAGAT 211

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1847328181 231 FLDVTVSGLGRGAGNCPLELLLG--FLKNP-----KYKqMPVLEFIENYIVD 275
Cdd:cd07948   212 HIDTTVLGIGERNGITPLGGLIArmYTADPeyvvsKYK-LELLPELERLVAD 262
PLN03228 PLN03228
methylthioalkylmalate synthase; Provisional
 153-256 1.60e-09

methylthioalkylmalate synthase; Provisional


Pssm-ID: 178767 [Multi-domain]  Cd Length: 503  Bit Score: 58.78  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 153 KSFDDELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKYLSFAEK-SGKKVGIHAHNNLQLAYANTLEAMIYGASF 231
Cdd:PLN03228  235 RSDKEFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPGiDDIVFSVHCHNDLGLATANTIAGICAGARQ 314

                          90       100
                  ....*....|....*....|....*
gi 1847328181 232 LDVTVSGLGRGAGNCPLELLLGFLK 256
Cdd:PLN03228  315 VEVTINGIGERSGNASLEEVVMALK 339
citramal_synth TIGR00977
citramalate synthase; This model includes GSU1798 and is now known to represent citramalate ...
 15-248 1.07e-08

citramalate synthase; This model includes GSU1798 and is now known to represent citramalate synthase. Members are related to 2-isopropylmalate synthases and homocitrate synthases but phylogenetically distinct. The role is isoleucine biosynthesis, the first dedicated step. [Unknown function, General]


Pssm-ID: 130050 [Multi-domain]  Cd Length: 526  Bit Score: 56.06  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  15 LKVFDCTIRDGGLVN--NFHFTDEFVKAhyEMCVASGVDYMEigknvsptlmsedeyGPWNFCKEQDI---RRIVGENNT 89
Cdd:TIGR00977   2 LWLYDTTLRDGAQREgvSFSLEDKIRIA--ERLDDLGIHYIE---------------GGWPGANPKDVqffWQLKEMNFK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181  90 NLKIAVMSDIGRSLKE-ELRPKSESVVDM-IRIATY------IHQIPAAIELIEDAHAKGYETtvniMAISKSFDDELD- 160
Cdd:TIGR00977  65 NAKIVAFCSTRRPHKKvEEDKMLQALIKAeTPVVTIfgkswdLHVLEALQTTLEENLAMIYDT----VAYLKRQGDEVIy 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 161 -----------------EVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKylsfAEKSGK--KVGIHAHNNLQLAYANT 221
Cdd:TIGR00977 141 daehffdgykanpeyalATLATAQQAGADWLVLCDTNGGTLPHEISEITTK----VKRSLKqpQLGIHAHNDSGTAVANS 216

                         250       260
                  ....*....|....*....|....*..
gi 1847328181 222 LEAMIYGASFLDVTVSGLGRGAGNCPL 248
Cdd:TIGR00977 217 LLAVEAGATMVQGTINGYGERCGNANL 243
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 129-247 4.50e-08

3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163676  Cd Length: 274  Bit Score: 53.55  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 129 AAIELIEDAHAKGYETTVnimAISKSFD---------DELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKYLsfA 199
Cdd:cd07938   115 RFEPVAELAKAAGLRVRG---YVSTAFGcpyegevppERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVL--E 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1847328181 200 EKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGrGagnCP 247
Cdd:cd07938   190 RFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLG-G---CP 233
DRE_TIM_Re_CS cd07947
Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain; ...
 185-270 2.84e-07

Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain; Re-citrate synthase (Re-CS) is a Clostridium kluyveri enzyme that converts acetyl-CoA and oxaloacetate to citrate. In most organisms, this reaction is catalyzed by Si-citrate synthase which is Si-face stereospecific with respect to C-2 of oxaloacetate, and phylogenetically unrelated to Re-citrate synthase. Re-citrate synthase is also found in a few other strictly anaerobic organisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163684  Cd Length: 279  Bit Score: 51.17  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 185 PEQIRKLTEKYLSFAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLELLLGFL-----KNPK 259
Cdd:cd07947   185 PRSVPKIIYGLRKDCGVPSENLEWHGHNDFYKAVANAVAAWLYGASWVNCTLLGIGERTGNCPLEAMVIEYaqlkgNFDG 264

                          90
                  ....*....|.
gi 1847328181 260 YKQMPVLEFIE 270
Cdd:cd07947   265 MNLEVITEIAE 275
DRE_TIM_LeuA3 cd07941
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ...
 161-259 4.99e-07

Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163679  Cd Length: 273  Bit Score: 50.15  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 161 EVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKYLsfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLG 240
Cdd:cd07941   155 ATLKAAAEAGADWLVLCDTNGGTLPHEIAEIVKEVR--ERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQVQGTINGYG 232

                          90       100
                  ....*....|....*....|....*.
gi 1847328181 241 RGAGNC------P-LELLLGFLKNPK 259
Cdd:cd07941   233 ERCGNAnlcsiiPnLQLKMGYECLPE 258
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 157-279 1.13e-05

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 47.02  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 157 DELDEVLEQLAKTPVDVIYIADSFGSFYPEQIrklTEKYLSFAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTV 236
Cdd:PRK14042  154 DNFLELGKKLAEMGCDSIAIKDMAGLLTPTVT---VELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAI 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1847328181 237 SGLGRGAGNCPLELLLGFLKNPKYK---QMPVLEFIENYIVDLEKK 279
Cdd:PRK14042  231 SSFSGGASHPPTEALVAALTDTPYDtelDLNILLEIDDYFKAVRKK 276
PRK12344 PRK12344
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
 185-254 1.43e-05

putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional


Pssm-ID: 237068 [Multi-domain]  Cd Length: 524  Bit Score: 46.62  E-value: 1.43e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1847328181 185 PEQIRKLTEKylsFAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGN---CP----LELLLGF 254
Cdd:PRK12344  186 PHEVAEIVAE---VRAAPGVPLGIHAHNDSGCAVANSLAAVEAGARQVQGTINGYGERCGNanlCSiipnLQLKMGY 259
PLN02321 PLN02321
2-isopropylmalate synthase
 209-249 1.30e-04

2-isopropylmalate synthase


Pssm-ID: 215182 [Multi-domain]  Cd Length: 632  Bit Score: 43.42  E-value: 1.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1847328181 209 HAHNNLQLAYANTLEAMIYGASFLDVTVSGLGRGAGNCPLE 249
Cdd:PLN02321  293 HCQNDLGLSTANTLAGAHAGARQVEVTINGIGERAGNASLE 333
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 157-247 3.84e-03

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 38.33  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1847328181 157 DELDEVLEQLAKTPVDVIYIADSFGSFYPEQIRKLTEKYLsfAEKSGKKVGIHAHNNLQLAYANTLEAMIYGASFLDVTV 236
Cdd:PRK05692  155 EAVADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVL--AEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASV 232

                          90
                  ....*....|.
gi 1847328181 237 SGLgrgaGNCP 247
Cdd:PRK05692  233 GGL----GGCP 239
 
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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