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Conserved domains on  [gi|72387992|ref|XP_844420|]
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hydroxymethylglutaryl-CoA lyase, putative [Trypanosoma brucei brucei TREU927]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 15-291 3.18e-99

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: 297.38  E-value: 3.18e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  15 ECPRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANCWKtmqeeKAAPKLSVVVASLAG 94
Cdd:cd07938   4 VGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPR-----RPGVRYSALVPNLRG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  95 FKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEATDAfnaqrssnpvapnedvNGRELLIYISMAFGNP 174
Cdd:cd07938  79 AERALAA-GVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKA----------------AGLRVRGYVSTAFGCP 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 175 YGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTM 254
Cdd:cd07938 142 YEGEVPPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRR 221

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 72387992 255 IDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:cd07938 222 FDSSVGGLGGCPFAP--GATGNVATEDLVYMLEGMGI 256
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 335-401 1.62e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


The actual alignment was detected with superfamily member cd00051:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 63  Bit Score: 42.15  E-value: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72387992 335 CQEHFKLYDVNDDGTLDyegfRDSMIHVFAELGaPQPSEEKIRSSFAKVDIQNLGFITIDAYTMGAR 401
Cdd:cd00051   2 LREAFRLFDKDGDGTIS----ADELKAALKSLG-EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
 
Name Accession Description Interval E-value
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 15-291 3.18e-99

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: 297.38  E-value: 3.18e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  15 ECPRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANCWKtmqeeKAAPKLSVVVASLAG 94
Cdd:cd07938   4 VGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPR-----RPGVRYSALVPNLRG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  95 FKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEATDAfnaqrssnpvapnedvNGRELLIYISMAFGNP 174
Cdd:cd07938  79 AERALAA-GVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKA----------------AGLRVRGYVSTAFGCP 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 175 YGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTM 254
Cdd:cd07938 142 YEGEVPPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRR 221

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 72387992 255 IDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:cd07938 222 FDSSVGGLGGCPFAP--GATGNVATEDLVYMLEGMGI 256
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 7-291 2.16e-52

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 177.39  E-value: 2.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    7 LRSSIRMVEC-PRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANCwktmqEEKAAPKL 85
Cdd:PRK05692   1 LPKRVKIVEVgPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGI-----QRRPGVTY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   86 SVVVASLAGFKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEAtdafnaqrssnpvAPNEDVNGRElli 165
Cdd:PRK05692  76 AALTPNLKGLEAALAA-GADEVAVFASASEAFSQKNINCSIAESLERFEPVAEA-------------AKQAGVRVRG--- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  166 YISMAFGNPYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIV 245
Cdd:PRK05692 139 YVSCVLGCPYEGEVPPEAVADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIY 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 72387992  246 AALDAGCTMIDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:PRK05692 219 ASLEEGITVFDASVGGLGGCPYAP--GASGNVATEDVLYMLHGLGI 262
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 17-293 1.76e-21

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: 93.17  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    17 PRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGsfvSPRAVPQMRDSTEVIAncwKTMQEekaAPKLSVVVASLAGFK 96
Cdd:pfam00682   9 LRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVG---FPAASEDDFEVVRAIA---KVIPH---ARILVLCRAREHDIK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    97 QALETP---GVSVIGYPIGCCERFQqrnaKKSIAMSLDEIrnIKEATDAFNAQRSSNpvapnedvngrelliyISMAFGN 173
Cdd:pfam00682  80 AAVEALkgaGAVRVHVFIATSDLHR----KYKLGKDREEV--AKRAVAAVKAARSRG----------------IDVEFSP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   174 PYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPD-VTFAGHFHSNAVEARGKIVAALDAGC 252
Cdd:pfam00682 138 EDASRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGA 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 72387992   253 TMIDSALCGMGgcpfakddGLVGNVATEVVVKALEERGVLP 293
Cdd:pfam00682 218 DRVDGTVNGIG--------ERAGNAALEEVAAALEGLGVDT 250
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 179-287 2.94e-07

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: 52.48  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 179 HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFH-------SNAveargkiVAALDAG 251
Cdd:COG0119 145 TDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHndlglavANS-------LAAVEAG 217

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72387992 252 CTMIDSALCGMGG-CpfakddglvGNVATEVVVKALE 287
Cdd:COG0119 218 ADQVEGTINGIGErA---------GNAALEEVVMNLK 245
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 335-401 1.62e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.15  E-value: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72387992 335 CQEHFKLYDVNDDGTLDyegfRDSMIHVFAELGaPQPSEEKIRSSFAKVDIQNLGFITIDAYTMGAR 401
Cdd:cd00051   2 LREAFRLFDKDGDGTIS----ADELKAALKSLG-EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
336-394 9.25e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 9.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 72387992   336 QEHFKLYDVNDDGTLDYEGFRDSMIHVfaELGAPqPSEEKIRSSFAKVDIQNLGFITID 394
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEP-LSDEEVEELFKEFDLDKDGRISFE 60
 
Name Accession Description Interval E-value
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 15-291 3.18e-99

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: 297.38  E-value: 3.18e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  15 ECPRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANCWKtmqeeKAAPKLSVVVASLAG 94
Cdd:cd07938   4 VGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWVPQMADAEEVLAGLPR-----RPGVRYSALVPNLRG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  95 FKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEATDAfnaqrssnpvapnedvNGRELLIYISMAFGNP 174
Cdd:cd07938  79 AERALAA-GVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKA----------------AGLRVRGYVSTAFGCP 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 175 YGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTM 254
Cdd:cd07938 142 YEGEVPPERVAEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRR 221

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 72387992 255 IDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:cd07938 222 FDSSVGGLGGCPFAP--GATGNVATEDLVYMLEGMGI 256
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 16-293 9.12e-60

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: 195.75  E-value: 9.12e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  16 CPRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIancwKTMQEEKAAPKLSVVV-ASLAG 94
Cdd:cd03174   4 TLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASPKAVPQMEDDWEVL----RAIRKLVPNVKLQALVrNREKG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  95 FKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRN-IKEATDAfnaqrssnpvapnedvnGRELLIYISMAFGN 173
Cdd:cd03174  80 IERALEA-GVDEVRIFDSASETHSRKNLNKSREEDLENAEEaIEAAKEA-----------------GLEVEGSLEDAFGC 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 174 PygesHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCT 253
Cdd:cd03174 142 K----TDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGAD 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 72387992 254 MIDSALCGMGgcpfakddGLVGNVATEVVVKALEERGVLP 293
Cdd:cd03174 218 RVDGSVNGLG--------ERAGNAATEDLVAALEGLGIDT 249
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 7-291 2.16e-52

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 177.39  E-value: 2.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    7 LRSSIRMVEC-PRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANCwktmqEEKAAPKL 85
Cdd:PRK05692   1 LPKRVKIVEVgPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWVPQMADAAEVMAGI-----QRRPGVTY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   86 SVVVASLAGFKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEAtdafnaqrssnpvAPNEDVNGRElli 165
Cdd:PRK05692  76 AALTPNLKGLEAALAA-GADEVAVFASASEAFSQKNINCSIAESLERFEPVAEA-------------AKQAGVRVRG--- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  166 YISMAFGNPYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIV 245
Cdd:PRK05692 139 YVSCVLGCPYEGEVPPEAVADVAERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIY 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 72387992  246 AALDAGCTMIDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:PRK05692 219 ASLEEGITVFDASVGGLGGCPYAP--GASGNVATEDVLYMLHGLGI 262
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
 7-291 7.56e-38

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 140.31  E-value: 7.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    7 LRSSIRMVEC-PRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAVPQMRDSTEVIANcwktMQEEKAApKL 85
Cdd:PLN02746  43 LPKFVKIVEVgPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWVPQLADAKDVMAA----VRNLEGA-RF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   86 SVVVASLAGFKQALETpGVSVIGYPIGCCERFQQRNAKKSIAMSLDEIRNIKEAtdafnAQRSSNPVAPnedvngrelli 165
Cdd:PLN02746 118 PVLTPNLKGFEAAIAA-GAKEVAVFASASESFSKSNINCSIEESLVRYREVALA-----AKKHSIPVRG----------- 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  166 YISMAFGNPYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIV 245
Cdd:PLN02746 181 YVSCVVGCPIEGPVPPSKVAYVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANIL 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 72387992  246 AALDAGCTMIDSALCGMGGCPFAKddGLVGNVATEVVVKALEERGV 291
Cdd:PLN02746 261 VSLQMGISTVDSSVAGLGGCPYAK--GASGNVATEDVVYMLNGLGV 304
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 17-293 1.76e-21

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: 93.17  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    17 PRDAMQGLPHFIPTEQKIRYLKALLKCGFYALDCGsfvSPRAVPQMRDSTEVIAncwKTMQEekaAPKLSVVVASLAGFK 96
Cdd:pfam00682   9 LRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVG---FPAASEDDFEVVRAIA---KVIPH---ARILVLCRAREHDIK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992    97 QALETP---GVSVIGYPIGCCERFQqrnaKKSIAMSLDEIrnIKEATDAFNAQRSSNpvapnedvngrelliyISMAFGN 173
Cdd:pfam00682  80 AAVEALkgaGAVRVHVFIATSDLHR----KYKLGKDREEV--AKRAVAAVKAARSRG----------------IDVEFSP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   174 PYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPD-VTFAGHFHSNAVEARGKIVAALDAGC 252
Cdd:pfam00682 138 EDASRTDPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGA 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 72387992   253 TMIDSALCGMGgcpfakddGLVGNVATEVVVKALEERGVLP 293
Cdd:pfam00682 218 DRVDGTVNGIG--------ERAGNAALEEVAAALEGLGVDT 250
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
 27-263 2.84e-08

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: 54.65  E-value: 2.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  27 FIPTEQKIRYLKALLKCGfyaLDCGSFVSPRAVPQMRDSTEVIANCwktmqeEKAAPKLSVVVASLAGFKQALETpGVSV 106
Cdd:cd07948  18 FFDTEDKIEIAKALDAFG---VDYIELTSPAASPQSRADCEAIAKL------GLKAKILTHIRCHMDDARIAVET-GVDG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 107 IGYPIGCCERFQQRNAKKSIamslDEIrnIKEATDAFNAQRSsnpvapnedvNGRELLIYISMAFGNPYGESHSIDL-VE 185
Cdd:cd07948  88 VDLVFGTSPFLREASHGKSI----TEI--IESAVEVIEFVKS----------KGIEVRFSSEDSFRSDLVDLLRVYRaVD 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 72387992 186 KLvgelvasGARDISLADTTGVAQPPLIFDTFTQLRKKFP-DVTFagHFHSNAVEARGKIVAALDAGCTMIDSALCGMG 263
Cdd:cd07948 152 KL-------GVNRVGIADTVGIATPRQVYELVRTLRGVVScDIEF--HGHNDTGCAIANAYAALEAGATHIDTTVLGIG 221
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 179-287 2.94e-07

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: 52.48  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 179 HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFH-------SNAveargkiVAALDAG 251
Cdd:COG0119 145 TDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHndlglavANS-------LAAVEAG 217

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72387992 252 CTMIDSALCGMGG-CpfakddglvGNVATEVVVKALE 287
Cdd:COG0119 218 ADQVEGTINGIGErA---------GNAALEEVVMNLK 245
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
 176-263 3.56e-06

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: 48.53  E-value: 3.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 176 GESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTMI 255
Cdd:cd07945 141 GMRDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGL 220


                ....*...
gi 72387992 256 DSALCGMG 263
Cdd:cd07945 221 HTTVNGLG 228
PLN03228 PLN03228
methylthioalkylmalate synthase; Provisional
 171-290 4.87e-06

methylthioalkylmalate synthase; Provisional


Pssm-ID: 178767 [Multi-domain]  Cd Length: 503  Bit Score: 48.76  E-value: 4.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  171 FGNPYGESHSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFP---DVTFAGHFHSNAVEARGKIVAA 247
Cdd:PLN03228 228 FGCEDGGRSDKEFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAG 307

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 72387992  248 LDAGCTMIDSALCGMGgcpfakddGLVGNVATEVVVKALEERG 290
Cdd:PLN03228 308 ICAGARQVEVTINGIG--------ERSGNASLEEVVMALKCRG 342
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
 178-291 5.58e-06

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


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 47.91  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  178 SHSIDlVEKLV--GELVAS-GARDISLADTTGVAQPPLIFDTFTQLRKKF-PDVTFAGHFHSNAVEARGKIVAALDAGCT 253
Cdd:PRK08195 138 SHMAP-PEKLAeqAKLMESyGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGAT 216

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 72387992  254 MIDSALCGMG-GcpfakddglVGNVATEVVVKALEERGV 291
Cdd:PRK08195 217 RIDGSLAGLGaG---------AGNTPLEVLVAVLDRMGW 246
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
 179-290 6.60e-06

Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. 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: 163675  Cd Length: 275  Bit Score: 47.43  E-value: 6.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 179 HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTfagHFHS-----NAVEArgkIVAALDAGCT 253
Cdd:cd07937 146 HTLEYYVKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGLPI---HLHThdtsgLAVAT---YLAAAEAGVD 219

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72387992 254 MIDSALCGMGgcpfakddGLVGNVATEVVVKALEERG 290
Cdd:cd07937 220 IVDTAISPLS--------GGTSQPSTESMVAALRGTG 248
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
 181-290 9.42e-06

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: 47.06  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 181 IDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFP--DVTFAGHFH-------SNAveargkiVAALDAG 251
Cdd:cd07940 142 LDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCHndlglavANS-------LAAVEAG 214

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 72387992 252 CTMIDSALCGMGgcpfakddGLVGNVATEVVVKALEERG 290
Cdd:cd07940 215 ARQVECTINGIG--------ERAGNAALEEVVMALKTRY 245
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
179-303 1.13e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 47.39  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  179 HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLrKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTMIDSA 258
Cdd:PRK12331 151 HTIDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRI-KEAVTVPLEVHTHATSGIAEMTYLKAIEAGADIIDTA 229

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 72387992  259 LcgmggCPFAkddGLVGNVATEVVVKALEERGvLPAALNKEQLKK 303
Cdd:PRK12331 230 I-----SPFA---GGTSQPATESMVAALQDLG-YDTGLDLEELSE 265
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 335-401 1.62e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.15  E-value: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72387992 335 CQEHFKLYDVNDDGTLDyegfRDSMIHVFAELGaPQPSEEKIRSSFAKVDIQNLGFITIDAYTMGAR 401
Cdd:cd00051   2 LREAFRLFDKDGDGTIS----ADELKAALKSLG-EGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PRK12581 PRK12581
oxaloacetate decarboxylase; Provisional
 18-290 6.20e-05

oxaloacetate decarboxylase; Provisional


Pssm-ID: 79056 [Multi-domain]  Cd Length: 468  Bit Score: 45.11  E-value: 6.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   18 RDAMQGL-PHFIPTEQKIRYLKALLKCGFYALDCGSFVSPRAvpqmrdstevianCWKTMQEEKAApKLSVVVASLAGFK 96
Cdd:PRK12581  21 RDGHQSLmATRLSIEDMLPVLTILDKIGYYSLECWGGATFDA-------------CIRFLNEDPWE-RLRTLKKGLPNTR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992   97 QALETPGVSVIGYpigccERFQQRNAKKSIAMSLDEIRNIKEATDAFNAQRSSNPVAPNEDVNGRELLIYISmafgnpYG 176
Cdd:PRK12581  87 LQMLLRGQNLLGY-----RHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIA------YT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  177 ES--HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLrKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTM 254
Cdd:PRK12581 156 TSpvHTLNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGI-KAMTNLPLIVHTHATSGISQMTYLAAVEAGADR 234

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 72387992  255 IDSALcgmggCPFAKDdglVGNVATEVVVKALEERG 290
Cdd:PRK12581 235 IDTAL-----SPFSEG---TSQPATESMYLALKEAG 262
EF-hand_7 pfam13499
EF-hand domain pair;
336-394 9.25e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 9.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 72387992   336 QEHFKLYDVNDDGTLDYEGFRDSMIHVfaELGAPqPSEEKIRSSFAKVDIQNLGFITID 394
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKL--EEGEP-LSDEEVEELFKEFDLDKDGRISFE 60
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
 178-291 9.46e-05

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: 43.64  E-value: 9.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 178 SHSIDlVEKLVGE---LVASGARDISLADTTGVAQPPLIFDTFTQLRKKFPDVTFAGHFHSNAVEARGKIVAALDAGCTM 254
Cdd:cd07943 135 SHMAS-PEELAEQaklMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATR 213

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72387992 255 IDSALCGMGGCpfakddglVGNVATEVVVKALEERGV 291
Cdd:cd07943 214 IDGSLAGLGAG--------AGNTPLEVLVAVLERMGI 242
PRK14041 PRK14041
pyruvate carboxylase subunit B;
109-305 1.06e-04

pyruvate carboxylase subunit B;


Pssm-ID: 237593 [Multi-domain]  Cd Length: 467  Bit Score: 44.39  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  109 YPIGCCERFqqrnAKKSIAMSLDEIRNIKEATDAFNAQRSSNpVAPNEDvngrellIYISMAFGNPYGESHSIDLVEKLV 188
Cdd:PRK14041  92 YADDVVELF----VKKVAEYGLDIIRIFDALNDIRNLEKSIE-VAKKHG-------AHVQGAISYTVSPVHTLEYYLEFA 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  189 GELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFpDVTFAGHFHSNAVEARGKIVAALDAGCTMIDSALcgmggCPFA 268
Cdd:PRK14041 160 RELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAI-----SPFS 233

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 72387992  269 KDdglVGNVATEVVVKALEERGVLPaALNKEQLKKCV 305
Cdd:PRK14041 234 MG---TSQPPFESMYYAFRENGKET-DFDRKALKFLV 266
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 164-289 1.67e-04

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: 42.94  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 164 LIYISMafgnpYGESHSIDLVEKlVGELVASGardISLADTTGVAQPPLIFDTFTQLRKKF-PDVTFAGHFH-------S 235
Cdd:cd07944 129 LMAISG-----YSDEELLELLEL-VNEIKPDV---FYIVDSFGSMYPEDIKRIISLLRSNLdKDIKLGFHAHnnlqlalA 199

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 72387992 236 NAVEArgkivaaLDAGCTMIDSALCGMGGCPfakddglvGNVATEVVVKALEER 289
Cdd:cd07944 200 NTLEA-------IELGVEIIDATVYGMGRGA--------GNLPTELLLDYLNNK 238
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
 181-287 5.80e-03

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: 38.26  E-value: 5.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992 181 IDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFP-DVTFagHFH-------SNAveargkiVAALDAGC 252
Cdd:cd07939 138 PDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAATDlPLEF--HAHndlglatANT-------LAAVRAGA 208

                        90       100       110
                ....*....|....*....|....*....|....*
gi 72387992 253 TMIDSALCGMGgcpfakddGLVGNVATEVVVKALE 287
Cdd:cd07939 209 THVSVTVNGLG--------ERAGNAALEEVVMALK 235
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
179-288 8.79e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 38.37  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72387992  179 HSIDLVEKLVGELVASGARDISLADTTGVAQPPLIFDTFTQLRKKFpDVTFAGHFHSNAVEARGKIVAALDAGCTMIDSA 258
Cdd:PRK14040 152 HTLQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTA 230

                         90       100       110
                 ....*....|....*....|....*....|
gi 72387992  259 LCGMGGCpfakddglVGNVATEVVVKALEE 288
Cdd:PRK14040 231 ISSMSMT--------YGHSATETLVATLEG 252
 
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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