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Conserved domains on  [gi|1622834318|ref|XP_028694053|]
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hydroxymethylglutaryl-CoA lyase, mitochondrial isoform X4 [Macaca mulatta]

Protein Classification

hydroxymethylglutaryl-CoA lyase( domain architecture ID 10168151)

hydroxymethylglutaryl-CoA lyase catalyzes the formation of acetoacetate and acetyl-CoA from 3-hydroxy-3-methylglutaryl-CoA

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; ...
 45-282 1.29e-151

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: 425.27  E-value: 1.29e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  45 IVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIPNLKGFE 88
Cdd:cd07938     1 IVEVGPRDGLQNEKtfiptedkielidalsaaglrrievtsfvspkwvpqMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  89 AAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEVTKKFYS 168
Cdd:cd07938    81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGCPYEGEVPPERVAEVAERLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 169 MGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASG 248
Cdd:cd07938   161 LGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLGGCPFAPGATG 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1622834318 249 NLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQ 282
Cdd:cd07938   241 NVATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
 
Name Accession Description Interval E-value
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 45-282 1.29e-151

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: 425.27  E-value: 1.29e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  45 IVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIPNLKGFE 88
Cdd:cd07938     1 IVEVGPRDGLQNEKtfiptedkielidalsaaglrrievtsfvspkwvpqMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  89 AAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEVTKKFYS 168
Cdd:cd07938    81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGCPYEGEVPPERVAEVAERLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 169 MGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASG 248
Cdd:cd07938   161 LGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLGGCPFAPGATG 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1622834318 249 NLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQ 282
Cdd:cd07938   241 NVATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 39-289 8.75e-151

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 423.53  E-value: 8.75e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  39 LPKQVKIVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIP 82
Cdd:PRK05692    1 LPKRVKIVEVGPRDGLQNEKrfiptadkialidrlsaaglsyievasfvspkwvpqMADAAEVMAGIQRRPGVTYAALTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  83 NLKGFEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEV 162
Cdd:PRK05692   81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYVSCVLGCPYEGEVPPEAVADV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 163 TKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPY 242
Cdd:PRK05692  161 AERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGGCPY 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834318 243 AQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTS 289
Cdd:PRK05692  241 APGASGNVATEDVLYMLHGLGIETGIDLDKLVRAGQFIQSKLGRPLP 287
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 42-280 7.54e-78

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: 237.62  E-value: 7.54e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  42 QVKIVEVGPRDGLQN--------EKMA----------------------DHAEVLKGIQKFPGIT--YPVLIPNLKGFEA 89
Cdd:pfam00682   1 AVAICDTTLRDGEQAlgvafsidEKLAiaraldaagvdeievgfpaaseDDFEVVRAIAKVIPHAriLVLCRAREHDIKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  90 AVA----AGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRgyvscvLGCPYEGKISPAKVAEVTKK 165
Cdd:pfam00682  81 AVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVE------FSPEDASRTDPEFLAEVVEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 166 FYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPP-AALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaq 244
Cdd:pfam00682 155 AIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIG------ 228

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622834318 245 GASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFI 280
Cdd:pfam00682 229 ERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANLV 264
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 87-287 2.51e-20

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: 90.23  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  87 FEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRgyVSCvlgcpyE--GKISPAKVAEVTK 164
Cdd:COG0119    84 LEALKGAGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVE--FSA------EdaTRTDPDFLLEVLE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 165 KFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGG-Cpya 243
Cdd:COG0119   156 AAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIGErA--- 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834318 244 qgasGNLATEDLV---YMLegLGIHTGVNLQKLLEAGNFICQALNRK 287
Cdd:COG0119   233 ----GNAALEEVVmnlKLK--YGVDTGIDLSKLTELSRLVSEITGLP 273
 
Name Accession Description Interval E-value
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 45-282 1.29e-151

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: 425.27  E-value: 1.29e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  45 IVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIPNLKGFE 88
Cdd:cd07938     1 IVEVGPRDGLQNEKtfiptedkielidalsaaglrrievtsfvspkwvpqMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  89 AAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEVTKKFYS 168
Cdd:cd07938    81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGCPYEGEVPPERVAEVAERLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 169 MGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASG 248
Cdd:cd07938   161 LGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLGGCPFAPGATG 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1622834318 249 NLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQ 282
Cdd:cd07938   241 NVATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 39-289 8.75e-151

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 423.53  E-value: 8.75e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  39 LPKQVKIVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIP 82
Cdd:PRK05692    1 LPKRVKIVEVGPRDGLQNEKrfiptadkialidrlsaaglsyievasfvspkwvpqMADAAEVMAGIQRRPGVTYAALTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  83 NLKGFEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEV 162
Cdd:PRK05692   81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYVSCVLGCPYEGEVPPEAVADV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 163 TKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPY 242
Cdd:PRK05692  161 AERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGGCPY 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834318 243 AQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTS 289
Cdd:PRK05692  241 APGASGNVATEDVLYMLHGLGIETGIDLDKLVRAGQFIQSKLGRPLP 287
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
 39-299 8.12e-150

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 423.43  E-value: 8.12e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  39 LPKQVKIVEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKFPGITYPVLIP 82
Cdd:PLN02746   43 LPKFVKIVEVGPRDGLQNEKnivptsvkveliqrlvssglpvveatsfvspkwvpqLADAKDVMAAVRNLEGARFPVLTP 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  83 NLKGFEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYEGKISPAKVAEV 162
Cdd:PLN02746  123 NLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYVSCVVGCPIEGPVPPSKVAYV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 163 TKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPY 242
Cdd:PLN02746  203 AKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGCPY 282

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622834318 243 AQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKL 299
Cdd:PLN02746  283 AKGASGNVATEDVVYMLNGLGVSTNVDLGKLMAAGDFISKHLGRPSGSKTAVALSAR 339
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 46-282 1.21e-87

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: 262.78  E-value: 1.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  46 VEVGPRDGLQNEK------------------------------------MADHAEVLKGIQKF-PGITYPVLIPN-LKGF 87
Cdd:cd03174     1 TDTTLRDGLQSEGatfstedkleiaealdeagvdsievgsgaspkavpqMEDDWEVLRAIRKLvPNVKLQALVRNrEKGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  88 EAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPYegkiSPAKVAEVTKKFY 167
Cdd:cd03174    81 ERALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAAKEAGLEVEGSLEDAFGCKT----DPEYVLEVAKALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 168 SMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaqGAS 247
Cdd:cd03174   157 EAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGADRVDGSVNGLG------ERA 230

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622834318 248 GNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQ 282
Cdd:cd03174   231 GNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE 265
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 42-280 7.54e-78

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: 237.62  E-value: 7.54e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  42 QVKIVEVGPRDGLQN--------EKMA----------------------DHAEVLKGIQKFPGIT--YPVLIPNLKGFEA 89
Cdd:pfam00682   1 AVAICDTTLRDGEQAlgvafsidEKLAiaraldaagvdeievgfpaaseDDFEVVRAIAKVIPHAriLVLCRAREHDIKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  90 AVA----AGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRgyvscvLGCPYEGKISPAKVAEVTKK 165
Cdd:pfam00682  81 AVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVE------FSPEDASRTDPEFLAEVVEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 166 FYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPP-AALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaq 244
Cdd:pfam00682 155 AIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIG------ 228

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622834318 245 GASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFI 280
Cdd:pfam00682 229 ERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANLV 264
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 87-287 2.51e-20

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: 90.23  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  87 FEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRgyVSCvlgcpyE--GKISPAKVAEVTK 164
Cdd:COG0119    84 LEALKGAGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVE--FSA------EdaTRTDPDFLLEVLE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 165 KFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGG-Cpya 243
Cdd:COG0119   156 AAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIGErA--- 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834318 244 qgasGNLATEDLV---YMLegLGIHTGVNLQKLLEAGNFICQALNRK 287
Cdd:COG0119   233 ----GNAALEEVVmnlKLK--YGVDTGIDLSKLTELSRLVSEITGLP 273
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
 154-280 5.24e-19

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: 84.47  E-value: 5.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 154 ISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSS 233
Cdd:cd07943   138 ASPEELAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGS 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622834318 234 VAGLGGCpyaqgaSGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFI 280
Cdd:cd07943   218 LAGLGAG------AGNTPLEVLVAVLERMGIETGIDLYKLMDAAEDL 258
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
 160-276 4.72e-16

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: 76.32  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 160 AEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVP-PaaLAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLG 238
Cdd:cd07937   152 VKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGlP--IHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLS 229

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622834318 239 GCpYAQGasgnlATEDLVYMLEGLGIHTGVNLQKLLEA 276
Cdd:cd07937   230 GG-TSQP-----STESMVAALRGTGRDTGLDLEKLEEI 261
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
 170-276 1.91e-15

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: 74.41  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 170 GCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAA--LAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaqGAS 247
Cdd:cd07940   156 GATTINIPDTVGYLTPEEFGELIKKLKENVPNIKvpISVHCHNDLGLAVANSLAAVEAGARQVECTINGIG------ERA 229

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622834318 248 GNLATEDLV----YMLEGLGIHTGVNLQKLLEA 276
Cdd:cd07940   230 GNAALEEVVmalkTRYDYYGVETGIDTEELYET 262
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
 154-276 1.47e-14

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


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 72.94  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 154 ISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAA-LAVHCHDTYGQALANTLMALQMGVSVVDS 232
Cdd:PRK08195  141 APPEKLAEQAKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALKPDTqVGFHGHNNLGLGVANSLAAVEAGATRIDG 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622834318 233 SVAGLGGcpyaqGAsGNLATEDLVYMLEGLGIHTGVNLQKLLEA 276
Cdd:PRK08195  221 SLAGLGA-----GA-GNTPLEVLVAVLDRMGWETGVDLYKLMDA 258
aksA PRK11858
trans-homoaconitate synthase; Reviewed
 88-287 3.53e-14

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 72.13  E-value: 3.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  88 EAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRF-DAI-------LKAAQSANISVRgyvscvlgCPYEGKISPAKV 159
Cdd:PRK11858   82 DASIDCGVDAVHIFIATSDIHIKHKLKKTREEVLERMvEAVeyakdhgLYVSFSAEDASR--------TDLDFLIEFAKA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 160 AEvtkkfySMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPpAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGg 239
Cdd:PRK11858  154 AE------EAGADRVRFCDTVGILDPFTMYELVKELVEAVD-IPIEVHCHNDFGMATANALAGIEAGAKQVHTTVNGLG- 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622834318 240 cpyaqGASGNLATEDLVYMLEGL-GIHTGVNLQKLLEAGNFICQALNRK 287
Cdd:PRK11858  226 -----ERAGNAALEEVVMALKYLyGIDLGIDTERLYELSRLVSKASGIP 269
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 121-287 2.36e-13

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 70.26  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 121 FQRFDAI---------LKAAQSANISVRGYVScvlgcpYegKISP----AKVAEVTKKFYSMGCYEISLGDTIGVGTPGI 187
Cdd:PRK09282  113 FRIFDALndvrnmevaIKAAKKAGAHVQGTIS------Y--TTSPvhtiEKYVELAKELEEMGCDSICIKDMAGLLTPYA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 188 MKDMLSAVMQEVP-PaaLAVHCHDTYGQALANTLMALQMGVSVVDSSVAglggcPYAQGASgNLATEDLVYMLEGLGIHT 266
Cdd:PRK09282  185 AYELVKALKEEVDlP--VQLHSHCTSGLAPMTYLKAVEAGVDIIDTAIS-----PLAFGTS-QPPTESMVAALKGTPYDT 256

                         170       180
                  ....*....|....*....|.
gi 1622834318 267 GVNLQKLLEAGNfICQALNRK 287
Cdd:PRK09282  257 GLDLELLFEIAE-YFREVRKK 276
PRK00915 PRK00915
2-isopropylmalate synthase; Validated
 174-296 5.54e-12

2-isopropylmalate synthase; Validated


Pssm-ID: 234864 [Multi-domain]  Cd Length: 513  Bit Score: 65.90  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 174 ISLGDTIGVGTPGIMKDMLSAVMQEVP---PAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaQGAsGNL 250
Cdd:PRK00915  166 INIPDTVGYTTPEEFGELIKTLRERVPnidKAIISVHCHNDLGLAVANSLAAVEAGARQVECTINGIG-----ERA-GNA 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622834318 251 ATEDLVYML----EGLGIHTGVNLQKLLEagnficqalnrkTSSKVAQAT 296
Cdd:PRK00915  240 ALEEVVMALktrkDIYGVETGINTEEIYR------------TSRLVSQLT 277
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
124-275 2.11e-11

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 63.95  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 124 FDAI-----LKAAQSANISVRGYVSCVLGcpYegKISPAKVAE----VTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSA 194
Cdd:PRK12331  116 FDALndvrnLETAVKATKKAGGHAQVAIS--Y--TTSPVHTIDyfvkLAKEMQEMGADSICIKDMAGILTPYVAYELVKR 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 195 VMQE--VPpaaLAVHCHDTYGQALANTLMALQMGVSVVDSSVAglggcPYAQGASgNLATEDLVYMLEGLGIHTGVNLQK 272
Cdd:PRK12331  192 IKEAvtVP---LEVHTHATSGIAEMTYLKAIEAGADIIDTAIS-----PFAGGTS-QPATESMVAALQDLGYDTGLDLEE 262


                  ...
gi 1622834318 273 LLE 275
Cdd:PRK12331  263 LSE 265
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 121-276 3.33e-11

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: 62.20  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 121 FQRFDAILKAAQSanISVRGY-VSCVLgcPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEV 199
Cdd:cd07944   105 KHEFDEALPLIKA--IKEKGYeVFFNL--MAISGYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNL 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834318 200 PPA-ALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaQGAsGNLATEDLVYMLEGLGIHTgVNLQKLLEA 276
Cdd:cd07944   181 DKDiKLGFHAHNNLQLALANTLEAIELGVEIIDATVYGMG-----RGA-GNLPTELLLDYLNNKFGKK-YNLEPVLEL 251
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
 157-295 1.44e-10

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: 60.21  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 157 AKVAEvtkkfySMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPpAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAG 236
Cdd:cd07939   145 AEVAQ------EAGADRLRFADTVGILDPFTTYELIRRLRAATD-LPLEFHAHNDLGLATANTLAAVRAGATHVSVTVNG 217

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 237 LGgcpyaQGAsGNLATEDLVYMLEGL-GIHTGVNLQKLLEagnfICQalnrktssKVAQA 295
Cdd:cd07939   218 LG-----ERA-GNAALEEVVMALKHLyGRDTGIDTTRLPE----LSQ--------LVARA 259
PRK09389 PRK09389
(R)-citramalate synthase; Provisional
 178-288 1.56e-10

(R)-citramalate synthase; Provisional


Pssm-ID: 236493 [Multi-domain]  Cd Length: 488  Bit Score: 61.49  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 178 DTIGVGTPGIMKDMLSAvMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpyaqGASGNLATEDLVY 257
Cdd:PRK09389  164 DTVGILTPEKTYELFKR-LSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTINGIG------ERAGNASLEEVVM 236

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622834318 258 MLEGL-GIHTGVNLQKLLEagnfICQALNRKT 288
Cdd:PRK09389  237 ALKHLyDVETGIKLEELYE----LSRLVSRLT 264
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
161-275 1.08e-09

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 59.17  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 161 EVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQE--VPpaaLAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLg 238
Cdd:PRK14040  159 DLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRvdVP---LHLHCHATTGLSTATLLKAIEAGIDGVDTAISSM- 234

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622834318 239 GCPYaqgasGNLATEDLVYMLEGLGIHTGVNLQKLLE 275
Cdd:PRK14040  235 SMTY-----GHSATETLVATLEGTERDTGLDILKLEE 266
PRK12330 PRK12330
methylmalonyl-CoA carboxytransferase subunit 5S;
155-276 2.68e-09

methylmalonyl-CoA carboxytransferase subunit 5S;


Pssm-ID: 183445 [Multi-domain]  Cd Length: 499  Bit Score: 57.85  E-value: 2.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 155 SPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPP-AALAVHCHDTYGQALANTLMALQMGVSVVDSS 233
Cdd:PRK12330  153 TVEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACGEdTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTA 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622834318 234 VAGLGGCPyaqgasGNLATEDLVYMLEGLGIHTGVNLQKLLEA 276
Cdd:PRK12330  233 ISSMSLGP------GHNPTESLVEMLEGTGYTTKLDMDRLLKI 269
PLN03228 PLN03228
methylthioalkylmalate synthase; Provisional
 87-274 3.40e-09

methylthioalkylmalate synthase; Provisional


Pssm-ID: 178767 [Multi-domain]  Cd Length: 503  Bit Score: 57.24  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  87 FEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSAnisvrGYVSCVLGCPYEGKISPAKVAEVTKKF 166
Cdd:PLN03228  174 WEALKYAKRPRILAFTSTSDIHMKYKLKKTKEEVIEMAVSSIRYAKSL-----GFHDIQFGCEDGGRSDKEFLCKILGEA 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 167 YSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPA---ALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGgcpya 243
Cdd:PLN03228  249 IKAGATSVGIADTVGINMPHEFGELVTYVKANTPGIddiVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIG----- 323

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622834318 244 qGASGNLATEDLV--------YMLEGLgiHTGVNLQKLL 274
Cdd:PLN03228  324 -ERSGNASLEEVVmalkcrgaYLMNGV--YTGIDTRQIM 359
DRE_TIM_LeuA3 cd07941
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ...
 82-238 1.57e-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: 51.69  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  82 PNLKgfeAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQR-FDAI--LKAAqsanisVR-----------GYvscvlg 147
Cdd:cd07941    82 PNLQ---ALLEAGTPVVTIFGKSWDLHVTEALGTTLEENLAMiRDSVayLKSH------GRevifdaehffdGY------ 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 148 cpyegKISPAKVAEVTKKFYSMGCYEISLGDTIGvGT-PGIMKDMLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMG 226
Cdd:cd07941   147 -----KANPEYALATLKAAAEAGADWLVLCDTNG-GTlPHEIAEIVKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAG 220

                         170
                  ....*....|..
gi 1622834318 227 VSVVDSSVAGLG 238
Cdd:cd07941   221 ATQVQGTINGYG 232
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
 57-280 5.81e-07

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: 50.07  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  57 EKMADHAEVLKGIQKFPGITYpvlIPNLKGFEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANI 136
Cdd:cd07945    53 QKIIDWAAEEGLLDRIEVLGF---VDGDKSVDWIKSAGAKVLNLLTKGSLKHCTEQLRKTPEEHFADIREVIEYAIKNGI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 137 SVRGYVscvlgcpyEG-----KISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPPAALAVHCHDT 211
Cdd:cd07945   130 EVNIYL--------EDwsngmRDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHND 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 212 YGQALANTLMALQMGVSVVDSSVAGLGgcpyaqGASGNLATEDLVYML-EGLGIHTGVNLQKLLEAGNFI 280
Cdd:cd07945   202 YDLAVANVLAAVKAGIKGLHTTVNGLG------ERAGNAPLASVIAVLkDKLKVKTNIDEKRLNRASRLV 265
DRE_TIM_Re_CS cd07947
Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain; ...
 71-280 5.94e-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: 50.01  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  71 KFPGITYPVLiPNLKGFEAAVAAGAKEVSIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCVLGCPY 150
Cdd:cd07947    65 KFPEVTGWIR-ANKEDLKLVKEMGLKETGILMSVSDYHIFKKLKMTREEAMEKYLEIVEEALDHGIKPRCHLEDITRADI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 151 EGKISP--AKVAEVTKKfYSMGCYeISLGDTIGVGTP---------------GIMKDMlsavmqEVPPAALAVHCHDTYG 213
Cdd:cd07947   144 YGFVLPfvNKLMKLSKE-SGIPVK-IRLCDTLGYGVPypgaslprsvpkiiyGLRKDC------GVPSENLEWHGHNDFY 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622834318 214 QALANTLMALQMGVSVVDSSVAGLGgcpyaqGASGNLATEDLVYMLEGL-GIHTGVNLQKLLEAGNFI 280
Cdd:cd07947   216 KAVANAVAAWLYGASWVNCTLLGIG------ERTGNCPLEAMVIEYAQLkGNFDGMNLEVITEIAEYF 277
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
 168-238 1.57e-06

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: 48.48  E-value: 1.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622834318 168 SMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPpAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLG 238
Cdd:cd07948   152 KLGVNRVGIADTVGIATPRQVYELVRTLRGVVS-CDIEFHGHNDTGCAIANAYAALEAGATHIDTTVLGIG 221
PRK12581 PRK12581
oxaloacetate decarboxylase; Provisional
 162-283 3.15e-06

oxaloacetate decarboxylase; Provisional


Pssm-ID: 79056 [Multi-domain]  Cd Length: 468  Bit Score: 48.19  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 162 VTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAV--MQEVPpaaLAVHCHDTYGQALANTLMALQMGVSVVDSSVAglgg 239
Cdd:PRK12581  168 LVKELVEMGADSICIKDMAGILTPKAAKELVSGIkaMTNLP---LIVHTHATSGISQMTYLAAVEAGADRIDTALS---- 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622834318 240 cPYAQGASgNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQA 283
Cdd:PRK12581  241 -PFSEGTS-QPATESMYLALKEAGYDITLDETLLEQAANHLRQA 282
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 186-273 3.42e-06

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 48.60  E-value: 3.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318  186 GImKDMlSAVMQevPPAA------------LAVHCH--DTYGQALANTLMALQMGVSVVD---SSVAGLggcpYAQGASG 248
Cdd:PRK12999   709 AI-KDM-AGLLK--PAAAyelvsalkeevdLPIHLHthDTSGNGLATYLAAAEAGVDIVDvavASMSGL----TSQPSLN 780

                           90       100
                   ....*....|....*....|....*
gi 1622834318  249 NlatedLVYMLEGLGIHTGVNLQKL 273
Cdd:PRK12999   781 S-----IVAALEGTERDTGLDLDAI 800
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 161-295 4.03e-05

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 45.10  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622834318 161 EVTKKFYSMGCYEISLGDTIGVGTPGIMKDmLSAVMQEVPPAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGc 240
Cdd:PRK14042  158 ELGKKLAEMGCDSIAIKDMAGLLTPTVTVE-LYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG- 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622834318 241 pyaqGASgNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFIcQALNRKTSSKVAQA 295
Cdd:PRK14042  236 ----GAS-HPPTEALVAALTDTPYDTELDLNILLEIDDYF-KAVRKKYSQFESEA 284
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 206-275 9.65e-05

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 43.91  E-value: 9.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622834318  206 VHCHDTYGQALANTLMALQMGVSVVD---SSVAGLGGCPyaqgasgNLATedLVYMLEGLGIHTGVNLQKLLE 275
Cdd:COG1038    739 LHTHDTSGNQLATYLAAIEAGVDIVDvalASMSGLTSQP-------SLNS--LVAALEGTERDTGLDLDALQE 802
PRK12344 PRK12344
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
 176-238 1.82e-04

putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional


Pssm-ID: 237068 [Multi-domain]  Cd Length: 524  Bit Score: 42.77  E-value: 1.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622834318 176 LGDTIGvGT-PGIMKDMLSAVMQEVPpAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLG 238
Cdd:PRK12344  177 LCDTNG-GTlPHEVAEIVAEVRAAPG-VPLGIHAHNDSGCAVANSLAAVEAGARQVQGTINGYG 238
 
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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