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Conserved domains on  [gi|2502273086|ref|NP_001407959|]
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hydroxymethylglutaryl-CoA lyase, mitochondrial isoform 7 precursor [Mus musculus]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 17-322 5.57e-179

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member PLN02746:

Pssm-ID: 473867  Cd Length: 347  Bit Score: 498.55  E-value: 5.57e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  17 SLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQ 93
Cdd:PLN02746   31 GVAHMHNKLLKGLPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWvpqLADAKDVMAAVR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  94 KFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPY 173
Cdd:PLN02746  111 NLEGARFPVLTPNLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYVSCVVGCPI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 174 EGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVV 253
Cdd:PLN02746  191 EGPVPPSKVAYVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTV 270

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502273086 254 DSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL 322
Cdd:PLN02746  271 DSSVAGLGGCPYAKGASGNVATEDVVYMLNGLGVSTNVDLGKLMAAGDFISKHLGRPSGSKTAVALSAR 339
 
Name Accession Description Interval E-value
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
 17-322 5.57e-179

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 498.55  E-value: 5.57e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  17 SLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQ 93
Cdd:PLN02746   31 GVAHMHNKLLKGLPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWvpqLADAKDVMAAVR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  94 KFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPY 173
Cdd:PLN02746  111 NLEGARFPVLTPNLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYVSCVVGCPI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 174 EGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVV 253
Cdd:PLN02746  191 EGPVPPSKVAYVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTV 270

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502273086 254 DSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL 322
Cdd:PLN02746  271 DSSVAGLGGCPYAKGASGNVATEDVVYMLNGLGVSTNVDLGKLMAAGDFISKHLGRPSGSKTAVALSAR 339
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 35-305 1.78e-178

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: 494.22  E-value: 1.78e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  35 IVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQKFPGINYPVLTPNMKGFE 111
Cdd:cd07938     1 IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWvpqMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 112 EAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYS 191
Cdd:cd07938    81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGCPYEGEVPPERVAEVAERLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 192 MGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASG 271
Cdd:cd07938   161 LGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLGGCPFAPGATG 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2502273086 272 NLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQ 305
Cdd:cd07938   241 NVATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 32-303 4.57e-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: 239.17  E-value: 4.57e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  32 QVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEAT-SFVSPkwmaDHSDVLKGIQKFPGIN--YPVLTPNMK 108
Cdd:pfam00682   1 AVAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGfPAASE----DDFEVVRAIAKVIPHAriLVLCRAREH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 109 GFEEAVA----AGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyvscaLGCPYEGKVSPAKVAE 184
Cdd:pfam00682  77 DIKAAVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVE------FSPEDASRTDPEFLAE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 185 VAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPV-TALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgc 263
Cdd:pfam00682 151 VVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIG-- 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2502273086 264 pyakGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFI 303
Cdd:pfam00682 229 ----ERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANLV 264
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 30-310 1.78e-19

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


Pssm-ID: 439889 [Multi-domain]  Cd Length: 452  Bit Score: 88.30  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  30 PKQVKIVEVGPRDGLQNEkSIVPTPV-KIRLIDMLSEAGLPVIEATSFV-SP------KWMAD---HSDVLkgiqkfpgi 98
Cdd:COG0119     1 PDRIIIFDTTLRDGEQAP-GVSFSVEeKLRIARLLDELGVDEIEAGFPAaSPgdfeavRRIAElglDATIC--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  99 nypVLTPNMKGFEEAVA-----AGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyVSCalgcpy 173
Cdd:COG0119    71 ---ALARARRKDIDAALealkgAGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVE--FSA------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 174 E--GKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVS 251
Cdd:COG0119   140 EdaTRTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGAD 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502273086 252 VVDSSVAGLGG-CpyakgasGNLATEDLV-YMLNGLGIHTGVNLQKLLEAGDFICQALNRK 310
Cdd:COG0119   220 QVEGTINGIGErA-------GNAALEEVVmNLKLKYGVDTGIDLSKLTELSRLVSEITGLP 273
 
Name Accession Description Interval E-value
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
 17-322 5.57e-179

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 498.55  E-value: 5.57e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  17 SLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQ 93
Cdd:PLN02746   31 GVAHMHNKLLKGLPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWvpqLADAKDVMAAVR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  94 KFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPY 173
Cdd:PLN02746  111 NLEGARFPVLTPNLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVRGYVSCVVGCPI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 174 EGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVV 253
Cdd:PLN02746  191 EGPVPPSKVAYVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTV 270

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502273086 254 DSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL 322
Cdd:PLN02746  271 DSSVAGLGGCPYAKGASGNVATEDVVYMLNGLGVSTNVDLGKLMAAGDFISKHLGRPSGSKTAVALSAR 339
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
 35-305 1.78e-178

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: 494.22  E-value: 1.78e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  35 IVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQKFPGINYPVLTPNMKGFE 111
Cdd:cd07938     1 IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSFVSPKWvpqMADAEEVLAGLPRRPGVRYSALVPNLRGAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 112 EAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYS 191
Cdd:cd07938    81 RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVRGYVSTAFGCPYEGEVPPERVAEVAERLLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 192 MGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASG 271
Cdd:cd07938   161 LGCDEISLGDTIGVATPAQVRRLLEAVLERFPDEKLALHFHDTRGQALANILAALEAGVRRFDSSVGGLGGCPFAPGATG 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2502273086 272 NLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQ 305
Cdd:cd07938   241 NVATEDLVYMLEGMGIETGIDLDKLLAAARWISE 274
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
 29-312 4.20e-176

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 488.63  E-value: 4.20e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  29 LPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQKFPGINYPVLTP 105
Cdd:PRK05692    1 LPKRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASFVSPKWvpqMADAAEVMAGIQRRPGVTYAALTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 106 NMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEV 185
Cdd:PRK05692   81 NLKGLEAALAAGADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVRGYVSCVLGCPYEGEVPPEAVADV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 186 AKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPY 265
Cdd:PRK05692  161 AERLFALGCYEISLGDTIGVGTPGQVRAVLEAVLAEFPAERLAGHFHDTYGQALANIYASLEEGITVFDASVGGLGGCPY 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2502273086 266 AKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTS 312
Cdd:PRK05692  241 APGASGNVATEDVLYMLHGLGIETGIDLDKLVRAGQFIQSKLGRPLP 287
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 36-305 9.31e-106

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: 309.39  E-value: 9.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  36 VEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKW---MADHSDVLKGIQKF-PGINYPVLTPN-MKGF 110
Cdd:cd03174     1 TDTTLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASPKAvpqMEDDWEVLRAIRKLvPNVKLQALVRNrEKGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 111 EEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCpyegKVSPAKVAEVAKKLY 190
Cdd:cd03174    81 ERALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAAKEAGLEVEGSLEDAFGC----KTDPEYVLEVAKALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 191 SMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgcpyakGAS 270
Cdd:cd03174   157 EAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGADRVDGSVNGLG------ERA 230

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2502273086 271 GNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQ 305
Cdd:cd03174   231 GNAATEDLVAALEGLGIDTGIDLEKLLEISRYVEE 265
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
 32-303 4.57e-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: 239.17  E-value: 4.57e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  32 QVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEAT-SFVSPkwmaDHSDVLKGIQKFPGIN--YPVLTPNMK 108
Cdd:pfam00682   1 AVAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGfPAASE----DDFEVVRAIAKVIPHAriLVLCRAREH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 109 GFEEAVA----AGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyvscaLGCPYEGKVSPAKVAE 184
Cdd:pfam00682  77 DIKAAVEalkgAGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVE------FSPEDASRTDPEFLAE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 185 VAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPV-TALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgc 263
Cdd:pfam00682 151 VVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIG-- 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2502273086 264 pyakGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFI 303
Cdd:pfam00682 229 ----ERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANLV 264
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
 177-303 5.88e-20

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: 87.55  E-value: 5.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 177 VSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSS 256
Cdd:cd07943   138 ASPEELAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRIDGS 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2502273086 257 VAGLGGCpyakgaSGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFI 303
Cdd:cd07943   218 LAGLGAG------AGNTPLEVLVAVLERMGIETGIDLYKLMDAAEDL 258
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
 30-310 1.78e-19

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


Pssm-ID: 439889 [Multi-domain]  Cd Length: 452  Bit Score: 88.30  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  30 PKQVKIVEVGPRDGLQNEkSIVPTPV-KIRLIDMLSEAGLPVIEATSFV-SP------KWMAD---HSDVLkgiqkfpgi 98
Cdd:COG0119     1 PDRIIIFDTTLRDGEQAP-GVSFSVEeKLRIARLLDELGVDEIEAGFPAaSPgdfeavRRIAElglDATIC--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  99 nypVLTPNMKGFEEAVA-----AGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyVSCalgcpy 173
Cdd:COG0119    71 ---ALARARRKDIDAALealkgAGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVE--FSA------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 174 E--GKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVS 251
Cdd:COG0119   140 EdaTRTDPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHNDLGLAVANSLAAVEAGAD 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502273086 252 VVDSSVAGLGG-CpyakgasGNLATEDLV-YMLNGLGIHTGVNLQKLLEAGDFICQALNRK 310
Cdd:COG0119   220 QVEGTINGIGErA-------GNAALEEVVmNLKLKYGVDTGIDLSKLTELSRLVSEITGLP 273
aksA PRK11858
trans-homoaconitate synthase; Reviewed
 30-298 9.40e-16

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 77.14  E-value: 9.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  30 PKQVKIVEVGPRDGLQneksivpTP-V------KIRLIDMLSEAGLPVIEAtSF--VSpkwmADHSDVLKGIQKFpGINY 100
Cdd:PRK11858    2 PKDIEIVDTTLRDGEQ-------TPgVvftneeKLAIARMLDEIGVDQIEA-GFpaVS----EDEKEAIKAIAKL-GLNA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 101 PVLT---PNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyvscalgcpyegkV 177
Cdd:PRK11858   69 SILAlnrAVKSDIDASIDCGVDAVHIFIATSDIHIKHKLKKTREEVLERMVEAVEYAKDHGLYVS--------------F 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 178 SP--------AKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMG 249
Cdd:PRK11858  135 SAedasrtdlDFLIEFAKAAEEAGADRVRFCDTVGILDPFTMYELVKELVEAVDI-PIEVHCHNDFGMATANALAGIEAG 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2502273086 250 VSVVDSSVAGLGgcpyakGASGNLATEDLVYMLNGL-GIHTGVNLQKLLE 298
Cdd:PRK11858  214 AKQVHTTVNGLG------ERAGNAALEEVVMALKYLyGIDLGIDTERLYE 257
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
 178-301 3.03e-15

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


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 75.25  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 178 SPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEV-PVTALAVHCHDTYGQALANTLVALQMGVSVVDSS 256
Cdd:PRK08195  142 PPEKLAEQAKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGS 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2502273086 257 VAGLGGcpyakGAsGNLATEDLVYMLNGLGIHTGVNLQKLLEAGD 301
Cdd:PRK08195  222 LAGLGA-----GA-GNTPLEVLVAVLDRMGWETGVDLYKLMDAAE 260
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
 183-302 7.29e-15

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: 73.23  E-value: 7.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 183 AEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGG 262
Cdd:cd07937   152 VKLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVGL-PIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSG 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2502273086 263 cpyakGASGNlATEDLVYMLNGLGIHTGVNLQKLLEAGDF 302
Cdd:cd07937   231 -----GTSQP-STESMVAALRGTGRDTGLDLEKLEEISEY 264
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
 193-299 2.49e-13

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: 68.63  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 193 GCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTA--LAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgcpyakGAS 270
Cdd:cd07940   156 GATTINIPDTVGYLTPEEFGELIKKLKENVPNIKvpISVHCHNDLGLAVANSLAAVEAGARQVECTINGIG------ERA 229

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2502273086 271 GNLATEDLV----YMLNGLGIHTGVNLQKLLEA 299
Cdd:cd07940   230 GNAALEEVVmalkTRYDYYGVETGIDTEELYET 262
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
 33-261 4.70e-13

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: 68.13  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  33 VKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATS-FVSPKWMADhsdvLKGIQKFpGINYPVLTP---NMK 108
Cdd:cd07948     1 FKIIDSTLREGEQFANAFFDTEDKIEIAKALDAFGVDYIELTSpAASPQSRAD----CEAIAKL-GLKAKILTHircHMD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 109 GFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyVSC--ALGCPYegkvspAKVAEVA 186
Cdd:cd07948    76 DARIAVETGVDGVDLVFGTSPFLREASHGKSITEIIESAVEVIEFVKSKGIEVR--FSSedSFRSDL------VDLLRVY 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502273086 187 KKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPvTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLG 261
Cdd:cd07948   148 RAVDKLGVNRVGIADTVGIATPRQVYELVRTLRGVVS-CDIEFHGHNDTGCAIANAYAALEAGATHIDTTVLGIG 221
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
 176-299 5.12e-13

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: 67.97  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 176 KVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEV-PVTALAVHCHDTYGQALANTLVALQMGVSVVD 254
Cdd:cd07944   134 GYSDEELLELLELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLdKDIKLGFHAHNNLQLALANTLEAIELGVEIID 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2502273086 255 SSVAGLGgcpyaKGAsGNLATEDLVYMLNGLGIHTgVNLQKLLEA 299
Cdd:cd07944   214 ATVYGMG-----RGA-GNLPTELLLDYLNNKFGKK-YNLEPVLEL 251
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
184-302 1.63e-12

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 67.80  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 184 EVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMGVSVVDSSVAglggc 263
Cdd:PRK12331  158 KLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTV-PLEVHTHATSGIAEMTYLKAIEAGADIIDTAIS----- 231

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2502273086 264 PYAKGASgNLATEDLVYMLNGLGIHTGVNLQKLLEAGDF 302
Cdd:PRK12331  232 PFAGGTS-QPATESMVAALQDLGYDTGLDLEELSEIAEY 269
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
 177-301 3.23e-12

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 67.17  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 177 VSP----AKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMGVSV 252
Cdd:PRK09282  147 TSPvhtiEKYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEVDL-PVQLHSHCTSGLAPMTYLKAVEAGVDI 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2502273086 253 VDSSVAglggcPYAKGASgNLATEDLVYMLNGLGIHTGVNLQKLLEAGD 301
Cdd:PRK09282  226 IDTAIS-----PLAFGTS-QPPTESMVAALKGTPYDTGLDLELLFEIAE 268
PRK00915 PRK00915
2-isopropylmalate synthase; Validated
 183-319 3.09e-10

2-isopropylmalate synthase; Validated


Pssm-ID: 234864 [Multi-domain]  Cd Length: 513  Bit Score: 60.90  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 183 AEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVP---VTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAG 259
Cdd:PRK00915  152 CRVVEAAIDAGATTINIPDTVGYTTPEEFGELIKTLRERVPnidKAIISVHCHNDLGLAVANSLAAVEAGARQVECTING 231

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2502273086 260 LGgcpyaKGAsGNLATEDLVYMLN----GLGIHTGVNLQKLLEagdficqalnrkTSSKVAQAT 319
Cdd:PRK00915  232 IG-----ERA-GNAALEEVVMALKtrkdIYGVETGINTEEIYR------------TSRLVSQLT 277
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
 56-318 4.56e-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: 59.06  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  56 KIRLIDMLSEAGLPVIEATSfvsPKWMADHSDVLKGIQkfpGINYPV-LTP----NMKGFEEAVAAGAKEVSVFGAVSEL 130
Cdd:cd07939    22 KLAIARALDEAGVDEIEVGI---PAMGEEEREAIRAIV---ALGLPArLIVwcraVKEDIEAALRCGVTAVHISIPVSDI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 131 FTRKNANCSIEESFQRFAGVMQAAQAASIsvrgYVScaLGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGL 210
Cdd:cd07939    96 HLAHKLGKDRAWVLDQLRRLVGRAKDRGL----FVS--VGAEDASRADPDFLIEFAEVAQEAGADRLRFADTVGILDPFT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 211 MKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgcpyakGASGNLATEDLVYMLNGL-GIHT 289
Cdd:cd07939   170 TYELIRRLRAATDL-PLEFHAHNDLGLATANTLAAVRAGATHVSVTVNGLG------ERAGNAALEEVVMALKHLyGRDT 242

                         250       260
                  ....*....|....*....|....*....
gi 2502273086 290 GVNLQKLLEagdfICQalnrktssKVAQA 318
Cdd:cd07939   243 GIDTTRLPE----LSQ--------LVARA 259
PRK12330 PRK12330
methylmalonyl-CoA carboxytransferase subunit 5S;
178-301 7.36e-10

methylmalonyl-CoA carboxytransferase subunit 5S;


Pssm-ID: 183445 [Multi-domain]  Cd Length: 499  Bit Score: 59.77  E-value: 7.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 178 SPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEV-PVTALAVHCHDTYGQALANTLVALQMGVSVVDSS 256
Cdd:PRK12330  153 TVEGFVEQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTA 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2502273086 257 VAGLGGCPyakgasGNLATEDLVYMLNGLGIHTGVNLQKLLEAGD 301
Cdd:PRK12330  233 ISSMSLGP------GHNPTESLVEMLEGTGYTTKLDMDRLLKIRD 271
DRE_TIM_Re_CS cd07947
Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain; ...
 41-303 9.88e-10

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: 58.49  E-value: 9.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  41 RDGlQNEKSIVPTPVKIRLIDMLSEAGLP--VIEATSFV--SPKwmadHSDVLKGIQKFpGINYPVLT----PNMKGFEE 112
Cdd:cd07947     9 RDG-QQARPPYTVEQIVKIYDYLHELGGGsgVIRQTEFFlyTEK----DREAVEACLDR-GYKFPEVTgwirANKEDLKL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 113 AVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRgyvsCALG----CPYEGKVSP--AKVAEVA 186
Cdd:cd07947    83 VKEMGLKETGILMSVSDYHIFKKLKMTREEAMEKYLEIVEEALDHGIKPR----CHLEditrADIYGFVLPfvNKLMKLS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 187 KKlYSMGCYeISLGDTIGVGTP---------------GLMKDMltavmhEVPVTALAVHCHDTYGQALANTLVALQMGVS 251
Cdd:cd07947   159 KE-SGIPVK-IRLCDTLGYGVPypgaslprsvpkiiyGLRKDC------GVPSENLEWHGHNDFYKAVANAVAAWLYGAS 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2502273086 252 VVDSSVAGLGgcpyakGASGNLATEDLVYMLNGL-GIHTGVNLQKLLEAGDFI 303
Cdd:cd07947   231 WVNCTLLGIG------ERTGNCPLEAMVIEYAQLkGNFDGMNLEVITEIAEYF 277
PRK09389 PRK09389
(R)-citramalate synthase; Provisional
 187-311 1.26e-09

(R)-citramalate synthase; Provisional


Pssm-ID: 236493 [Multi-domain]  Cd Length: 488  Bit Score: 58.80  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 187 KKLYSMGcyeISLG-------DTIGVGTPGLMKDmLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAG 259
Cdd:PRK09389  146 KELYKAG---IEAGadricfcDTVGILTPEKTYE-LFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTING 221

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2502273086 260 LGgcpyakGASGNLATEDLVYMLNGL-GIHTGVNLQKLLEagdfICQALNRKT 311
Cdd:PRK09389  222 IG------ERAGNASLEEVVMALKHLyDVETGIKLEELYE----LSRLVSRLT 264
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
184-298 1.66e-09

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 58.79  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 184 EVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTaLAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLgGC 263
Cdd:PRK14040  159 DLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRVDVP-LHLHCHATTGLSTATLLKAIEAGIDGVDTAISSM-SM 236

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2502273086 264 PYakgasGNLATEDLVYMLNGLGIHTGVNLQKLLE 298
Cdd:PRK14040  237 TY-----GHSATETLVATLEGTERDTGLDILKLEE 266
PLN03228 PLN03228
methylthioalkylmalate synthase; Provisional
 121-297 1.08e-07

methylthioalkylmalate synthase; Provisional


Pssm-ID: 178767 [Multi-domain]  Cd Length: 503  Bit Score: 53.00  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 121 VSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAAsisvrGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLG 200
Cdd:PLN03228  185 ILAFTSTSDIHMKYKLKKTKEEVIEMAVSSIRYAKSL-----GFHDIQFGCEDGGRSDKEFLCKILGEAIKAGATSVGIA 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 201 DTIGVGTPGLMKDMLTAVMHEVPV---TALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgcpyakGASGNLATED 277
Cdd:PLN03228  260 DTVGINMPHEFGELVTYVKANTPGiddIVFSVHCHNDLGLATANTIAGICAGARQVEVTINGIG------ERSGNASLEE 333

                         170       180
                  ....*....|....*....|....*...
gi 2502273086 278 LV--------YMLNGLgiHTGVNLQKLL 297
Cdd:PLN03228  334 VVmalkcrgaYLMNGV--YTGIDTRQIM 359
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
 113-299 6.76e-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: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 113 AVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYV---SCALgcpyegKVSPAKVAEVAKKL 189
Cdd:cd07945    83 IKSAGAKVLNLLTKGSLKHCTEQLRKTPEEHFADIREVIEYAIKNGIEVNIYLedwSNGM------RDSPDYVFQLVDFL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 190 YSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGgcpyakGA 269
Cdd:cd07945   157 SDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHTTVNGLG------ER 230

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2502273086 270 SGNLATEDLVYMLNG-LGIHTGVNLQKLLEA 299
Cdd:cd07945   231 AGNAPLASVIAVLKDkLKVKTNIDEKRLNRA 261
DRE_TIM_LeuA3 cd07941
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ...
 197-261 5.19e-06

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: 47.06  E-value: 5.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2502273086 197 ISLGDTIGvGT-PGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLG 261
Cdd:cd07941   168 LVLCDTNG-GTlPHEIAEIVKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQVQGTINGYG 232
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
 184-318 9.69e-06

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 47.02  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 184 EVAKKLYSMGCYEISLGDTIGVGTPGLMKDmLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGc 263
Cdd:PRK14042  158 ELGKKLAEMGCDSIAIKDMAGLLTPTVTVE-LYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAISSFSG- 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2502273086 264 pyakGASgNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFIcQALNRKTSSKVAQA 318
Cdd:PRK14042  236 ----GAS-HPPTEALVAALTDTPYDTELDLNILLEIDDYF-KAVRKKYSQFESEA 284
PRK12581 PRK12581
oxaloacetate decarboxylase; Provisional
 185-306 3.72e-05

oxaloacetate decarboxylase; Provisional


Pssm-ID: 79056 [Multi-domain]  Cd Length: 468  Bit Score: 45.11  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086 185 VAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAV--MHEVPvtaLAVHCHDTYGQALANTLVALQMGVSVVDSSVAglgg 262
Cdd:PRK12581  168 LVKELVEMGADSICIKDMAGILTPKAAKELVSGIkaMTNLP---LIVHTHATSGISQMTYLAAVEAGADRIDTALS---- 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2502273086 263 cPYAKGASgNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQA 306
Cdd:PRK12581  241 -PFSEGTS-QPATESMYLALKEAGYDITLDETLLEQAANHLRQA 282
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 185-302 6.95e-05

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 44.74  E-value: 6.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502273086  185 VAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEV--PVtalAVHCHDTYGQALANTLVALQMGVSVVD---SSVAG 259
Cdd:PRK12999   696 LAKELEKAGAHILAIKDMAGLLKPAAAYELVSALKEEVdlPI---HLHTHDTSGNGLATYLAAAEAGVDIVDvavASMSG 772

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2502273086  260 LGGCPyakgasgNLATedLVYMLNGLGIHTGVNLQKLLEAGDF 302
Cdd:PRK12999   773 LTSQP-------SLNS--IVAALEGTERDTGLDLDAIRKLSPY 806
PRK12344 PRK12344
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
 199-261 2.90e-03

putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional


Pssm-ID: 237068 [Multi-domain]  Cd Length: 524  Bit Score: 39.30  E-value: 2.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2502273086 199 LGDTIGvGT-PGLMKDMLTAVMHEVPVtALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLG 261
Cdd:PRK12344  177 LCDTNG-GTlPHEVAEIVAEVRAAPGV-PLGIHAHNDSGCAVANSLAAVEAGARQVQGTINGYG 238
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 229-298 6.46e-03

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: 38.14  E-value: 6.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502273086  229 VHCHDTYGQALANTLVALQMGVSVVD---SSVAGLGGCPyakgasgNLATedLVYMLNGLGIHTGVNLQKLLE 298
Cdd:COG1038    739 LHTHDTSGNQLATYLAAIEAGVDIVDvalASMSGLTSQP-------SLNS--LVAALEGTERDTGLDLDALQE 802
 
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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