NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|575523326|gb|AHG98018|]
View 

NifV [Cloning vector pCV_cistron14]

Protein Classification

homocitrate synthase( domain architecture ID 11494668)

homocitrate synthase (NifV) is a Fe-Mo-cofactor biosynthetic component

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
nifV_homocitr TIGR02660
homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, ...
3-367 0e+00

homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, most of which are found in operons for nitrogen fixation. Members are closely homologous to enzymes that include 2-isopropylmalate synthase, (R)-citramalate synthase, and homocitrate synthases associated with other processes. The homocitrate made by this enzyme becomes a part of the iron-molybdenum cofactor of nitrogenase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


:

Pssm-ID: 274248 [Multi-domain]  Cd Length: 365  Bit Score: 571.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQ 82
Cdd:TIGR02660   1 PVIINDTTLRDGEQAPGVAFTAAEKLAIARALDEAGVDELEVGIPAMGEEERAVIRAIVALGLPARLMAWCRARDADIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   83 SADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLR 162
Cdd:TIGR02660  81 AARCGVDAVHISIPVSDLQIEAKLRKDRAWVLERLARLVSFARDRGLFVSVGGEDASRADPDFLVELAEVAAEAGADRFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  163 YADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERC 242
Cdd:TIGR02660 161 FADTVGILDPFSTYELVRALRQAVDLPLEMHAHNDLGMATANTLAAVRAGATHVNTTVNGLGERAGNAALEEVAMALKRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  243 LGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSGRQ 322
Cdd:TIGR02660 241 LGRDTGIDTSRLPALSQLVARASGRPIPPQKPVVGESVFTHESGIHVDGLLKDPRTYEPFDPELVGRSRRIVIGKHSGRA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 575523326  323 AVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIY 367
Cdd:TIGR02660 321 ALINALAQLGIPLSEEEAAALLPAVRAFATRLKRPLSDAELIALY 365
 
Name Accession Description Interval E-value
nifV_homocitr TIGR02660
homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, ...
3-367 0e+00

homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, most of which are found in operons for nitrogen fixation. Members are closely homologous to enzymes that include 2-isopropylmalate synthase, (R)-citramalate synthase, and homocitrate synthases associated with other processes. The homocitrate made by this enzyme becomes a part of the iron-molybdenum cofactor of nitrogenase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 274248 [Multi-domain]  Cd Length: 365  Bit Score: 571.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQ 82
Cdd:TIGR02660   1 PVIINDTTLRDGEQAPGVAFTAAEKLAIARALDEAGVDELEVGIPAMGEEERAVIRAIVALGLPARLMAWCRARDADIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   83 SADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLR 162
Cdd:TIGR02660  81 AARCGVDAVHISIPVSDLQIEAKLRKDRAWVLERLARLVSFARDRGLFVSVGGEDASRADPDFLVELAEVAAEAGADRFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  163 YADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERC 242
Cdd:TIGR02660 161 FADTVGILDPFSTYELVRALRQAVDLPLEMHAHNDLGMATANTLAAVRAGATHVNTTVNGLGERAGNAALEEVAMALKRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  243 LGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSGRQ 322
Cdd:TIGR02660 241 LGRDTGIDTSRLPALSQLVARASGRPIPPQKPVVGESVFTHESGIHVDGLLKDPRTYEPFDPELVGRSRRIVIGKHSGRA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 575523326  323 AVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIY 367
Cdd:TIGR02660 321 ALINALAQLGIPLSEEEAAALLPAVRAFATRLKRPLSDAELIALY 365
aksA PRK11858
trans-homoaconitate synthase; Reviewed
1-377 5.39e-138

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 398.01  E-value: 5.39e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEI 80
Cdd:PRK11858   2 PKDIEIVDTTLRDGEQTPGVVFTNEEKLAIARMLDEIGVDQIEAGFPAVSEDEKEAIKAIAKLGLNASILALNRAVKSDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  81 RQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAAR 160
Cdd:PRK11858  82 DASIDCGVDAVHIFIATSDIHIKHKLKKTREEVLERMVEAVEYAKDHGLYVSFSAEDASRTDLDFLIEFAKAAEEAGADR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 161 LRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLE 240
Cdd:PRK11858 162 VRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTVNGLGERAGNAALEEVVMALK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 241 RCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSG 320
Cdd:PRK11858 242 YLYGIDLGIDTERLYELSRLVSKASGIPVPPNKAIVGENAFAHESGIHVDGVLKNPLTYEPFLPEEVGLERRIVLGKHSG 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 575523326 321 RQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDELCGESALR 377
Cdd:PRK11858 322 RHALKNKLKEYGIELSREELCELLEKVKELSERKKRSLTDEELKELVEDVRRSRKAA 378
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
1-374 5.84e-135

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: 392.99  E-value: 5.84e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEI 80
Cdd:COG0119    1 PDRIIIFDTTLRDGEQAPGVSFSVEEKLRIARLLDELGVDEIEAGFPAASPGDFEAVRRIAELGLDATICALARARRKDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  81 RQSADL----GIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQC 156
Cdd:COG0119   81 DAALEAlkgaGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVEFSAEDATRTDPDFLLEVLEAAIEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 157 AAARLRYADTVGLLDPFTTAAQISALRD-VWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETV 235
Cdd:COG0119  161 GADRINLPDTVGGATPNEVADLIEELRErVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIGERAGNAALEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 236 ALGLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVL 315
Cdd:COG0119  241 VMNLKLKYGVDTGIDLSKLTELSRLVSEITGLPVPPNKPIVGENAFAHESGIHQDGILKNPETYEPIDPEDVGRERRIVL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 575523326 316 GKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDELCGES 374
Cdd:COG0119  321 GKHSGRAAIAYKLEELGIELDDEELQEILERVKELADKGKREVTDADLEALVRDVLGEK 379
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
6-264 1.10e-119

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: 347.19  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQSAD 85
Cdd:cd07939    1 INDTTLRDGEQAPGVAFSREEKLAIARALDEAGVDEIEVGIPAMGEEEREAIRAIVALGLPARLIVWCRAVKEDIEAALR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  86 LGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLRYAD 165
Cdd:cd07939   81 CGVTAVHISIPVSDIHLAHKLGKDRAWVLDQLRRLVGRAKDRGLFVSVGAEDASRADPDFLIEFAEVAQEAGADRLRFAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 166 TVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERCLGV 245
Cdd:cd07939  161 TVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVNGLGERAGNAALEEVVMALKHLYGR 240
                        250
                 ....*....|....*....
gi 575523326 246 ETGVHFSALPALCQRVAEA 264
Cdd:cd07939  241 DTGIDTTRLPELSQLVARA 259
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
3-261 1.82e-71

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: 224.14  E-value: 1.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQ 82
Cdd:pfam00682   1 AVAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCRAREHDIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   83 SADL----GIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAA 158
Cdd:pfam00682  81 AVEAlkgaGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVEFSPEDASRTDPEFLAEVVEAAIEAGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  159 ARLRYADTVGLLDPFTTAAQISALRDVWSGE--IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVA 236
Cdd:pfam00682 161 TRINIPDTVGVLTPNEAAELISALKARVPNKaiISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIGERAGNAALEEVA 240
                         250       260
                  ....*....|....*....|....*
gi 575523326  237 LGLERcLGVETGVHFSALPALCQRV 261
Cdd:pfam00682 241 AALEG-LGVDTGLDLQRLRSIANLV 264
 
Name Accession Description Interval E-value
nifV_homocitr TIGR02660
homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, ...
3-367 0e+00

homocitrate synthase NifV; This family consists of the NifV clade of homocitrate synthases, most of which are found in operons for nitrogen fixation. Members are closely homologous to enzymes that include 2-isopropylmalate synthase, (R)-citramalate synthase, and homocitrate synthases associated with other processes. The homocitrate made by this enzyme becomes a part of the iron-molybdenum cofactor of nitrogenase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 274248 [Multi-domain]  Cd Length: 365  Bit Score: 571.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQ 82
Cdd:TIGR02660   1 PVIINDTTLRDGEQAPGVAFTAAEKLAIARALDEAGVDELEVGIPAMGEEERAVIRAIVALGLPARLMAWCRARDADIEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   83 SADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLR 162
Cdd:TIGR02660  81 AARCGVDAVHISIPVSDLQIEAKLRKDRAWVLERLARLVSFARDRGLFVSVGGEDASRADPDFLVELAEVAAEAGADRFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  163 YADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERC 242
Cdd:TIGR02660 161 FADTVGILDPFSTYELVRALRQAVDLPLEMHAHNDLGMATANTLAAVRAGATHVNTTVNGLGERAGNAALEEVAMALKRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  243 LGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSGRQ 322
Cdd:TIGR02660 241 LGRDTGIDTSRLPALSQLVARASGRPIPPQKPVVGESVFTHESGIHVDGLLKDPRTYEPFDPELVGRSRRIVIGKHSGRA 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 575523326  323 AVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIY 367
Cdd:TIGR02660 321 ALINALAQLGIPLSEEEAAALLPAVRAFATRLKRPLSDAELIALY 365
aksA PRK11858
trans-homoaconitate synthase; Reviewed
1-377 5.39e-138

trans-homoaconitate synthase; Reviewed


Pssm-ID: 183341 [Multi-domain]  Cd Length: 378  Bit Score: 398.01  E-value: 5.39e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEI 80
Cdd:PRK11858   2 PKDIEIVDTTLRDGEQTPGVVFTNEEKLAIARMLDEIGVDQIEAGFPAVSEDEKEAIKAIAKLGLNASILALNRAVKSDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  81 RQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAAR 160
Cdd:PRK11858  82 DASIDCGVDAVHIFIATSDIHIKHKLKKTREEVLERMVEAVEYAKDHGLYVSFSAEDASRTDLDFLIEFAKAAEEAGADR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 161 LRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLE 240
Cdd:PRK11858 162 VRFCDTVGILDPFTMYELVKELVEAVDIPIEVHCHNDFGMATANALAGIEAGAKQVHTTVNGLGERAGNAALEEVVMALK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 241 RCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSG 320
Cdd:PRK11858 242 YLYGIDLGIDTERLYELSRLVSKASGIPVPPNKAIVGENAFAHESGIHVDGVLKNPLTYEPFLPEEVGLERRIVLGKHSG 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 575523326 321 RQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDELCGESALR 377
Cdd:PRK11858 322 RHALKNKLKEYGIELSREELCELLEKVKELSERKKRSLTDEELKELVEDVRRSRKAA 378
LeuA COG0119
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ...
1-374 5.84e-135

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: 392.99  E-value: 5.84e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEI 80
Cdd:COG0119    1 PDRIIIFDTTLRDGEQAPGVSFSVEEKLRIARLLDELGVDEIEAGFPAASPGDFEAVRRIAELGLDATICALARARRKDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  81 RQSADL----GIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQC 156
Cdd:COG0119   81 DAALEAlkgaGVDRVHLFIKTSDLHVEYKLRKTREEVLEMAVEAVKYAKEHGLEVEFSAEDATRTDPDFLLEVLEAAIEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 157 AAARLRYADTVGLLDPFTTAAQISALRD-VWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETV 235
Cdd:COG0119  161 GADRINLPDTVGGATPNEVADLIEELRErVPDVILSVHCHNDLGLAVANSLAAVEAGADQVEGTINGIGERAGNAALEEV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 236 ALGLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVL 315
Cdd:COG0119  241 VMNLKLKYGVDTGIDLSKLTELSRLVSEITGLPVPPNKPIVGENAFAHESGIHQDGILKNPETYEPIDPEDVGRERRIVL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 575523326 316 GKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDELCGES 374
Cdd:COG0119  321 GKHSGRAAIAYKLEELGIELDDEELQEILERVKELADKGKREVTDADLEALVRDVLGEK 379
DRE_TIM_NifV cd07939
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ...
6-264 1.10e-119

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: 347.19  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQSAD 85
Cdd:cd07939    1 INDTTLRDGEQAPGVAFSREEKLAIARALDEAGVDEIEVGIPAMGEEEREAIRAIVALGLPARLIVWCRAVKEDIEAALR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  86 LGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLRYAD 165
Cdd:cd07939   81 CGVTAVHISIPVSDIHLAHKLGKDRAWVLDQLRRLVGRAKDRGLFVSVGAEDASRADPDFLIEFAEVAQEAGADRLRFAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 166 TVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERCLGV 245
Cdd:cd07939  161 TVGILDPFTTYELIRRLRAATDLPLEFHAHNDLGLATANTLAAVRAGATHVSVTVNGLGERAGNAALEEVVMALKHLYGR 240
                        250
                 ....*....|....*....
gi 575523326 246 ETGVHFSALPALCQRVAEA 264
Cdd:cd07939  241 DTGIDTTRLPELSQLVARA 259
PRK09389 PRK09389
(R)-citramalate synthase; Provisional
2-372 1.22e-90

(R)-citramalate synthase; Provisional


Pssm-ID: 236493 [Multi-domain]  Cd Length: 488  Bit Score: 281.06  E-value: 1.22e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   2 ERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIR 81
Cdd:PRK09389   1 MMVRILDTTLRDGEQTPGVSLTPEEKLEIARKLDELGVDVIEAGSAITSEGEREAIKAVTDEGLNAEICSFARAVKVDID 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  82 QSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARL 161
Cdd:PRK09389  81 AALECDVDSVHLVVPTSDLHIEYKLKKTREEVLETAVEAVEYAKDHGLIVELSGEDASRADLDFLKELYKAGIEAGADRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 162 RYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLER 241
Cdd:PRK09389 161 CFCDTVGILTPEKTYELFKRLSELVKGPVSIHCHNDFGLAVANTLAALAAGADQVHVTINGIGERAGNASLEEVVMALKH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 242 CLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHSGR 321
Cdd:PRK09389 241 LYDVETGIKLEELYELSRLVSRLTGIPVPPNKAIVGENAFAHESGIHVDGLLKDTETYEPITPETVGRERRIVLGKHAGR 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 575523326 322 QAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSpKDYELVAIYDELCG 372
Cdd:PRK09389 321 AALKAALKEMGIEVSDDQLNEIVSRVKELGDRGKRV-TDADLLAIAEDVLG 370
PRK00915 PRK00915
2-isopropylmalate synthase; Validated
1-366 1.54e-78

2-isopropylmalate synthase; Validated


Pssm-ID: 234864 [Multi-domain]  Cd Length: 513  Bit Score: 250.41  E-value: 1.54e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAM--GD-EEIARI-QLVRrqlpDATLMTWCRMN 76
Cdd:PRK00915   2 MDRVIIFDTTLRDGEQSPGASLTVEEKLQIAKQLERLGVDVIEAGFPASspGDfEAVKRIaRTVK----NSTVCGLARAV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  77 ALEIRQSA----DLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEV 152
Cdd:PRK00915  78 KKDIDAAAealkPAEAPRIHTFIATSPIHMEYKLKMSREEVLEMAVEAVKYARSYTDDVEFSAEDATRTDLDFLCRVVEA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 153 AQQCAAARLRYADTVGLLDPFTTAAQISALRD--------VWSgeieMHAHNDLGMATANTLAAVSAGATSVNTTVLGLG 224
Cdd:PRK00915 158 AIDAGATTINIPDTVGYTTPEEFGELIKTLRErvpnidkaIIS----VHCHNDLGLAVANSLAAVEAGARQVECTINGIG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 225 ERAGNAALETVALGL---ERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQS 301
Cdd:PRK00915 234 ERAGNAALEEVVMALktrKDIYGVETGINTEEIYRTSRLVSQLTGMPVQPNKAIVGANAFAHESGIHQDGVLKNRETYEI 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523326 302 IAPSLMGRSYR-LVLGKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENwKRSPKDYELVAI 366
Cdd:PRK00915 314 MTPESVGLKANrLVLGKHSGRHAFKHRLEELGYKLSDEELDKAFERFKELADK-KKEVFDEDLEAL 378
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
8-263 2.11e-75

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: 234.27  E-value: 2.11e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   8 DTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDE------EIARIQLVRRQLPDATLMTWCRMNALEIR 81
Cdd:cd03174    2 DTTLRDGLQSEGATFSTEDKLEIAEALDEAGVDSIEVGSGASPKAvpqmedDWEVLRAIRKLVPNVKLQALVRNREKGIE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  82 QSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASR--ASGQTLRAIAEVAQQCAAA 159
Cdd:cd03174   82 RALEAGVDEVRIFDSASETHSRKNLNKSREEDLENAEEAIEAAKEAGLEVEGSLEDAFGckTDPEYVLEVAKALEEAGAD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 160 RLRYADTVGLLDPFTTAAQISALRDVWSG-EIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALG 238
Cdd:cd03174  162 EISLKDTVGLATPEEVAELVKALREALPDvPLGLHTHNTLGLAVANSLAALEAGADRVDGSVNGLGERAGNAATEDLVAA 241
                        250       260
                 ....*....|....*....|....*
gi 575523326 239 LERcLGVETGVHFSALPALCQRVAE 263
Cdd:cd03174  242 LEG-LGIDTGIDLEKLLEISRYVEE 265
HMGL-like pfam00682
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ...
3-261 1.82e-71

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: 224.14  E-value: 1.82e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQ 82
Cdd:pfam00682   1 AVAICDTTLRDGEQALGVAFSIDEKLAIARALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCRAREHDIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   83 SADL----GIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAA 158
Cdd:pfam00682  81 AVEAlkgaGAVRVHVFIATSDLHRKYKLGKDREEVAKRAVAAVKAARSRGIDVEFSPEDASRTDPEFLAEVVEAAIEAGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  159 ARLRYADTVGLLDPFTTAAQISALRDVWSGE--IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVA 236
Cdd:pfam00682 161 TRINIPDTVGVLTPNEAAELISALKARVPNKaiISVHCHNDLGMAVANSLAAVEAGADRVDGTVNGIGERAGNAALEEVA 240
                         250       260
                  ....*....|....*....|....*
gi 575523326  237 LGLERcLGVETGVHFSALPALCQRV 261
Cdd:pfam00682 241 AALEG-LGVDTGLDLQRLRSIANLV 264
DRE_TIM_IPMS cd07940
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ...
6-263 1.19e-66

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: 211.92  E-value: 1.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTWCRMNALEIRQSAD 85
Cdd:cd07940    1 IFDTTLRDGEQTPGVSLTPEEKLEIARQLDELGVDVIEAGFPAASPGDFEAVKRIAREVLNAEICGLARAVKKDIDAAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  86 LG----IDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARL 161
Cdd:cd07940   81 ALkpakVDRIHTFIATSDIHLKYKLKKTREEVLERAVEAVEYAKSHGLDVEFSAEDATRTDLDFLIEVVEAAIEAGATTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 162 RYADTVGLLDPFTTAAQISALRDVWSG---EIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALG 238
Cdd:cd07940  161 NIPDTVGYLTPEEFGELIKKLKENVPNikvPISVHCHNDLGLAVANSLAAVEAGARQVECTINGIGERAGNAALEEVVMA 240
                        250       260
                 ....*....|....*....|....*...
gi 575523326 239 LE---RCLGVETGVHFSALPALCQRVAE 263
Cdd:cd07940  241 LKtryDYYGVETGIDTEELYETSRLVSR 268
PLN03228 PLN03228
methylthioalkylmalate synthase; Provisional
4-356 4.70e-58

methylthioalkylmalate synthase; Provisional


Pssm-ID: 178767 [Multi-domain]  Cd Length: 503  Bit Score: 196.68  E-value: 4.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   4 VLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQL-----------PDATLMTW 72
Cdd:PLN03228  85 VRVLDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEEFEAVKTIAKTVgnevdeetgyvPVICGIAR 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  73 CRMNALEIRQSAdlgIDW-----VDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLK-VCIGCEDASRASGQTL 146
Cdd:PLN03228 165 CKKRDIEAAWEA---LKYakrprILAFTSTSDIHMKYKLKKTKEEVIEMAVSSIRYAKSLGFHdIQFGCEDGGRSDKEFL 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 147 RAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSG----EIEMHAHNDLGMATANTLAAVSAGATSVNTTVLG 222
Cdd:PLN03228 242 CKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPGiddiVFSVHCHNDLGLATANTIAGICAGARQVEVTING 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 223 LGERAGNAALETVALGLeRCL------GVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDS 296
Cdd:PLN03228 322 IGERSGNASLEEVVMAL-KCRgaylmnGVYTGIDTRQIMATSKMVQEYTGMYVQPHKPIVGANCFVHESGIHQDGILKNR 400
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523326 297 ESYQSIAPSLMG----RSYRLVLGKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKR 356
Cdd:PLN03228 401 STYEILSPEDIGivksQNSGIVLGKLSGRHAVKDRLKELGYELDDEKLNEVFSRFRDLTKEKKR 464
LysS_fung_arch TIGR02146
homocitrate synthase; This model includes the yeast LYS21 gene which carries out the first ...
6-348 4.75e-56

homocitrate synthase; This model includes the yeast LYS21 gene which carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. A related pathway is found in Thermus thermophilus. This enzyme is closely related to 2-isopropylmalate synthase (LeuA) and citramalate synthase (CimA), both of which are present in the euryarchaeota. Some archaea have a separate homocitrate synthase (AksA) which also synthesizes longer homocitrate analogs.


Pssm-ID: 162728 [Multi-domain]  Cd Length: 344  Bit Score: 186.92  E-value: 4.75e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQLPDATLMTW--CRMNALEIrqS 83
Cdd:TIGR02146   1 IIDSTLREGEQFPGANFSTEQKIEIAKALDEFGIDYIEVTHPAASKQSRIDIEIIASLGLKANIVTHirCRLDDAKV--A 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   84 ADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLRY 163
Cdd:TIGR02146  79 VELGVDGIDIFFGTSKLLRIAEHRSDAKSILESARETIEYAKSAGLEVRFSAEDTFRSELADLLSIYETVGVFGVDRVGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  164 ADTVGLLDPFTTAAQISALRDVWSG-EIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGnaalETVALGLERC 242
Cdd:TIGR02146 159 ADTVGKAAPRQVYELIRTVVRVVPGvDIELHAHNDTGCAVANAYNAIEGGATIVDTTVLGIGERNG----ITPLGGILAR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  243 LGVETGVHFSAL---PALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRDSESYQSIAPSLMGRSYRLVLGKHS 319
Cdd:TIGR02146 235 LYYHTPMYVYKLgklIELTRMVAGEVGVTIPFNNPITGELAFTHKAGIHVKAILGNPRTYEFLPPEVFGRKRHILIARLT 314
                         330       340
                  ....*....|....*....|....*....
gi 575523326  320 GRQAVNGVFDQMGYHLNAAQINQLLPAIR 348
Cdd:TIGR02146 315 GKHAIKARKEKLGVKLIEEELKRVTAKIK 343
PLN02321 PLN02321
2-isopropylmalate synthase
4-370 2.42e-47

2-isopropylmalate synthase


Pssm-ID: 215182 [Multi-domain]  Cd Length: 632  Bit Score: 170.15  E-value: 2.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   4 VLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARIQLVRRQL-----PDATLMTWC---RM 75
Cdd:PLN02321  87 VRIFDTTLRDGEQSPGATLTSKEKLDIARQLAKLGVDIIEAGFPIASPDDLEAVKTIAKEVgnevdEDGYVPVICglsRC 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  76 NALEIRQSadlgidW----------VDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLK-VCIGCEDASRASGQ 144
Cdd:PLN02321 167 NKKDIDAA------WeavkhakrprIHTFIATSEIHMEHKLRKTPDEVVEIARDMVKYARSLGCEdVEFSPEDAGRSDPE 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 145 TLRAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGE----IEMHAHNDLGMATANTLAAVSAGATSVNTTV 220
Cdd:PLN02321 241 FLYRILGEVIKAGATTLNIPDTVGYTLPSEFGQLIADIKANTPGIenviISTHCQNDLGLSTANTLAGAHAGARQVEVTI 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 221 LGLGERAGNAALETVAL-----GLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVHVAALLRD 295
Cdd:PLN02321 321 NGIGERAGNASLEEVVMaikcrGDEQLGGLYTGINPVHITPTSKMVSEYTGMQVQPHKAIVGANAFAHESGIHQDGMLKH 400
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575523326 296 SESYQSIAPSLMG----RSYRLVLGKHSGRQAVNGVFDQMGYHLNAAQINQLLPAIRRFAENWKRSPKDYELVAIYDEL 370
Cdd:PLN02321 401 KGTYEIISPEDIGlfrgNDAGIVLGKLSGRHALKSRLKELGYELDDDELDDVFKRFKAVAEKKKGVTDEDLIALVSDEV 479
DRE_TIM_HCS cd07948
Saccharomyces cerevisiae homocitrate synthase and related proteins, catalytic TIM barrel ...
6-263 5.94e-47

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: 160.96  E-value: 5.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEIARI-QLVRRQLPdATLMTWCRMNALEIRQSA 84
Cdd:cd07948    3 IIDSTLREGEQFANAFFDTEDKIEIAKALDAFGVDYIELTSPAASPQSRADCeAIAKLGLK-AKILTHIRCHMDDARIAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  85 DLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQTLRAIAEVAQQCAAARLRYA 164
Cdd:cd07948   82 ETGVDGVDLVFGTSPFLREASHGKSITEIIESAVEVIEFVKSKGIEVRFSSEDSFRSDLVDLLRVYRAVDKLGVNRVGIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 165 DTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALE---TVALGLER 241
Cdd:cd07948  162 DTVGIATPRQVYELVRTLRGVVSCDIEFHGHNDTGCAIANAYAALEAGATHIDTTVLGIGERNGITPLGgliARMYTADP 241
                        250       260
                 ....*....|....*....|..
gi 575523326 242 cLGVETGVHFSALPALCQRVAE 263
Cdd:cd07948  242 -EYVVSKYKLELLPELERLVAD 262
PRK12344 PRK12344
putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional
1-321 1.06e-40

putative alpha-isopropylmalate/homocitrate synthase family transferase; Provisional


Pssm-ID: 237068 [Multi-domain]  Cd Length: 524  Bit Score: 150.24  E-value: 1.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPamG----DEEI-ARIQlvRRQLPDATL----MT 71
Cdd:PRK12344   3 MERIELYDTTLRDGAQGEGISFSVEDKLRIARKLDELGVDYIEGGWP--GsnpkDTEFfKRAK--ELKLKHAKLaafgST 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  72 wCR----------MNALeirqsADLGIDWVDISIPASDklrqYKLREPLAVLLER-LAMfIH--LAH--TLGLKVCIGCE 136
Cdd:PRK12344  79 -RRagvsaeedpnLQAL-----LDAGTPVVTIFGKSWD----LHVTEALRTTLEEnLAM-IRdsVAYlkAHGREVIFDAE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 137 ---DASRASGQTLRAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGA 213
Cdd:PRK12344 148 hffDGYKANPEYALATLKAAAEAGADWVVLCDTNGGTLPHEVAEIVAEVRAAPGVPLGIHAHNDSGCAVANSLAAVEAGA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 214 TSVNTTVLGLGERAGNAALETVALGLE-----RCLGVEtgvHFSALPALCQRVAEAAQRAIDPQQPLVGELVFTHESGVH 288
Cdd:PRK12344 228 RQVQGTINGYGERCGNANLCSIIPNLQlkmgyECLPEE---KLKELTEVSRFVSEIANLAPDPHQPYVGASAFAHKGGIH 304
                        330       340       350
                 ....*....|....*....|....*....|...
gi 575523326 289 VAALLRDSESYQSIAPSLMGRSYRLVLGKHSGR 321
Cdd:PRK12344 305 VSAVLKDPRTYEHIDPELVGNRRRVLVSELAGR 337
DRE_TIM_CMS cd07945
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ...
8-276 2.08e-32

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: 122.87  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   8 DTTLRDGEQSPGVAFRTSEKVAIAEALYA-AGITAMEVGTPAMGDEEIARIQlvrrqlpdaTLMTWCRMNAL----EIRQ 82
Cdd:cd07945    2 DTTLRDGEQTSGVSFSPSEKLNIAKILLQeLKVDRIEVASARVSEGEFEAVQ---------KIIDWAAEEGLldriEVLG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  83 SADLG--IDW--------VDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDAS---RASGQTLRAI 149
Cdd:cd07945   73 FVDGDksVDWiksagakvLNLLTKGSLKHCTEQLRKTPEEHFADIREVIEYAIKNGIEVNIYLEDWSngmRDSPDYVFQL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 150 AEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVW-SGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAG 228
Cdd:cd07945  153 VDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYpNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHTTVNGLGERAG 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 575523326 229 NAALETVALGLERCLGVETGVHFSALPALCQRVAEAAQRAIDPQQPLV 276
Cdd:cd07945  233 NAPLASVIAVLKDKLKVKTNIDEKRLNRASRLVETFSGKRIPANKPIV 280
DRE_TIM_Re_CS cd07947
Clostridium kluyveri Re-citrate synthase and related proteins, catalytic TIM barrel domain; ...
4-254 1.47e-26

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: 107.02  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   4 VLINDTTLRDGEQSPGvAFRTSEKVAIAEALYAAG-----ITAMEVGTPAMGDEEIARIQLVRR-QLPDATlmTWCRMNA 77
Cdd:cd07947    1 IWITDTTFRDGQQARP-PYTVEQIVKIYDYLHELGggsgvIRQTEFFLYTEKDREAVEACLDRGyKFPEVT--GWIRANK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  78 LEIRQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRAS--GQTL---RAIAEV 152
Cdd:cd07947   78 EDLKLVKEMGLKETGILMSVSDYHIFKKLKMTREEAMEKYLEIVEEALDHGIKPRCHLEDITRADiyGFVLpfvNKLMKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 153 AQQCAA-ARLRYADTVGLLDPFTTAAQ-------ISALR---DVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVL 221
Cdd:cd07947  158 SKESGIpVKIRLCDTLGYGVPYPGASLprsvpkiIYGLRkdcGVPSENLEWHGHNDFYKAVANAVAAWLYGASWVNCTLL 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 575523326 222 GLGERAGNAALETVALGLERCLGVETGVHFSAL 254
Cdd:cd07947  238 GIGERTGNCPLEAMVIEYAQLKGNFDGMNLEVI 270
PRK08195 PRK08195
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
1-276 6.16e-26

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


Pssm-ID: 181282 [Multi-domain]  Cd Length: 337  Bit Score: 106.46  E-value: 6.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGeqSPGVAFR-TSEKV-AIAEALYAAGITAMEV-------------GTPAMGDEEIarIQLVRRQLP 65
Cdd:PRK08195   1 GKKIYISDVTLRDG--MHAVRHQyTLEQVrAIARALDAAGVPVIEVthgdglggssfnyGFGAHTDEEY--IEAAAEVVK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  66 DATLMT-----WCRMNalEIRQSADLGIDWV---------DISIPasdklrqyklreplavllerlamFIHLAHTLGLKV 131
Cdd:PRK08195  77 QAKIAAlllpgIGTVD--DLKMAYDAGVRVVrvathcteaDVSEQ-----------------------HIGLARELGMDT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 132 CIGCEDASRASGQTLRAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIE--MHAHNDLGMATANTLAAV 209
Cdd:PRK08195 132 VGFLMMSHMAPPEKLAEQAKLMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALKPDTQvgFHGHNNLGLGVANSLAAV 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523326 210 SAGATSVNTTVLGLGERAGNAALETVALGLERcLGVETGVHFSALpalcQRVAEAAQRAIDPQQPLV 276
Cdd:PRK08195 212 EAGATRIDGSLAGLGAGAGNTPLEVLVAVLDR-MGWETGVDLYKL----MDAAEDLVRPLMDRPVRV 273
4OH_2_O_val_ald TIGR03217
4-hydroxy-2-oxovalerate aldolase; Members of this protein family are 4-hydroxy-2-oxovalerate ...
3-276 1.34e-24

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


Pssm-ID: 274481 [Multi-domain]  Cd Length: 333  Bit Score: 102.81  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    3 RVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEV-------------GTPAMGDEE-IARIQLVRRQLPDAT 68
Cdd:TIGR03217   2 KLYITDVTLRDGMHAIRHQFTIEQVRAIAAALDEAGVDAIEVthgdglggssfnyGFSAHTDLEyIEAAADVVKRAKVAV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   69 LMTWCRMNALEIRQSADLGIDWVDISI--PASDKLRQYklreplavllerlamfIHLAHTLGLKVCIGCEDASRASGQTL 146
Cdd:TIGR03217  82 LLLPGIGTVHDLKAAYDAGARTVRVAThcTEADVSEQH----------------IGMARELGMDTVGFLMMSHMTPPEKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  147 RAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIE--MHAHNDLGMATANTLAAVSAGATSVNTTVLGLG 224
Cdd:TIGR03217 146 AEQAKLMESYGADCVYIVDSAGAMLPDDVRDRVRALKAVLKPETQvgFHAHHNLSLAVANSIAAIEAGATRIDASLRGLG 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 575523326  225 ERAGNAALETVALGLERcLGVETGVHFSALpalcQRVAEAAQRAIDPQQPLV 276
Cdd:TIGR03217 226 AGAGNAPLEVFVAVLDR-LGWNTGCDLFKL----MDAAEDIVRPLMDRPVRV 272
DRE_TIM_HOA cd07943
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ...
4-254 2.71e-24

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: 100.27  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   4 VLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEV-------------GTPAMGDEEIarIQLVRRQLPDATLM 70
Cdd:cd07943    1 VYIHDVTLRDGMHAVRHQFTLEQVRAIARALDAAGVPLIEVghgdglggsslnyGFAAHTDEEY--LEAAAEALKQAKLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  71 T-----WCRMNalEIRQSADLGIDWVDISIPASDklrqyklreplAVLLERlamFIHLAHTLGLKVCIGCEDASRASGQT 145
Cdd:cd07943   79 VlllpgIGTVD--DLKMAADLGVDVVRVATHCTE-----------ADVSEQ---HIGAARKLGMDVVGFLMMSHMASPEE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 146 LRAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWS-GEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLG 224
Cdd:cd07943  143 LAEQAKLMESYGADCVYVTDSAGAMLPDDVRERVRALREALDpTPVGFHGHNNLGLAVANSLAAVEAGATRIDGSLAGLG 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 575523326 225 ERAGNAALETVALGLERcLGVETGVHFSAL 254
Cdd:cd07943  223 AGAGNTPLEVLVAVLER-MGIETGIDLYKL 251
DRE_TIM_HMGL cd07938
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ...
6-263 2.01e-23

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: 98.23  E-value: 2.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGT-------PAMGD-EEIARiQLVRRqlPDATLMTWC-RMN 76
Cdd:cd07938    1 IVEVGPRDGLQNEKTFIPTEDKIELIDALSAAGLRRIEVTSfvspkwvPQMADaEEVLA-GLPRR--PGVRYSALVpNLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  77 ALEirQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKV------CIGC--EDASRASgqtlrA 148
Cdd:cd07938   78 GAE--RALAAGVDEVAVFVSASETFSQKNINCSIAESLERFEPVAELAKAAGLRVrgyvstAFGCpyEGEVPPE-----R 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 149 IAEVAQQCAAA---RLRYADTVGLLDPFTTAAQISALRDVWSGE-IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLG 224
Cdd:cd07938  151 VAEVAERLLDLgcdEISLGDTIGVATPAQVRRLLEAVLERFPDEkLALHFHDTRGQALANILAALEAGVRRFDSSVGGLG 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 575523326 225 ------ERAGNAALETVALGLERcLGVETGVHFSALPALCQRVAE 263
Cdd:cd07938  231 gcpfapGATGNVATEDLVYMLEG-MGIETGIDLDKLLAAARWISE 274
DRE_TIM_LeuA3 cd07941
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ...
6-263 1.25e-21

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: 93.29  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGTPamG----DEE-IARIQlvRRQLPDATL----MTwCR-- 74
Cdd:cd07941    1 IYDTTLRDGTQGEGISFSVEDKLRIARKLDELGVDYIEGGWP--GsnpkDTEfFARAK--KLKLKHAKLaafgST-RRag 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  75 --------MNALeirqsADLGIDWVDISIPASDklrqYKLREPLAVLLER-LAMfIH--LAH--TLGLKVCIGCE---DA 138
Cdd:cd07941   76 vkaeedpnLQAL-----LEAGTPVVTIFGKSWD----LHVTEALGTTLEEnLAM-IRdsVAYlkSHGREVIFDAEhffDG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 139 SRASG----QTLRAiaevAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSG-EIEMHAHNDLGMATANTLAAVSAGA 213
Cdd:cd07941  146 YKANPeyalATLKA----AAEAGADWLVLCDTNGGTLPHEIAEIVKEVRERLPGvPLGIHAHNDSGLAVANSLAAVEAGA 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 575523326 214 TSVNTTVLGLGERAGNAALETVALGLE-----RCLGVEtgvHFSALPALCQRVAE 263
Cdd:cd07941  222 TQVQGTINGYGERCGNANLCSIIPNLQlkmgyECLPEE---NLKKLTELSRFVSE 273
DRE_TIM_HOA_like cd07944
4-hydroxy-2-oxovalerate aldolase-like, N-terminal catalytic TIM barrel domain; This family of ...
8-233 7.98e-19

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: 85.31  E-value: 7.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   8 DTTLRDGeqspGV----AFRTSEKVAIAEALYAAGITAMEVG------------TPAMGDEEIARIQLVRRQLPDATLMT 71
Cdd:cd07944    3 DCTLRDG----GYvnnwDFGDEFVKAIYRALAAAGIDYVEIGyrsspekefkgkSAFCDDEFLRRLLGDSKGNTKIAVMV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  72 WCRMNALE-IRQSADLGIDWVDISIpasdklRQYKLREPLAvllerlamFIHLAHTLGLKVCIGCEDASRASGQTLRAIA 150
Cdd:cd07944   79 DYGNDDIDlLEPASGSVVDMIRVAF------HKHEFDEALP--------LIKAIKEKGYEVFFNLMAISGYSDEELLELL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 151 EVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEM--HAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAG 228
Cdd:cd07944  145 ELVNEIKPDVFYIVDSFGSMYPEDIKRIISLLRSNLDKDIKLgfHAHNNLQLALANTLEAIELGVEIIDATVYGMGRGAG 224

                 ....*
gi 575523326 229 NAALE 233
Cdd:cd07944  225 NLPTE 229
PRK03739 PRK03739
2-isopropylmalate synthase; Validated
190-311 1.75e-14

2-isopropylmalate synthase; Validated


Pssm-ID: 235154 [Multi-domain]  Cd Length: 552  Bit Score: 74.81  E-value: 1.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 190 IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLeRCLGVETGVHFSALPALCQRVAEAAQRAI 269
Cdd:PRK03739 241 LSLHPHNDRGTGVAAAELALMAGADRVEGCLFGNGERTGNVDLVTLALNL-YTQGVDPGLDFSDIDEIRRTVEYCNQLPV 319
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 575523326 270 DPQQPLVGELVFTHESGVH-------VAALLRDSE----SYQSIAPSLMGRSY 311
Cdd:PRK03739 320 HPRHPYAGDLVFTAFSGSHqdaikkgFAAQKADAIvwevPYLPIDPADVGRSY 372
PRK05692 PRK05692
hydroxymethylglutaryl-CoA lyase; Provisional
2-268 2.33e-13

hydroxymethylglutaryl-CoA lyase; Provisional


Pssm-ID: 180206  Cd Length: 287  Bit Score: 69.92  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   2 ERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGT-------PAMGD--EEIARIQlvRRqlPDAT---L 69
Cdd:PRK05692   3 KRVKIVEVGPRDGLQNEKRFIPTADKIALIDRLSAAGLSYIEVASfvspkwvPQMADaaEVMAGIQ--RR--PGVTyaaL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  70 MTwcRMNALEIRQSAdlGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKV-----CI-GCEdasrASG 143
Cdd:PRK05692  79 TP--NLKGLEAALAA--GADEVAVFASASEAFSQKNINCSIAESLERFEPVAEAAKQAGVRVrgyvsCVlGCP----YEG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 144 QT-LRAIAEVAQQCAA---ARLRYADTVGLLDPFTTAAQISALRDVWSGE-IEMHAHNDLGMATANTLAAVSAGATSVNT 218
Cdd:PRK05692 151 EVpPEAVADVAERLFAlgcYEISLGDTIGVGTPGQVRAVLEAVLAEFPAErLAGHFHDTYGQALANIYASLEEGITVFDA 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 575523326 219 TVLGLG------ERAGNAALETVALGLERcLGVETGVHFSALPALCQRVAEAAQRA 268
Cdd:PRK05692 231 SVGGLGgcpyapGASGNVATEDVLYMLHG-LGIETGIDLDKLVRAGQFIQSKLGRP 285
PRK14847 PRK14847
2-isopropylmalate synthase;
190-277 6.86e-12

2-isopropylmalate synthase;


Pssm-ID: 184849  Cd Length: 333  Bit Score: 65.80  E-value: 6.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 190 IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLERcLGVETGVHFSALPALCQRVAEAAQRAI 269
Cdd:PRK14847 243 LSVHPHNDRGTAVAAAELAVLAGAERIEGCLFGNGERTGNVDLVALALNLER-QGIASGLDFRDMAALRACVSECNQLPI 321

                 ....*...
gi 575523326 270 DPQQPLVG 277
Cdd:PRK14847 322 DVFHPYAW 329
DRE_TIM_PC_TC_5S cd07937
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ...
6-245 1.24e-10

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: 61.68  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   6 INDTTLRDGEQSpgvAF----RTSEKVAIAEALYAAGITAMEVGTPAMGDEEI--------ARIQLVRRQLPDATLMTWC 73
Cdd:cd07937    1 ITDTTLRDAHQS---LLatrmRTEDMLPIAEALDEAGFFSLEVWGGATFDVCMrflnedpwERLRELRKAMPNTPLQMLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  74 R-MNALE------------IRQSADLGID---------WVDISIPASDKLRQYKlreplavllerlamfihlahtlglKV 131
Cdd:cd07937   78 RgQNLVGyrhypddvvelfVEKAAKNGIDifrifdalnDVRNLEVAIKAVKKAG------------------------KH 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 132 CIGCEDASRASGQTLRAIAEVAQQCAAARlryADTV------GLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANT 205
Cdd:cd07937  134 VEGAICYTGSPVHTLEYYVKLAKELEDMG---ADSIcikdmaGLLTPYAAYELVKALKKEVGLPIHLHTHDTSGLAVATY 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 575523326 206 LAAVSAGATSVNTTVLGLGERAGNAALETV--AL-GLERCLGV 245
Cdd:cd07937  211 LAAAEAGVDIVDTAISPLSGGTSQPSTESMvaALrGTGRDTGL 253
DRE_TIM_LeuA cd07942
Mycobacterium tuberculosis LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; ...
190-263 2.69e-10

Mycobacterium tuberculosis LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Alpha-isopropylmalate synthase (LeuA), a key enzyme in leucine biosynthesis, catalyzes the first committed step in the pathway, converting acetyl-CoA and alpha-ketoisovalerate to alpha-isopropyl malate and CoA. Although the reaction catalyzed by LeuA is similar to that of the Arabidopsis thaliana IPMS1 protein, the two fall into phylogenetically distinct families within the same superfamily. LeuA has and N-terminal TIM barrel catalytic domain, a helical linker domain, and a C-terminal regulatory domain. LeuA forms a homodimer in which the linker domain of one monomer sits over the catalytic domain of the other, inserting residues into the active site that may be important for catalysis. Homologs of LeuA are found in bacteria as well as fungi. This family includes alpha-isopropylmalate synthases I (LEU4) and II (LEU9) from Saccharomyces cerevisiae. 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: 163680  Cd Length: 284  Bit Score: 60.66  E-value: 2.69e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523326 190 IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLErCLGVETGVHFSALPALCQRVAE 263
Cdd:cd07942  212 ISLHPHNDRGTGVAAAELALLAGADRVEGTLFGNGERTGNVDLVTLALNLY-SQGVDPGLDFSDIDEIIRVVEE 284
PLN02746 PLN02746
hydroxymethylglutaryl-CoA lyase
2-249 1.26e-09

hydroxymethylglutaryl-CoA lyase


Pssm-ID: 178347  Cd Length: 347  Bit Score: 59.03  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   2 ERVLINDTTLRDGEQSPGVAFRTSEKVAIAEALYAAGITAMEVGT-------PAMGD--EEIARIqlvrRQLPDATL--M 70
Cdd:PLN02746  45 KFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSfvspkwvPQLADakDVMAAV----RNLEGARFpvL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  71 TwcrMNALEIRQSADLGIDWVDISIPASDKLRQYKLREPLAVLLERLAMFIHLAHTLGLKV-----C-IGCEDASRASGQ 144
Cdd:PLN02746 121 T---PNLKGFEAAIAAGAKEVAVFASASESFSKSNINCSIEESLVRYREVALAAKKHSIPVrgyvsCvVGCPIEGPVPPS 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 145 TLRAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGE-IEMHAHNDLGMATANTLAAVSAGATSVNTTVLGL 223
Cdd:PLN02746 198 KVAYVAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDkLAVHFHDTYGQALANILVSLQMGISTVDSSVAGL 277
                        250       260       270
                 ....*....|....*....|....*....|..
gi 575523326 224 G------ERAGNAALETVALGLERcLGVETGV 249
Cdd:PLN02746 278 GgcpyakGASGNVATEDVVYMLNG-LGVSTNV 308
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
1-254 7.58e-09

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 57.02  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPgVAFR--TSEKVAIAEALYAAGITAMEVGTPAMGDEEI--------ARIQLVRRQLPDATLM 70
Cdd:PRK12331   1 MTKIKITETVLRDGQQSL-IATRmtTEEMLPILEKLDNAGYHSLEMWGGATFDACLrflnedpwERLRKIRKAVKKTKLQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  71 TWCR-MNALEIRQSAD------------LGIDWVDIsIPASDKLRQykLREPLAVLLE-----RLAMF--IHLAHTLGLK 130
Cdd:PRK12331  80 MLLRgQNLLGYRNYADdvvesfvqksveNGIDIIRI-FDALNDVRN--LETAVKATKKagghaQVAISytTSPVHTIDYF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 131 VcigcedasrasgqtlrAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVS 210
Cdd:PRK12331 157 V----------------KLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAVTVPLEVHTHATSGIAEMTYLKAIE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 575523326 211 AGATSVNTTVLGLGERAGNAALETVALGLERcLGVETGVHFSAL 254
Cdd:PRK12331 221 AGADIIDTAISPFAGGTSQPATESMVAALQD-LGYDTGLDLEEL 263
PRK14041 PRK14041
pyruvate carboxylase subunit B;
3-254 3.03e-08

pyruvate carboxylase subunit B;


Pssm-ID: 237593 [Multi-domain]  Cd Length: 467  Bit Score: 55.17  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   3 RVLINDTTLRDGEQS-PGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGDEEI--------ARIQLVRRQLPDATLMTWC 73
Cdd:PRK14041   2 KVMFVDTTLRDGHQSlIATRMRTEDMLPALEAFDRMGFYSMEVWGGATFDVCVrflnenpwERLKEIRKRLKNTKIQMLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  74 R-MNALEIRQSADlgiDWVDISIPAS-----DKLRQYKlreplAVLLER-LAMFIHLAHTLGLKVcIGCEDASRASGQTL 146
Cdd:PRK14041  82 RgQNLVGYRHYAD---DVVELFVKKVaeyglDIIRIFD-----ALNDIRnLEKSIEVAKKHGAHV-QGAISYTVSPVHTL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 147 RAIAEVAQQCAAA---RLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGL 223
Cdd:PRK14041 153 EYYLEFARELVDMgvdSICIKDMAGLLTPKRAYELVKALKKKFGVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 575523326 224 GERAGNAALETVALGLeRCLGVETGVHFSAL 254
Cdd:PRK14041 233 SMGTSQPPFESMYYAF-RENGKETDFDRKAL 262
PRK14042 PRK14042
pyruvate carboxylase subunit B; Provisional
1-239 2.42e-06

pyruvate carboxylase subunit B; Provisional


Pssm-ID: 172536 [Multi-domain]  Cd Length: 596  Bit Score: 49.33  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQS-PGVAFRTSEKVAIAEALYAAGITAMEVGTPAMGD--------EEIARIQLVRRQLPDATLMT 71
Cdd:PRK14042   1 MSKTFITDVTLRDAHQClIATRMRTEDMLPICNKMDDVGFWAMEVWGGATFDaclrflkeDPWSRLRQLRQALPNTQLSM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  72 WCR-MNALEIRQSADlgidwvdisipasDKLRQYkLREPLAVLLERLAMFIHLAHTLGLKVCIGCEDASRASGQ------ 144
Cdd:PRK14042  81 LLRgQNLLGYRNYAD-------------DVVRAF-VKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQgaicyt 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 145 -----TLRAIAEVAQQCAAA---RLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSV 216
Cdd:PRK14042 147 tspvhTLDNFLELGKKLAEMgcdSIAIKDMAGLLTPTVTVELYAGLKQATGLPVHLHSHSTSGLASICHYEAVLAGCNHI 226
                        250       260
                 ....*....|....*....|...
gi 575523326 217 NTTVLGLGERAGNAALETVALGL 239
Cdd:PRK14042 227 DTAISSFSGGASHPPTEALVAAL 249
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
1-235 3.21e-06

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 49.07  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   1 MERVLINDTTLRDGEQSPgVA--FRTSEKVAIAEALYAAGITAMEVGTPAMGDEEI--------ARIQLVRRQLPDATLM 70
Cdd:PRK09282   1 MKKVKITDTTLRDAHQSL-LAtrMRTEDMLPIAEKLDKVGFWSLEVWGGATFDVCIrylnedpwERLRKLKKALPNTPLQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  71 TWCR-MNALEIRQSADlgiDWVDisipasdklrqyklreplavllerlaMFIHLAHTLG---------------LKVCIg 134
Cdd:PRK09282  80 MLLRgQNLVGYRHYPD---DVVE--------------------------KFVEKAAENGidifrifdalndvrnMEVAI- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 135 ceDASRASG--------------QTLRAIAEVAQQCAAarlRYADTV------GLLDPFTTAAQISALRDVWSGEIEMHA 194
Cdd:PRK09282 130 --KAAKKAGahvqgtisyttspvHTIEKYVELAKELEE---MGCDSIcikdmaGLLTPYAAYELVKALKEEVDLPVQLHS 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 575523326 195 HNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETV 235
Cdd:PRK09282 205 HCTSGLAPMTYLKAVEAGVDIIDTAISPLAFGTSQPPTESM 245
PRK12581 PRK12581
oxaloacetate decarboxylase; Provisional
2-240 1.47e-05

oxaloacetate decarboxylase; Provisional


Pssm-ID: 79056 [Multi-domain]  Cd Length: 468  Bit Score: 46.65  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   2 ERVLINDTTLRDGEQSPgVAFRTS--EKVAIAEALYAAGITAMEVGTPAMGDEEI--------ARIQLVRRQLPDATLMT 71
Cdd:PRK12581  11 QQVAITETVLRDGHQSL-MATRLSieDMLPVLTILDKIGYYSLECWGGATFDACIrflnedpwERLRTLKKGLPNTRLQM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326  72 WCR-MNALEIRQSADlgiDWVD--ISIPASDKLRQYKLREPLAVLlERLAMFIHLAHTLG--LKVCIGCEDASRASGQTL 146
Cdd:PRK12581  90 LLRgQNLLGYRHYAD---DIVDkfISLSAQNGIDVFRIFDALNDP-RNIQQALRAVKKTGkeAQLCIAYTTSPVHTLNYY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326 147 RAIAEVAQQCAAARLRYADTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGER 226
Cdd:PRK12581 166 LSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIKAMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTALSPFSEG 245
                        250
                 ....*....|....
gi 575523326 227 AGNAALETVALGLE 240
Cdd:PRK12581 246 TSQPATESMYLALK 259
PRK14040 PRK14040
oxaloacetate decarboxylase subunit alpha;
165-240 6.65e-05

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 237592 [Multi-domain]  Cd Length: 593  Bit Score: 44.92  E-value: 6.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523326 165 DTVGLLDPFTTAAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTVLGLGERAGNAALETVALGLE 240
Cdd:PRK14040 176 DMAGLLKPYAAYELVSRIKKRVDVPLHLHCHATTGLSTATLLKAIEAGIDGVDTAISSMSMTYGHSATETLVATLE 251
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
2-220 6.22e-04

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 42.05  E-value: 6.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326    2 ERVLINDTTLRDGEQS-PGVAFRTSEKVAIAEAL--YAAGITAMEVGTPAMGDeeIA----------RIQLVRRQLPDAT 68
Cdd:PRK12999  531 KRVLLTDTTFRDAHQSlLATRVRTKDLLRIAPATarLLPNLFSLEMWGGATFD--VAyrflkedpweRLAELREAAPNVL 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   69 LmtwcRM-----NAL------------EIRQSADLGID---------WV-------------------------DISIPA 97
Cdd:PRK12999  609 F----QMllrgsNAVgytnypdnvvraFVREAAAAGIDvfrifdslnWVenmrvaidavretgkiaeaaicytgDILDPA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523326   98 SDK--LrQYKLRepLAVLLERLAmfihlAHTLGLKvcigcedasrasgqtlraiaevaqqcaaarlryaDTVGLLDPFTT 175
Cdd:PRK12999  685 RAKydL-DYYVD--LAKELEKAG-----AHILAIK----------------------------------DMAGLLKPAAA 722
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 575523326  176 AAQISALRDVWSGEIEMHAHNDLGMATANTLAAVSAGATSVNTTV 220
Cdd:PRK12999  723 YELVSALKEEVDLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAV 767
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH