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Conserved domains on  [gi|239823749|gb|EEQ95317|]
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dihydrodipicolinate synthase [Brucella intermedia LMG 3301]

Protein Classification

4-hydroxy-tetrahydrodipicolinate synthase family protein( domain architecture ID 10097240)

4-hydroxy-tetrahydrodipicolinate synthase family protein may catalyze a key step in lysine biosynthesis, the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue

CATH:  3.20.20.70
EC:  4.3.3.7
Gene Ontology:  GO:0008840|GO:0009089
SCOP:  3000445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 53-337 1.47e-161

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


:

Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 452.72  E-value: 1.47e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 132
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 133 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGV 212
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 213 KDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLH 292
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 239823749 293 KALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAM 337
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
 
Name Accession Description Interval E-value
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 53-337 1.47e-161

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 452.72  E-value: 1.47e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 132
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 133 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGV 212
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 213 KDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLH 292
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 239823749 293 KALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAM 337
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 52-343 2.58e-151

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 426.88  E-value: 2.58e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVrDHKNIVG 211
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 212 VKDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPL 291
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239823749 292 HKALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHAGLV 343
Cdd:COG0329  240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 55-340 5.48e-127

4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129757 [Multi-domain]  Cd Length: 285  Bit Score: 365.11  E-value: 5.48e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749   55 GSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 134
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  135 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGVKD 214
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAE-EPNIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  215 ATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLHKA 294
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 239823749  295 LFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHA 340
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 52-340 9.52e-116

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 336.65  E-value: 9.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749   52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVG 211
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  212 VKDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPL 291
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 239823749  292 HKALFIEPNPSGPKYALSRLG-RVENALRSPMVTVEAATAEKIDQAMKHA 340
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
PLN02417 PLN02417
dihydrodipicolinate synthase
 52-342 2.33e-87

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 264.20  E-value: 2.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLIIYNIPGRSVIDMTPETMGALVrDHKNIVG 211
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIA-QHPNFAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 212 VKDATGKiERVSEqraACGKDFIQLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQDAcqagdfARALELQDRLMP 290
Cdd:PLN02417 158 VKECTGN-DRVKQ---YTEKGILLWSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKLLP 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239823749 291 LHKALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHAGL 342
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGR 279
 
Name Accession Description Interval E-value
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 53-337 1.47e-161

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 452.72  E-value: 1.47e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 132
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 133 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGV 212
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 213 KDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLH 292
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 239823749 293 KALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAM 337
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 52-343 2.58e-151

4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440098 [Multi-domain]  Cd Length: 291  Bit Score: 426.88  E-value: 2.58e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVrDHKNIVG 211
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 212 VKDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPL 291
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239823749 292 HKALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHAGLV 343
Cdd:COG0329  240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 57-337 6.74e-130

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 372.27  E-value: 6.74e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  57 ITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEA 136
Cdd:cd00408    2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 137 IELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGVKDAT 216
Cdd:cd00408   82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAE-HPNIVGIKDSS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 217 GKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLHKALF 296
Cdd:cd00408  161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALF 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 239823749 297 IEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAM 337
Cdd:cd00408  241 KEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 55-340 5.48e-127

4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 129757 [Multi-domain]  Cd Length: 285  Bit Score: 365.11  E-value: 5.48e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749   55 GSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 134
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  135 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVGVKD 214
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAE-EPNIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  215 ATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLHKA 294
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 239823749  295 LFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHA 340
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 52-340 9.52e-116

Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 336.65  E-value: 9.52e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749   52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVRdHKNIVG 211
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  212 VKDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPL 291
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 239823749  292 HKALFIEPNPSGPKYALSRLG-RVENALRSPMVTVEAATAEKIDQAMKHA 340
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGlVVGPTCRLPLTPLSEEERPELEAILKAA 289
HpaI-NOT-DapA TIGR02313
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents a subset of the DapA ...
 53-343 4.80e-89

2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase; This model represents a subset of the DapA (dihydrodipicolinate synthase) family which has apparently evolved a separate function. The product of DapA, dihydrodipicolinate, results from the non-enzymatic cyclization and dehydration of 6-amino-2,4-dihydroxyhept-2-ene-1,7-dioic acid, which is different from the substrate of this reaction only in the presence of the amino group. In the absence of this amino group, and running the reaction in the opposite direction, the reaction corresponds to the HpaI aldolase component of the 4-hydroxyphenylacetic acid catabolism pathway (see TIGR02311). At present, this variant of DapA is found only in Oceanobacillus iheyensis HTE831 and Thermus thermophilus HB27. In both of these cases, one or more other DapA genes can be found and the one identified by this model is part of an operon for 4-hydroxyphenylacetic acid catabolism.


Pssm-ID: 131366  Cd Length: 294  Bit Score: 269.15  E-value: 4.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749   53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 132
Cdd:TIGR02313   1 FRGSIAPLITPFKRNGDIDEEALRELIEFQIEGGSHAISVGGTSGEPGSLTLEERKQAIENAIDQIAGRIPFAPGTGALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  133 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSIS-IPLIIYNIPGRSVIDMTPETMGALVRDHKNIVG 211
Cdd:TIGR02313  81 HDETLELTKFAEEAGADAAMVIVPYYNKPNQEALYDHFAEVADAVPdFPIIIYNIPGRAAQEIAPKTMARLRKDCPNIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  212 VKDATGKIERVSEQRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPL 291
Cdd:TIGR02313 161 AKESNKDFEHLNHLFLEAGRDFLLFCGIELLCLPMLAIGAAGSIAATANVEPKEVAELCEAAEAGDIKGAQDLHFELLEA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 239823749  292 HKALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHAGLV 343
Cdd:TIGR02313 241 NDAIFKDTNPAPLKAALGMMGLIEKELRPPLGLPSDALEEEIRDMAEKYGKI 292
PLN02417 PLN02417
dihydrodipicolinate synthase
 52-342 2.33e-87

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 264.20  E-value: 2.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  52 MLKGSITALVTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLIIYNIPGRSVIDMTPETMGALVrDHKNIVG 211
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIA-QHPNFAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 212 VKDATGKiERVSEqraACGKDFIQLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQDAcqagdfARALELQDRLMP 290
Cdd:PLN02417 158 VKECTGN-DRVKQ---YTEKGILLWSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKLLP 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239823749 291 LHKALFIEPNPSGPKYALSRLGRVENALRSPMVTVEAATAEKIDQAMKHAGL 342
Cdd:PLN02417 228 LMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGR 279
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 61-338 3.59e-57

5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.


Pssm-ID: 188638  Cd Length: 289  Bit Score: 187.14  E-value: 3.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  61 VTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 140
Cdd:cd00951    9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 141 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNipgRSVIDMTPETMGALVRDHKNIVGVKDATGKIE 220
Cdd:cd00951   88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERCPNLVGFKDGVGDIE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 221 RVSEQRAACGKDFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALE-LQDRLMPlhkalF 296
Cdd:cd00951  165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRlLRDFFLP-----Y 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 239823749 297 IEPNPSGPKYALS------RL-GRVENALRSPMVTVEAATAEKIDQAMK 338
Cdd:cd00951  240 VDIRNRRKGYAVSivkagaRLvGRDAGPVRPPLTDLTEEELAQLTALIK 288
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 53-286 4.57e-56

N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.


Pssm-ID: 188641 [Multi-domain]  Cd Length: 288  Bit Score: 184.05  E-value: 4.57e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRV-ARSISIPLIIYNIPGRSVIDMTPETMGALvRDHKNIV 210
Cdd:cd00954   81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLEL-FEIPNVI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239823749 211 GVKDATG---KIERVseqRAACGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQD 286
Cdd:cd00954  160 GVKFTATdlyDLERI---RAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 61-341 7.12e-56

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 184.25  E-value: 7.12e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  61 VTPFDSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 140
Cdd:PRK03620  16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 141 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNipgRSVIDMTPETMGALVRDHKNIVGVKDATGKIE 220
Cdd:PRK03620  95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAERCPNLVGFKDGVGDIE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 221 RVSEQRAACGKDFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALE-LQDRLMPlhkalF 296
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRlLDDFFLP-----Y 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 239823749 297 IEPNPSGPKYALS------RL-GRVENALRSPMVTVEAATAEKIDQAMKHAG 341
Cdd:PRK03620 247 VALRNRKKGYAVSivkagaRLvGLDAGPVRAPLTDLTPEELAELAALIAKGG 298
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 53-285 3.92e-48

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 163.63  E-value: 3.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  53 LKGSITALVTPFDSEGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 131
Cdd:PRK04147   4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 132 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLIIYNIPGRSVIDMTPETMGALVrDHKNIVG 211
Cdd:PRK04147  84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELF-TLPKVIG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 212 VKDATG---KIERVseqRAACgKDFIQLSGED---ATALGFNAHGGVGCisvTSNI-APRLCAEFqDACQAGDFARALEL 284
Cdd:PRK04147 163 VKQTAGdlyQLERI---RKAF-PDKLIYNGFDemfASGLLAGADGAIGS---TYNVnGWRARQIF-EAAKAGDIQEAQEL 234


                 .
gi 239823749 285 Q 285
Cdd:PRK04147 235 Q 235
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 56-285 9.18e-20

KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.


Pssm-ID: 188640  Cd Length: 279  Bit Score: 87.44  E-value: 9.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  56 SITALVTPFdSEGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAgrvPVIAGAGSNNTVE 135
Cdd:cd00953    4 KITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 136 AIELAQHAEKAGADAVLVVTPYY-NKPNQRGLYEHFSRVARsiSIPLIIYNIPGRSVIDMTPETMGALVRDHKNIVGVKD 214
Cdd:cd00953   80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239823749 215 ATGKIERVSEQRAAcGKDFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACqagDFARALELQ 285
Cdd:cd00953  158 TNEDISHMLEYKRL-VPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV---AIEDAFKLQ 224
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 79-296 3.29e-17

Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.


Pssm-ID: 188639  Cd Length: 309  Bit Score: 80.95  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749  79 VNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEAIELAQHAEKAGADAVLVVTPYY 158
Cdd:cd00952   35 VERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMW 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 159 NKPNQRGLYEHFSRVARSI-SIPLIIYNIPGRSVIDMtPETMGALVRDHKNIVGVKdATGKIERV-SEQRAACGK-DFIQ 235
Cdd:cd00952  115 LPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDF-PRAAWAELAQIPQVVAAK-YLGDIGALlSDLAAVKGRmRLLP 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239823749 236 LSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQDACQAGDFARALELQDRLMPLHKALF 296
Cdd:cd00952  193 LEDDYYAAARLFPEEVTAFWSSGAACGPAPVTALRDAVATGDWTDARALTDRMRWAAEPLF 253
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 107-232 1.84e-04

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 41.93  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239823749 107 HKRVIEVCIEVAAG-RVPVIAGAGSNN----TVEAIELAQHAEKAGADAVLVVTPYYNKP--NQRGLYEHFSRVARSIS- 178
Cdd:cd00945   33 NPGYVRLAADALAGsDVPVIVVVGFPTglttTEVKVAEVEEAIDLGADEIDVVINIGSLKegDWEEVLEEIAAVVEAADg 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239823749 179 -IPLIIYNIPGRSVidmTPETMGALVRD--HKNIVGVKDATGK------IERVSEQRAACGKD 232
Cdd:cd00945  113 gLPLKVILETRGLK---TADEIAKAARIaaEAGADFIKTSTGFggggatVEDVKLMKEAVGGR 172
PRK08637 PRK08637
hypothetical protein; Provisional
 64-126 2.38e-03

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 39.55  E-value: 2.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239823749  64 FDSEGAFDEKAFRAFVNWQIEEGTKGLV---PVGTTGETPTlsHDEHKRVIEVCIEVAAGRVPVIA 126
Cdd:PRK08637 124 FDEDGGFDTDALKEALQAAYNKGKVIVIlnfPNNPTGYTPT--EKEATAIVEAIKELADAGTKVVA 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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