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Conserved domains on  [gi|237789938|gb|EEP64148|]
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dihydrodipicolinate synthase [Brucella abortus str. 2308 A]

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 ...
 16-300 3.85e-159

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: 445.01  E-value: 3.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGV 175
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 176 KDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLH 255
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 237789938 256 KALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
 
Name Accession Description Interval E-value
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 16-300 3.85e-159

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: 445.01  E-value: 3.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGV 175
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 176 KDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLH 255
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 237789938 256 KALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 15-306 1.46e-146

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: 413.39  E-value: 1.46e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVrDCKNIVG 174
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 237789938 255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAVLI 306
Cdd:COG0329  240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 18-303 1.88e-124

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: 357.02  E-value: 1.88e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   18 GSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 97
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   98 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDCkNIVGVKD 177
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  178 ATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKA 257
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 237789938  258 LFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 15-303 1.12e-114

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 332.41  E-value: 1.12e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVG 174
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 237789938  255 HKALFLEPNPSGPKYALSRLGRI-ENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVvGPTCRLPLTPLSEEERPELEAILKAA 289
PLN02417 PLN02417
dihydrodipicolinate synthase
 15-301 1.68e-83

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 253.03  E-value: 1.68e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 175 VKDATG--KIERVSEQRAICgkefiqLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQEAcqagnfAKALELQDRL 251
Cdd:PLN02417 158 VKECTGndRVKQYTEKGILL------WSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKL 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 237789938 252 MPLHKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMK 301
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVK 275
 
Name Accession Description Interval E-value
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 16-300 3.85e-159

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: 445.01  E-value: 3.85e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:cd00950    1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGV 175
Cdd:cd00950   81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 176 KDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLH 255
Cdd:cd00950  160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 237789938 256 KALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00950  240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
 15-306 1.46e-146

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: 413.39  E-value: 1.46e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:COG0329    1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVrDCKNIVG 174
Cdd:COG0329   81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:COG0329  160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 237789938 255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAVLI 306
Cdd:COG0329  240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 20-300 1.89e-127

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: 364.56  E-value: 1.89e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  20 ITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEA 99
Cdd:cd00408    2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 100 IELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGVKDAT 179
Cdd:cd00408   82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAE-HPNIVGIKDSS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 180 GKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKALF 259
Cdd:cd00408  161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALF 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 237789938 260 LEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00408  241 KEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
dapA TIGR00674
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ...
 18-303 1.88e-124

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: 357.02  E-value: 1.88e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   18 GSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 97
Cdd:TIGR00674   1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   98 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDCkNIVGVKD 177
Cdd:TIGR00674  81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  178 ATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKA 257
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 237789938  258 LFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
 15-303 1.12e-114

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 332.41  E-value: 1.12e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:pfam00701   1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVG 174
Cdd:pfam00701  81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 237789938  255 HKALFLEPNPSGPKYALSRLGRI-ENVLRSPMVTIEAATAEKIDHAMKHA 303
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 ...
 16-305 5.72e-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: 267.61  E-value: 5.72e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:TIGR02313   1 FRGSIAPLITPFKRNGDIDEEALRELIEFQIEGGSHAISVGGTSGEPGSLTLEERKQAIENAIDQIAGRIPFAPGTGALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938   96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSIS-IPLVIYNIPGRSIIDMTPETMGALVRDCKNIVG 174
Cdd:TIGR02313  81 HDETLELTKFAEEAGADAAMVIVPYYNKPNQEALYDHFAEVADAVPdFPIIIYNIPGRAAQEIAPKTMARLRKDCPNIVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:TIGR02313 161 AKESNKDFEHLNHLFLEAGRDFLLFCGIELLCLPMLAIGAAGSIAATANVEPKEVAELCEAAEAGDIKGAQDLHFELLEA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 237789938  255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKI-DHAMKHAVL 305
Cdd:TIGR02313 241 NDAIFKDTNPAPLKAALGMMGLIEKELRPPLGLPSDALEEEIrDMAEKYGKI 292
PLN02417 PLN02417
dihydrodipicolinate synthase
 15-301 1.68e-83

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 253.03  E-value: 1.68e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PLN02417   1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PLN02417  81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 175 VKDATG--KIERVSEQRAICgkefiqLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQEAcqagnfAKALELQDRL 251
Cdd:PLN02417 158 VKECTGndRVKQYTEKGILL------WSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKL 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 237789938 252 MPLHKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMK 301
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVK 275
KDGDH cd00951
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ...
 24-297 1.59e-55

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: 181.75  E-value: 1.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  24 VTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 103
Cdd:cd00951    9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 104 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNipgRSIIDMTPETMGALVRDCKNIVGVKDATGKIE 183
Cdd:cd00951   88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERCPNLVGFKDGVGDIE 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 184 RVSEQRAICGKEFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALE-LQDRLMPlhkalF 259
Cdd:cd00951  165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRlLRDFFLP-----Y 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 237789938 260 LEPNPSGPKYALS------RL-GRIENVLRSPMVTIEAATAEKID 297
Cdd:cd00951  240 VDIRNRRKGYAVSivkagaRLvGRDAGPVRPPLTDLTEEELAQLT 284
PRK03620 PRK03620
5-dehydro-4-deoxyglucarate dehydratase; Provisional
 24-254 4.52e-54

5-dehydro-4-deoxyglucarate dehydratase; Provisional


Pssm-ID: 235141  Cd Length: 303  Bit Score: 178.09  E-value: 4.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  24 VTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 103
Cdd:PRK03620  16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 104 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNipgRSIIDMTPETMGALVRDCKNIVGVKDATGKIE 183
Cdd:PRK03620  95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAERCPNLVGFKDGVGDIE 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237789938 184 RVSEQRAICGKEFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALE-LQDRLMPL 254
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRlLDDFFLPY 246
NAL cd00954
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ...
 16-249 8.98e-53

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: 174.42  E-value: 8.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:cd00954    1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRV-ARSISIPLVIYNIPGRSIIDMTPETMGALVRDcKNIV 173
Cdd:cd00954   81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEI-PNVI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237789938 174 GVKDATG---KIERVseqRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQD 249
Cdd:cd00954  160 GVKFTATdlyDLERI---RAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQH 235
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
 16-248 2.98e-46

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 157.85  E-value: 2.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PRK04147   4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PRK04147  84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTL-PKVIG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 175 VKDATG---KIERVseQRAICGKefIQLSGED---ATALGFNAHGGVGCisvTSNI-APRLCAEFqEACQAGNFAKALEL 247
Cdd:PRK04147 163 VKQTAGdlyQLERI--RKAFPDK--LIYNGFDemfASGLLAGADGAIGS---TYNVnGWRARQIF-EAAKAGDIQEAQEL 234


                 .
gi 237789938 248 Q 248
Cdd:PRK04147 235 Q 235
KDG_aldolase cd00953
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ...
 19-248 1.89e-19

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: 86.28  E-value: 1.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  19 SITALVTPFdREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAgrvPVIAGAGSNNTVE 98
Cdd:cd00953    4 KITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  99 AIELAQHAEKAGADAVLVVTPYY-NKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDCKNIVGVKD 177
Cdd:cd00953   80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237789938 178 ATGKIERVSEQRAIcGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAgnfAKALELQ 248
Cdd:cd00953  158 TNEDISHMLEYKRL-VPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAI---EDAFKLQ 224
CHBPH_aldolase cd00952
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ...
 42-263 3.39e-18

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: 83.26  E-value: 3.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  42 VNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEAIELAQHAEKAGADAVLVVTPYY 121
Cdd:cd00952   35 VERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMW 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938 122 NKPNQRGLYEHFSRVARSI-SIPLVIYNIPGRSIIDMtPETMGALVRDCKNIVGVKdATGKIERV-SEQRAICGK-EFIQ 198
Cdd:cd00952  115 LPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDF-PRAAWAELAQIPQVVAAK-YLGDIGALlSDLAAVKGRmRLLP 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237789938 199 LSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKALFLEPN 263
Cdd:cd00952  193 LEDDYYAAARLFPEEVTAFWSSGAACGPAPVTALRDAVATGDWTDARALTDRMRWAAEPLFPRGD 257
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
 70-184 6.05e-05

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: 43.09  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237789938  70 HKRVIEVCIEVAAG-RVPVIAGAGSNN----TVEAIELAQHAEKAGADAVLVVTPYYNKP--NQRGLYEHFSRVARSIS- 141
Cdd:cd00945   33 NPGYVRLAADALAGsDVPVIVVVGFPTglttTEVKVAEVEEAIDLGADEIDVVINIGSLKegDWEEVLEEIAAVVEAADg 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 237789938 142 -IPLVIYNIPGRsiiDMTPETMGALVRDCK--NIVGVKDATGKIER 184
Cdd:cd00945  113 gLPLKVILETRG---LKTADEIAKAARIAAeaGADFIKTSTGFGGG 155
PRK08637 PRK08637
hypothetical protein; Provisional
 27-89 7.62e-04

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 40.71  E-value: 7.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237789938  27 FDREGAFDEKAFRAFVNWQIEEGTKGLV---PVGTTGETPTlsHDEHKRVIEVCIEVAAGRVPVIA 89
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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