|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
19-310 |
8.08e-112 |
|
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: 325.57 E-value: 8.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 19 DIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAAC 98
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 99 STRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGL 178
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVN 258
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1084751584 259 RFLeYDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLALRAIGLN 310
Cdd:COG0329 241 RAL-FAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
23-304 |
2.45e-99 |
|
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: 293.30 E-value: 2.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 23 IIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACSTRE 102
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 103 CLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLKQSC 182
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 183 VDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVNRFLe 262
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1084751584 263 YDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLAL 304
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
22-305 |
4.10e-74 |
|
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: 229.52 E-value: 4.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 22 GIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACSTR 101
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 102 ECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLKQS 181
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 182 CVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVNR-- 259
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKal 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1084751584 260 FLEYDPgyvSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLALR 305
Cdd:TIGR00674 241 FIETNP---IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
19-307 |
7.12e-68 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 213.38 E-value: 7.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 19 DIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAAC 98
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 99 STRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGL 178
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVN 258
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1084751584 259 --RFLEYDPgyvSPAKEALNMIGLPAGV-VRRPMPNLTPGQKEDLRLALRAI 307
Cdd:pfam00701 241 kiLFAEPNP---IPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
18-301 |
7.08e-46 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 157.08 E-value: 7.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 18 KDIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDG-GVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTA 96
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 97 ACSTRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNII 176
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 177 GLKQSCVDMGQLvEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKdlhiKLQI 256
Cdd:PRK04147 162 GVKQTAGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQ----ELQH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1084751584 257 V-NRFLE--YDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLR 301
Cdd:PRK04147 237 EcNDVIDllIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALK 284
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
19-310 |
8.08e-112 |
|
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: 325.57 E-value: 8.08e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 19 DIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAAC 98
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 99 STRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGL 178
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLAEIPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVN 258
Cdd:COG0329 161 KEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1084751584 259 RFLeYDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLALRAIGLN 310
Cdd:COG0329 241 RAL-FAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
23-304 |
2.45e-99 |
|
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: 293.30 E-value: 2.45e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 23 IIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACSTRE 102
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 103 CLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLKQSC 182
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 183 VDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVNRFLe 262
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1084751584 263 YDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLAL 304
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
20-304 |
4.82e-88 |
|
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: 264.74 E-value: 4.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 20 IKGIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACS 99
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 100 TRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLK 179
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAEHPNIVGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 180 QSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVNR 259
Cdd:cd00950 161 EATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLIK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1084751584 260 FLEYDPGyVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLAL 304
Cdd:cd00950 241 ALFAEPN-PIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
22-305 |
4.10e-74 |
|
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: 229.52 E-value: 4.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 22 GIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACSTR 101
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 102 ECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLKQS 181
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 182 CVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVNR-- 259
Cdd:TIGR00674 161 TGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKal 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1084751584 260 FLEYDPgyvSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLALR 305
Cdd:TIGR00674 241 FIETNP---IPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLK 283
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
19-307 |
7.12e-68 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 213.38 E-value: 7.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 19 DIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAAC 98
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 99 STRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGL 178
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDLHIKLQIVN 258
Cdd:pfam00701 161 KEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1084751584 259 --RFLEYDPgyvSPAKEALNMIGLPAGV-VRRPMPNLTPGQKEDLRLALRAI 307
Cdd:pfam00701 241 kiLFAEPNP---IPIKTALELLGLVVGPtCRLPLTPLSEEERPELEAILKAA 289
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
21-301 |
2.68e-61 |
|
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: 196.76 E-value: 2.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 21 KGIIAAIVTPFSENEEVDYSGLRVITEYLLD-GGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACS 99
Cdd:cd00954 2 KGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 100 TRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHF-KILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGL 178
Cdd:cd00954 82 LKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYrEIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKDL-HIKLQIV 257
Cdd:cd00954 162 KFTATDLYDLERIRAASPEDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELqHVINDVI 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1084751584 258 NRFLEYdpGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLR 301
Cdd:cd00954 242 TVLIKN--GLYPTLKAILRLMGLDAGPCRLPLRKVTEKALAKAK 283
|
|
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
18-301 |
7.08e-46 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 157.08 E-value: 7.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 18 KDIKGIIAAIVTPFSENEEVDYSGLRVITEYLLDG-GVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTA 96
Cdd:PRK04147 2 KNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEKqGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 97 ACSTRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNII 176
Cdd:PRK04147 82 SVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTLPKVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 177 GLKQSCVDMGQLvEIIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFLQGRLAQAKdlhiKLQI 256
Cdd:PRK04147 162 GVKQTAGDLYQL-ERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQ----ELQH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1084751584 257 V-NRFLE--YDPGYVSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLR 301
Cdd:PRK04147 237 EcNDVIDllIKNGVYPGLKEILHYMGVDAGLCRKPFKPVDEKYLPALK 284
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
22-309 |
6.63e-44 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 151.33 E-value: 6.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 22 GIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAACSTR 101
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 102 ECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKilSQANILPLVIYNNPLYTGNPMSPALIVKLLEMKNIIGLKQs 181
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFE--TVLDMGPTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 182 CVD---MGQLVEiirmskGGSSICTGVDSQFYPA-LTIGAVGVYSTAGGIFPNQMkqvHNLFLQGRLAQ----AKDLHIK 253
Cdd:PLN02417 161 CTGndrVKQYTE------KGILLWSGNDDECHDArWDYGADGVISVTSNLVPGLM---HKLMFAGKNKElndkLLPLMDW 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1084751584 254 LqivnrFLEYDPgyvSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLRLALRAIGL 309
Cdd:PLN02417 232 L-----FCEPNP---IGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGR 279
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
22-301 |
3.48e-31 |
|
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: 118.19 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 22 GIIAAIVTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGTAAcSTR 101
Cdd:cd00951 3 GLLSFPVTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 102 ECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYN--NPLYTgnpmsPALIVKLLEM-KNIIGL 178
Cdd:cd00951 82 TAIAYAQAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYNraNAVLT-----ADSLARLAERcPNLVGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 179 KQSCVDMGQLVEIIRmsKGGSSIC--TGV---DSQFYPALTIGaVGVYSTAggIFpNQMKQVHNLFLQGrLAQAKDLHIK 253
Cdd:cd00951 157 KDGVGDIELMRRIVA--KLGDRLLylGGLptaEVFALAYLAMG-VPTYSSA--VF-NFVPEIALAFYAA-VRAGDHATVK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1084751584 254 LQIVNRFLEY------DPGY-VSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDLR 301
Cdd:cd00951 230 RLLRDFFLPYvdirnrRKGYaVSIVKAGARLVGRDAGPVRPPLTDLTEEELAQLT 284
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
28-300 |
3.16e-29 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 113.37 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 28 VTPFSENEEVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPIIAGtAACSTRECLSLM 107
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAG-AGGGTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 108 EDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQANILPLVIYN--NPLYTgnpmsPALIVKLLEM-KNIIGLKQSCVD 184
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYNrdNAVLT-----ADTLARLAERcPNLVGFKDGVGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 185 MGQLVEIIRMSKGGSSICTGVDS--QFYPA-LTIGaVGVYSTAggIF---PNQMKQVHNLFLQGRLAQAKDLhIK----- 253
Cdd:PRK03620 170 IELMQRIVRALGDRLLYLGGLPTaeVFAAAyLALG-VPTYSSA--VFnfvPEIALAFYRALRAGDHATVDRL-LDdfflp 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1084751584 254 -LQIVNRfleyDPGY-VSPAKEALNMIGLPAGVVRRPMPNLTPGQKEDL 300
Cdd:PRK03620 246 yVALRNR----KKGYaVSIVKAGARLVGLDAGPVRAPLTDLTPEELAEL 290
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
19-217 |
5.76e-23 |
|
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: 96.36 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 19 DIKGIIAAIVTPFSENEE-------VDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKGKVPI 91
Cdd:cd00952 1 DIKGVWAIVPTPSKPDASdwratdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 92 IAGTAACSTRECLSLMEDAKESGADAAIMVPPYYFVLNEEAIFNHFKILSQAniLP---LVIYNNPLYTGNPMSPALIVK 168
Cdd:cd00952 81 FVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEA--VPemaIAIYANPEAFKFDFPRAAWAE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084751584 169 LLEMKNIIGLKQSCvDMGQLVEIIRMSKGGSSICTgVDSQFYPALTIGA 217
Cdd:cd00952 159 LAQIPQVVAAKYLG-DIGALLSDLAAVKGRMRLLP-LEDDYYAAARLFP 205
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
23-301 |
3.38e-21 |
|
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: 90.90 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 23 IIAAIVTPFSENEeVDYSGLRVITEYLLDGGVDGIMTSGGTGEFPHLTREEKKLVVKTIVEVCKgkvPIIAGTAACSTRE 102
Cdd:cd00953 4 KITPVITPFTGNK-IDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 103 CLSLMEDAKESGADAAIMVPPYYFV-LNEEAIFNHFKILSqaNILPLVIYNNPLYTGNPMSPALIVKLLEMK-NIIGLKQ 180
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYFPgIPEEWLIKYFTDIS--SPYPTFIYNYPKATGYDINARMAKEIKKAGgDIIGVKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 181 SCVDMGQLVEiIRMSKGGSSICTGVDSQFYPALTIGAVGVYSTAGGIFPNQMKQVHNLFlqgrlaqAKDLHIKLQI-VNR 259
Cdd:cd00953 158 TNEDISHMLE-YKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHV-------AIEDAFKLQFlINE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1084751584 260 FLEYDP--GYVSPAKEALNMI-GLPAGVVRRPMPNLTPGQKEDLR 301
Cdd:cd00953 230 VLDASRkyGSWSANYSLVKIFqGYDAGEPRPPFYPLDEEEEEKLR 274
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
23-171 |
1.34e-07 |
|
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: 51.17 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084751584 23 IIAAIVTPFSENEEVDYsglrvITEYLLDGGVDGIMTSGGtgefphltreekklVVKTIVEVCKG-KVPIIA----GTAA 97
Cdd:cd00945 1 IDLTLLHPDATLEDIAK-----LCDEAIEYGFAAVCVNPG--------------YVRLAADALAGsDVPVIVvvgfPTGL 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084751584 98 CSTRECLSLMEDAKESGADAAIMVPPYYFVL--NEEAIFNHFKILSQA--NILPLVIYnnpLYTGNPMSPALIVKLLE 171
Cdd:cd00945 62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKegDWEEVLEEIAAVVEAadGGLPLKVI---LETRGLKTADEIAKAAR 136
|
|
| |
