|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
16-300 |
3.13e-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: 3.13e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGV 175
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 176 KDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLH 255
Cdd:cd00950 160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 225617983 256 KALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00950 240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
15-306 |
3.72e-148 |
|
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: 417.25 E-value: 3.72e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVrDCKNIVG 174
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 225617983 255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAGLI 306
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
18-303 |
1.41e-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: 357.41 E-value: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 18 GSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 97
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 98 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDCkNIVGVKD 177
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 178 ATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKA 257
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 225617983 258 LFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
15-303 |
1.06e-114 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 332.79 E-value: 1.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVG 174
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 225617983 255 HKALFLEPNPSGPKYALSRLGRI-ENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVvGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
15-306 |
4.45e-85 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 256.88 E-value: 4.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATG--KIERVSEQRAICgkefiqLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQEAcqagnfAKALELQDRL 251
Cdd:PLN02417 158 VKECTGndRVKQYTEKGILL------WSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 225617983 252 MPLHKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAGLI 306
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
16-300 |
3.13e-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: 3.13e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGV 175
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATDLPVILYNVPGRTGVNIEPETVLRLAE-HPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 176 KDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLH 255
Cdd:cd00950 160 KEATGDLDRVSELIALCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 225617983 256 KALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00950 240 KALFAEPNPIPVKAALALLGLISGELRLPLVPLSEELRAKLRAAL 284
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
15-306 |
3.72e-148 |
|
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: 417.25 E-value: 3.72e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVrDCKNIVG 174
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVDLPIILYNIPGRTGVDLSPETLARLA-EIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:COG0329 160 IKEASGDLDRIAELIRATGDDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 225617983 255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAGLI 306
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPSGPVRLPLLPLSEEERAELRAALKELGLL 291
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
20-300 |
1.41e-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: 364.95 E-value: 1.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 20 ITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEA 99
Cdd:cd00408 2 IPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 100 IELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVGVKDAT 179
Cdd:cd00408 82 IELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASDLPVILYNIPGRTGVDLSPETIARLAE-HPNIVGIKDSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 180 GKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKALF 259
Cdd:cd00408 161 GDLDRLTRLIALLGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEALF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 225617983 260 LEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAM 300
Cdd:cd00408 241 KEGNPAPVKAALALLGLDAGPVRLPLVPLSEEERAKLEALL 281
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
18-303 |
1.41e-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: 357.41 E-value: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 18 GSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTV 97
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 98 EAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDCkNIVGVKD 177
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVDLPIILYNVPSRTGVSLYPETVKRLAEEP-NIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 178 ATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPLHKA 257
Cdd:TIGR00674 160 ATGNLERISEIKAIAPDDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 225617983 258 LFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHA 303
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGELRLPLTELSEEHRNKLRDVLKDL 285
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
15-303 |
1.06e-114 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 332.79 E-value: 1.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRdCKNIVG 174
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEATDLPMILYNVPSRTGVDLTPETVGRLAT-NPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:pfam00701 160 IKEASGDLDRMINIKKEAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 225617983 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 ... |
16-306 |
1.17e-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: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNN 95
Cdd:TIGR02313 1 FRGSIAPLITPFKRNGDIDEEALRELIEFQIEGGSHAISVGGTSGEPGSLTLEERKQAIENAIDQIAGRIPFAPGTGALN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 96 TVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSIS-IPLVIYNIPGRSIIDMTPETMGALVRDCKNIVG 174
Cdd:TIGR02313 81 HDETLELTKFAEEAGADAAMVIVPYYNKPNQEALYDHFAEVADAVPdFPIIIYNIPGRAAQEIAPKTMARLRKDCPNIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATGKIERVSEQRAICGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALELQDRLMPL 254
Cdd:TIGR02313 161 AKESNKDFEHLNHLFLEAGRDFLLFCGIELLCLPMLAIGAAGSIAATANVEPKEVAELCEAAEAGDIKGAQDLHFELLEA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 225617983 255 HKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAGLI 306
Cdd:TIGR02313 241 NDAIFKDTNPAPLKAALGMMGLIEKELRPPLGLPSDALEEEIRDMAEKYGKI 292
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
15-306 |
4.45e-85 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 256.88 E-value: 4.45e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 15 MLKGSITALVTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PLN02417 1 KKLRLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PLN02417 81 STREAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLD--MGPTIIYNVPGRTGQDIPPEVIFKIAQH-PNFAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATG--KIERVSEQRAICgkefiqLSGEDATALGFN-AHGGVGCISVTSNIAPRLCAEFQEAcqagnfAKALELQDRL 251
Cdd:PLN02417 158 VKECTGndRVKQYTEKGILL------WSGNDDECHDARwDYGADGVISVTSNLVPGLMHKLMFA------GKNKELNDKL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 225617983 252 MPLHKALFLEPNPSGPKYALSRLGRIENVLRSPMVTIEAATAEKIDHAMKHAGLI 306
Cdd:PLN02417 226 LPLMDWLFCEPNPIGLNTALAQLGLIRPVFRLPYVPLDLAKRAEFVALVKAIGRE 280
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
24-297 |
1.84e-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: 181.37 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 24 VTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 103
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 104 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNipgRSIIDMTPETMGALVRDCKNIVGVKDATGKIE 183
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTDLGVIVYN---RANAVLTADSLARLAERCPNLVGFKDGVGDIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 184 RVSEQRAICGKEFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALE-LQDRLMPlhkalF 259
Cdd:cd00951 165 LMRRIVAKLGDRLLYLGGlptAEVFALAYLAMGVPTYSSAVFNFVPEIALAFYAAVRAGDHATVKRlLRDFFLP-----Y 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 225617983 260 LEPNPSGPKYALS------RL-GRIENVLRSPMVTIEAATAEKID 297
Cdd:cd00951 240 VDIRNRRKGYAVSivkagaRLvGRDAGPVRPPLTDLTEEELAQLT 284
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
24-254 |
4.62e-54 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 178.09 E-value: 4.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 24 VTPFDREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSnNTVEAIELA 103
Cdd:PRK03620 16 VTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVIAGAGG-GTAQAIEYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 104 QHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNipgRSIIDMTPETMGALVRDCKNIVGVKDATGKIE 183
Cdd:PRK03620 95 QAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTDLGVIVYN---RDNAVLTADTLARLAERCPNLVGFKDGVGDIE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225617983 184 RVSEQRAICGKEFIQLSG---EDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAGNFAKALE-LQDRLMPL 254
Cdd:PRK03620 172 LMQRIVRALGDRLLYLGGlptAEVFAAAYLALGVPTYSSAVFNFVPEIALAFYRALRAGDHATVDRlLDDFFLPY 246
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
16-249 |
9.08e-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: 9.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRV-ARSISIPLVIYNIPGRSIIDMTPETMGALVRDcKNIV 173
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIiAAAASLPMIIYHIPALTGVNLTLEQFLELFEI-PNVI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225617983 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 225617983 16 LKGSITALVTPFDREGAFDEKAFRAFVNWQIE-EGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSN 94
Cdd:PRK04147 4 LKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQVGSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 95 NTVEAIELAQHAEKAGADAVLVVTPYYNKPNQRGLYEHFSRVARSISIPLVIYNIPGRSIIDMTPETMGALVRDcKNIVG 174
Cdd:PRK04147 84 NTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADNPMIVYNIPALTGVNLSLDQFNELFTL-PKVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 175 VKDATG---KIERVseQRAICGKefIQLSGED---ATALGFNAHGGVGCisvTSNI-APRLCAEFqEACQAGNFAKALEL 247
Cdd:PRK04147 163 VKQTAGdlyQLERI--RKAFPDK--LIYNGFDemfASGLLAGADGAIGS---TYNVnGWRARQIF-EAAKAGDIQEAQEL 234
|
.
gi 225617983 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 225617983 19 SITALVTPFdREGAFDEKAFRAFVNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAgrvPVIAGAGSNNTVE 98
Cdd:cd00953 4 KITPVITPF-TGNKIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 99 AIELAQHAEKAGADAVLVVTPYY-NKPNQRGLYEHFSRVARsiSIPLVIYNIPGRSIIDMTPETMGALVRDCKNIVGVKD 177
Cdd:cd00953 80 SIELARAAKSFGIYAIASLPPYYfPGIPEEWLIKYFTDISS--PYPTFIYNYPKATGYDINARMAKEIKKAGGDIIGVKD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225617983 178 ATGKIERVSEQRAIcGKEFIQLSGEDATALGFNAHGGVGCISVTSNIAPRLCAEFQEACQAgnfAKALELQ 248
Cdd:cd00953 158 TNEDISHMLEYKRL-VPDFKVYSGPDSLIFSALRSGLDGSVAAASNYLPEVFVKIKDHVAI---EDAFKLQ 224
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
42-263 |
3.46e-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: 82.88 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 42 VNWQIEEGTKGLVPVGTTGETPTLSHDEHKRVIEVCIEVAAGRVPVIAGAGSNNTVEAIELAQHAEKAGADAVLVVTPYY 121
Cdd:cd00952 35 VERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPVFVGATTLNTRDTIARTRALLDLGADGTMLGRPMW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 122 NKPNQRGLYEHFSRVARSI-SIPLVIYNIPGRSIIDMtPETMGALVRDCKNIVGVKdATGKIERV-SEQRAICGK-EFIQ 198
Cdd:cd00952 115 LPLDVDTAVQFYRDVAEAVpEMAIAIYANPEAFKFDF-PRAAWAELAQIPQVVAAK-YLGDIGALlSDLAAVKGRmRLLP 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225617983 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 |
5.51e-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: 43.47 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225617983 70 HKRVIEVCIEVAAG-RVPVIAGAGSNN----TVEAIELAQHAEKAGADAVLVVTPYYNKP--NQRGLYEHFSRVARSIS- 141
Cdd:cd00945 33 NPGYVRLAADALAGsDVPVIVVVGFPTglttTEVKVAEVEEAIDLGADEIDVVINIGSLKegDWEEVLEEIAAVVEAADg 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 225617983 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 225617983 27 FDREGAFDEKAFRAFVNWQIEEGTKGLV---PVGTTGETPTlsHDEHKRVIEVCIEVAAGRVPVIA 89
Cdd:PRK08637 124 FDEDGGFDTDALKEALQAAYNKGKVIVIlnfPNNPTGYTPT--EKEATAIVEAIKELADAGTKVVA 187
|
|
| |
