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Conserved domains on  [gi|1288431239|ref|WP_100539908|]
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MULTISPECIES: dihydrodipicolinate synthase family protein [Paenibacillus]

Protein Classification

dihydrodipicolinate synthase family protein( domain architecture ID 10001092)

dihydrodipicolinate synthase family protein belongs to the pyruvate-dependent class I aldolases, similar to 4-hydroxy-tetrahydrodipicolinate synthase which catalyzes 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 residu

CATH:  3.20.20.70
EC:  4.-.-.-
Gene Ontology:  GO:0071704|GO:0016829
PubMed:  9047371

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
24-341 9.55e-44

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: 152.61  E-value: 9.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVGVHSTQF-----EIRDKgidlyepVLRLAAEEVRKAeldrpFM 98
Cdd:COG0329     5 VIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESatltdEERKR-------VLEAVVEAAAGR-----VP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  99 LVAGVCGE-TDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKR--MPVIgFYLQPSVGGKIFSFDFWRSF 175
Cdd:COG0329    73 VIAGVGSNsTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAvdLPII-LYNIPGRTGVDLSPETLARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDDNIVNDLLTTYqfqvdgtlvakpiVGGLLGHWAVWTKK 255
Cdd:COG0329   152 AEIPNIVGIKEASGDLDRIAELIRAT-----GDDFAVLSGDDALALPALALGA-------------DGVISVTANVAPEL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 256 AVELLEEIKEARTQDrfAKEWltrNVEITDANAAFFDPAHqfagcIPGIHEVLRRQGLLQGTwCLNPHETLSPGQSEEID 335
Cdd:COG0329   214 MVALYEAALAGDLAE--ARAL---QDRLLPLIRALFAEGN-----PAPVKAALALLGLPSGP-VRLPLLPLSEEERAELR 282

                  ....*.
gi 1288431239 336 RVYRDY 341
Cdd:COG0329   283 AALKEL 288
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
24-341 9.55e-44

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: 152.61  E-value: 9.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVGVHSTQF-----EIRDKgidlyepVLRLAAEEVRKAeldrpFM 98
Cdd:COG0329     5 VIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESatltdEERKR-------VLEAVVEAAAGR-----VP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  99 LVAGVCGE-TDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKR--MPVIgFYLQPSVGGKIFSFDFWRSF 175
Cdd:COG0329    73 VIAGVGSNsTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAvdLPII-LYNIPGRTGVDLSPETLARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDDNIVNDLLTTYqfqvdgtlvakpiVGGLLGHWAVWTKK 255
Cdd:COG0329   152 AEIPNIVGIKEASGDLDRIAELIRAT-----GDDFAVLSGDDALALPALALGA-------------DGVISVTANVAPEL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 256 AVELLEEIKEARTQDrfAKEWltrNVEITDANAAFFDPAHqfagcIPGIHEVLRRQGLLQGTwCLNPHETLSPGQSEEID 335
Cdd:COG0329   214 MVALYEAALAGDLAE--ARAL---QDRLLPLIRALFAEGN-----PAPVKAALALLGLPSGP-VRLPLLPLSEEERAELR 282

                  ....*.
gi 1288431239 336 RVYRDY 341
Cdd:COG0329   283 AALKEL 288
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
24-338 4.34e-22

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: 94.54  E-value: 4.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVG-----VHSTQFEIRDKgidlyepVLRLAAEEVRKaeldrPFM 98
Cdd:cd00408     1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLgttgeAPTLTDEERKE-------VIEAVVEAVAG-----RVP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  99 LVAGV-CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKR--MPVIgFYLQPSVGGKIFSFDFWRSF 175
Cdd:cd00408    69 VIAGVgANSTREAIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADAsdLPVI-LYNIPGRTGVDLSPETIARL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDDNIVNDLLttyqfqvdgtLVAKPIVGGlLGHwaVWTKK 255
Cdd:cd00408   148 AEHPNIVGIKDSSGDLDRLTRLIALL-----GPDFAVLSGDDDLLLPALA----------LGADGAISG-AAN--VAPKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 256 AVELLEEIKEARTQDrfAKEWltrNVEITDANAAFFDpahqfAGCIPGIHEVLRRQGLLQGTwCLNPHETLSPGQSEEID 335
Cdd:cd00408   210 AVALYEAARAGDLEE--ARAL---QDRLLPLIEALFK-----EGNPAPVKAALALLGLDAGP-VRLPLVPLSEEERAKLE 278

                  ...
gi 1288431239 336 RVY 338
Cdd:cd00408   279 ALL 281
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
24-218 5.37e-09

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 56.61  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVGvhSTQFEIRDKGIDLYEPVLRLAAEEVrkaelDRPFMLVAGV 103
Cdd:pfam00701   5 IITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVG--GTTGESFTLSTEEREQLVEITVNEA-----KGRIPVIAGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 104 -CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAK--RMPVIgFYLQPSVGGKIFSFDFWRSFAEIPN 180
Cdd:pfam00701  78 gSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEatDLPMI-LYNVPSRTGVDLTPETVGRLATNPN 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1288431239 181 IVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDD 218
Cdd:pfam00701 157 IVGIKEASGDLDRMINIKKEA-----GPDFVILSGDDE 189
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
24-193 3.08e-05

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 44.98  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRY-YAASGAGGVAVGVHSTQFEIRDKgiDLYEPVLRLAAEEVRKAeldrpFMLVAG 102
Cdd:PRK04147    7 VYAALLTPFDEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLST--EEKKQVLEIVAEEAKGK-----VKLIAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 103 V-CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKRM--PVIGFYLqPSVGGKIFSFDFWRSFAEIP 179
Cdd:PRK04147   80 VgSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSAdnPMIVYNI-PALTGVNLSLDQFNELFTLP 158
                         170
                  ....*....|....
gi 1288431239 180 NIVAIKMAPFNRYQ 193
Cdd:PRK04147  159 KVIGVKQTAGDLYQ 172
 
Name Accession Description Interval E-value
DapA COG0329
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ...
24-341 9.55e-44

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: 152.61  E-value: 9.55e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVGVHSTQF-----EIRDKgidlyepVLRLAAEEVRKAeldrpFM 98
Cdd:COG0329     5 VIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESatltdEERKR-------VLEAVVEAAAGR-----VP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  99 LVAGVCGE-TDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKR--MPVIgFYLQPSVGGKIFSFDFWRSF 175
Cdd:COG0329    73 VIAGVGSNsTAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAvdLPII-LYNIPGRTGVDLSPETLARL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDDNIVNDLLTTYqfqvdgtlvakpiVGGLLGHWAVWTKK 255
Cdd:COG0329   152 AEIPNIVGIKEASGDLDRIAELIRAT-----GDDFAVLSGDDALALPALALGA-------------DGVISVTANVAPEL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 256 AVELLEEIKEARTQDrfAKEWltrNVEITDANAAFFDPAHqfagcIPGIHEVLRRQGLLQGTwCLNPHETLSPGQSEEID 335
Cdd:COG0329   214 MVALYEAALAGDLAE--ARAL---QDRLLPLIRALFAEGN-----PAPVKAALALLGLPSGP-VRLPLLPLSEEERAELR 282

                  ....*.
gi 1288431239 336 RVYRDY 341
Cdd:COG0329   283 AALKEL 288
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
24-338 4.34e-22

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: 94.54  E-value: 4.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVG-----VHSTQFEIRDKgidlyepVLRLAAEEVRKaeldrPFM 98
Cdd:cd00408     1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLgttgeAPTLTDEERKE-------VIEAVVEAVAG-----RVP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  99 LVAGV-CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKR--MPVIgFYLQPSVGGKIFSFDFWRSF 175
Cdd:cd00408    69 VIAGVgANSTREAIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADAsdLPVI-LYNIPGRTGVDLSPETIARL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDDNIVNDLLttyqfqvdgtLVAKPIVGGlLGHwaVWTKK 255
Cdd:cd00408   148 AEHPNIVGIKDSSGDLDRLTRLIALL-----GPDFAVLSGDDDLLLPALA----------LGADGAISG-AAN--VAPKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 256 AVELLEEIKEARTQDrfAKEWltrNVEITDANAAFFDpahqfAGCIPGIHEVLRRQGLLQGTwCLNPHETLSPGQSEEID 335
Cdd:cd00408   210 AVALYEAARAGDLEE--ARAL---QDRLLPLIEALFK-----EGNPAPVKAALALLGLDAGP-VRLPLVPLSEEERAKLE 278

                  ...
gi 1288431239 336 RVY 338
Cdd:cd00408   279 ALL 281
DHDPS pfam00701
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
24-218 5.37e-09

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


Pssm-ID: 395570 [Multi-domain]  Cd Length: 289  Bit Score: 56.61  E-value: 5.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRYYAASGAGGVAVGvhSTQFEIRDKGIDLYEPVLRLAAEEVrkaelDRPFMLVAGV 103
Cdd:pfam00701   5 IITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVG--GTTGESFTLSTEEREQLVEITVNEA-----KGRIPVIAGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 104 -CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAK--RMPVIgFYLQPSVGGKIFSFDFWRSFAEIPN 180
Cdd:pfam00701  78 gSNSTSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIAEatDLPMI-LYNVPSRTGVDLTPETVGRLATNPN 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1288431239 181 IVAIKMAPFNRYQTIDVVRAVcyssrRDDIALYTGNDD 218
Cdd:pfam00701 157 IVGIKEASGDLDRMINIKKEA-----GPDFVILSGDDE 189
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
33-221 4.55e-07

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: 50.57  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  33 DENRKLDERRQRALTRYYAASGAGG-VAVG----VHSTQFEIRDKgidlyepVLRLAAEEVRKAeldrpFMLVAGVCG-E 106
Cdd:cd00950    13 KDDGSVDFDALERLIEFQIENGTDGlVVCGttgeSPTLSDEEHEA-------VIEAVVEAVNGR-----VPVIAGTGSnN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 107 TDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAK--RMPVIgFY---------LQPSVGGKIfsfdfwrsf 175
Cdd:cd00950    81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEatDLPVI-LYnvpgrtgvnIEPETVLRL--------- 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1288431239 176 AEIPNIVAIKMAPFNRYQTIDVVRAvcyssRRDDIALYTGNDDNIV 221
Cdd:cd00950   151 AEHPNIVGIKEATGDLDRVSELIAL-----CPDDFAVLSGDDALTL 191
PRK04147 PRK04147
N-acetylneuraminate lyase; Provisional
24-193 3.08e-05

N-acetylneuraminate lyase; Provisional


Pssm-ID: 179749 [Multi-domain]  Cd Length: 293  Bit Score: 44.98  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  24 VIPAHPLALDENRKLDERRQRALTRY-YAASGAGGVAVGVHSTQFEIRDKgiDLYEPVLRLAAEEVRKAeldrpFMLVAG 102
Cdd:PRK04147    7 VYAALLTPFDEDGQIDEQGLRRLVRFnIEKQGIDGLYVGGSTGEAFLLST--EEKKQVLEIVAEEAKGK-----VKLIAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 103 V-CGETDQAVEETEIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKRM--PVIGFYLqPSVGGKIFSFDFWRSFAEIP 179
Cdd:PRK04147   80 VgSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSAdnPMIVYNI-PALTGVNLSLDQFNELFTLP 158
                         170
                  ....*....|....
gi 1288431239 180 NIVAIKMAPFNRYQ 193
Cdd:PRK04147  159 KVIGVKQTAGDLYQ 172
PLN02417 PLN02417
dihydrodipicolinate synthase
37-218 6.04e-04

dihydrodipicolinate synthase


Pssm-ID: 178038  Cd Length: 280  Bit Score: 41.17  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239  37 KLDERRQRALTRYYAASGAGGVAVGvhSTQFEIRDKGIDLYEPVLRLAAEEVRKAeldrpfMLVAGVCG--ETDQAVEET 114
Cdd:PLN02417   18 RFDLEAYDSLVNMQIENGAEGLIVG--GTTGEGQLMSWDEHIMLIGHTVNCFGGK------IKVIGNTGsnSTREAIHAT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288431239 115 EIARKLGYDAVLLSMGGLSGWSEEDILERTEEIAKRMPVIgFYLQPSVGGKIFSFDFWRSFAEIPNIVAIKMAPFNRyqt 194
Cdd:PLN02417   90 EQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMGPTI-IYNVPGRTGQDIPPEVIFKIAQHPNFAGVKECTGND--- 165
                         170       180
                  ....*....|....*....|....
gi 1288431239 195 idvvRAVCYSSrrDDIALYTGNDD 218
Cdd:PLN02417  166 ----RVKQYTE--KGILLWSGNDD 183
 
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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