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Conserved domains on  [gi|1851000570|dbj|GFF02923|]
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phospho-2-dehydro-3-deoxyheptonate aldolase [Bartonella henselae]

Protein Classification

3-deoxy-7-phosphoheptulonate synthase class II( domain architecture ID 10007047)

3-deoxy-7-phosphoheptulonate (DAHP) synthase catalyzes the conversion of phosphoenolpyruvate and D-erythrose 4-phosphate to DAHP and phosphate

CATH:  3.20.20.70
EC:  2.5.1.54
Gene Ontology:  GO:0009073|GO:0003849
SCOP:  4002361

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
AroG2 COG3200
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport ...
1-446 0e+00

3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 442433  Cd Length: 447  Bit Score: 956.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   1 MIKKWTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADN 80
Cdd:COG3200     1 MASRWTPDSWRSKPAKQQPTYPDAAALAAVEAELASLPPLVFAGEARRLKAQLAAVARGEAFLLQGGDCAESFAEFTADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  81 IRDFFRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQ 160
Cdd:COG3200    81 IRDKFKVLLQMAVVLTYGASKPVVKVGRIAGQFAKPRSSDTETRDGVTLPSYRGDIVNGFEFTPEARRPDPQRMLRAYHQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 161 SAATLNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSKTNSSLRETSFYTSHEALLL 240
Cdd:COG3200   161 SAATLNLLRAFTQGGFADLHQVHQWNLGFVRNSPAGERYEELADRIDEALRFMEACGIDSETTPQLREVDFYTSHEALLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 241 SYEEALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLI 320
Cdd:COG3200   241 DYEEALTRIDSRTGDWYDTSAHMLWIGERTRQLDGAHVEFLRGIRNPIGVKVGPSTTPDDLLRLIDRLNPENEPGRLTLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 321 TRFGYDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGR 399
Cdd:COG3200   321 TRMGADKVRDHLPPLVRAVKAEGRKVVWSCDPMHGNTIKSsSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGD 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1851000570 400 DVTECTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKK 446
Cdd:COG3200   401 DVTECLGGARAITEEDLADRYETACDPRLNAEQSLELAFLVAEMLRE 447
 
Name Accession Description Interval E-value
AroG2 COG3200
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport ...
1-446 0e+00

3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 442433  Cd Length: 447  Bit Score: 956.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   1 MIKKWTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADN 80
Cdd:COG3200     1 MASRWTPDSWRSKPAKQQPTYPDAAALAAVEAELASLPPLVFAGEARRLKAQLAAVARGEAFLLQGGDCAESFAEFTADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  81 IRDFFRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQ 160
Cdd:COG3200    81 IRDKFKVLLQMAVVLTYGASKPVVKVGRIAGQFAKPRSSDTETRDGVTLPSYRGDIVNGFEFTPEARRPDPQRMLRAYHQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 161 SAATLNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSKTNSSLRETSFYTSHEALLL 240
Cdd:COG3200   161 SAATLNLLRAFTQGGFADLHQVHQWNLGFVRNSPAGERYEELADRIDEALRFMEACGIDSETTPQLREVDFYTSHEALLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 241 SYEEALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLI 320
Cdd:COG3200   241 DYEEALTRIDSRTGDWYDTSAHMLWIGERTRQLDGAHVEFLRGIRNPIGVKVGPSTTPDDLLRLIDRLNPENEPGRLTLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 321 TRFGYDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGR 399
Cdd:COG3200   321 TRMGADKVRDHLPPLVRAVKAEGRKVVWSCDPMHGNTIKSsSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGD 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1851000570 400 DVTECTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKK 446
Cdd:COG3200   401 DVTECLGGARAITEEDLADRYETACDPRLNAEQSLELAFLVAEMLRE 447
DAHP_synth_2 pfam01474
Class-II DAHP synthetase family; Members of this family are aldolase enzymes that catalyze the ...
5-441 0e+00

Class-II DAHP synthetase family; Members of this family are aldolase enzymes that catalyze the first step of the shikimate pathway.


Pssm-ID: 426279  Cd Length: 437  Bit Score: 897.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   5 WTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIRDF 84
Cdd:pfam01474   1 WSPSSWRSKPAKQQPTYPDPAALEAVLAELASLPPLVFAGEIRRLKAQLADVARGEAFLLQGGDCAESFDECTADNIRDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  85 FRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSAAT 164
Cdd:pfam01474  81 LKVLLQMAVVLTYGASKPVVKVGRIAGQYAKPRSSPTETVDGVTLPSYRGDIVNGFEFTEEARRPDPERLLRAYFHSAAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 165 LNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSkTNSSLRETSFYTSHEALLLSYEE 244
Cdd:pfam01474 161 LNLLRAFASGGFADLHRVHDWNLDFVRDSPLGERYEELADRIDDALRFMRACGVDS-EDPALRTVDFYTSHEALLLDYEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 245 ALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITRFG 324
Cdd:pfam01474 240 ALTRVDSTTGDWYDTSAHFLWIGDRTRQLDGAHVEFFRGIRNPIGVKVGPTTTPDELLRLLDILNPDNEPGRLTLITRMG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 325 YDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDVTE 403
Cdd:pfam01474 320 ADKVRDLLPPLIEAVKASGHKVVWSCDPMHGNTITTsSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGDDVTE 399
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1851000570 404 CTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVA 441
Cdd:pfam01474 400 CLGGSRGLTEEDLSLRYETFCDPRLNAEQSLELAFLIA 437
PLN02291 PLN02291
phospho-2-dehydro-3-deoxyheptonate aldolase
3-449 0e+00

phospho-2-dehydro-3-deoxyheptonate aldolase


Pssm-ID: 177928  Cd Length: 474  Bit Score: 733.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   3 KKWTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIR 82
Cdd:PLN02291   18 KKWSPDSWRSKKALQLPEYPDQAELEEVLKTLEAFPPLVFAGEARSLEERLAEAAMGRAFLLQGGDCAESFKEFNANNIR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  83 DFFRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSA 162
Cdd:PLN02291   98 DTFRVLLQMGVVLMFGGQMPVVKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNINGDAFDEKSRRPDPQRMVRAYSQSA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 163 ATLNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSkTNSSLRETSFYTSHEALLLSY 242
Cdd:PLN02291  178 ATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELAHRVDEALGFMAACGLTT-DHPIMTTTEFWTSHECLLLPY 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 243 EEALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITR 322
Cdd:PLN02291  257 EQALTREDSTSGLYYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSDKMDPEELVKLIEILNPQNKPGRLTIIVR 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 323 FGYDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDV 401
Cdd:PLN02291  337 MGAEKLRVKLPHLIRAVRRAGQIVTWVSDPMHGNTIKApSGLKTRPFDAIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNV 416
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1851000570 402 TECTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKKNRD 449
Cdd:PLN02291  417 TECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRI 464
DAHP_synth_II TIGR01358
3-deoxy-7-phosphoheptulonate synthase, class II; This model represents the class II family of ...
5-448 0e+00

3-deoxy-7-phosphoheptulonate synthase, class II; This model represents the class II family of 3-deoxy-7-phosphoheptulonate synthase, aka phospho-2-dehydro-3-deoxyheptonate aldolase, as found in plants and some bacteria. It shows some similarity to the class I family found in many bacteria. The enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids. Homologs scoring between trusted and noise cutoff include proteins involved in antibiotic biosynthesis; one example is active as this enzyme, while another acts on an amino analog. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130425  Cd Length: 443  Bit Score: 722.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   5 WTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIRDF 84
Cdd:TIGR01358   1 WSPQSWRSKPAAQQPTYPDAGALEAVLDTLRSLPPLVFAGEIRRLKRQLAQVAEGEAFLLQGGDCAESFKDCTADHIRNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  85 FRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSAAT 164
Cdd:TIGR01358  81 LRVLLQMAVVLTYGASLPVVKVGRIAGQYAKPRSAPTETRDGVTLPSYRGDIINGPAFTEAARVPDPRRLVRAYHQSAAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 165 LNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSKTNssLRETSFYTSHEALLLSYEE 244
Cdd:TIGR01358 161 LNLVRALTTGGYADLHQVHYWNLEFVGYSPAGARYEKLASEIDEALRFMSACGLAPRYN--LQTVEFYTSHEALLLPYEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 245 ALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITRFG 324
Cdd:TIGR01358 239 ALTRVDSRSGGWFDLSAHMLWIGERTRQLDGAHVEFLRGVRNPIGIKVGPSMTPDELLRLIERLNPENEPGRLTLISRMG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 325 YDKVENYLPKLIRAVEREKRKVIWSCDPMHGNT-VTVNGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDVTE 403
Cdd:TIGR01358 319 ADKIADKLPPLLRAVKAAGRRVVWVCDPMHGNTeEAASGYKTRRFDDIRSEVKGFFEVHRAEGTHPGGVHLELTGEDVTE 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1851000570 404 CTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKKNR 448
Cdd:TIGR01358 399 CLGGAREITETDLASRYETACDPRLNAEQSLELAFLVAEKLRDVR 443
 
Name Accession Description Interval E-value
AroG2 COG3200
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport ...
1-446 0e+00

3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, class II is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 442433  Cd Length: 447  Bit Score: 956.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   1 MIKKWTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADN 80
Cdd:COG3200     1 MASRWTPDSWRSKPAKQQPTYPDAAALAAVEAELASLPPLVFAGEARRLKAQLAAVARGEAFLLQGGDCAESFAEFTADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  81 IRDFFRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQ 160
Cdd:COG3200    81 IRDKFKVLLQMAVVLTYGASKPVVKVGRIAGQFAKPRSSDTETRDGVTLPSYRGDIVNGFEFTPEARRPDPQRMLRAYHQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 161 SAATLNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSKTNSSLRETSFYTSHEALLL 240
Cdd:COG3200   161 SAATLNLLRAFTQGGFADLHQVHQWNLGFVRNSPAGERYEELADRIDEALRFMEACGIDSETTPQLREVDFYTSHEALLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 241 SYEEALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLI 320
Cdd:COG3200   241 DYEEALTRIDSRTGDWYDTSAHMLWIGERTRQLDGAHVEFLRGIRNPIGVKVGPSTTPDDLLRLIDRLNPENEPGRLTLI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 321 TRFGYDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGR 399
Cdd:COG3200   321 TRMGADKVRDHLPPLVRAVKAEGRKVVWSCDPMHGNTIKSsSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGD 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1851000570 400 DVTECTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKK 446
Cdd:COG3200   401 DVTECLGGARAITEEDLADRYETACDPRLNAEQSLELAFLVAEMLRE 447
DAHP_synth_2 pfam01474
Class-II DAHP synthetase family; Members of this family are aldolase enzymes that catalyze the ...
5-441 0e+00

Class-II DAHP synthetase family; Members of this family are aldolase enzymes that catalyze the first step of the shikimate pathway.


Pssm-ID: 426279  Cd Length: 437  Bit Score: 897.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   5 WTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIRDF 84
Cdd:pfam01474   1 WSPSSWRSKPAKQQPTYPDPAALEAVLAELASLPPLVFAGEIRRLKAQLADVARGEAFLLQGGDCAESFDECTADNIRDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  85 FRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSAAT 164
Cdd:pfam01474  81 LKVLLQMAVVLTYGASKPVVKVGRIAGQYAKPRSSPTETVDGVTLPSYRGDIVNGFEFTEEARRPDPERLLRAYFHSAAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 165 LNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSkTNSSLRETSFYTSHEALLLSYEE 244
Cdd:pfam01474 161 LNLLRAFASGGFADLHRVHDWNLDFVRDSPLGERYEELADRIDDALRFMRACGVDS-EDPALRTVDFYTSHEALLLDYEE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 245 ALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITRFG 324
Cdd:pfam01474 240 ALTRVDSTTGDWYDTSAHFLWIGDRTRQLDGAHVEFFRGIRNPIGVKVGPTTTPDELLRLLDILNPDNEPGRLTLITRMG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 325 YDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDVTE 403
Cdd:pfam01474 320 ADKVRDLLPPLIEAVKASGHKVVWSCDPMHGNTITTsSGYKTRRFDDILDEVRGFFEVHRAEGTHPGGVHLELTGDDVTE 399
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1851000570 404 CTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVA 441
Cdd:pfam01474 400 CLGGSRGLTEEDLSLRYETFCDPRLNAEQSLELAFLIA 437
PLN02291 PLN02291
phospho-2-dehydro-3-deoxyheptonate aldolase
3-449 0e+00

phospho-2-dehydro-3-deoxyheptonate aldolase


Pssm-ID: 177928  Cd Length: 474  Bit Score: 733.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   3 KKWTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIR 82
Cdd:PLN02291   18 KKWSPDSWRSKKALQLPEYPDQAELEEVLKTLEAFPPLVFAGEARSLEERLAEAAMGRAFLLQGGDCAESFKEFNANNIR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  83 DFFRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSA 162
Cdd:PLN02291   98 DTFRVLLQMGVVLMFGGQMPVVKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNINGDAFDEKSRRPDPQRMVRAYSQSA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 163 ATLNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSkTNSSLRETSFYTSHEALLLSY 242
Cdd:PLN02291  178 ATLNLLRAFATGGYAAMQRVTQWNLDFTEHSEQGDRYRELAHRVDEALGFMAACGLTT-DHPIMTTTEFWTSHECLLLPY 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 243 EEALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITR 322
Cdd:PLN02291  257 EQALTREDSTSGLYYDCSAHMLWVGERTRQLDGAHVEFLRGVANPLGIKVSDKMDPEELVKLIEILNPQNKPGRLTIIVR 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 323 FGYDKVENYLPKLIRAVEREKRKVIWSCDPMHGNTVTV-NGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDV 401
Cdd:PLN02291  337 MGAEKLRVKLPHLIRAVRRAGQIVTWVSDPMHGNTIKApSGLKTRPFDAIRAEVRAFFDVHEQEGSHPGGVHLEMTGQNV 416
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1851000570 402 TECTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKKNRD 449
Cdd:PLN02291  417 TECIGGSRTVTFDDLSSRYHTHCDPRLNASQSLELAFIIAERLRKRRI 464
DAHP_synth_II TIGR01358
3-deoxy-7-phosphoheptulonate synthase, class II; This model represents the class II family of ...
5-448 0e+00

3-deoxy-7-phosphoheptulonate synthase, class II; This model represents the class II family of 3-deoxy-7-phosphoheptulonate synthase, aka phospho-2-dehydro-3-deoxyheptonate aldolase, as found in plants and some bacteria. It shows some similarity to the class I family found in many bacteria. The enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids. Homologs scoring between trusted and noise cutoff include proteins involved in antibiotic biosynthesis; one example is active as this enzyme, while another acts on an amino analog. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130425  Cd Length: 443  Bit Score: 722.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570   5 WTPDSWRARPVKQVPTYPDKSVLADVERKLRSYPPLVFAGEARDLKNELATVARGQAFLLQGGDCAESFAEHEADNIRDF 84
Cdd:TIGR01358   1 WSPQSWRSKPAAQQPTYPDAGALEAVLDTLRSLPPLVFAGEIRRLKRQLAQVAEGEAFLLQGGDCAESFKDCTADHIRNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570  85 FRVFLQMAIVLTFGSSKPVVKIGRIAGQFAKPRSSEMESKEGVELPSYRGDIINDIEFDMNSRIPDPQRMSMAYRQSAAT 164
Cdd:TIGR01358  81 LRVLLQMAVVLTYGASLPVVKVGRIAGQYAKPRSAPTETRDGVTLPSYRGDIINGPAFTEAARVPDPRRLVRAYHQSAAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 165 LNLLRAFSQGGYANLENVHAWMLSFVFNSPQGERYEMLAERISEAIDFMRSIGISSKTNssLRETSFYTSHEALLLSYEE 244
Cdd:TIGR01358 161 LNLVRALTTGGYADLHQVHYWNLEFVGYSPAGARYEKLASEIDEALRFMSACGLAPRYN--LQTVEFYTSHEALLLPYEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 245 ALTRIDSTSGDWYATSGHMLWIGDRTRQIDHAHVEYCRGIKNPLGLKCGPSIESDELLRLIDILNPENEPGRLTLITRFG 324
Cdd:TIGR01358 239 ALTRVDSRSGGWFDLSAHMLWIGERTRQLDGAHVEFLRGVRNPIGIKVGPSMTPDELLRLIERLNPENEPGRLTLISRMG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851000570 325 YDKVENYLPKLIRAVEREKRKVIWSCDPMHGNT-VTVNGYKTRPFDYVLKEVESFFSVHYGEGTYPGGIHIEMTGRDVTE 403
Cdd:TIGR01358 319 ADKIADKLPPLLRAVKAAGRRVVWVCDPMHGNTeEAASGYKTRRFDDIRSEVKGFFEVHRAEGTHPGGVHLELTGEDVTE 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1851000570 404 CTGGARAISVEDLSDRYHTQCDPRLNADQALELAFLVAELLKKNR 448
Cdd:TIGR01358 399 CLGGAREITETDLASRYETACDPRLNAEQSLELAFLVAEKLRDVR 443
 
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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