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Conserved domains on  [gi|16129178|ref|NP_415733|]
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3-deoxy-D-manno-octulosonate 8-phosphate synthase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

3-deoxy-8-phosphooctulonate synthase( domain architecture ID 10012268)

3-deoxy-8-phosphooctulonate synthase catalyzes the condensation reaction between arabinose 5-phosphate and phosphoenolpyruvate to synthesize 3-deoxy-D-manno-octulosonate-8-phosphate (KDO8P), the precursor of the 8-carbon sugar KDO, which is an essential component of gram-negative bacterial lipopolysaccharides

Gene Ontology:  GO:0019294|GO:0008676
SCOP:  4003245

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05198 PRK05198
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
 9-274 0e+00

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


:

Pssm-ID: 235363  Cd Length: 264  Bit Score: 531.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    9 GDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTF 88
Cdd:PRK05198   1 GDIEVGNDLPFFLIAGPCVIESRDLALRIAEHLKEITDKLGIPYVFKASFDKANRSSIHSFRGPGLEEGLKILQEVKETF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   89 GVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDR 168
Cdd:PRK05198  81 GVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNIKKGQFLAPWDMKNVVDKVREAGNDKIILCER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  169 GANFGYDNLVVDMLGFSIMKKVsgNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAK 248
Cdd:PRK05198 161 GTSFGYNNLVVDMRGLPIMRET--GAPVIFDATHSVQLPGGQGGSSGGQREFVPVLARAAVAVGVAGLFIETHPDPDNAL 238

                        250       260
                 ....*....|....*....|....*.
gi 16129178  249 CDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:PRK05198 239 SDGPNMLPLDKLEPLLEQLKAIDDLV 264
 
Name Accession Description Interval E-value
PRK05198 PRK05198
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
 9-274 0e+00

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 235363  Cd Length: 264  Bit Score: 531.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    9 GDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTF 88
Cdd:PRK05198   1 GDIEVGNDLPFFLIAGPCVIESRDLALRIAEHLKEITDKLGIPYVFKASFDKANRSSIHSFRGPGLEEGLKILQEVKETF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   89 GVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDR 168
Cdd:PRK05198  81 GVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNIKKGQFLAPWDMKNVVDKVREAGNDKIILCER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  169 GANFGYDNLVVDMLGFSIMKKVsgNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAK 248
Cdd:PRK05198 161 GTSFGYNNLVVDMRGLPIMRET--GAPVIFDATHSVQLPGGQGGSSGGQREFVPVLARAAVAVGVAGLFIETHPDPDNAL 238

                        250       260
                 ....*....|....*....|....*.
gi 16129178  249 CDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:PRK05198 239 SDGPNMLPLDKLEPLLEQLKAIDDLV 264
KdsA COG2877
3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope ...
 8-274 0e+00

3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 442124  Cd Length: 265  Bit Score: 518.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   8 IGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQT 87
Cdd:COG2877   1 IGGIEVGNDKPLFLIAGPCVIESEDLALEIAEKLKEITDKLGIPYIFKASFDKANRSSIDSFRGPGLEEGLKILAEVKEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  88 FGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCD 167
Cdd:COG2877  81 FGVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNVKKGQFLAPWDMKNVVEKVREAGNDNILLTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178 168 RGANFGYDNLVVDMLGFSIMKKvsGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHA 247
Cdd:COG2877 161 RGTSFGYNNLVVDMRSLPIMRE--TGYPVVFDATHSVQLPGGQGGSSGGQREFVPVLARAAVAVGVDGLFMETHPDPDKA 238

                       250       260
                ....*....|....*....|....*..
gi 16129178 248 KCDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:COG2877 239 LSDGPNMLPLDKLEELLEQLKAIDELV 265
KDO8P_synth TIGR01362
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate ...
 18-276 4.71e-162

3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate synthase. Alternate names include 2-dehydro-3-deoxyphosphooctonate aldolase, 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130429  Cd Length: 258  Bit Score: 450.27  E-value: 4.71e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    18 PFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVH 97
Cdd:TIGR01362   2 KFFLIAGPCVIESEDHALRVAEKLKELTSKLGVPFIFKSSFDKANRSSIHSFRGPGLEEGLKILQKVKEEFGVPILTDVH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    98 EPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNL 177
Cdd:TIGR01362  82 ESSQCEPVAEVVDIIQIPAFLCRQTDLLVAAAKTGRIVNVKKGQFLSPWDMKNVVEKVLSTGNKNILLCERGTSFGYNNL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   178 VVDMLGFSIMKKVsgNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPL 257
Cdd:TIGR01362 162 VVDMRSLPIMREL--GCPVIFDATHSVQQPGGLGGASGGLREFVPTLARAAVAVGIDGLFMETHPDPKNAKSDGPNMLPL 239

                         250
                  ....*....|....*....
gi 16129178   258 AKLEPFLKQMKAIDDLVKG 276
Cdd:TIGR01362 240 SELEGLLEKLLAIDALTKS 258
DAHP_synth_1 pfam00793
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
 9-275 1.33e-86

DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.


Pssm-ID: 395641  Cd Length: 271  Bit Score: 259.56  E-value: 1.33e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178     9 GDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSsIHSYRGPGLEEGMKIFQELKQTF 88
Cdd:pfam00793   8 QDIIIGKDDRLLVIAGPCSIEDPEAAMEYARRLKKLGAKLKLIIIMRAYFEKPRTS-PVGFKGLGNDPDLNILFRIKDGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    89 GVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDK-FKEGGNEKVILCD 167
Cdd:pfam00793  87 GLPIATEVLDPIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYhLFLGVTKGNILCE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   168 RGANFGY--DNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDpfgaasGGRRAQVAELARAGMAVGLAGLFIEAHPDPE 245
Cdd:pfam00793 167 RGIRGGEgpNRNTLDVSAVAILKEETGHLPVMVDVSHANGRKD------GGRQPLVLPLAKAAIAVGIDGLMIEVHPNPG 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 16129178   246 HAKCDGPSALPLAKLEPFLKQMKAIDDLVK 275
Cdd:pfam00793 241 NALSDGPQQLKYGKSETDACILWELTELLL 270
BagF_FevY NF041229
phospho-2-dehydro-3-deoxyheptonate aldolase BagF/FevY;
63-268 5.35e-25

phospho-2-dehydro-3-deoxyheptonate aldolase BagF/FevY;


Pssm-ID: 469132 [Multi-domain]  Cd Length: 340  Bit Score: 102.04  E-value: 5.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGavinvkKPQF 142
Cdd:NF041229 129 RTSPYAFQGLG-EAGLKILADVRAETGLPIVTEVVDAHDVELVASYADMLQIGTRNAQNFALLQAVGDVG------KPVM 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  143 VSPGQMGNI------VDKFKEGGNEKVILCDRGANfGYDNLVVDMLGFSIMKKVSGNS--PVIFDVTHalqcrdpfgaaS 214
Cdd:NF041229 202 LKRGMSGTIeewlmaAEYVAQRGNLDIVLCERGIR-TFETATRNTLDIAAVPIVQRLShlPVIVDPSH-----------S 269

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129178  215 GGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMK 268
Cdd:NF041229 270 GGRRDLVLPLTRAALAVGADGVIVDVHPDPRTALCDGPQALVHEDLEELGAVMR 323
 
Name Accession Description Interval E-value
PRK05198 PRK05198
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
 9-274 0e+00

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 235363  Cd Length: 264  Bit Score: 531.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    9 GDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTF 88
Cdd:PRK05198   1 GDIEVGNDLPFFLIAGPCVIESRDLALRIAEHLKEITDKLGIPYVFKASFDKANRSSIHSFRGPGLEEGLKILQEVKETF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   89 GVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDR 168
Cdd:PRK05198  81 GVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNIKKGQFLAPWDMKNVVDKVREAGNDKIILCER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  169 GANFGYDNLVVDMLGFSIMKKVsgNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAK 248
Cdd:PRK05198 161 GTSFGYNNLVVDMRGLPIMRET--GAPVIFDATHSVQLPGGQGGSSGGQREFVPVLARAAVAVGVAGLFIETHPDPDNAL 238

                        250       260
                 ....*....|....*....|....*.
gi 16129178  249 CDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:PRK05198 239 SDGPNMLPLDKLEPLLEQLKAIDDLV 264
PRK12457 PRK12457
3-deoxy-8-phosphooctulonate synthase;
5-281 0e+00

3-deoxy-8-phosphooctulonate synthase;


Pssm-ID: 237105  Cd Length: 281  Bit Score: 525.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    5 VVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQEL 84
Cdd:PRK12457   3 VAISPGITVGNDLPFVLFGGINVLESLDFTLDVCGEYVEVTRKLGIPFVFKASFDKANRSSIHSYRGVGLDEGLRIFEEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   85 KQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVI 164
Cdd:PRK12457  83 KARFGVPVITDVHEVEQAAPVAEVADVLQVPAFLARQTDLVVAIAKTGKPVNIKKPQFMSPTQMKHVVSKCREAGNDRVI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  165 LCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDP 244
Cdd:PRK12457 163 LCERGSSFGYDNLVVDMLGFRQMKRTTGDLPVIFDVTHSLQCRDPLGAASGGRRRQVLDLARAGMAVGLAGLFLEAHPDP 242

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 16129178  245 EHAKCDGPSALPLAKLEPFLKQMKAIDDLVKGFEELD 281
Cdd:PRK12457 243 DRARCDGPSALPLDQLEPFLSQVKALDDLVKSFPPLD 279
KdsA COG2877
3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope ...
 8-274 0e+00

3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 442124  Cd Length: 265  Bit Score: 518.05  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   8 IGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQT 87
Cdd:COG2877   1 IGGIEVGNDKPLFLIAGPCVIESEDLALEIAEKLKEITDKLGIPYIFKASFDKANRSSIDSFRGPGLEEGLKILAEVKEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  88 FGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCD 167
Cdd:COG2877  81 FGVPVLTDVHEPEQAAPVAEVVDVLQIPAFLCRQTDLLVAAAKTGKVVNVKKGQFLAPWDMKNVVEKVREAGNDNILLTE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178 168 RGANFGYDNLVVDMLGFSIMKKvsGNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHA 247
Cdd:COG2877 161 RGTSFGYNNLVVDMRSLPIMRE--TGYPVVFDATHSVQLPGGQGGSSGGQREFVPVLARAAVAVGVDGLFMETHPDPDKA 238

                       250       260
                ....*....|....*....|....*..
gi 16129178 248 KCDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:COG2877 239 LSDGPNMLPLDKLEELLEQLKAIDELV 265
KDO8P_synth TIGR01362
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate ...
 18-276 4.71e-162

3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate synthase. Alternate names include 2-dehydro-3-deoxyphosphooctonate aldolase, 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130429  Cd Length: 258  Bit Score: 450.27  E-value: 4.71e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    18 PFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVH 97
Cdd:TIGR01362   2 KFFLIAGPCVIESEDHALRVAEKLKELTSKLGVPFIFKSSFDKANRSSIHSFRGPGLEEGLKILQKVKEEFGVPILTDVH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    98 EPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNL 177
Cdd:TIGR01362  82 ESSQCEPVAEVVDIIQIPAFLCRQTDLLVAAAKTGRIVNVKKGQFLSPWDMKNVVEKVLSTGNKNILLCERGTSFGYNNL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   178 VVDMLGFSIMKKVsgNSPVIFDVTHALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPL 257
Cdd:TIGR01362 162 VVDMRSLPIMREL--GCPVIFDATHSVQQPGGLGGASGGLREFVPTLARAAVAVGIDGLFMETHPDPKNAKSDGPNMLPL 239

                         250
                  ....*....|....*....
gi 16129178   258 AKLEPFLKQMKAIDDLVKG 276
Cdd:TIGR01362 240 SELEGLLEKLLAIDALTKS 258
PLN03033 PLN03033
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
 18-280 8.62e-97

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 178601  Cd Length: 290  Bit Score: 286.37  E-value: 8.62e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   18 PFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVH 97
Cdd:PLN03033  16 PFFLLAGPNVIESEEHILRMAKHIKDISTKLGLPLVFKSSFDKANRTSSKSFRGPGMAEGLKILEKVKVAYDLPIVTDVH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   98 EPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDKFKEGGNEKVILCDRGANFGYDNL 177
Cdd:PLN03033  96 ESSQCEAVGKVADIIQIPAFLCRQTDLLVAAAKTGKIINIKKGQFCAPSVMRNSAEKVRLAGNPNVMVCERGTMFGYNDL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  178 VVDMLGFSIMKKvsGNSPVIFDVTHALQ-----CRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGP 252
Cdd:PLN03033 176 IVDPRNLEWMRE--ANCPVVADITHSLQqpagkKLDGGGVASGGLRELIPCIARTAVAVGVDGIFMEVHDDPLSAPVDGP 253

                        250       260
                 ....*....|....*....|....*...
gi 16129178  253 SALPLAKLEPFLKQMKAIDDLVKGFEEL 280
Cdd:PLN03033 254 TQWPLRHLEELLEELIAIARVTKGKQRF 281
DAHP_synth_1 pfam00793
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
 9-275 1.33e-86

DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.


Pssm-ID: 395641  Cd Length: 271  Bit Score: 259.56  E-value: 1.33e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178     9 GDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGIPYVFKASFDKANRSsIHSYRGPGLEEGMKIFQELKQTF 88
Cdd:pfam00793   8 QDIIIGKDDRLLVIAGPCSIEDPEAAMEYARRLKKLGAKLKLIIIMRAYFEKPRTS-PVGFKGLGNDPDLNILFRIKDGL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178    89 GVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGNIVDK-FKEGGNEKVILCD 167
Cdd:pfam00793  87 GLPIATEVLDPIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYhLFLGVTKGNILCE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   168 RGANFGY--DNLVVDMLGFSIMKKVSGNSPVIFDVTHALQCRDpfgaasGGRRAQVAELARAGMAVGLAGLFIEAHPDPE 245
Cdd:pfam00793 167 RGIRGGEgpNRNTLDVSAVAILKEETGHLPVMVDVSHANGRKD------GGRQPLVLPLAKAAIAVGIDGLMIEVHPNPG 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 16129178   246 HAKCDGPSALPLAKLEPFLKQMKAIDDLVK 275
Cdd:pfam00793 241 NALSDGPQQLKYGKSETDACILWELTELLL 270
AroGA COG2876
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
 63-274 3.73e-32

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


Pssm-ID: 442123  Cd Length: 283  Bit Score: 119.79  E-value: 3.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGavinvkKPQF 142
Cdd:COG2876  79 RTSPYSFQGLG-EEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELLKEVGRTG------KPVL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178 143 VSPGqMGNIVDKF---KE----GGNEKVILCDRG--------ANfgydnlVVDMLGFSIMKKVSgNSPVIFDVTHAlqcr 207
Cdd:COG2876 152 LKRG-LSATIEEWlmaAEyilsEGNPNVILCERGirtfetatRN------TLDLSAVPVLKELT-HLPVIVDPSHA---- 219

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129178 208 dpfgaasGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLV 274
Cdd:COG2876 220 -------TGRRDLVPPMAKAAVAAGADGLMIEVHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAV 279
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
 63-275 6.28e-31

3-deoxy-7-phosphoheptulonate synthase; Reviewed


Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 117.68  E-value: 6.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTgavinvKKPQF 142
Cdd:PRK08673 132 RTSPYSFQGLG-EEGLKLLAEAREETGLPIVTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKT------NKPVL 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  143 VSPGqMGNIVDKF-------KEGGNEKVILCDRG----ANFGYDNLvvDMLGFSIMKKVSgNSPVIFDVTHAlqcrdpfg 211
Cdd:PRK08673 205 LKRG-MSATIEEWlmaaeyiLAEGNPNVILCERGirtfETATRNTL--DLSAVPVIKKLT-HLPVIVDPSHA-------- 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129178  212 aasGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVK 275
Cdd:PRK08673 273 ---TGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEELMKKLRAIAEALG 333
BagF_FevY NF041229
phospho-2-dehydro-3-deoxyheptonate aldolase BagF/FevY;
63-268 5.35e-25

phospho-2-dehydro-3-deoxyheptonate aldolase BagF/FevY;


Pssm-ID: 469132 [Multi-domain]  Cd Length: 340  Bit Score: 102.04  E-value: 5.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTGavinvkKPQF 142
Cdd:NF041229 129 RTSPYAFQGLG-EAGLKILADVRAETGLPIVTEVVDAHDVELVASYADMLQIGTRNAQNFALLQAVGDVG------KPVM 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  143 VSPGQMGNI------VDKFKEGGNEKVILCDRGANfGYDNLVVDMLGFSIMKKVSGNS--PVIFDVTHalqcrdpfgaaS 214
Cdd:NF041229 202 LKRGMSGTIeewlmaAEYVAQRGNLDIVLCERGIR-TFETATRNTLDIAAVPIVQRLShlPVIVDPSH-----------S 269

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16129178  215 GGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMK 268
Cdd:NF041229 270 GGRRDLVLPLTRAALAVGADGVIVDVHPDPRTALCDGPQALVHEDLEELGAVMR 323
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 63-270 3.98e-20

bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 88.49  E-value: 3.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAFLARQTDLVEAMAKTgavinvKKPQF 142
Cdd:PRK12595 157 RTSPYDFQGLG-VEGLKILKQVADEYGLAVISEIVNPADVEVALDYVDVIQIGARNMQNFELLKAAGRV------NKPVL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  143 VSPGQMGNIvDKFKEG-------GNEKVILCDRGANfGYDNLVVDMLGFS---IMKKVSgNSPVIFDVTHalqcrdpfga 212
Cdd:PRK12595 230 LKRGLSATI-EEFIYAaeyimsqGNGQIILCERGIR-TYEKATRNTLDISavpILKQET-HLPVMVDVTH---------- 296

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129178  213 aSGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAI 270
Cdd:PRK12595 297 -STGRRDLLLPTAKAALAIGADGVMAEVHPDPAVALSDSAQQMDIPEFDRFLDELKPL 353
PRK13396 PRK13396
3-deoxy-7-phosphoheptulonate synthase; Provisional
 63-275 1.46e-14

3-deoxy-7-phosphoheptulonate synthase; Provisional


Pssm-ID: 237376 [Multi-domain]  Cd Length: 352  Bit Score: 72.87  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178   63 RSSIHSYRGPGlEEGMKIFQELKQTFGVKIITDVHEPSQAQPVADVVDVIQLPAflaRQTDLVEAMAKTGAVinvKKPQF 142
Cdd:PRK13396 140 RTSPYAFQGHG-ESALELLAAAREATGLGIITEVMDAADLEKIAEVADVIQVGA---RNMQNFSLLKKVGAQ---DKPVL 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129178  143 VSPGQMGNIVDKFKE------GGNEKVILCDRGANFGYDNLVVDMLGFSIMkkvsgnsPVIFDVTHALQCRDPfgAASGG 216
Cdd:PRK13396 213 LKRGMAATIDEWLMAaeyilaAGNPNVILCERGIRTFDRQYTRNTLDLSVI-------PVLRSLTHLPIMIDP--SHGTG 283

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16129178  217 RRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCDGPSALPLAKLEPFLKQMKAIDDLVK 275
Cdd:PRK13396 284 KSEYVPSMAMAAIAAGTDSLMIEVHPNPAKALSDGPQSLTPDRFDRLMQELAVIGKTVG 342
 
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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