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Conserved domains on  [gi|1308832072|gb|PKN66203|]
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bifunctional hexulose-6-phosphate synthase/ribonuclease regulator [Deltaproteobacteria bacterium HGW-Deltaproteobacteria-15]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07028 super family cl35534
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 4-445 0e+00

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


The actual alignment was detected with superfamily member PRK07028:

Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 635.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   4 LPPIQIALDLLDLPRAIRIAEEAVKGILEetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK07028    3 RPILQVALDLLELDRAVEIAKEAVAGGAD--------WIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELV 163
Cdd:PRK07028   75 EMAAKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 164 RRIAAAISgkAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSGKPIVSKEFVKYDSEHLVEA 243
Cdd:PRK07028  155 KEVSEEVS--IPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGKPVKIDKFKKSLDEEIREI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 244 FMKVSTANVSDAMHRTGELRGLKPVWvgapGDLKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDACQGEIAIWGEL 323
Cdd:PRK07028  233 FMQVSTPNISDAMHRKGAMKGIKPLV----RGTKMVGKAVTVQTFAGDWAKPVEAIDVAKPGDVIVIYNSSKDIAPWGEL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 324 ATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVVVPRG 403
Cdd:PRK07028  309 ATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1308832072 404 NAMEMANRAIDVLERENRIREEIKRGSTLGQTAYLRKWDVKK 445
Cdd:PRK07028  389 RAYEIARRALEVKKTEDRIREEIRRGRTLSEVIELKKWEKKK 430
 
Name Accession Description Interval E-value
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 4-445 0e+00

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 635.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   4 LPPIQIALDLLDLPRAIRIAEEAVKGILEetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK07028    3 RPILQVALDLLELDRAVEIAKEAVAGGAD--------WIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELV 163
Cdd:PRK07028   75 EMAAKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 164 RRIAAAISgkAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSGKPIVSKEFVKYDSEHLVEA 243
Cdd:PRK07028  155 KEVSEEVS--IPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGKPVKIDKFKKSLDEEIREI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 244 FMKVSTANVSDAMHRTGELRGLKPVWvgapGDLKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDACQGEIAIWGEL 323
Cdd:PRK07028  233 FMQVSTPNISDAMHRKGAMKGIKPLV----RGTKMVGKAVTVQTFAGDWAKPVEAIDVAKPGDVIVIYNSSKDIAPWGEL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 324 ATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVVVPRG 403
Cdd:PRK07028  309 ATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1308832072 404 NAMEMANRAIDVLERENRIREEIKRGSTLGQTAYLRKWDVKK 445
Cdd:PRK07028  389 RAYEIARRALEVKKTEDRIREEIRRGRTLSEVIELKKWEKKK 430
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
5-223 1.09e-82

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 440039  Cd Length: 212  Bit Score: 253.16  E-value: 1.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAVKGILeetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVE 84
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKEVAGGVD---------IIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELVR 164
Cdd:COG0269    75 MAFKAGADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLK 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832072 165 RIAAAISGKamISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKS 223
Cdd:COG0269   155 KIKELVGVP--VAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 5-217 2.47e-73

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 229.00  E-value: 2.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAVKGILeetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVE 84
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVD---------IIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVeLEKMGVDIVNIHVGLDQQVLGIK-PVELV 163
Cdd:cd04726    72 MAFKAGADIVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGGWwPEDDL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308832072 164 RRIAAAIsgKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:cd04726   151 KKVKKLL--GVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 7-221 2.95e-69

3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.


Pssm-ID: 132172 [Multi-domain]  Cd Length: 206  Bit Score: 218.78  E-value: 2.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   7 IQIALDLLDLPRAIRIAEEAVKGIleetrddskAWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVEMA 86
Cdd:TIGR03128   2 LQLALDLLDIEEALELAEKVADYV---------DIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  87 AKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELVRRI 166
Cdd:TIGR03128  73 FAAGADIVTVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 167 AAAISgKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSL 221
Cdd:TIGR03128 153 LKLVK-EARVAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 250-398 3.27e-58

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 188.10  E-value: 3.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 250 ANVSDAMH----RTGELRGLKPVWVGapgdlKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDACQGEIAIWGELAT 325
Cdd:pfam03737   1 ADLSDALGsyggRLGAMPGIRPLNPG-----PFVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVVDGGGGSRAALGDLLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832072 326 HSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVV 398
Cdd:pfam03737  76 TLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 6-217 6.00e-34

Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.


Pssm-ID: 214921  Cd Length: 212  Bit Score: 126.51  E-value: 6.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072    6 PIQIALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDKFPQLTIcADMKTMDAGATEVEM 85
Cdd:smart00934   1 RLIVALDVPDLEEALELADAL---------GDSVDIIKVGTELFLAEGPEGVKELKELFGFPVF-LDLKLHDIPNTVARA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   86 A---AKAGANVVFVLGCSPDSCISEAVLAAKKYGVK-IAADLISVTDPEK-----------RAVELEKM--GVDIVNIHV 148
Cdd:smart00934  71 AraaAELGADAVTVHAYAGSDMIEAALEAAKKYGPGlLAVTVLTSPGAEDlqelgdesleeQVLRLAKLakEAGLDGVVC 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832072  149 GLDQQvlgikpvELVRRIAAAisgKAMISAAGG---LNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:smart00934 151 SATEP-------ELIRRALGP---DFLILTPGIgdqGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
 
Name Accession Description Interval E-value
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 4-445 0e+00

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 635.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   4 LPPIQIALDLLDLPRAIRIAEEAVKGILEetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK07028    3 RPILQVALDLLELDRAVEIAKEAVAGGAD--------WIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELV 163
Cdd:PRK07028   75 EMAAKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 164 RRIAAAISgkAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSGKPIVSKEFVKYDSEHLVEA 243
Cdd:PRK07028  155 KEVSEEVS--IPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGKPVKIDKFKKSLDEEIREI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 244 FMKVSTANVSDAMHRTGELRGLKPVWvgapGDLKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDACQGEIAIWGEL 323
Cdd:PRK07028  233 FMQVSTPNISDAMHRKGAMKGIKPLV----RGTKMVGKAVTVQTFAGDWAKPVEAIDVAKPGDVIVIYNSSKDIAPWGEL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 324 ATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVVVPRG 403
Cdd:PRK07028  309 ATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKE 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1308832072 404 NAMEMANRAIDVLERENRIREEIKRGSTLGQTAYLRKWDVKK 445
Cdd:PRK07028  389 RAYEIARRALEVKKTEDRIREEIRRGRTLSEVIELKKWEKKK 430
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
5-223 1.09e-82

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 440039  Cd Length: 212  Bit Score: 253.16  E-value: 1.09e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAVKGILeetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVE 84
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKEVAGGVD---------IIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELVR 164
Cdd:COG0269    75 MAFKAGADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLK 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1308832072 165 RIAAAISGKamISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKS 223
Cdd:COG0269   155 KIKELVGVP--VAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 5-217 2.47e-73

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 229.00  E-value: 2.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAVKGILeetrddskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVE 84
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVD---------IIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVeLEKMGVDIVNIHVGLDQQVLGIK-PVELV 163
Cdd:cd04726    72 MAFKAGADIVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGGWwPEDDL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1308832072 164 RRIAAAIsgKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:cd04726   151 KKVKKLL--GVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 7-221 2.95e-69

3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.


Pssm-ID: 132172 [Multi-domain]  Cd Length: 206  Bit Score: 218.78  E-value: 2.95e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   7 IQIALDLLDLPRAIRIAEEAVKGIleetrddskAWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEVEMA 86
Cdd:TIGR03128   2 LQLALDLLDIEEALELAEKVADYV---------DIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  87 AKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNIHVGLDQQVLGIKPVELVRRI 166
Cdd:TIGR03128  73 FAAGADIVTVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTI 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 167 AAAISgKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSL 221
Cdd:TIGR03128 153 LKLVK-EARVAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
 237-432 4.34e-69

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 218.12  E-value: 4.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 237 SEHLVEAFMKVSTANVSDAMHRTGE---LRGLKPVWVGApgdlKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDAC 313
Cdd:COG0684     4 DAELLERLAAVSTATVSDALDRLLRgalDPGIRPLHPGA----RLVGPAVTVRYRPGDNLMLHEAIDLAPPGDVLVIDAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 314 QG-EIAIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPK-GFGEINVPIEVCGRKVEPGDWII 391
Cdd:COG0684    80 GDtDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRvGPGEINVPVSIGGVTVRPGDLVV 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1308832072 392 GDESGVVVVPRGNAMEMANRAIDVLERENRIREEIKRGSTL 432
Cdd:COG0684   160 ADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESL 200
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
 250-398 3.27e-58

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 188.10  E-value: 3.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 250 ANVSDAMH----RTGELRGLKPVWVGapgdlKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDACQGEIAIWGELAT 325
Cdd:pfam03737   1 ADLSDALGsyggRLGAMPGIRPLNPG-----PFVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVVDGGGGSRAALGDLLA 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832072 326 HSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVV 398
Cdd:pfam03737  76 TLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIVADEDGVV 148
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
 250-400 3.37e-55

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 180.35  E-value: 3.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 250 ANVSDAMHRTGELRG--LKPVWvgapGDLKFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDA-CQGEIAIWGELATH 326
Cdd:cd16841     1 ADLSDALDRLGGVLPgiIRPLG----GGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGgGSLRCALWGDLLAT 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832072 327 SCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVVV 400
Cdd:cd16841    77 LAKARGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIVADEDGVVVI 150
PRK06201 PRK06201
hypothetical protein; Validated
 240-429 4.03e-46

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 158.96  E-value: 4.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 240 LVEAFMKVSTANVSDAMHR-TGELRGLKPVWVGAPgdlkFAGPAVTVRTYNGDWSAPVQAIDHAKQGDILVVDAcQGEI- 317
Cdd:PRK06201   18 LVEAFRELPVANISDSMNRmTAGGAGLRPMHRGGR----LAGTALTVRTRPGDNLMIHRALDLARPGDVIVVDG-GGDLt 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 318 -AIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPtAGEPK-GFGEINVPIEVCGRKVEPGDWIIGDES 395
Cdd:PRK06201   93 nALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTH-RGPYKdGPGEINVPVAIGGMVIEPGDLIVGDDD 171

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1308832072 396 GVVVVPRGNAMEMANRAIDVLERENRIREEIKRG 429
Cdd:PRK06201  172 GLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
5-222 5.09e-35

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 133.98  E-value: 5.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PP-IQIALDLLDLprairiaeEAVKGILEETRDDSKAWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK13307  172 PPyLQVALDLPDL--------EEVERVLSQLPKSDHIIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRaveLEKMGV--DIVNIHVGLDQQvLGIKPVE 161
Cdd:PRK13307  244 RMAADATADAVVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKL---LESLKVkpDVVELHRGIDEE-GTEHAWG 319

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1308832072 162 LVRRIAAAiSGKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLK 222
Cdd:PRK13307  320 NIKEIKKA-GGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLK 379
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 6-217 6.00e-34

Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.


Pssm-ID: 214921  Cd Length: 212  Bit Score: 126.51  E-value: 6.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072    6 PIQIALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDKFPQLTIcADMKTMDAGATEVEM 85
Cdd:smart00934   1 RLIVALDVPDLEEALELADAL---------GDSVDIIKVGTELFLAEGPEGVKELKELFGFPVF-LDLKLHDIPNTVARA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   86 A---AKAGANVVFVLGCSPDSCISEAVLAAKKYGVK-IAADLISVTDPEK-----------RAVELEKM--GVDIVNIHV 148
Cdd:smart00934  71 AraaAELGADAVTVHAYAGSDMIEAALEAAKKYGPGlLAVTVLTSPGAEDlqelgdesleeQVLRLAKLakEAGLDGVVC 150

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1308832072  149 GLDQQvlgikpvELVRRIAAAisgKAMISAAGG---LNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:smart00934 151 SATEP-------ELIRRALGP---DFLILTPGIgdqGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 5-217 8.30e-31

Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.


Pssm-ID: 395160  Cd Length: 215  Bit Score: 118.14  E-value: 8.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDKFpqLTICADMKTMDAGATEVE 84
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADEL---------GPYVDILKVGTPLFEAFGLKLVAELRKHG--FLIFLDLKFADIGNTVAK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MA---AKAGANVVFVLGCSPDSCISEAVLAAKKYGVK-IAADLISVTDPEKRAvELEKMGVDIVNIHVGLDQQ--VLGIK 158
Cdd:pfam00215  70 QAkykAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGlLLVAELSSKGSLDLQ-EEGDLGYTQEIVHRAADLAagVDGVV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832072 159 PVELVRRIAAAISGKAM-------ISAAGGLNSETA-VQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:pfam00215 149 ASATEALREILPDFLILtpgiglqGGDAGGQQRVTTpAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PRK08245 PRK08245
hypothetical protein; Validated
 237-432 4.03e-30

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 116.92  E-value: 4.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 237 SEHLVEAFMKVSTANVSDAMHRTG----ELRGLKPVwvgAPGDLKFAGPAVTVR--------TYNGDWSAPV----QAID 300
Cdd:PRK08245    7 SPATREALKRVSTATLTTALFKRGlrnqFIRGVRPL---RPGGPRMVGPAFTLRfvparedlNTPESFADPEspqrAAIE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 301 HAKQGDILVVDAcQGEI--AIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTP----TAGEPKGfgeIN 374
Cdd:PRK08245   84 TCPPGCVLVVDA-RGDAraGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVWCAGPSAptnlTGLTAVD---IN 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832072 375 VPIEVCGRKVEPGDWIIGDESGVVVVPRGNAMEMANRAIDVLERENRIREEIKRGSTL 432
Cdd:PRK08245  160 VPIGCGGVAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREEVAAGASL 217
PRK09262 PRK09262
hypothetical protein; Provisional
 238-429 1.19e-29

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 115.03  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 238 EHLVEAFMKVSTANVSDAMHRTGELR-GLKPVWVGApgdlKFAGPAVTVRTYNGD-WSAPVqAIDHAKQGDILVVdACQG 315
Cdd:PRK09262   14 AAVVDRLAEFGVATVHEAQGRVGLLKpYMRPIYQGA----RIAGTAVTVLVQPGDnWMMHV-AVEQCQPGDVLVV-APTS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 316 EIA--IWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARyftptAGEPKG-----FGEINVPIEVCGRKVEPGD 388
Cdd:PRK09262   88 PCTdgFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSR-----AISAQGtvkatLGSVNVPVVCAGALVNPGD 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1308832072 389 WIIGDESGVVVVPRGNAMEMANRAIDVLERENRIREEIKRG 429
Cdd:PRK09262  163 VVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAG 203
ligK_PcmE TIGR02798
4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein ...
 241-412 1.37e-24

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase.


Pssm-ID: 131845  Cd Length: 222  Bit Score: 101.07  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 241 VEAFMKVSTANVSDAMHRTGELRG-LKPVWVGApgdlKFAGPAVTVRTYNGD-WSAPVqAIDHAKQGDILVVdACQGEI- 317
Cdd:TIGR02798  15 VDGLAAFGVATVHEAMGRVGLLAPyMRPIYTGA----RVCGTAVTVLLQPGDnWMMHV-AAEQIQEGDVVVA-ACTAECe 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 318 -AIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESG 396
Cdd:TIGR02798  89 dGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKATLGSVNIPVVCANALVNPGDVVVADDDG 168

                         170
                  ....*....|....*.
gi 1308832072 397 VVVVPRGNAMEMANRA 412
Cdd:TIGR02798 169 VVVVPRANAGAVLDAA 184
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
4-217 2.85e-20

3-dehydro-L-gulonate-6-phosphate decarboxylase;


Pssm-ID: 237344  Cd Length: 216  Bit Score: 88.83  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   4 LPPIQIALDLLDLPRAIRIAEEAVKGIleetrdDSkawVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK13306    3 KPLLQIALDNQDLESAIEDAKKVAEEV------DI---IEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEkRAVELEKMGVDIVNIHVGLDQQVLGI----KP 159
Cdd:PRK13306   74 KMAFEAGADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWE-QAQQWRDAGISQVIYHRSRDAQLAGVawgeKD 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832072 160 VELVRRIAAAisgKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:PRK13306  153 LNKVKKLSDM---GFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAF 207
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
237-432 2.76e-18

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 87.12  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 237 SEHLVEAFMKVSTANVSDAMHRTG----ELRGLKPVwvgAPGdLKFAGPAVTVR----------TYNGDWSAPVQAIDHA 302
Cdd:PRK12764  268 SPELKAKLASVATATLSAQLRKRGlnnvSIDGLTPT---RPG-RRMVGRARTLRyvpnredlfkEHGGGFNAQKRAFDSV 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 303 KQGDILVVDAcQGE--IAIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFPVYAryftpTAGEPKGFGEINVPIEV- 379
Cdd:PRK12764  344 NPGEVLVIEA-RGEkgTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVFF-----AGPHPAVLGRRHVPWDVd 417

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832072 380 ----CG-RKVEPGDWIIGDESGVVVVPRGNAMEMANRAIDVLERENRIREEIKRGSTL 432
Cdd:PRK12764  418 itvaCGgATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAERVAEGASV 475
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
 249-400 9.55e-18

RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein. [Unknown function, General]


Pssm-ID: 130990  Cd Length: 150  Bit Score: 79.68  E-value: 9.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 249 TANVSDAMHRtgELRGLKPVWVGAPGDLKFAGPAVTVRTYNgDWSAPVQAIDHAKQGDILVVDAcQGEI--AIWGELATH 326
Cdd:TIGR01935   1 TPDLCDAYPD--KVRVLEPMFRNFGGRAAFAGPIVTVKCFE-DNSLVREVLEQPGAGRVLVVDG-GGSLrcALLGDNLAV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308832072 327 SCISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVVV 400
Cdd:TIGR01935  77 LAEENGWEGVIVNGCVRDVAELAGMDLGVKALAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLYADEDGILVS 150
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
278-399 3.53e-17

putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;


Pssm-ID: 183553  Cd Length: 163  Bit Score: 78.46  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 278 FAGPAVTVRTYNgDWSAPVQAIDHAKQGDILVVD---ACQGeiAIWGELATHSCISKGVAAVIIDGAVRDIDDIRKLKFP 354
Cdd:PRK12487   32 FWGEIVTVRCFE-DNSKVKEVLAQDGKGKVLVVDgggSCRR--ALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLG 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1308832072 355 VYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESGVVV 399
Cdd:PRK12487  109 VKALGASPIKTEKRGQGEVNVTLTMGNVIIEPGDMLYADENGIAV 153
PRK09372 PRK09372
ribonuclease E inhibitor RraA;
245-401 3.05e-14

ribonuclease E inhibitor RraA;


Pssm-ID: 236487  Cd Length: 159  Bit Score: 70.17  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 245 MKVSTANVSDAMHrtGELRGLKPVWVGAPGDLKFAGPAVTVRTYNgDWSAPVQAIDHAKQGDILVVDA-----CQ---GE 316
Cdd:PRK09372    1 MEYDTSDLCDIYP--DDVRVVEPLFSSFGGRSSFGGPITTVKCFE-DNGLVKELLEEPGEGRVLVVDGggslrRAlvgDN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 317 IAiwgELAthscISKGVAAVIIDGAVRDIDDIRKLKFPVYARYFTPTAGEPKGFGEINVPIEVCGRKVEPGDWIIGDESG 396
Cdd:PRK09372   78 LA---ELA----VDNGWEGIVVYGCVRDVDELAELDIGIQALAAIPVKSDKEGIGERDVPVNFGGVTFFPGDYLYADNDG 150


                  ....*
gi 1308832072 397 VVVVP 401
Cdd:PRK09372  151 IIVSP 155
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
4-223 2.15e-12

3-keto-L-gulonate-6-phosphate decarboxylase UlaD;


Pssm-ID: 183962  Cd Length: 218  Bit Score: 66.38  E-value: 2.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   4 LPPIQIALDLLDLPRAIRIAEEavkgiLEETRDdskaWVELGTPLIKSEGMNAIREMRDKFPQLTICADMKTMDAGATEV 83
Cdd:PRK13305    3 RPLLQLALDHTSLEAAQRDVTL-----LKDHVD----IVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  84 EMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKIAADLI---SVTDpekrAVELEKMGVDIVNIHVGLDQQVLGIK-- 158
Cdd:PRK13305   74 QQAFGAGANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFgnwTLDD----ARDWHRIGVRQAIYHRGRDAQASGQQwg 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 159 PVELVRRIAAAISGKAMiSAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKS 223
Cdd:PRK13305  150 EADLARMKALSDIGLEL-SITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDA 213
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 5-222 1.61e-10

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 60.77  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDKFPqltICADMKTMDAGATE-- 82
Cdd:PRK13813    4 SRIILALDVTDRERALKIAEEL---------DDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPNTNrl 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  83 -VEMAAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKI----------AADLI-SVTDpekravELEKMGVDIvnihvGL 150
Cdd:PRK13813   72 iCEAVFEAGAWGIIVHGFTGRDSLKAVVEAAAESGGKVfvvvemshpgALEFIqPHAD------KLAKLAQEA-----GA 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832072 151 DQQVLGIKPVELVRRIAAAISGKAMI-----SAAGGlnseTAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLK 222
Cdd:PRK13813  141 FGVVAPATRPERVRYIRSRLGDELKIispgiGAQGG----KAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIR 213
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 9-217 3.32e-07

orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273785  Cd Length: 214  Bit Score: 50.82  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   9 IALDLLDLPRAIRIAEEavkgiLEETRDdskaWVELGTPLIKSEGMNAIREMRDKFPQltICADMKTMDAGAT---EVEM 85
Cdd:TIGR01740   3 VALDVTTKEEALDLADS-----LGEEIC----VIKVGYDLLLSGGEKIIDELAKLNKL--IFLDLKFADIPNTvklQYES 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  86 AAKAGANVVFVLGCSPDSCISEAVLAAKKYGVKiaaDLISVT------------DPEKRAVELEKMGVDIVNIHVgldqq 153
Cdd:TIGR01740  72 KIKLGADMVNVHGFAGSESVEAAKEAASEFGRR---GLLAVTeltsmgseeygeDTMEKVVEYAKEAKEFGLIGP----- 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1308832072 154 vlgIKPVELVRRIAAAISGKAMISAAGGLNSE---------TAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:TIGR01740 144 ---VCSAEEAKEIRKATGDFLILTPGIRLDSKdaddqkrvvTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRI 213
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 160-224 6.83e-07

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 50.07  E-value: 6.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 160 VELVRRIAAAISGKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSG 224
Cdd:COG0036   154 IRRLRELIDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 9-217 3.36e-06

Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.


Pssm-ID: 240076  Cd Length: 216  Bit Score: 47.94  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   9 IALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDK-FPqltICADMKTMDAGATeVEMAA 87
Cdd:cd04725     3 VALDPPDEEFALALIDAL---------GPYVCAVKVGLELFEAAGPEIVKELRELgFL---VFLDLKLGDIPNT-VAAAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  88 KAGANvvfvLGCspDSCI------SEAVLAAKKYGVKIAADLISVT----------------DPEKRAVELEKMGVDivn 145
Cdd:cd04725    70 EALLG----LGA--DAVTvhpyggSDMLKAALEAAEEKGKGLFAVTvlsspgaldlqegipgSLEDLVERLAKLARE--- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 146 ihVGLDQQVLGIKPVELVRRIAAaisGKAMI---------SAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRK 216
Cdd:cd04725   141 --AGVDGVVCGATEPEALRRALG---PDFLIltpgigaqgSGDDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEA 215


                  .
gi 1308832072 217 I 217
Cdd:cd04725   216 I 216
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 5-223 6.47e-06

Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440053  Cd Length: 228  Bit Score: 47.02  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072   5 PPIQIALDLLDLPRAIRIAEEAvkgileetrDDSKAWVELGTPLIKSEGMNAIREMRDKfpQLTICADMKTMDAGATeVE 84
Cdd:COG0284     3 SPLIVALDLPDAAEALAIVDAL---------ADLVCAYKPGLALFEAYGPEGVEALKER--GLPVFLDLKRHDIPNT-VA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  85 MAAKAganvVFVLGCS---------PDScISEAVLAAKKYGVKI----------AADLISV---TDPEKRAVELEKMGVD 142
Cdd:COG0284    71 AAARA----AAELGVDavtvhayggRDM-LEPALEAADESGKGVfavtvltspgAADLQELgieGPLYEVVLRLAKLAKE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 143 IvnihvGLDQQVLGIKPVELVRRIAaaisGKAM------ISAAGGLNSE-----TAVQAWEAGADIIIVGGSLYKAASPE 211
Cdd:COG0284   146 A-----GLDGVVCSATEAAALRAAL----GPDFllltpgIRPQGGDAGDqkrvgTPAEAIAAGADYLVVGRPITYAGDPR 216

                         250
                  ....*....|..
gi 1308832072 212 ESVRKIIQSLKS 223
Cdd:COG0284   217 AAAEAIREEIAA 228
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 160-217 9.90e-06

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 46.32  E-value: 9.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1308832072 160 VELVRRIAAAISGKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:cd00429   153 IRKLRELIPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 32-217 1.28e-05

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 45.59  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  32 EETRDDSKAWVELGTPLIK-----SEGMNAIREMRDKFPQLTICAdmktmdaG----ATEVEMAAKAGANVVFVLGCSPd 102
Cdd:cd00452    16 EDALALAEALIEGGIRAIEitlrtPGALEAIRALRKEFPEALIGA-------GtvltPEQADAAIAAGAQFIVSPGLDP- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 103 scisEAVLAAKKYGVKIAADLISVTDpekrAVELEKMGVDIVNIHVGldqQVLGIKpveLVRRIAAAISGkAMISAAGGL 182
Cdd:cd00452    88 ----EVVKAANRAGIPLLPGVATPTE----IMQALELGADIVKLFPA---EAVGPA---YIKALKGPFPQ-VRFMPTGGV 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1308832072 183 NSETAVQAWEAGADIIIVGGSLYKAASPEESVRKI 217
Cdd:cd00452   153 SLDNAAEWLAAGVVAVGGGSLLPKDAVAAGDWAAI 187
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 105-210 4.23e-05

Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439927 [Multi-domain]  Cd Length: 272  Bit Score: 45.01  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 105 ISEAVLAAKKY---GVKIAadlISVTDPE--KRAVELekmGVDIV---NIhvgldqqvlgikPVELVRRIAAAISGKAMI 176
Cdd:COG0157   169 IAEAVARARARappEKKIE---VEVETLEelEEALAA---GADIImldNM------------SPEELREAVALLRGRALL 230

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1308832072 177 SAAGGLNSETAVQAWEAGADIIIVgGSLYKAASP 210
Cdd:COG0157   231 EASGGITLENIRAYAETGVDYISV-GALTHSAPA 263
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 180-223 6.24e-05

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 44.02  E-value: 6.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1308832072 180 GGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKS 223
Cdd:PRK05581  177 GGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 176-220 1.38e-04

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 43.05  E-value: 1.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1308832072 176 ISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESV---RKIIQS 220
Cdd:PTZ00170  176 IQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIellRESVQK 223
PRK02227 PRK02227
(5-formylfuran-3-yl)methyl phosphate synthase;
123-214 4.83e-04

(5-formylfuran-3-yl)methyl phosphate synthase;


Pssm-ID: 235014  Cd Length: 238  Bit Score: 41.44  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 123 LISVTDPEKrAVELEKMGVDIV---NIHVGldqqVLGIKPVELVRRIAAAISGKAMISAA-GGLN------SETAVQAWE 192
Cdd:PRK02227    4 LVSVRNLEE-ALEALAGGADIIdvkNPKEG----SLGANFPWVIREIVAAVPGRKPVSATiGDVPykpgtiSLAALGAAA 78

                          90       100
                  ....*....|....*....|..
gi 1308832072 193 AGADIIIVGgsLYKAASPEESV 214
Cdd:PRK02227   79 TGADYVKVG--LYGGKTAEEAV 98
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 83-225 7.67e-04

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 40.76  E-value: 7.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  83 VEMAAKAGANVV-FVLGCSPDSCISEAVLAAKKYGVKIAADLISVTDPEKRAVELEKMGVDIVNI---HVGLDQQVLGIK 158
Cdd:PLN02334   81 VPDFAKAGASIFtFHIEQASTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKGLVDMVLVmsvEPGFGGQSFIPS 160

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1308832072 159 PVELVRRIAAAISGKaMISAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEEsvrkIIQSLKSGK 225
Cdd:PLN02334  161 MMDKVRALRKKYPEL-DIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAE----VISGLRASV 222
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
159-222 1.67e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 39.79  E-value: 1.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 159 PVELVRRIAAAISGKAMIsAAGGLNS-ETAVQAWEAGADIIIVGGSLYKAasPEESVRKIIQSLK 222
Cdd:PRK04169  171 PPEMVKAVKKALDITPLI-YGGGIRSpEQARELMAAGADTIVVGNIIEED--PKKTVKAIKKAIK 232
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 56-198 1.99e-03

DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163674 [Multi-domain]  Cd Length: 265  Bit Score: 39.75  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  56 AIREMRDKFPQLTICAdmkTMDAGATEVEMAAKAGANVV------------FVLGCSPD---SCISEAVLAAKKYGVKIA 120
Cdd:cd03174    56 VLRAIRKLVPNVKLQA---LVRNREKGIERALEAGVDEVrifdsasethsrKNLNKSREedlENAEEAIEAAKEAGLEVE 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 121 ADLISVTDPE-------KRAVELEKMGVDIVNI--HVGLdqqvlgIKPVELVRRIaaaisgKAMISAAGGL--------N 183
Cdd:cd03174   133 GSLEDAFGCKtdpeyvlEVAKALEEAGADEISLkdTVGL------ATPEEVAELV------KALREALPDVplglhthnT 200

                         170
                  ....*....|....*....
gi 1308832072 184 SETAV----QAWEAGADII 198
Cdd:cd03174   201 LGLAVanslAALEAGADRV 219
thiE PRK00043
thiamine phosphate synthase;
160-225 3.15e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 39.01  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308832072 160 VELVRRIAAAISGKAMIsAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSGK 225
Cdd:PRK00043  148 LEGLREIRAAVGDIPIV-AIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 83-228 3.67e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 38.72  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072  83 VEMAAKAGANVVFVLGCSPDSCISEAV------LAAKKYGVKIAADlISVTDPEKRAVEL----EKMGVDIVNIHVglDQ 152
Cdd:cd04722    18 AKAAAEAGADAIIVGTRSSDPEEAETDdkevlkEVAAETDLPLGVQ-LAINDAAAAVDIAaaaaRAAGADGVEIHG--AV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 153 QVLGIKPVELVRRIAAAISGKAMISAAGGLNSETAVQAWEAGADIIIV----GGSLYKAASPEESVRKIIQSLKSGKPIV 228
Cdd:cd04722    95 GYLAREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLgnggGGGGGRDAVPIADLLLILAKRGSKVPVI 174
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 105-210 3.73e-03

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 38.99  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 105 ISEAVLAAKKYG---VKIAadlISVTDPEkRAVELEKMGVDIVNihvgLDQQvlgikPVELVRRIAAAISG--KAMISAA 179
Cdd:cd01568   167 ITEAVKRARAAApfeKKIE---VEVETLE-EAEEALEAGADIIM----LDNM-----SPEELKEAVKLLKGlpRVLLEAS 233

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308832072 180 GGLNSETAVQAWEAGADIIIVgGSLYKAASP 210
Cdd:cd01568   234 GGITLENIRAYAETGVDVIST-GALTHSAPA 263
PRK12331 PRK12331
oxaloacetate decarboxylase subunit alpha;
108-198 4.25e-03

oxaloacetate decarboxylase subunit alpha;


Pssm-ID: 183446 [Multi-domain]  Cd Length: 448  Bit Score: 39.30  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308832072 108 AVLAAKKYGVKIAADLISVTDP-------EKRAVELEKMGVDIVNIhvgldQQVLGI----KPVELVRRIAAAISGKAMI 176
Cdd:PRK12331  128 AVKATKKAGGHAQVAISYTTSPvhtidyfVKLAKEMQEMGADSICI-----KDMAGIltpyVAYELVKRIKEAVTVPLEV 202

                          90       100
                  ....*....|....*....|....
gi 1308832072 177 S--AAGGLNSETAVQAWEAGADII 198
Cdd:PRK12331  203 HthATSGIAEMTYLKAIEAGADII 226
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
186-224 5.50e-03

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 38.19  E-value: 5.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1308832072 186 TAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSG 224
Cdd:PRK00230  192 TPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEIAGA 230
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 160-224 6.03e-03

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 37.86  E-value: 6.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308832072 160 VELVRRIAAAISGKAMisAAGGLNSETAVQAWEAGADIIIVGGSLYKAASPEESVRKIIQSLKSG 224
Cdd:COG0352   144 LEGLAWWAELVEIPVV--AIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 159-207 6.18e-03

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 37.99  E-value: 6.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1308832072 159 PVELVRRIAAAISGKAMISAAGGLNSETAVQAWEAGADIIIVGGSLYKA 207
Cdd:cd02812   162 PPEVVRAVKKVLGDTPLIVGGGIRSGEQAKEMAEAGADTIVVGNIVEED 210
 
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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