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Conserved domains on  [gi|1668256575|ref|WP_138145967|]
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flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase [Bathymodiolus heckerae thiotrophic gill symbiont]

Protein Classification

flavodoxin/ferredoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase( domain architecture ID 10011395)

flavodoxin/ferredoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, part of an alternative non-mevalonate pathway for isoprenoid biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IspG COG0821
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
3-357 0e+00

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis


:

Pssm-ID: 440583 [Multi-domain]  Cd Length: 363  Bit Score: 622.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   3 PIHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIP 82
Cdd:COG0821     2 PSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAALPEIKKQLPVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  83 LITDIHFDYKIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAF 162
Cdd:COG0821    82 LVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSLEKDLLEKYGDPTPEALVESAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 163 RHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLAS 242
Cdd:COG0821   162 EHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAGTGRKGTVKSAAGLGILLAEGIGDTIRVSLTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 243 DPVDEIKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTG 322
Cdd:COG0821   242 DPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLIQLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAG 321
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1668256575 323 G-DPNLMYIDGLTHSKVTNENLVDEFEAQIRQRLKK 357
Cdd:COG0821   322 GgGEGLLFKKGEIIRKVPEDEIVEELLEEIEKYVAE 357
 
Name Accession Description Interval E-value
IspG COG0821
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
3-357 0e+00

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440583 [Multi-domain]  Cd Length: 363  Bit Score: 622.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   3 PIHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIP 82
Cdd:COG0821     2 PSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAALPEIKKQLPVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  83 LITDIHFDYKIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAF 162
Cdd:COG0821    82 LVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSLEKDLLEKYGDPTPEALVESAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 163 RHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLAS 242
Cdd:COG0821   162 EHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAGTGRKGTVKSAAGLGILLAEGIGDTIRVSLTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 243 DPVDEIKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTG 322
Cdd:COG0821   242 DPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLIQLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAG 321
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1668256575 323 G-DPNLMYIDGLTHSKVTNENLVDEFEAQIRQRLKK 357
Cdd:COG0821   322 GgGEGLLFKKGEIIRKVPEDEIVEELLEEIEKYVAE 357
ispG PRK00366
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
1-357 0e+00

flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;


Pssm-ID: 234737 [Multi-domain]  Cd Length: 360  Bit Score: 616.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   1 MKPIHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVN 80
Cdd:PRK00366    1 MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAAALPEIKKQLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  81 IPLITDIHFDYKIALKVAEYGADCLRINPGNIGRAD-RVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVE 159
Cdd:PRK00366   81 VPLVADIHFDYRLALAAAEAGADALRINPGNIGKRDeRVREVVEAAKDYGIPIRIGVNAGSLEKDLLEKYGEPTPEALVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 160 SAFRHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVS 239
Cdd:PRK00366  161 SALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTEAGMGFKGTVKSAAGLGALLQEGIGDTIRVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 240 LASDPVDEIKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVG 319
Cdd:PRK00366  241 LTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFDVIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIG 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1668256575 320 LTGGDP-NLMYIDGLTHSKVTNENLVDEFEAQIRQRLKK 357
Cdd:PRK00366  321 IAGGNPkGPVFVDGEKIKTLPEENIVEELEAEIEAYAEE 359
GcpE pfam04551
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
12-353 0e+00

GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids are synthesized by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. GcpE gene of Escherichia coli is involved in this pathway.


Pssm-ID: 428003 [Multi-domain]  Cd Length: 343  Bit Score: 595.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  12 SKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIPLITDIHFDY 91
Cdd:pfam04551   1 TRQVRVGNVPIGGGAPIVVQSMTNTDTRDVEATVAQIRRLAEAGCEIVRVAVPDMEAAEALKEIKKRLPIPLVADIHFDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  92 KIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAFRHIDILDKL 171
Cdd:pfam04551  81 RLALEAAEAGVDKIRINPGNIGSEEKVREVVEAAKERGIPIRIGVNSGSLEKDLLEKYGGPTPEALVESALEHVRILEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 172 NFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLASDPVDEIKVG 251
Cdd:pfam04551 161 GFDDIVISLKASDVPLTVEAYRLLAERCDYPLHLGVTEAGTGESGTIKSAVGIGALLAEGIGDTIRVSLTGDPVEEVKVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 252 FDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTGGDP-NLMYI 330
Cdd:pfam04551 241 KEILQSLGLRKRGVEIISCPTCGRTEIDLIELAEEVEERLEHLKKPLKVAVMGCVVNGPGEAKEADIGIAGGKGeGLLFK 320
                         330       340
                  ....*....|....*....|...
gi 1668256575 331 DGLTHSKVTNENLVDEFEAQIRQ 353
Cdd:pfam04551 321 KGEIVRKVPEEELVEELLEEIEK 343
ispG_gcpE TIGR00612
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-351 3.50e-162

1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown biochemical function has now been identified as an enzyme of the non-mevalonate pathway of IPP biosynthesis. Chlamydial members of the family have a long insert. The family is largely restricted to Bacteria, where it is widely but not universally distributed. No homology can be detected between the GcpE family and other proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273174 [Multi-domain]  Cd Length: 346  Bit Score: 457.27  E-value: 3.50e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   9 RRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIPLITDIH 88
Cdd:TIGR00612   1 RRKTRQVRVGNVKVGGDAPIVVQSMTNTDTHDVDATVAQIRRLEEAGCEIVRVTVPDKESAEALEEIKEGSNVPLVADIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  89 FDYKIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAFRHIDIL 168
Cdd:TIGR00612  81 FAYSYAALAMAKGVAKVRINPGNIGFEERVRDIVEKARRHGKAMRIGVNHGSLERRLLEKYGDPTAEAMVQSALEWAEIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 169 DKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLASDPVDEI 248
Cdd:TIGR00612 161 EKLGFRNVVVSMKASDVLQTVAAYRLLAERSDYPLHLGVTEAGMGVKGIIKSSVGIGILLAMGIGDTIRVSLTDDPVVEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 249 KVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTGG--DPN 326
Cdd:TIGR00612 241 PVAYEILQSLGLRRRGVEIVACPSCGRTGFDLEKVVKEVQEALSHLKTPLKVAVMGCVVNGPGEAKHADIGISGPgtGFA 320
                         330       340
                  ....*....|....*....|....*
gi 1668256575 327 LMYIDGLTHSKVTNENLVDEFEAQI 351
Cdd:TIGR00612 321 WLFKHGKPKAKVPETDMVDELIKLI 345
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
45-85 4.98e-03

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 38.42  E-value: 4.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1668256575  45 VAQIQAIQNAGADLV---------RV-----SVPTMGAAEAFKAIKKQVNIPLIT 85
Cdd:cd02930   227 VALAKALEAAGADILntgigwheaRVptiatSVPRGAFAWATAKLKRAVDIPVIA 281
 
Name Accession Description Interval E-value
IspG COG0821
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
3-357 0e+00

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440583 [Multi-domain]  Cd Length: 363  Bit Score: 622.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   3 PIHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIP 82
Cdd:COG0821     2 PSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAALPEIKKQLPVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  83 LITDIHFDYKIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAF 162
Cdd:COG0821    82 LVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSLEKDLLEKYGDPTPEALVESAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 163 RHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLAS 242
Cdd:COG0821   162 EHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAGTGRKGTVKSAAGLGILLAEGIGDTIRVSLTA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 243 DPVDEIKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTG 322
Cdd:COG0821   242 DPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLIQLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAG 321
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1668256575 323 G-DPNLMYIDGLTHSKVTNENLVDEFEAQIRQRLKK 357
Cdd:COG0821   322 GgGEGLLFKKGEIIRKVPEDEIVEELLEEIEKYVAE 357
ispG PRK00366
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
1-357 0e+00

flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;


Pssm-ID: 234737 [Multi-domain]  Cd Length: 360  Bit Score: 616.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   1 MKPIHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVN 80
Cdd:PRK00366    1 MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAAALPEIKKQLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  81 IPLITDIHFDYKIALKVAEYGADCLRINPGNIGRAD-RVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVE 159
Cdd:PRK00366   81 VPLVADIHFDYRLALAAAEAGADALRINPGNIGKRDeRVREVVEAAKDYGIPIRIGVNAGSLEKDLLEKYGEPTPEALVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 160 SAFRHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVS 239
Cdd:PRK00366  161 SALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTEAGMGFKGTVKSAAGLGALLQEGIGDTIRVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 240 LASDPVDEIKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVG 319
Cdd:PRK00366  241 LTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFDVIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIG 320
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1668256575 320 LTGGDP-NLMYIDGLTHSKVTNENLVDEFEAQIRQRLKK 357
Cdd:PRK00366  321 IAGGNPkGPVFVDGEKIKTLPEENIVEELEAEIEAYAEE 359
GcpE pfam04551
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
12-353 0e+00

GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids are synthesized by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. GcpE gene of Escherichia coli is involved in this pathway.


Pssm-ID: 428003 [Multi-domain]  Cd Length: 343  Bit Score: 595.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  12 SKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIPLITDIHFDY 91
Cdd:pfam04551   1 TRQVRVGNVPIGGGAPIVVQSMTNTDTRDVEATVAQIRRLAEAGCEIVRVAVPDMEAAEALKEIKKRLPIPLVADIHFDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  92 KIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAFRHIDILDKL 171
Cdd:pfam04551  81 RLALEAAEAGVDKIRINPGNIGSEEKVREVVEAAKERGIPIRIGVNSGSLEKDLLEKYGGPTPEALVESALEHVRILEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 172 NFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLASDPVDEIKVG 251
Cdd:pfam04551 161 GFDDIVISLKASDVPLTVEAYRLLAERCDYPLHLGVTEAGTGESGTIKSAVGIGALLAEGIGDTIRVSLTGDPVEEVKVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 252 FDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTGGDP-NLMYI 330
Cdd:pfam04551 241 KEILQSLGLRKRGVEIISCPTCGRTEIDLIELAEEVEERLEHLKKPLKVAVMGCVVNGPGEAKEADIGIAGGKGeGLLFK 320
                         330       340
                  ....*....|....*....|...
gi 1668256575 331 DGLTHSKVTNENLVDEFEAQIRQ 353
Cdd:pfam04551 321 KGEIVRKVPEEELVEELLEEIEK 343
ispG_gcpE TIGR00612
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-351 3.50e-162

1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown biochemical function has now been identified as an enzyme of the non-mevalonate pathway of IPP biosynthesis. Chlamydial members of the family have a long insert. The family is largely restricted to Bacteria, where it is widely but not universally distributed. No homology can be detected between the GcpE family and other proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273174 [Multi-domain]  Cd Length: 346  Bit Score: 457.27  E-value: 3.50e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   9 RRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVNIPLITDIH 88
Cdd:TIGR00612   1 RRKTRQVRVGNVKVGGDAPIVVQSMTNTDTHDVDATVAQIRRLEEAGCEIVRVTVPDKESAEALEEIKEGSNVPLVADIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  89 FDYKIALKVAEYGADCLRINPGNIGRADRVAEVVASAKDHNIPIRIGVNAGSLEKDLQKKYTEPTPEAMVESAFRHIDIL 168
Cdd:TIGR00612  81 FAYSYAALAMAKGVAKVRINPGNIGFEERVRDIVEKARRHGKAMRIGVNHGSLERRLLEKYGDPTAEAMVQSALEWAEIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 169 DKLNFDNYKISLKASEVFMSVFAYKQLASQIDNPLHLGITEAGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLASDPVDEI 248
Cdd:TIGR00612 161 EKLGFRNVVVSMKASDVLQTVAAYRLLAERSDYPLHLGVTEAGMGVKGIIKSSVGIGILLAMGIGDTIRVSLTDDPVVEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 249 KVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDINEPIDAAVIGCVVNGPGEAKAVSVGLTGG--DPN 326
Cdd:TIGR00612 241 PVAYEILQSLGLRRRGVEIVACPSCGRTGFDLEKVVKEVQEALSHLKTPLKVAVMGCVVNGPGEAKHADIGISGPgtGFA 320
                         330       340
                  ....*....|....*....|....*
gi 1668256575 327 LMYIDGLTHSKVTNENLVDEFEAQI 351
Cdd:TIGR00612 321 WLFKHGKPKAKVPETDMVDELIKLI 345
PLN02925 PLN02925
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
4-248 2.32e-69

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase


Pssm-ID: 178513  Cd Length: 733  Bit Score: 230.80  E-value: 2.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   4 IHTIVRRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQV---- 79
Cdd:PLN02925   72 IHKTVRRKTRTVMVGNVALGSEHPIRIQTMTTTDTKDVEATVDQVMRIADKGADIVRITVQGKKEADACFEIKNTLvqkg 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  80 -NIPLITDIHFDYKIALKVAEYgADCLRINPGNIgrADRVAE------------------------VVASAKDHNIPIRI 134
Cdd:PLN02925  152 yNIPLVADIHFAPSVALRVAEC-FDKIRVNPGNF--ADRRAQfekleyteddyqkelehieevftpLVEKCKKYGRAMRI 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 135 GVNAGSLEKDLQKKYTEpTPEAMVESAFRHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQI-----DNPLHLGITE 209
Cdd:PLN02925  229 GTNHGSLSDRIMSYYGD-SPRGMVESAFEFARICRKLDYHNFVFSMKASNPVVMVQAYRLLVAEMyvlgwDYPLHLGVTE 307
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1668256575 210 AGSLRSGSVKSSVGLGLLLAEGIGDTIRVSLASDPVDEI 248
Cdd:PLN02925  308 AGEGEDGRMKSAIGIGTLLQDGLGDTIRVSLTEPPEEEI 346
PRK02048 PRK02048
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional
9-263 9.20e-63

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional


Pssm-ID: 179361  Cd Length: 611  Bit Score: 210.84  E-value: 9.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   9 RRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQVN-----IPL 83
Cdd:PRK02048    8 RRKTSVVNIGATPLGGPNPIRIQSMTNTSTMDTEACVAQAKRIIDAGGEYVRLTTQGVREAENLMNINIGLRsqgymVPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  84 ITDIHFDYKIALKVAEYgADCLRINPGNI---GRA-------------------DRVAEVVASAKDHNIPIRIGVNAGSL 141
Cdd:PRK02048   88 VADVHFNPKVADVAAQY-AEKVRINPGNYvdpGRTfkkleytdeeyaqeiqkirDRFVPFLNICKENHTAIRIGVNHGSL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 142 EKDLQKKYTEpTPEAMVESAFRHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDN-----PLHLGITEAGSLRSG 216
Cdd:PRK02048  167 SDRIMSRYGD-TPEGMVESCMEFLRICVEEHFTDVVISIKASNTVVMVRTVRLLVAVMEAegmhyPLHLGVTEAGDGEDG 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1668256575 217 SVKSSVGLGLLLAEGIGDTIRVSLASDPVDEIKVGFDILKSLGLRQK 263
Cdd:PRK02048  246 RIKSAVGIGALLADGIGDTIRVSLSEEPEAEIPVARKLVDYIRSREN 292
PRK00694 PRK00694
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Validated
9-256 1.15e-62

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Validated


Pssm-ID: 234812  Cd Length: 606  Bit Score: 210.47  E-value: 1.15e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575   9 RRKSKQIFVGNVAIGGDAPISVQSMTNTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGAAEAFKAIKKQ-----VNIPL 83
Cdd:PRK00694   12 RRKTHPVRIGNLFVGSEHSIKIQSMTTTATTDVDGTVRQICALQEWGCDIVRVTVQGLKEAQACEHIKERliqqgISIPL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  84 ITDIHFDYKIALKVAEYgADCLRINPGNI--------GRA--------------DRVAEVVASAKDHNIPIRIGVNAGSL 141
Cdd:PRK00694   92 VADIHFFPQAAMHVADF-VDKVRINPGNYvdkrnmftGKIytdeqyahsllrleEKFSPLVEKCKRLGKAMRIGVNHGSL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 142 EKDLQKKYTEpTPEAMVESAFRHIDILDKLNFDNYKISLKASEVFMSVFAYKQLASQIDN-----PLHLGITEAGSLRSG 216
Cdd:PRK00694  171 SERVMQRYGD-TIEGMVYSALEYIEVCEKLDYRDVVFSMKSSNPKVMVAAYRQLAKDLDArgwlyPLHLGVTEAGSGTDG 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1668256575 217 SVKSSVGLGLLLAEGIGDTIRVSLASDPVDEIKVGFDILK 256
Cdd:PRK00694  250 IIKSAVGIGTLLSEGLGDTIRCSLTGCPTNEIPVCISLLK 289
PLN02925 PLN02925
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
218-325 1.48e-09

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase


Pssm-ID: 178513  Cd Length: 733  Bit Score: 59.39  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 218 VKSSVGLGLLLAEGIGDTIRVSLASDPVDEIK-VGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLEDIne 296
Cdd:PLN02925  584 IQAGSQAGALLVDGLGDGVLLEAPDQDFDFLRnTSFGLLQGCRMRNTKTEYVSCPSCGRTLFDLQEVSAEIREKTSHL-- 661
                          90       100       110
                  ....*....|....*....|....*....|
gi 1668256575 297 P-IDAAVIGCVVNGPGEAKAVSVGLTGGDP 325
Cdd:PLN02925  662 PgVSIAIMGCIVNGPGEMADADFGYVGGAP 691
PRK02048 PRK02048
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional
218-325 3.60e-09

4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional


Pssm-ID: 179361  Cd Length: 611  Bit Score: 58.31  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575 218 VKSSVGLGLLLAEGIGDTIRV----SLASDPVDeiKVGFDILKSLGLRQKGVNLIACPSCSRQKFDVIKVVNELEARLED 293
Cdd:PRK02048  467 LKAAADMGALIFDGLCDGIFLfnqgKLSHVVVD--ATAFGILQAGRLRTSKTEYISCPGCGRTLYDLQSTIARIKEATSH 544
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1668256575 294 INEpIDAAVIGCVVNGPGEAKAVSVGLTGGDP 325
Cdd:PRK02048  545 LKG-LKIGIMGCIVNGPGEMADADYGYVGAGR 575
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
45-85 4.98e-03

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 38.42  E-value: 4.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1668256575  45 VAQIQAIQNAGADLV---------RV-----SVPTMGAAEAFKAIKKQVNIPLIT 85
Cdd:cd02930   227 VALAKALEAAGADILntgigwheaRVptiatSVPRGAFAWATAKLKRAVDIPVIA 281
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
21-103 7.86e-03

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 37.94  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668256575  21 AIGGDAPISVQ-SMT--NTDTNDVKATVAQIQAIQNAGADLVRVSVPTMGA---------------AEAFKAIKKQVNIP 82
Cdd:cd02803   204 AVGPDFPVGVRlSADdfVPGGLTLEEAIEIAKALEEAGVDALHVSGGSYESpppiipppyvpegyfLELAEKIKKAVKIP 283
                          90       100
                  ....*....|....*....|...
gi 1668256575  83 LITD--IHFDYKIALKVAEYGAD 103
Cdd:cd02803   284 VIAVggIRDPEVAEEILAEGKAD 306
 
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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