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Conserved domains on  [gi|494857327|ref|WP_007583427|]
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MULTISPECIES: flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase [Pseudoalteromonas]

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 PRK00366
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
1-360 0e+00

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


:

Pssm-ID: 234737 [Multi-domain]  Cd Length: 360  Bit Score: 629.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   1 MFSESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVT 80
Cdd:PRK00366   1 MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAAALPEIKKQLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  81 IPLVADIHFDYRIALKVAKYGVDCLRINPGNIGS-EERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLE 159
Cdd:PRK00366  81 VPLVADIHFDYRLALAAAEAGADALRINPGNIGKrDERVREVVEAAKDYGIPIRIGVNAGSLEKDLLEKYGEPTPEALVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 160 SAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVS 239
Cdd:PRK00366 161 SALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTEAGMGFKGTVKSAAGLGALLQEGIGDTIRVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 240 LAADPVQEIKVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIG 319
Cdd:PRK00366 241 LTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFDVIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIG 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494857327 320 LAGANRRSGLYINGERQKaRIDNNNIVDQLEGYVRDFIEKK 360
Cdd:PRK00366 321 IAGGNPKGPVFVDGEKIK-TLPEENIVEELEAEIEAYAEER 360
 
Name Accession Description Interval E-value
ispG PRK00366
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
1-360 0e+00

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


Pssm-ID: 234737 [Multi-domain]  Cd Length: 360  Bit Score: 629.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   1 MFSESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVT 80
Cdd:PRK00366   1 MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAAALPEIKKQLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  81 IPLVADIHFDYRIALKVAKYGVDCLRINPGNIGS-EERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLE 159
Cdd:PRK00366  81 VPLVADIHFDYRLALAAAEAGADALRINPGNIGKrDERVREVVEAAKDYGIPIRIGVNAGSLEKDLLEKYGEPTPEALVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 160 SAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVS 239
Cdd:PRK00366 161 SALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTEAGMGFKGTVKSAAGLGALLQEGIGDTIRVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 240 LAADPVQEIKVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIG 319
Cdd:PRK00366 241 LTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFDVIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIG 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494857327 320 LAGANRRSGLYINGERQKaRIDNNNIVDQLEGYVRDFIEKK 360
Cdd:PRK00366 321 IAGGNPKGPVFVDGEKIK-TLPEENIVEELEAEIEAYAEER 360
IspG COG0821
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
3-363 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 494857327   3 SESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIP 82
Cdd:COG0821    2 PSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAALPEIKKQLPVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  83 LVADIHFDYRIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAM 162
Cdd:COG0821   82 LVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSLEKDLLEKYGDPTPEALVESAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 163 RHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAA 242
Cdd:COG0821  162 EHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAGTGRKGTVKSAAGLGILLAEGIGDTIRVSLTA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 243 DPVQEIKVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAG 322
Cdd:COG0821  242 DPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLIQLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAG 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494857327 323 ANRRSGLYINGErQKARIDNNNIVDQLEGYVRDFIEKKQSQ 363
Cdd:COG0821  322 GGGEGLLFKKGE-IIRKVPEDEIVEELLEEIEKYVAERYGE 361
GcpE pfam04551
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
13-355 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 494857327   13 TR-INVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIHFDY 91
Cdd:pfam04551   1 TRqVRVGNVPIGGGAPIVVQSMTNTDTRDVEATVAQIRRLAEAGCEIVRVAVPDMEAAEALKEIKKRLPIPLVADIHFDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   92 RIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAMRHVDILRRL 171
Cdd:pfam04551  81 RLALEAAEAGVDKIRINPGNIGSEEKVREVVEAAKERGIPIRIGVNSGSLEKDLLEKYGGPTPEALVESALEHVRILEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  172 DFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEIKVG 251
Cdd:pfam04551 161 GFDDIVISLKASDVPLTVEAYRLLAERCDYPLHLGVTEAGTGESGTIKSAVGIGALLAEGIGDTIRVSLTGDPVEEVKVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  252 FDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAGANRRSGLYI 331
Cdd:pfam04551 241 KEILQSLGLRKRGVEIISCPTCGRTEIDLIELAEEVEERLEHLKKPLKVAVMGCVVNGPGEAKEADIGIAGGKGEGLLFK 320
                         330       340
                  ....*....|....*....|....
gi 494857327  332 NGERQKaRIDNNNIVDQLEGYVRD 355
Cdd:pfam04551 321 KGEIVR-KVPEEELVEELLEEIEK 343
ispG_gcpE TIGR00612
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-350 2.06e-155

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: 440.71  E-value: 2.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327    9 RRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIH 88
Cdd:TIGR00612   1 RRKTRQVRVGNVKVGGDAPIVVQSMTNTDTHDVDATVAQIRRLEEAGCEIVRVTVPDKESAEALEEIKEGSNVPLVADIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   89 FDYRIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAMRHVDIL 168
Cdd:TIGR00612  81 FAYSYAALAMAKGVAKVRINPGNIGFEERVRDIVEKARRHGKAMRIGVNHGSLERRLLEKYGDPTAEAMVQSALEWAEIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  169 RRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEI 248
Cdd:TIGR00612 161 EKLGFRNVVVSMKASDVLQTVAAYRLLAERSDYPLHLGVTEAGMGVKGIIKSSVGIGILLAMGIGDTIRVSLTDDPVVEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  249 KVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAGANRRSG 328
Cdd:TIGR00612 241 PVAYEILQSLGLRRRGVEIVACPSCGRTGFDLEKVVKEVQEALSHLKTPLKVAVMGCVVNGPGEAKHADIGISGPGTGFA 320
                         330       340
                  ....*....|....*....|..
gi 494857327  329 LYINGERQKARIDNNNIVDQLE 350
Cdd:TIGR00612 321 WLFKHGKPKAKVPETDMVDELI 342
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
32-180 8.12e-03

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 37.70  E-value: 8.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  32 SMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIHFDYRIALKVAkygvdclRINPGN 111
Cdd:cd01292   56 GSTPPPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLA-------GPYTAT 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494857327 112 IGSEERIRAVVDSAREHNIPIRIGVNGGSLE----RDLQEKYGEPTPEALLESAMRHVDILRRLDFDQFKISV 180
Cdd:cd01292  129 GLSDESLRRVLEEARKLGLPVVIHAGELPDPtralEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEV 201
 
Name Accession Description Interval E-value
ispG PRK00366
flavodoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase;
1-360 0e+00

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


Pssm-ID: 234737 [Multi-domain]  Cd Length: 360  Bit Score: 629.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   1 MFSESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVT 80
Cdd:PRK00366   1 MRPSTPIPRRKTRQVKVGNVPIGGDAPIVVQSMTNTDTADVEATVAQIKRLARAGCEIVRVAVPDMEAAAALPEIKKQLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  81 IPLVADIHFDYRIALKVAKYGVDCLRINPGNIGS-EERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLE 159
Cdd:PRK00366  81 VPLVADIHFDYRLALAAAEAGADALRINPGNIGKrDERVREVVEAAKDYGIPIRIGVNAGSLEKDLLEKYGEPTPEALVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 160 SAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVS 239
Cdd:PRK00366 161 SALRHAKILEELGFDDIKISVKASDVQDLIAAYRLLAKRCDYPLHLGVTEAGMGFKGTVKSAAGLGALLQEGIGDTIRVS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 240 LAADPVQEIKVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIG 319
Cdd:PRK00366 241 LTADPVEEVKVGQEILQSLGLRSRGPEVISCPTCGRTEFDVIQELAEVEQRLEHIKMPLKVAVMGCVVNGPGEAKEADIG 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494857327 320 LAGANRRSGLYINGERQKaRIDNNNIVDQLEGYVRDFIEKK 360
Cdd:PRK00366 321 IAGGNPKGPVFVDGEKIK-TLPEENIVEELEAEIEAYAEER 360
IspG COG0821
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
3-363 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 494857327   3 SESPIKRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIP 82
Cdd:COG0821    2 PSSPIPRRKTRQVRVGNVAIGGGAPISVQSMTNTDTADVEATVAQIKALAEAGCEIVRVAVPDEEAAAALPEIKKQLPVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  83 LVADIHFDYRIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAM 162
Cdd:COG0821   82 LVADIHFDYRLALEAAEAGVDKLRINPGNIGSDEKVREVVEAAKERGIPIRIGVNAGSLEKDLLEKYGDPTPEALVESAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 163 RHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAA 242
Cdd:COG0821  162 EHARILEELGFDDIKISLKASDVQDTIAAYRLLAERCDYPLHLGVTEAGTGRKGTVKSAAGLGILLAEGIGDTIRVSLTA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 243 DPVQEIKVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAG 322
Cdd:COG0821  242 DPVEEVKVAQEILKSLGLRSRGPEVISCPTCGRTEIDLIQLAEEVEERLRDIKEPLKVAVMGCVVNGPGEAKEADIGIAG 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 494857327 323 ANRRSGLYINGErQKARIDNNNIVDQLEGYVRDFIEKKQSQ 363
Cdd:COG0821  322 GGGEGLLFKKGE-IIRKVPEDEIVEELLEEIEKYVAERYGE 361
GcpE pfam04551
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
13-355 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 494857327   13 TR-INVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIHFDY 91
Cdd:pfam04551   1 TRqVRVGNVPIGGGAPIVVQSMTNTDTRDVEATVAQIRRLAEAGCEIVRVAVPDMEAAEALKEIKKRLPIPLVADIHFDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   92 RIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAMRHVDILRRL 171
Cdd:pfam04551  81 RLALEAAEAGVDKIRINPGNIGSEEKVREVVEAAKERGIPIRIGVNSGSLEKDLLEKYGGPTPEALVESALEHVRILEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  172 DFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEIKVG 251
Cdd:pfam04551 161 GFDDIVISLKASDVPLTVEAYRLLAERCDYPLHLGVTEAGTGESGTIKSAVGIGALLAEGIGDTIRVSLTGDPVEEVKVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  252 FDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAGANRRSGLYI 331
Cdd:pfam04551 241 KEILQSLGLRKRGVEIISCPTCGRTEIDLIELAEEVEERLEHLKKPLKVAVMGCVVNGPGEAKEADIGIAGGKGEGLLFK 320
                         330       340
                  ....*....|....*....|....
gi 494857327  332 NGERQKaRIDNNNIVDQLEGYVRD 355
Cdd:pfam04551 321 KGEIVR-KVPEEELVEELLEEIEK 343
ispG_gcpE TIGR00612
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-350 2.06e-155

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: 440.71  E-value: 2.06e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327    9 RRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIH 88
Cdd:TIGR00612   1 RRKTRQVRVGNVKVGGDAPIVVQSMTNTDTHDVDATVAQIRRLEEAGCEIVRVTVPDKESAEALEEIKEGSNVPLVADIH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   89 FDYRIALKVAKYGVDCLRINPGNIGSEERIRAVVDSAREHNIPIRIGVNGGSLERDLQEKYGEPTPEALLESAMRHVDIL 168
Cdd:TIGR00612  81 FAYSYAALAMAKGVAKVRINPGNIGFEERVRDIVEKARRHGKAMRIGVNHGSLERRLLEKYGDPTAEAMVQSALEWAEIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  169 RRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQPLHLGITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEI 248
Cdd:TIGR00612 161 EKLGFRNVVVSMKASDVLQTVAAYRLLAERSDYPLHLGVTEAGMGVKGIIKSSVGIGILLAMGIGDTIRVSLTDDPVVEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  249 KVGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDIIEPMSVSVIGCVVNGPGEALVSDIGLAGANRRSG 328
Cdd:TIGR00612 241 PVAYEILQSLGLRRRGVEIVACPSCGRTGFDLEKVVKEVQEALSHLKTPLKVAVMGCVVNGPGEAKHADIGISGPGTGFA 320
                         330       340
                  ....*....|....*....|..
gi 494857327  329 LYINGERQKARIDNNNIVDQLE 350
Cdd:TIGR00612 321 WLFKHGKPKAKVPETDMVDELI 342
PRK02048 PRK02048
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional
8-294 3.90e-71

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


Pssm-ID: 179361  Cd Length: 611  Bit Score: 233.19  E-value: 3.90e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   8 KRRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQV-----TIP 82
Cdd:PRK02048   7 SRRKTSVVNIGATPLGGPNPIRIQSMTNTSTMDTEACVAQAKRIIDAGGEYVRLTTQGVREAENLMNINIGLrsqgyMVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  83 LVADIHFDYRIALKVAKYgVDCLRINPGNI----------------------GSEERIRAVVDSAREHNIPIRIGVNGGS 140
Cdd:PRK02048  87 LVADVHFNPKVADVAAQY-AEKVRINPGNYvdpgrtfkkleytdeeyaqeiqKIRDRFVPFLNICKENHTAIRIGVNHGS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 141 LERDLQEKYGEpTPEALLESAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQ-----PLHLGITEAGGMRS 215
Cdd:PRK02048 166 LSDRIMSRYGD-TPEGMVESCMEFLRICVEEHFTDVVISIKASNTVVMVRTVRLLVAVMEAegmhyPLHLGVTEAGDGED 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494857327 216 GSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEIKVGFDILNSLRIRsRGINFIACPSCSRqeFDVVSTMNQLEERLEDI 294
Cdd:PRK02048 245 GRIKSAVGIGALLADGIGDTIRVSLSEEPEAEIPVARKLVDYIRSR-ENHPYIPGMEAPG--FDYLSPSRRKTRAVRNI 320
PLN02925 PLN02925
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
9-248 1.46e-68

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


Pssm-ID: 178513  Cd Length: 733  Bit Score: 228.87  E-value: 1.46e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   9 RRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQV-----TIPL 83
Cdd:PLN02925  77 RRKTRTVMVGNVALGSEHPIRIQTMTTTDTKDVEATVDQVMRIADKGADIVRITVQGKKEADACFEIKNTLvqkgyNIPL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  84 VADIHFDYRIALKVAKYgVDCLRINPGNIGS----------------------EERIRAVVDSAREHNIPIRIGVNGGSL 141
Cdd:PLN02925 157 VADIHFAPSVALRVAEC-FDKIRVNPGNFADrraqfekleyteddyqkelehiEEVFTPLVEKCKKYGRAMRIGTNHGSL 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 142 ERDLQEKYGEpTPEALLESAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEI-----DQPLHLGITEAGGMRSG 216
Cdd:PLN02925 236 SDRIMSYYGD-SPRGMVESAFEFARICRKLDYHNFVFSMKASNPVVMVQAYRLLVAEMyvlgwDYPLHLGVTEAGEGEDG 314
                        250       260       270
                 ....*....|....*....|....*....|..
gi 494857327 217 SVKSAVGLGMLLAEGIGDTLRVSLAADPVQEI 248
Cdd:PLN02925 315 RMKSAIGIGTLLQDGLGDTIRVSLTEPPEEEI 346
PRK00694 PRK00694
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Validated
1-255 9.47e-66

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


Pssm-ID: 234812  Cd Length: 606  Bit Score: 218.94  E-value: 9.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327   1 MFSESPIK---RRKSTRINVGNVPIGDGAPIAVQSMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKE 77
Cdd:PRK00694   1 MMATPCIQnafRRKTHPVRIGNLFVGSEHSIKIQSMTTTATTDVDGTVRQICALQEWGCDIVRVTVQGLKEAQACEHIKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  78 Q-----VTIPLVADIHFDYRIALKVAKYgVDCLRINPGN----------------------IGSEERIRAVVDSAREHNI 130
Cdd:PRK00694  81 RliqqgISIPLVADIHFFPQAAMHVADF-VDKVRINPGNyvdkrnmftgkiytdeqyahslLRLEEKFSPLVEKCKRLGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 131 PIRIGVNGGSLERDLQEKYGEpTPEALLESAMRHVDILRRLDFDQFKISVKASDVFLAVGAYRLLAKEIDQ-----PLHL 205
Cdd:PRK00694 160 AMRIGVNHGSLSERVMQRYGD-TIEGMVYSALEYIEVCEKLDYRDVVFSMKSSNPKVMVAAYRQLAKDLDArgwlyPLHL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 494857327 206 GITEAGGMRSGSVKSAVGLGMLLAEGIGDTLRVSLAADPVQEIKVGFDIL 255
Cdd:PRK00694 239 GVTEAGSGTDGIIKSAVGIGTLLSEGLGDTIRCSLTGCPTNEIPVCISLL 288
PRK02048 PRK02048
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Provisional
218-343 8.68e-14

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


Pssm-ID: 179361  Cd Length: 611  Bit Score: 72.56  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 218 VKSAVGLGMLLAEGIGDTLRVsLAADPVQEIKV---GFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERLEDI 294
Cdd:PRK02048 467 LKAAADMGALIFDGLCDGIFL-FNQGKLSHVVVdatAFGILQAGRLRTSKTEYISCPGCGRTLYDLQSTIARIKEATSHL 545
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494857327 295 IEpMSVSVIGCVVNGPGEALVSDIGLAGANR-RSGLYingeRQKARIDNN 343
Cdd:PRK02048 546 KG-LKIGIMGCIVNGPGEMADADYGYVGAGRgKISLY----KQKECVEKN 590
PLN02925 PLN02925
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
218-355 1.40e-13

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


Pssm-ID: 178513  Cd Length: 733  Bit Score: 72.10  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 218 VKSAVGLGMLLAEGIGDTLRVSLAADPVQEIK-VGFDILNSLRIRSRGINFIACPSCSRQEFDVVSTMNQLEERlEDIIE 296
Cdd:PLN02925 584 IQAGSQAGALLVDGLGDGVLLEAPDQDFDFLRnTSFGLLQGCRMRNTKTEYVSCPSCGRTLFDLQEVSAEIREK-TSHLP 662
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327 297 PMSVSVIGCVVNGPGEALVSDIG-LAGANRRSGLYINGERQKARIDNNNIVDQLEGYVRD 355
Cdd:PLN02925 663 GVSIAIMGCIVNGPGEMADADFGyVGGAPGKIDLYVGKEVVKRGIAMEEATDALIQLIKD 722
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
32-180 8.12e-03

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 37.70  E-value: 8.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494857327  32 SMTNTDTMDVDATVAQIQAIQDAGADIVRVSVPTMDAAEAFKSIKEQVTIPLVADIHFDYRIALKVAkygvdclRINPGN 111
Cdd:cd01292   56 GSTPPPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLA-------GPYTAT 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494857327 112 IGSEERIRAVVDSAREHNIPIRIGVNGGSLE----RDLQEKYGEPTPEALLESAMRHVDILRRLDFDQFKISV 180
Cdd:cd01292  129 GLSDESLRRVLEEARKLGLPVVIHAGELPDPtralEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEV 201
 
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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