NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1197401055|gb|ART43638|]
View 

imidazole glycerol phosphate synthase, HisF subunit [Escherichia coli]

Protein Classification

imidazole glycerol phosphate synthase cyclase subunit( domain architecture ID 17615137)

imidazole glycerol phosphate synthase cyclase subunit HisF catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring.

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 1.08e-156

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


:

Pssm-ID: 273241  Cd Length: 254  Bit Score: 435.64  E-value: 1.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  81 GGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAET--GKYHVNQYTGDESrtrvTQWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 1197401055 239 INIGELKAYLATQGVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
 
Name Accession Description Interval E-value
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 1.08e-156

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 435.64  E-value: 1.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  81 GGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAET--GKYHVNQYTGDESrtrvTQWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 1197401055 239 INIGELKAYLATQGVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 1.91e-153

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 427.13  E-value: 1.91e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAEtGKYHVNQYTGDESrtrvTQWETLD 161
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPD-GGWEVYTHGGRKP----TGLDAVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINI 241
Cdd:COG0107   156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                         250
                  ....*....|....*.
gi 1197401055 242 GELKAYLATQGVEIRI 257
Cdd:COG0107   236 AELKAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 1.78e-131

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 371.41  E-value: 1.78e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  84 KSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGkyhvnQYTGDESRTRVTQWETLDWV 163
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGG-----YEVYTHGGRKPTGLDAVEWA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGE 243
Cdd:cd04731   156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                  ....*...
gi 1197401055 244 LKAYLATQ 251
Cdd:cd04731   236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 4.67e-97

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 283.60  E-value: 4.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYdaetGKyhVNQYTGDEsrtrVTQWETLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARR----GK--VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDAdVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-248 3.19e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAeTGKYHVnqYTgdESRTRVTQWETLD 161
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNL-FGGYEV--YT--HNGTKKTKLDPVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAAS--VFHkqii 239
Cdd:NF038364  156 FAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFK---- 231


                  ....*....
gi 1197401055 240 niGELKAYL 248
Cdd:NF038364  232 --GKHRAVL 238
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 9.52e-47

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 162.96  E-value: 9.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYAEEGADELVFYDITASSDGRVVDKSWVS- 67
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  68 --RVAEVIDIPFCVAGGIK-----------SLEDAAKILSFGADKISINSPAL------------ADPTLITRLADRFGV 122
Cdd:PLN02617  306 lrRASENVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVyaaeeyiasgvkTGKTSIEQISRVYGN 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 123 QCIVVGIDTwydaetGKYHVNQYTGDESRT-RVTQ----WETLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617  386 QAVVVSIDP------RRVYVKDPSDVPFKTvKVTNpgpnGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197401055 179 MNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLATQGVEIRI 257
Cdd:PLN02617  460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
 
Name Accession Description Interval E-value
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 1.08e-156

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 435.64  E-value: 1.08e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  81 GGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAET--GKYHVNQYTGDESrtrvTQWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 1197401055 239 INIGELKAYLATQGVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 1.91e-153

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 427.13  E-value: 1.91e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAEtGKYHVNQYTGDESrtrvTQWETLD 161
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPD-GGWEVYTHGGRKP----TGLDAVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINI 241
Cdd:COG0107   156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                         250
                  ....*....|....*.
gi 1197401055 242 GELKAYLATQGVEIRI 257
Cdd:COG0107   236 AELKAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 1.78e-131

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 371.41  E-value: 1.78e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  84 KSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGkyhvnQYTGDESRTRVTQWETLDWV 163
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGG-----YEVYTHGGRKPTGLDAVEWA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGE 243
Cdd:cd04731   156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                  ....*...
gi 1197401055 244 LKAYLATQ 251
Cdd:cd04731   236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 4.67e-97

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 283.60  E-value: 4.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYdaetGKyhVNQYTGDEsrtrVTQWETLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARR----GK--VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDAdVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-235 6.71e-88

glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli, IfnA in P. aeriginosa and PseA in C. jejuni. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensible in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a amoonium channel to the WbuX protein which does the enzymatic work.


Pssm-ID: 132611 [Multi-domain]  Cd Length: 232  Bit Score: 260.28  E-value: 6.71e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  81 GGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGKYHVNQYTGdesrTRVTQWETL 160
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNG----RRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1197401055 161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFH 235
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-248 3.19e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAeTGKYHVnqYTgdESRTRVTQWETLD 161
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNL-FGGYEV--YT--HNGTKKTKLDPVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAAS--VFHkqii 239
Cdd:NF038364  156 FAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFK---- 231


                  ....*....
gi 1197401055 240 niGELKAYL 248
Cdd:NF038364  232 --GKHRAVL 238
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 9.52e-47

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 162.96  E-value: 9.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYAEEGADELVFYDITASSDGRVVDKSWVS- 67
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  68 --RVAEVIDIPFCVAGGIK-----------SLEDAAKILSFGADKISINSPAL------------ADPTLITRLADRFGV 122
Cdd:PLN02617  306 lrRASENVFVPLTVGGGIRdftdangryysSLEVASEYFRSGADKISIGSDAVyaaeeyiasgvkTGKTSIEQISRVYGN 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 123 QCIVVGIDTwydaetGKYHVNQYTGDESRT-RVTQ----WETLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617  386 QAVVVSIDP------RRVYVKDPSDVPFKTvKVTNpgpnGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1197401055 179 MNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLATQGVEIRI 257
Cdd:PLN02617  460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-246 1.48e-35

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 126.44  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:cd04732     1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  82 GIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIdtwyDAETGKYHVNQYtgdesrTRVTQWETLD 161
Cdd:cd04732    81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGL----DAKDGKVATKGW------LETSEVSLEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDADVDGALAASVFHKQIINI 241
Cdd:cd04732   151 LAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDD-IKALKELGVAGVIVGKALYEGKITL 229


                  ....*
gi 1197401055 242 GELKA 246
Cdd:cd04732   230 EEALA 234
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-228 2.61e-29

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 110.51  E-value: 2.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADEL--VfyDITASSDGRVVDKSWVSRVAEVIDIPFCV 79
Cdd:COG0106     1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLhlV--DLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  80 AGGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQcIVVGIDT---------Wydaetgkyhvnqytgdes 150
Cdd:COG0106    79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDArdgkvatdgW------------------ 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197401055 151 rTRVTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDADVDGA 228
Cdd:COG0106   140 -QETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDD-LRALKELGVEGA 215
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-243 9.17e-29

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 109.23  E-value: 9.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   6 IIPCLDVRDGQVVKGVQFR---NHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK13585    5 VIPAVDMKGGKCVQLVQGEpgtETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIdtwyDAETGKYHVnqytgdESRTRVTQWETLDW 162
Cdd:PRK13585   85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSL----DAKDGEVVI------KGWTEKTGYTPVEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDADVDGALAASVFHKQIINIG 242
Cdd:PRK13585  155 AKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDD-LRALKEAGAAGVVVGSALYKGKFTLE 233


                  .
gi 1197401055 243 E 243
Cdd:PRK13585  234 E 234
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-243 1.67e-27

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 105.36  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   6 IIPCLDVRDGQVVKGVQ--FRNHEIIGD-IVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQgdYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIdtwyDAETGKYHVNQYtgdesrTRVTQWETLDW 162
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSL----DARGGEVAVKGW------LEKSEVSLEEL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDADVDGALAASVFHKQIINIG 242
Cdd:TIGR00007 151 AKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDD-LIALKKLGVYGVIVGKALYEGKITLE 229


                  .
gi 1197401055 243 E 243
Cdd:TIGR00007 230 E 230
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-246 4.74e-24

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 96.57  E-value: 4.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVVKGVQFR---------NHEIIGDIVPLAKRYAEEGADELVFYDITASSdGRVVDKSWVSRVAEVIDI 75
Cdd:cd04723     1 RIIPVIDLKDGVVVHGVGGDrdnyrpitsNLCSTSDPLDVARAYKELGFRGLYIADLDAIM-GRGDNDEAIRELAAAWPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  76 PFCVAGGIKSLEDAAKILSFGADKISINSPALADPTLITRLAdRFGVQCIVVGIDtwydaetgkyHVNQYTGDESRTRVT 155
Cdd:cd04723    80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLA-ALGEQRLVLSLD----------FRGGQLLKPTDFIGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 156 QwetlDWVQEVQKRgAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDADVDGALAASVFH 235
Cdd:cd04723   149 E----ELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVED-LELLKKLGASGALVASALH 222

                         250
                  ....*....|.
gi 1197401055 236 KQIINIGELKA 246
Cdd:cd04723   223 DGGLTLEDVVR 233
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-228 3.16e-22

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 91.67  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   6 IIPCLDVRDGQVVKGVQ--FRNHEIIG-DIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK00748    3 IIPAIDLKDGKCVRLYQgdYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQcIVVGIdtwyDAETGKYHVNQYTgDESRTRVTqwetlDW 162
Cdd:PRK00748   83 IRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGL----DARDGKVATDGWL-ETSGVTAE-----DL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197401055 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHfLEAFRDA-DVDGA 228
Cdd:PRK00748  152 AKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDD-IKALKGLgAVEGV 217
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-229 8.46e-12

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 63.05  E-value: 8.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   6 IIPCLDVRDGQVVKGVQFR--NHEIIGDIVPLAKRYAEEGADELVFYDITASSdGRVVDKSWVSRVAEVIDIPFCVAGGI 83
Cdd:PRK14024    6 LLPAVDVVDGQAVRLVQGEagSETSYGSPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELSGGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  84 KSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQcIVVGIDtwydaetgkyhVNQYT----------GDesrtr 153
Cdd:PRK14024   85 RDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLD-----------VRGHTlaargwtrdgGD----- 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197401055 154 vtQWETLDwvqEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHF--LEAFRDADVDGAL 229
Cdd:PRK14024  148 --LWEVLE---RLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLraLAELVPLGVEGAI 220
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-247 1.18e-10

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 172604  Cd Length: 241  Bit Score: 60.03  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   6 IIPCLDVRDGQVVKGVQFRNHEII---GDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDiPFCVAGG 82
Cdd:PRK14114    3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALADPTLITRLADrFGVQcIVVGIDTwydaETGKYHVNQYTGDEsrtrvtQWETLDW 162
Cdd:PRK14114   82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE-IDVE-PVFSLDT----RGGKVAFKGWLAEE------EIDPVSL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAG---TMEHFLEAFRDAD--VDGALAASVFHKQ 237
Cdd:PRK14114  150 LKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISsenSLKTAQRVHRETNglLKGVIVGRAFLEG 229

                         250
                  ....*....|
gi 1197401055 238 IINIGELKAY 247
Cdd:PRK14114  230 ILTVEVMKRY 239
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-189 1.83e-08

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 237439  Cd Length: 232  Bit Score: 53.59  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVVKGVQFRNHE--IIGDIVPLAKRYAEEGADELVFYDITASsDGRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK13586    3 KIIPSIDISLGKAVKRIRGVKGTglILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDtwYDaetgkyhvnqytgDESRTRVTQW----- 157
Cdd:PRK13586   82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID--YD-------------NTKRVLIRGWkeksm 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1197401055 158 ETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYD 189
Cdd:PRK13586  147 EVIDGIKKVNELELLGIIFTYISNEGTTKGID 178
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-245 2.20e-06

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 167709  Cd Length: 228  Bit Score: 47.46  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVVKGVQFRNHEI--IGDIVPLAKRYAEEgADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK04128    3 RIYPAIDLMNGKAVRLYKGRKEEVkvYGDPVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  83 IKSLEDAAKILSFGADKISINSPALaDPTLITRLADRFGvqcivvGIDTWYDAETGKYHVNQYTGDESRTRVTQWETLdw 162
Cdd:PRK04128   82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFE------GITVSLDVKGGRIAVKGWLEESSIKVEDAYEML-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 163 vqevqKRGAGEIVLNMMNQDGVRNGYD-LEQLKKVREvchvpLIASGGAGTMEHFLEAFRDAdVDGALAASVFHKQIINI 241
Cdd:PRK04128  153 -----KNYVNRFIYTSIERDGTLTGIEeIERFWGDEE-----FIYAGGVSSAEDVKKLAEIG-FSGVIIGKALYEGRISL 221


                  ....
gi 1197401055 242 GELK 245
Cdd:PRK04128  222 EELL 225
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 4-98 3.16e-06

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 46.70  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   4 KRIIPCLDVRDGQV-VKGVQfRNHEIigDIVPLAKRYAEEGADELVFYDItaSSDGRV--VDKSWVSRVAEVIDIPFCVA 80
Cdd:cd04732   122 ERIVVGLDAKDGKVaTKGWL-ETSEV--SLEELAKRFEELGVKAIIYTDI--SRDGTLsgPNFELYKELAAATGIPVIAS 196

                          90
                  ....*....|....*...
gi 1197401055  81 GGIKSLEDAAKILSFGAD 98
Cdd:cd04732   197 GGVSSLDDIKALKELGVA 214
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 29-118 3.81e-06

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: 47.18  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  29 IGDIVPLAKRYAEEGAD---------ELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKIL-SFGAD 98
Cdd:cd02803   227 LEEAIEIAKALEEAGVDalhvsggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILaEGKAD 306

                          90       100
                  ....*....|....*....|
gi 1197401055  99 KISINSPALADPTLITRLAD 118
Cdd:cd02803   307 LVALGRALLADPDLPNKARE 326
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 31-120 5.51e-06

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 46.63  E-value: 5.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  31 DIVPLAKRYAEEGADELV--------FYDITAssdgrvvDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILS-FGADKIS 101
Cdd:COG0042   147 NALEFARIAEDAGAAALTvhgrtreqRYKGPA-------DWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEeTGCDGVM 219

                          90
                  ....*....|....*....
gi 1197401055 102 INSPALADPTLITRLADRF 120
Cdd:COG0042   220 IGRGALGNPWLFREIDAYL 238
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-104 5.52e-06

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 46.05  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQVV-KGVQfrnhEIIG-DIVPLAKRYAEEGADELVFYDItaSSDGRV--VDKSWVSRVAEVIDIPFCVA 80
Cdd:PRK13585  126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNV--DVEGLLegVNTEPVKELVDSVDIPVIAS 199

                          90       100
                  ....*....|....*....|....
gi 1197401055  81 GGIKSLEDAAKILSFGADKISINS 104
Cdd:PRK13585  200 GGVTTLDDLRALKEAGAAGVVVGS 223
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 31-118 1.47e-05

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 45.55  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  31 DIVPLAKRYAEEGAD--ELV--FYDITASSDGRVVDKSWVS---RVAEVIDIPFCVAGGIKSLEDAAKILSFG-ADKISI 102
Cdd:COG1902   237 ESVELAKALEEAGVDylHVSsgGYEPDAMIPTIVPEGYQLPfaaRIRKAVGIPVIAVGGITTPEQAEAALASGdADLVAL 316

                          90
                  ....*....|....*.
gi 1197401055 103 NSPALADPTLITRLAD 118
Cdd:COG1902   317 GRPLLADPDLPNKAAA 332
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 4-88 2.42e-05

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 44.11  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   4 KRIIPCLDVRDGQV-VKGvqFRNHEIIgDIVPLAKRYAEEGADELVFYDItaSSDGRV--VDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKG--WLEKSEV-SLEELAKRLEELGLEGIIYTDI--SRDGTLsgPNFELTKELVKAVNVPVIAS 195


                  ....*...
gi 1197401055  81 GGIKSLED 88
Cdd:TIGR00007 196 GGVSSIDD 203
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 51-237 1.12e-04

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional


Pssm-ID: 172156  Cd Length: 234  Bit Score: 42.12  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  51 DITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILSFGADKISINSPALADPTLITRLADRFGVQcIVVGID 130
Cdd:PRK13587   53 DLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 131 TWYDaetgKYHVNQYTGDesrtrvTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGA 210
Cdd:PRK13587  132 AYGE----DIKVNGWEED------TELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGI 201

                         170       180
                  ....*....|....*....|....*..
gi 1197401055 211 GTMEHfLEAFRDADVDGALAASVFHKQ 237
Cdd:PRK13587  202 RHQQD-IQRLASLNVHAAIIGKAAHQA 227
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 58-118 1.19e-04

Old yellow enzyme (OYE)-related FMN binding domain, group 4. 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. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 42.58  E-value: 1.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197401055  58 GRVVDKSWVSRVAEVID--IPFCVAGGIKSLEDAAKILSFGADKISINSPALADPTLITRLAD 118
Cdd:cd04735   266 GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKE 328
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 35-120 2.05e-04

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 41.33  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  35 LAKRYAEEGADELVFYditassdGRV--------VDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILS-FGADKISINSP 105
Cdd:cd02801   143 LAKALEDAGASALTVH-------GRTreqrysgpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRG 215

                          90
                  ....*....|....*
gi 1197401055 106 ALADPTLITRLADRF 120
Cdd:cd02801   216 ALGNPWLFREIKELL 230
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
44-100 2.26e-04

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 41.30  E-value: 2.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197401055  44 ADEL----VFYdITASSD-GRVVDKSWVSRVAEVI-DIPFCVAGGIKSLEDAAKILSFGADKI 100
Cdd:COG1646   161 AEEYlgmpIVY-LEYGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGADTI 222
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 58-102 9.08e-04

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: 39.53  E-value: 9.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1197401055  58 GRVVDKSWVSRVAEVI-DIPFCVAGGIKSLEDAAKILSFGADKISI 102
Cdd:cd02812   158 GAYGPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVV 203
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 31-113 1.51e-03

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 39.23  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  31 DIVPLAKRYAEEGADELV--------FYDITAssdgrvvDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILSF-GADKIS 101
Cdd:pfam01207 139 NAVEIAKIVEDAGAQALTvhgrtraqNYEGTA-------DWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYtGADGVM 211

                          90
                  ....*....|..
gi 1197401055 102 INSPALADPTLI 113
Cdd:pfam01207 212 IGRGALGNPWLF 223
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 156-231 1.54e-03

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 39.01  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055 156 QWETLDWVQEVQKRGAGEIVL-----NMMNQDGVrngyDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALA 230
Cdd:cd02801   137 EEETLELAKALEDAGASALTVhgrtrEQRYSGPA----DWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMI 212


                  .
gi 1197401055 231 A 231
Cdd:cd02801   213 G 213
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-104 1.90e-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: 38.34  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055  26 HEIIGDIVPLAKRYAEEGADELV---FYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAAKILSFGADKISI 102
Cdd:cd04722   119 VKLSPTGELAAAAAEEAGVDEVGlgnGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIV 198


                  ..
gi 1197401055 103 NS 104
Cdd:cd04722   199 GS 200
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 5-97 2.49e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 38.12  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197401055   5 RIIPCLDVRDGQV-VKGVQfrnhEIIG-DIVPLAKRYAEEGADELVFYDItaSSDGRV--VDKSWVSRVAEVIDIPFCVA 80
Cdd:PRK00748  123 KIVVGLDARDGKVaTDGWL----ETSGvTAEDLAKRFEDAGVKAIIYTDI--SRDGTLsgPNVEATRELAAAVPIPVIAS 196

                          90
                  ....*....|....*..
gi 1197401055  81 GGIKSLEDAAKILSFGA 97
Cdd:PRK00748  197 GGVSSLDDIKALKGLGA 213
ER_like_FMN cd02931
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ...
 64-116 7.06e-03

Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.


Pssm-ID: 239241 [Multi-domain]  Cd Length: 382  Bit Score: 37.49  E-value: 7.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1197401055  64 SWVSRVAEVIDIPFCVAGGIKSLEDAAKILSFG-ADKISINSPALADPTLITRL 116
Cdd:cd02931   295 PYCKALKEVVDVPVIMAGRMEDPELASEAINEGiADMISLGRPLLADPDVVNKI 348
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 66-118 7.52e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 3. 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. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.


Pssm-ID: 240085 [Multi-domain]  Cd Length: 343  Bit Score: 37.21  E-value: 7.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1197401055  66 VSRVAEVIDIPFCVAGGIKSLEDAAKILSFG-ADKISINSPALADPTLITRLAD 118
Cdd:cd04734   277 AARIKQAVDLPVFHAGRIRDPAEAEQALAAGhADMVGMTRAHIADPHLVAKARE 330
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH