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Conserved domains on  [gi|763000671|ref|WP_043894587|]
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imidazole glycerol phosphate synthase subunit HisF [Glaesserella parasuis]

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

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List of domain hits

 Name Accession Description Interval E-value
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 4.93e-152

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


:

Pssm-ID: 273241  Cd Length: 254  Bit Score: 423.70  E-value: 4.93e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   81 GGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKET--GKYWVNQYTGDEKrtrqTNWQ 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 763000671  239 INIGELKEYLAQQNVEIR 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 4.93e-152

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 423.70  E-value: 4.93e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   81 GGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKET--GKYWVNQYTGDEKrtrqTNWQ 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 763000671  239 INIGELKEYLAQQNVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 9.78e-149

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: 415.19  E-value: 9.78e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEkETGKYWVNQYTGDEKrtrqTNWQLLD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGGRKP----TGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINI 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*.
gi 763000671 242 GELKEYLAQQNVEIRR 257
Cdd:COG0107  236 AELKAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 5.46e-126

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: 357.16  E-value: 5.46e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  84 KTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWfeKETGKYWvnqYTGDEKRTRQTNWQLLDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAK--RRGDGGY---EVYTHGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINIGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*...
gi 763000671 244 LKEYLAQQ 251
Cdd:cd04731  236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 5.64e-95

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: 278.21  E-value: 5.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKetgkywVNQYTGDEKrtrqTNWQLLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRED----TGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763000671  162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFiDANVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELF-TEGVDGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 3.11e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGID---SWFeketGKYWVnqYTGDekRTRQTNWQ 158
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEV--YTHN--GTKKTKLD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAAS--VFHK 236
Cdd:NF038364 153 PVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKG 232


                 .
gi 763000671 237 Q 237
Cdd:NF038364 233 K 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-256 7.17e-45

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 157.95  E-value: 7.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYAEEGADELVFYDITASSDGRTVDKSWVE- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  68 --RVAEVIDIPFCVAGGIKTIDD-----------AEQIFAFGADKISINSPAL--ADPDL----------ISRLADRFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIasgvktgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 123 QAIVVGIDSwfeketGKYWVNQYTGDEKRTRQT-----NWQLLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617 386 QAVVVSIDP------RRVYVKDPSDVPFKTVKVtnpgpNGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763000671 179 MNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINIGELKEYLAQQNVEIR 256
Cdd:PLN02617 460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
 
Name Accession Description Interval E-value
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 4.93e-152

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 423.70  E-value: 4.93e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   81 GGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKET--GKYWVNQYTGDEKrtrqTNWQ 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 763000671  239 INIGELKEYLAQQNVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 9.78e-149

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: 415.19  E-value: 9.78e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEkETGKYWVNQYTGDEKrtrqTNWQLLD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGGRKP----TGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINI 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*.
gi 763000671 242 GELKEYLAQQNVEIRR 257
Cdd:COG0107  236 AELKAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 5.46e-126

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: 357.16  E-value: 5.46e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  84 KTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWfeKETGKYWvnqYTGDEKRTRQTNWQLLDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAK--RRGDGGY---EVYTHGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINIGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*...
gi 763000671 244 LKEYLAQQ 251
Cdd:cd04731  236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 5.64e-95

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: 278.21  E-value: 5.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKetgkywVNQYTGDEKrtrqTNWQLLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRED----TGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763000671  162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFiDANVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELF-TEGVDGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-235 3.12e-83

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: 248.72  E-value: 3.12e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   81 GGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKETGKYWVNQYTGdekrTRQTNWQLL 160
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNG----RRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763000671  161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFH 235
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 3.11e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGID---SWFeketGKYWVnqYTGDekRTRQTNWQ 158
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEV--YTHN--GTKKTKLD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAAS--VFHK 236
Cdd:NF038364 153 PVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKG 232


                 .
gi 763000671 237 Q 237
Cdd:NF038364 233 K 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-256 7.17e-45

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 157.95  E-value: 7.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYAEEGADELVFYDITASSDGRTVDKSWVE- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  68 --RVAEVIDIPFCVAGGIKTIDD-----------AEQIFAFGADKISINSPAL--ADPDL----------ISRLADRFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIasgvktgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 123 QAIVVGIDSwfeketGKYWVNQYTGDEKRTRQT-----NWQLLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617 386 QAVVVSIDP------RRVYVKDPSDVPFKTVKVtnpgpNGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763000671 179 MNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFIDANVDGALAASVFHKQIINIGELKEYLAQQNVEIR 256
Cdd:PLN02617 460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-246 2.14e-34

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: 123.74  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:cd04732    1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  82 GIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKETGKYWvnqytgdekrTRQTNWQLLD 161
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGKVATKGW----------LETSEVSLEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRdAFIDANVDGALAASVFHKQIINI 241
Cdd:cd04732  151 LAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIK-ALKELGVAGVIVGKALYEGKITL 229


                 ....*
gi 763000671 242 GELKE 246
Cdd:cd04732  230 EEALA 234
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-228 3.17e-28

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: 107.43  E-value: 3.17e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYAEEGADEL--VfyDITASSDGRTVDKSWVERVAEVIDIPFCV 79
Cdd:COG0106    1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLhlV--DLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  80 AGGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQaIVVGIDSWFEKETGKYWvnqytgdekrTRQTNWQL 159
Cdd:COG0106   79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDARDGKVATDGW----------QETSGVDL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763000671 160 LDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRdAFIDANVDGA 228
Cdd:COG0106  148 EELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLR-ALKELGVEGA 215
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-211 1.54e-25

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: 100.35  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    6 IIPCLDVRDGQVVKGVQ--FRNHEIIGD-IVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQgdYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   83 IKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKETGKYWvnqytgdekrTRQTNWQLLDW 162
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGEVAVKGW----------LEKSEVSLEEL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 763000671  163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAG 211
Cdd:TIGR00007 151 AKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVS 199
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-209 3.39e-25

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 99.60  E-value: 3.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   6 IIPCLDVRDGQVVKGVQFR---NHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:PRK13585   5 VIPAVDMKGGKCVQLVQGEpgtETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  83 IKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGIDSWFEKETGKYWvnqytgdekrTRQTNWQLLDW 162
Cdd:PRK13585  85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAKDGEVVIKGW----------TEKTGYTPVEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 763000671 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGG 209
Cdd:PRK13585 155 AKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGG 201
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-246 4.39e-23

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: 93.87  E-value: 4.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQVVKGVQFR---------NHEIIGDIVPLAKRYAEEGADELVFYDITASSdGRTVDKSWVERVAEVIDI 75
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVGGDrdnyrpitsNLCSTSDPLDVARAYKELGFRGLYIADLDAIM-GRGDNDEAIRELAAAWPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  76 PFCVAGGIKTIDDAEQIFAFGADKISINSPALADPDLISRLAdRFGVQAIVVGIDSwfeKETGKYWVNQYTGDEkrtrqt 155
Cdd:cd04723   80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLA-ALGEQRLVLSLDF---RGGQLLKPTDFIGPE------ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 156 nwqllDWVQEVQKRgAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRDAFiDANVDGALAASVFH 235
Cdd:cd04723  150 -----ELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLK-KLGASGALVASALH 222

                        250
                 ....*....|.
gi 763000671 236 KQIINIGELKE 246
Cdd:cd04723  223 DGGLTLEDVVR 233
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-213 7.21e-21

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 87.81  E-value: 7.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   6 IIPCLDVRDGQVVKGVQ--FRNHEIIG-DIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:PRK00748   3 IIPAIDLKDGKCVRLYQgdYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  83 IKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGvQAIVVGIDSwfekETGKY----WVNqytgdekrtrQTNWQ 158
Cdd:PRK00748  83 IRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDA----RDGKVatdgWLE----------TSGVT 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 763000671 159 LLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEM 213
Cdd:PRK00748 148 AEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSL 202
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-229 1.42e-10

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 59.59  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   6 IIPCLDVRDGQVVKGVQFR--NHEIIGDIVPLAKRYAEEGADELVFYDITASSdGRTVDKSWVERVAEVIDIPFCVAGGI 83
Cdd:PRK14024   6 LLPAVDVVDGQAVRLVQGEagSETSYGSPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELSGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  84 KTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGvQAIVVGIDSWFEKETGKYWVNQyTGDekrtrqtnwqLLDWV 163
Cdd:PRK14024  85 RDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVRGHTLAARGWTRD-GGD----------LWEVL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763000671 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGGAGEMVHFRD--AFIDANVDGAL 229
Cdd:PRK14024 153 ERLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRAlaELVPLGVEGAI 220
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-247 6.11e-10

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 57.72  E-value: 6.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   6 IIPCLDVRDGQVVKGVQFRNHEII---GDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDiPFCVAGG 82
Cdd:PRK14114   3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  83 IKTIDDAEQIFAFGADKISINSPALADPDLISRLADrFGVQAiVVGIDSWFEKETGKYWVNQYTGDEkrtrqtnwqlLDW 162
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE-IDVEP-VFSLDTRGGKVAFKGWLAEEEIDP----------VSL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGG--------AGEMVHFRdafIDANVDGALAASVF 234
Cdd:PRK14114 150 LKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGissenslkTAQRVHRE---TNGLLKGVIVGRAF 226

                        250
                 ....*....|...
gi 763000671 235 HKQIINIGELKEY 247
Cdd:PRK14114 227 LEGILTVEVMKRY 239
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 29-118 3.45e-08

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: 53.34  E-value: 3.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  29 IGDIVPLAKRYAEEGAD---------ELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGGIKTIDDAEQIFAFG-AD 98
Cdd:cd02803  227 LEEAIEIAKALEEAGVDalhvsggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGkAD 306

                         90       100
                 ....*....|....*....|
gi 763000671  99 KISINSPALADPDLISRLAD 118
Cdd:cd02803  307 LVALGRALLADPDLPNKARE 326
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-130 1.67e-07

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 50.51  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQVVKGVQFRNHE--IIGDIVPLAKRYAEEGADELVFYDITASsDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:PRK13586   3 KIIPSIDISLGKAVKRIRGVKGTglILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 763000671  83 IKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQAIVVGID 130
Cdd:PRK13586  82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID 129
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 31-118 2.37e-07

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: 50.94  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  31 DIVPLAKRYAEEGADelvFYDItasSDGRTVDKSWV-------------ERVAEVIDIPFCVAGGIKTIDDAEQIFAFG- 96
Cdd:COG1902  237 ESVELAKALEEAGVD---YLHV---SSGGYEPDAMIptivpegyqlpfaARIRKAVGIPVIAVGGITTPEQAEAALASGd 310

                         90       100
                 ....*....|....*....|..
gi 763000671  97 ADKISINSPALADPDLISRLAD 118
Cdd:COG1902  311 ADLVALGRPLLADPDLPNKAAA 332
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-104 9.45e-07

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 48.37  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQVV-KGVQfrnhEIIG-DIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:PRK13585 126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGG 201

                         90       100
                 ....*....|....*....|..
gi 763000671  83 IKTIDDAEQIFAFGADKISINS 104
Cdd:PRK13585 202 VTTLDDLRALKEAGAAGVVVGS 223
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 31-120 1.02e-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: 48.94  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  31 DIVPLAKRYAEEGADELVFYditassdGRT--------VDKSWVERVAEVIDIPFCVAGGIKTIDDAEQIFA-FGADKIS 101
Cdd:COG0042  147 NALEFARIAEDAGAAALTVH-------GRTreqrykgpADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEeTGCDGVM 219

                         90
                 ....*....|....*....
gi 763000671 102 INSPALADPDLISRLADRF 120
Cdd:COG0042  220 IGRGALGNPWLFREIDAYL 238
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 51-209 1.77e-06

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 47.52  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  51 DITASSDGRTVDKSWVERVAEVIDIPFCVAGGIKTIDDAEQIFAFGADKISINSPALADPDLISRLADRFGVQaIVVGID 130
Cdd:PRK13587  53 DLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763000671 131 SWFEKETgkywVNQYTGDekrtrqTNWQLLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLVQLKKVREACHVPLIASGG 209
Cdd:PRK13587 132 AYGEDIK----VNGWEED------TELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-144 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 763000671   5 RIIPCLDVRDGQVVKGVQFRNHEI--IGDIVPLAKRYAEEgADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:PRK04128   3 RIYPAIDLMNGKAVRLYKGRKEEVkvYGDPVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763000671  83 IKTIDDAEQIFAFGADKISINSPALaDPDLISRLADRFGvqAIVVGIDSWFEKETGKYWVNQ 144
Cdd:PRK04128  82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFE--GITVSLDVKGGRIAVKGWLEE 140
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 3-98 4.20e-06

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: 46.49  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   3 AKRIIPCLDVRDGQVVKGVQF-RNHEIIgdivplakRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAG 81
Cdd:cd04723  125 EQRLVLSLDFRGGQLLKPTDFiGPEELL--------RRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAG 196

                         90
                 ....*....|....*..
gi 763000671  82 GIKTIDDAEQIFAFGAD 98
Cdd:cd04723  197 GVRSVEDLELLKKLGAS 213
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 4-98 4.72e-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: 46.32  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   4 KRIIPCLDVRDGQV-VKGVQfRNHEIigDIVPLAKRYAEEGADELVFYDItaSSDG--RTVDKSWVERVAEVIDIPFCVA 80
Cdd:cd04732  122 ERIVVGLDAKDGKVaTKGWL-ETSEV--SLEELAKRFEELGVKAIIYTDI--SRDGtlSGPNFELYKELAAATGIPVIAS 196

                         90
                 ....*....|....*...
gi 763000671  81 GGIKTIDDAEQIFAFGAD 98
Cdd:cd04732  197 GGVSSLDDIKALKELGVA 214
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 58-118 4.93e-06

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: 46.82  E-value: 4.93e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763000671  58 GRTVDKSWVERVAEVID--IPFCVAGGIKTIDDAEQIFAFGADKISINSPALADPDLISRLAD 118
Cdd:cd04735  266 GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKE 328
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 4-102 7.71e-06

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: 45.65  E-value: 7.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671    4 KRIIPCLDVRDGQV-VKGvqFRNHEIIgDIVPLAKRYAEEGADELVFYDITASSDGRTVDKSWVERVAEVIDIPFCVAGG 82
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKG--WLEKSEV-SLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGG 197

                          90       100
                  ....*....|....*....|
gi 763000671   83 IKTIDDAEQIFAFGADKISI 102
Cdd:TIGR00007 198 VSSIDDLIALKKLGVYGVIV 217
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 66-118 2.42e-05

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: 44.91  E-value: 2.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 763000671  66 VERVAEVIDIPFCVAGGIKTIDDAEQIFAFG-ADKISINSPALADPDLISRLAD 118
Cdd:cd04734  277 AARIKQAVDLPVFHAGRIRDPAEAEQALAAGhADMVGMTRAHIADPHLVAKARE 330
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 64-115 6.27e-05

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


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 43.43  E-value: 6.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 763000671  64 SWV-ERVAEVIDIPFCVAGGIKTIDDAEQIFAFG-ADKISINSPALADPDLISR 115
Cdd:cd02930  265 AWAtAKLKRAVDIPVIASNRINTPEVAERLLADGdADMVSMARPFLADPDFVAK 318
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 35-120 7.15e-05

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: 42.87  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  35 LAKRYAEEGADELVFYditassdGRT--------VDKSWVERVAEVIDIPFCVAGGIKTIDDAEQIFA-FGADKISINSP 105
Cdd:cd02801  143 LAKALEDAGASALTVH-------GRTreqrysgpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRG 215

                         90
                 ....*....|....*
gi 763000671 106 ALADPDLISRLADRF 120
Cdd:cd02801  216 ALGNPWLFREIKELL 230
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
44-100 2.37e-04

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 41.30  E-value: 2.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763000671  44 ADEL----VFYdITASSD-GRTVDKSWVERVAEVI-DIPFCVAGGIKTIDDAEQIFAFGADKI 100
Cdd:COG1646  161 AEEYlgmpIVY-LEYGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGADTI 222
ER_like_FMN cd02931
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ...
 64-116 4.19e-04

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: 40.95  E-value: 4.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 763000671  64 SWVERVAEVIDIPFCVAGGIKTIDDAEQIFAFG-ADKISINSPALADPDLISRL 116
Cdd:cd02931  295 PYCKALKEVVDVPVIMAGRMEDPELASEAINEGiADMISLGRPLLADPDVVNKI 348
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 5-88 1.18e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 39.28  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671   5 RIIPCLDVRDGQV-VKGVQfrnhEIIG-DIVPLAKRYAEEGADELVFYDItaSSDGrTVDKSWVE---RVAEVIDIPFCV 79
Cdd:PRK00748 123 KIVVGLDARDGKVaTDGWL----ETSGvTAEDLAKRFEDAGVKAIIYTDI--SRDG-TLSGPNVEatrELAAAVPIPVIA 195


                 ....*....
gi 763000671  80 AGGIKTIDD 88
Cdd:PRK00748 196 SGGVSSLDD 204
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-104 1.72e-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: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763000671  26 HEIIGDIVPLAKRYAEEGADELV---FYDITASSDGRTVDKSWVERVAEVIDIPFCVAGGIKTIDDAEQIFAFGADKISI 102
Cdd:cd04722  119 VKLSPTGELAAAAAEEAGVDEVGlgnGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIV 198


                 ..
gi 763000671 103 NS 104
Cdd:cd04722  199 GS 200
OYE_like_2_FMN cd04733
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ...
 67-116 9.72e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 2. 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: 240084 [Multi-domain]  Cd Length: 338  Bit Score: 36.79  E-value: 9.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 763000671  67 ERVAEVIDIPFCVAGGIKTIDDAEQIFAFGA-DKISINSPALADPDLISRL 116
Cdd:cd04733  285 EKIRKVTKTPLMVTGGFRTRAAMEQALASGAvDGIGLARPLALEPDLPNKL 335
 
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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