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Conserved domains on  [gi|2551227468|ref|WP_302406473|]
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imidazole glycerol phosphate synthase subunit HisF [Barnesiella intestinihominis]

Protein Classification

imidazole glycerol phosphate synthase subunit HisF( domain architecture ID 10785016)

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

EC:  4.3.2.10
Gene Symbol:  hisF
Gene Ontology:  GO:0000107|GO:0000105
PubMed:  12795596|12859215|9742729
SCOP:  4003056

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-251 4.66e-152

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: 423.28  E-value: 4.66e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANF-ENGNWVCYLNGGKVATQRTLFEWALEA 160
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRvPDGGWEVYTHGGRKPTGLDAVEWAKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 161 AERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKK 240
Cdd:COG0107   161 EELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKA 240

                         250
                  ....*....|.
gi 2551227468 241 YLSESGIPVRR 251
Cdd:COG0107   241 YLAEAGIPVRL 251
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-251 4.66e-152

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: 423.28  E-value: 4.66e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANF-ENGNWVCYLNGGKVATQRTLFEWALEA 160
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRvPDGGWEVYTHGGRKPTGLDAVEWAKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 161 AERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKK 240
Cdd:COG0107   161 EELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKA 240

                         250
                  ....*....|.
gi 2551227468 241 YLSESGIPVRR 251
Cdd:COG0107   241 YLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-244 1.69e-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: 358.32  E-value: 1.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   4 KRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  84 NSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANFENGN-WVCYLNGGKVATQRTLFEWALEAAE 162
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGgYEVYTHGGRKPTGLDAVEWAKEVEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 163 RGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKKYL 242
Cdd:cd04731   161 LGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYL 240


                  ..
gi 2551227468 243 SE 244
Cdd:cd04731   241 AE 242
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-250 3.67e-122

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 347.82  E-value: 3.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   1 MLAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVG 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  81 GGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANF----ENGNWVCYLNGGKVATQRTLFEW 156
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRvyvnSYCWYEVYIYGGRESTGLDAVEW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 157 ALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIP 236
Cdd:TIGR00735 161 AKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIG 240

                         250
                  ....*....|....
gi 2551227468 237 ELKKYLSESGIPVR 250
Cdd:TIGR00735 241 EVKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-234 2.07e-92

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: 271.27  E-value: 2.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTV---KGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDAnfENGNwvCYLNGGKVATQRTLFEWALEAA 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDA--RRGK--VAINGWREDTGIDAVEWAKELE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551227468 162 ERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKaDAALAAGVFHFGEIT 234
Cdd:pfam00977 157 ELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV-DGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-229 5.64e-69

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 212.72  E-value: 5.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDA--NFeNGNWVCYLNGGKVATQRTLFEWALE 159
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVkkNL-FGGYEVYTHNGTKKTKLDPVEFAKE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551227468 160 AAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAAlAAG---VFH 229
Cdd:NF038364  160 LEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAV-AAGslfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-250 5.36e-43

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 152.56  E-value: 5.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVK-----DGKTVKGTKFvDFKEA---------GDPVLLGEIYSKEGADELVYLDITASSEGrsTFTDL-- 65
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQY-DVREHsegrevrnlGKPVELAGQYYKDGADEVAFLNITGFRDF--PLGDLpm 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  66 --VKRVAS-RIDIPFTVGGGINSLQDID-----------RLLNVGADKVSLNSSALKNPQ------------IIDDVAKK 119
Cdd:PLN02617  303 leVLRRASeNVFVPLTVGGGIRDFTDANgryysslevasEYFRSGADKISIGSDAVYAAEeyiasgvktgktSIEQISRV 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 120 FGSQVCVIAIDA-----------------------NFENGNWV-CYLNGGKVATQRTLFEWALEAAERGAGEILFTSMTH 175
Cdd:PLN02617  383 YGNQAVVVSIDPrrvyvkdpsdvpfktvkvtnpgpNGEEYAWYqCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDC 462

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551227468 176 DGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKKYLSESGIPVR 250
Cdd:PLN02617  463 DGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-251 4.66e-152

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: 423.28  E-value: 4.66e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANF-ENGNWVCYLNGGKVATQRTLFEWALEA 160
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRvPDGGWEVYTHGGRKPTGLDAVEWAKEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 161 AERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKK 240
Cdd:COG0107   161 EELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAELKA 240

                         250
                  ....*....|.
gi 2551227468 241 YLSESGIPVRR 251
Cdd:COG0107   241 YLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-244 1.69e-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: 358.32  E-value: 1.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   4 KRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  84 NSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANFENGN-WVCYLNGGKVATQRTLFEWALEAAE 162
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGgYEVYTHGGRKPTGLDAVEWAKEVEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 163 RGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKKYL 242
Cdd:cd04731   161 LGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKEYL 240


                  ..
gi 2551227468 243 SE 244
Cdd:cd04731   241 AE 242
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-250 3.67e-122

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 347.82  E-value: 3.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   1 MLAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVG 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  81 GGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANF----ENGNWVCYLNGGKVATQRTLFEW 156
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRvyvnSYCWYEVYIYGGRESTGLDAVEW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 157 ALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIP 236
Cdd:TIGR00735 161 AKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIG 240

                         250
                  ....*....|....
gi 2551227468 237 ELKKYLSESGIPVR 250
Cdd:TIGR00735 241 EVKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-234 2.07e-92

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: 271.27  E-value: 2.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTV---KGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDAnfENGNwvCYLNGGKVATQRTLFEWALEAA 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDA--RRGK--VAINGWREDTGIDAVEWAKELE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551227468 162 ERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKaDAALAAGVFHFGEIT 234
Cdd:pfam00977 157 ELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV-DGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-230 2.05e-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: 261.44  E-value: 2.05e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   1 MLAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVG 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  81 GGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDA--NFENGNWVCYLNGGKVATQRTLFEWAL 158
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVkkELDGSDYKVYSDNGRRATGRDPVEWAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551227468 159 EAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHF 230
Cdd:TIGR03572 161 EAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-229 5.64e-69

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 212.72  E-value: 5.64e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDA--NFeNGNWVCYLNGGKVATQRTLFEWALE 159
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVkkNL-FGGYEVYTHNGTKKTKLDPVEFAKE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551227468 160 AAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAAlAAG---VFH 229
Cdd:NF038364  160 LEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAV-AAGslfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-250 5.36e-43

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 152.56  E-value: 5.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   2 LAKRIIPCLDVK-----DGKTVKGTKFvDFKEA---------GDPVLLGEIYSKEGADELVYLDITASSEGrsTFTDL-- 65
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQY-DVREHsegrevrnlGKPVELAGQYYKDGADEVAFLNITGFRDF--PLGDLpm 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  66 --VKRVAS-RIDIPFTVGGGINSLQDID-----------RLLNVGADKVSLNSSALKNPQ------------IIDDVAKK 119
Cdd:PLN02617  303 leVLRRASeNVFVPLTVGGGIRDFTDANgryysslevasEYFRSGADKISIGSDAVYAAEeyiasgvktgktSIEQISRV 382

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 120 FGSQVCVIAIDA-----------------------NFENGNWV-CYLNGGKVATQRTLFEWALEAAERGAGEILFTSMTH 175
Cdd:PLN02617  383 YGNQAVVVSIDPrrvyvkdpsdvpfktvkvtnpgpNGEEYAWYqCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDC 462

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2551227468 176 DGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGKADAALAAGVFHFGEITIPELKKYLSESGIPVR 250
Cdd:PLN02617  463 DGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-211 5.72e-39

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: 135.17  E-value: 5.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTVK------GTKFVdfkEAGDPVLLGEIYSKEGADEL--VYLDitASSEGRSTFTDLVKRVASRIDIP 76
Cdd:COG0106     1 IIIPAIDLKDGKCVRlvqgdyDQETV---YSDDPVEVAKRWEDAGAEWLhlVDLD--GAFAGKPVNLELIEEIAKATGLP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  77 FTVGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVcVIAIDAnfengnwvcylNGGKVATQR----- 151
Cdd:COG0106    76 VQVGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPERI-VVGLDA-----------RDGKVATDGwqets 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551227468 152 --TLFEWALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFK 211
Cdd:COG0106   144 gvDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLR 205
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-206 1.15e-37

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: 131.83  E-value: 1.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTV---KGtkfvDFKEA----GDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPF 77
Cdd:cd04732     1 IIIPAIDLKDGKCVrlyQG----DYDKKtvysDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  78 TVGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDAnfengnwvcylNGGKVATQ------- 150
Cdd:cd04732    77 QVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDA-----------KDGKVATKgwletse 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2551227468 151 RTLFEWALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGT 206
Cdd:cd04732   146 VSLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSS 201
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-211 6.14e-37

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 129.80  E-value: 6.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   6 IIPCLDVKDGKTV---KGtkfvDFKEA----GDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFT 78
Cdd:PRK00748    3 IIPAIDLKDGKCVrlyQG----DYDQAtvysDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  79 VGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCViAIDAnfengnwvcylNGGKVATQ-------R 151
Cdd:PRK00748   79 VGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGKIVV-GLDA-----------RDGKVATDgwletsgV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 152 TLFEWALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFK 211
Cdd:PRK00748  147 TAEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIK 206
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-206 8.40e-32

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: 116.53  E-value: 8.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   6 IIPCLDVKDGKTVK------GTKFVdfkEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTV 79
Cdd:TIGR00007   1 IIPAIDIKDGKCVRlyqgdyDKETV---YGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  80 GGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDAnfengnwvcylNGGKVA-------TQRT 152
Cdd:TIGR00007  78 GGGIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDA-----------RGGEVAvkgwlekSEVS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2551227468 153 LFEWALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGT 206
Cdd:TIGR00007 147 LEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSS 200
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-206 1.39e-30

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 113.46  E-value: 1.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   6 IIPCLDVKDGKTVK------GTKFVDFkeaGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTV 79
Cdd:PRK13585    5 VIPAVDMKGGKCVQlvqgepGTETVSY---GDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  80 GGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDAnfENGNWVcyLNGGKVATQRTLFEWALE 159
Cdd:PRK13585   82 GGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDA--KDGEVV--IKGWTEKTGYTPVEAAKR 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2551227468 160 AAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGT 206
Cdd:PRK13585  158 FEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTT 204
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-240 6.11e-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: 95.80  E-value: 6.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTVKG------------TKFVDfkeAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFtDLVKRVASR 72
Cdd:cd04723     1 RIIPVIDLKDGVVVHGvggdrdnyrpitSNLCS---TSDPLDVARAYKELGFRGLYIADLDAIMGRGDND-EAIRELAAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  73 IDIPFTVGGGINSLQDIDRLLNVGADKVSLNSSALKNpQIIDDVAKKFGSQVCVIAIDanFENGnwvcylNGGKVATQRT 152
Cdd:cd04723    77 WPLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLD--FRGG------QLLKPTDFIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 153 LFEWaLEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGkADAALAAGVFHFGE 232
Cdd:cd04723   148 PEEL-LRRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLG-ASGALVASALHDGG 225


                  ....*...
gi 2551227468 233 ITIPELKK 240
Cdd:cd04723   226 LTLEDVVR 233
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-181 1.90e-11

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 62.06  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTVK------GTKFVdfkeAGDPVLLG-EIYSkEGADELVYLDITASsEGRSTFTDLVKRVaSRIDIPF 77
Cdd:PRK13586    3 KIIPSIDISLGKAVKrirgvkGTGLI----LGNPIEIAsKLYN-EGYTRIHVVDLDAA-EGVGNNEMYIKEI-SKIGFDW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  78 T-VGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCVIAIDANfENGNwvCYLNGGKVATQrTLFEW 156
Cdd:PRK13586   76 IqVGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDYD-NTKR--VLIRGWKEKSM-EVIDG 151

                         170       180
                  ....*....|....*....|....*
gi 2551227468 157 ALEAAERGAGEILFTSMTHDGTRSG 181
Cdd:PRK13586  152 IKKVNELELLGIIFTYISNEGTTKG 176
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-206 1.46e-10

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 59.59  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   6 IIPCLDVKDGKTVK------GTKfvdfKEAGDPVLLGEIYSKEGADELVYLDITASSeGRSTFTDLVKRVASRIDIPFTV 79
Cdd:PRK14024    6 LLPAVDVVDGQAVRlvqgeaGSE----TSYGSPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  80 GGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVCV-IAIDANFENGN-WVcyLNGGKvatqrtLFEwA 157
Cdd:PRK14024   81 SGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDRVAVgLDVRGHTLAARgWT--RDGGD------LWE-V 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2551227468 158 LEAAER-GAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGGAGT 206
Cdd:PRK14024  152 LERLDSaGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSS 201
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 50-203 1.63e-10

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 59.46  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  50 LDITASSEGRSTFTDLVKRVASRIDIPFTVGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKKFGSQVcVIAI 129
Cdd:PRK13587   52 VDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGRI-YLSV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551227468 130 DANFENgnwvCYLNGGKVATQRTLFEWALEAAERGAGEILFTSMTHDGTRSGYAHEALLELHRLLPIPIIASGG 203
Cdd:PRK13587  131 DAYGED----IKVNGWEEDTELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-181 1.42e-08

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 53.62  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTV---KGTKfVDFKEAGDPVLLGEIYSkEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGG 81
Cdd:PRK04128    3 RIYPAIDLMNGKAVrlyKGRK-EEVKVYGDPVEIALRFS-EYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  82 GINSLQDIDRLLNVGADKVSLNSSALkNPQIIDDVAKKFGSqvCVIAIDAnfengnwvcylNGGKVATQRTLFEWALEAA 161
Cdd:PRK04128   81 GLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG--ITVSLDV-----------KGGRIAVKGWLEESSIKVE 146

                         170       180
                  ....*....|....*....|....*...
gi 2551227468 162 ErgAGEIL--------FTSMTHDGTRSG 181
Cdd:PRK04128  147 D--AYEMLknyvnrfiYTSIERDGTLTG 172
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-109 5.52e-08

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 52.22  E-value: 5.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGKTV-KGTKfvdfKEAG-DPVLLGEIYSKEGADELVYLDItaSSEG--RSTFTDLVKRVASRIDIPFTVG 80
Cdd:PRK13585  126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNV--DVEGllEGVNTEPVKELVDSVDIPVIAS 199

                          90       100
                  ....*....|....*....|....*....
gi 2551227468  81 GGINSLQDIDRLLNVGADKVSLNSSALKN 109
Cdd:PRK13585  200 GGVTTLDDLRALKEAGAAGVVVGSALYKG 228
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 4-98 1.77e-07

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: 50.56  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   4 KRIIPCLDVKDGKT-VKG-TKfvdfKEAGDPVLLGEIYSKEGADELVYLDItaSSEGrsTFT----DLVKRVASRIDIPF 77
Cdd:cd04732   122 ERIVVGLDAKDGKVaTKGwLE----TSEVSLEELAKRFEELGVKAIIYTDI--SRDG--TLSgpnfELYKELAAATGIPV 193

                          90       100
                  ....*....|....*....|.
gi 2551227468  78 TVGGGINSLQDIDRLLNVGAD 98
Cdd:cd04732   194 IASGGVSSLDDIKALKELGVA 214
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 4-100 1.00e-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: 48.35  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   4 KRIIPCLDVKDGKT-VKGTKFvdfKEAGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGGG 82
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKGWLE---KSEVSLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGG 197

                          90
                  ....*....|....*...
gi 2551227468  83 INSLQDIDRLLNVGADKV 100
Cdd:TIGR00007 198 VSSIDDLIALKKLGVYGV 215
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 29-226 7.46e-06

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: 45.27  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  29 AGDPVLLGEIYSKEGADELVYLDITASSEGRSTFTDLVKRVASRI-DIPFTVGGGINSLQDI-----DRLLNVGADKVSL 102
Cdd:cd04722    11 SGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAEtDLPLGVQLAINDAAAAvdiaaAAARAAGADGVEI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468 103 NSSALKNP----QIIDDVAKKFGSQVCVIAIDANFEngnwvcylngGKVAtqrtlfewalEAAERGAGEILFTSMTHDG- 177
Cdd:cd04722    91 HGAVGYLAredlELIRELREAVPDVKVVVKLSPTGE----------LAAA----------AAEEAGVDEVGLGNGGGGGg 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2551227468 178 --TRSGYAHEALLELHRLLPIPIIASGGAGTKAHFKDAFLRGkADAALAAG 226
Cdd:cd04722   151 grDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 41-118 7.25e-04

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: 40.25  E-value: 7.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468  41 KEGADelvYLDITA------------SSEGRSTFTDLVKRVASRIDIPFTVGGGINSLQDIDRLL-NVGADKVSLNSSAL 107
Cdd:cd02803   239 EAGVD---ALHVSGgsyespppiippPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILaEGKADLVALGRALL 315

                          90
                  ....*....|.
gi 2551227468 108 KNPQIIDDVAK 118
Cdd:cd02803   316 ADPDLPNKARE 326
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 64-120 1.35e-03

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: 39.31  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2551227468  64 DLVKRVASRIDIPFTVGGGINSLQDIDRLLNV-GADKVSLNSSALKNPQIIDDVAKKF 120
Cdd:COG0042   181 DAIARVKEAVSIPVIGNGDIFSPEDAKRMLEEtGCDGVMIGRGALGNPWLFREIDAYL 238
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 5-97 1.80e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 38.51  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   5 RIIPCLDVKDGK-------TVKGTKFVDfkeagdpvlLGEIYSKEGADELVYLDItaSSEGrsTFT----DLVKRVASRI 73
Cdd:PRK00748  123 KIVVGLDARDGKvatdgwlETSGVTAED---------LAKRFEDAGVKAIIYTDI--SRDG--TLSgpnvEATRELAAAV 189

                          90       100
                  ....*....|....*....|....
gi 2551227468  74 DIPFTVGGGINSLQDIDRLLNVGA 97
Cdd:PRK00748  190 PIPVIASGGVSSLDDIKALKGLGA 213
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 64-110 4.00e-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: 37.47  E-value: 4.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2551227468  64 DLVKRVASRIDIPFTVGGGINSLQDIDRLLNV-GADKVSLNSSALKNP 110
Cdd:cd02801   173 DYIAEIKEAVSIPVIANGDIFSLEDALRCLEQtGVDGVMIGRGALGNP 220
hisAF_rel TIGR00734
hisA/hisF family protein; This model models a family of proteins found so far in three ...
 4-100 4.15e-03

hisA/hisF family protein; This model models a family of proteins found so far in three archaeal species: Methanobacterium thermoautotrophicum, Methanococcus jannaschii, and Archaeoglobus fulgidus. This protein is homologous to phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase (HisA) and, with lower similarity, to the cyclase HisF, both of which are enzymes of histidine biosynthesis. Each species with this protein also encodes HisA. The function of this protein is unknown. [Unknown function, General]


Pssm-ID: 273240  Cd Length: 221  Bit Score: 37.59  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551227468   4 KRIIPCLDVKDGKTVKGTKFVDFKEAGDPVLLGEIyskegadELVYLDITASSEGRSTFTDLVKRVASRIDIPFTVGGGI 83
Cdd:TIGR00734 121 CYTVVSLDFKEKFLDASGLFESLEEVRDFLNSFDY-------GLIVLDIHSVGTMKGPNLELLTKTLELSEHPVMLGGGI 193

                          90
                  ....*....|....*..
gi 2551227468  84 NSLQDIDRLLNVGADKV 100
Cdd:TIGR00734 194 SGVEDLELLKEMGVSAV 210
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
46-98 5.66e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 37.10  E-value: 5.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2551227468  46 ELVYLDitASS-EGRSTFTDLVKRVASRIDI-PFTVGGGINSLQDIDRLLNVGAD 98
Cdd:PRK04169  156 PIVYLE--YGGgAGDPVPPEMVKAVKKALDItPLIYGGGIRSPEQARELMAAGAD 208
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 52-119 6.10e-03

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: 37.19  E-value: 6.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551227468  52 ITASSEGRSTFTDLVKRVASRIdiPFTVGGGINSLQDIDRLLNVGADKVSLNSSALKNPQIIDDVAKK 119
Cdd:cd04735   264 RRGRDDNQTIMELVKERIAGRL--PLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEG 329
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
46-98 7.54e-03

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 36.68  E-value: 7.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2551227468  46 ELVYLDitASSE-GRSTFTDLVKRVASRI-DIPFTVGGGINSLQDIDRLLNVGAD 98
Cdd:COG1646   168 PIVYLE--YGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGAD 220
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 54-118 8.85e-03

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


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 36.88  E-value: 8.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551227468  54 ASSEGRSTFTDLVKRVASRIDIPFTVGGGINSLQDIDRLLNVG-ADKVSLNSSALKNPQIiddVAK 118
Cdd:cd02930   256 ATSVPRGAFAWATAKLKRAVDIPVIASNRINTPEVAERLLADGdADMVSMARPFLADPDF---VAK 318
 
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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