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Conserved domains on  [gi|2285271422|ref|WP_257644936|]
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HisA/HisF-related TIM barrel protein, partial [Escherichia fergusonii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisF super family cl41873
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 1-87 2.35e-52

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


The actual alignment was detected with superfamily member COG0107:

Pssm-ID: 439877  Cd Length: 251  Bit Score: 163.27  E-value: 2.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:COG0107    50 DITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAID 129


                  ....*..
gi 2285271422  81 AKRTGSD 87
Cdd:COG0107   130 AKRVPDG 136
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 1-87 2.35e-52

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: 163.27  E-value: 2.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:COG0107    50 DITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAID 129


                  ....*..
gi 2285271422  81 AKRTGSD 87
Cdd:COG0107   130 AKRVPDG 136
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 1-85 9.86e-46

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: 146.46  E-value: 9.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:cd04731    48 DITASSEGRETMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSID 127


                  ....*
gi 2285271422  81 AKRTG 85
Cdd:cd04731   128 AKRRG 132
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 1-83 2.76e-38

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: 126.82  E-value: 2.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:pfam00977  50 DLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAID 129


                  ...
gi 2285271422  81 AKR 83
Cdd:pfam00977 130 ARR 132
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-83 1.41e-37

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 125.94  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:TIGR00735  51 DITASSEGRTTMIDVVERTAETVFIPLTVGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAID 130


                  ...
gi 2285271422  81 AKR 83
Cdd:TIGR00735 131 AKR 133
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
1-84 2.99e-32

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 111.80  E-value: 2.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:NF038364   50 DIDATKEGREPDYELIEDLASECFMPLCYGGGIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSID 129


                  ....
gi 2285271422  81 AKRT 84
Cdd:NF038364  130 VKKN 133
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 13-82 1.44e-18

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 76.26  E-value: 1.44e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQcIVVAIDAK 82
Cdd:PRK00748   63 LELIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR 131
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 1-87 2.35e-52

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: 163.27  E-value: 2.35e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:COG0107    50 DITASSEGRKTMLDVVRRVAEEVFIPLTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAID 129


                  ....*..
gi 2285271422  81 AKRTGSD 87
Cdd:COG0107   130 AKRVPDG 136
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 1-85 9.86e-46

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: 146.46  E-value: 9.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:cd04731    48 DITASSEGRETMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSID 127


                  ....*
gi 2285271422  81 AKRTG 85
Cdd:cd04731   128 AKRRG 132
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 1-83 2.76e-38

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: 126.82  E-value: 2.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:pfam00977  50 DLDAAKEGRPVNLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAID 129


                  ...
gi 2285271422  81 AKR 83
Cdd:pfam00977 130 ARR 132
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-83 1.41e-37

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 125.94  E-value: 1.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:TIGR00735  51 DITASSEGRTTMIDVVERTAETVFIPLTVGGGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAID 130


                  ...
gi 2285271422  81 AKR 83
Cdd:TIGR00735 131 AKR 133
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-85 1.37e-33

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: 115.06  E-value: 1.37e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:TIGR03572  51 DIDASKRGREPLFELISNLAEECFMPLTVGGGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSID 130


                  ....*
gi 2285271422  81 AKRTG 85
Cdd:TIGR03572 131 VKKEL 135
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
1-84 2.99e-32

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 111.80  E-value: 2.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:NF038364   50 DIDATKEGREPDYELIEDLASECFMPLCYGGGIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSID 129


                  ....
gi 2285271422  81 AKRT 84
Cdd:NF038364  130 VKKN 133
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 13-82 8.26e-20

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: 79.45  E-value: 8.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAIDAK 82
Cdd:cd04732    62 LELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAK 131
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 13-82 1.44e-18

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 76.26  E-value: 1.44e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQcIVVAIDAK 82
Cdd:PRK00748   63 LELIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR 131
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 7-82 2.35e-18

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: 75.46  E-value: 2.35e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2285271422   7 ENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQcIVVAIDAK 82
Cdd:COG0106    56 AGKPVNLELIEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR 130
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 1-82 9.33e-16

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: 68.76  E-value: 9.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAID 80
Cdd:TIGR00007  49 DLDGAKEGGPVNLPVIKKIVRETGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLD 128


                  ..
gi 2285271422  81 AK 82
Cdd:TIGR00007 129 AR 130
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 13-82 1.77e-13

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 62.62  E-value: 1.77e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAIDAK 82
Cdd:PRK13585   65 AEAIEKIIEAVGVPVQLGGGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK 134
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 12-83 1.20e-11

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 58.57  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422  12 ILDVVRRTAEACFMPLTVGGGVRTVDD--------IRTLLTY---GADKVSINSAAV-ARREFVK-----------EAAE 68
Cdd:PLN02617  302 MLEVLRRASENVFVPLTVGGGIRDFTDangryyssLEVASEYfrsGADKISIGSDAVyAAEEYIAsgvktgktsieQISR 381

                          90
                  ....*....|....*
gi 2285271422  69 KFGDQCIVVAIDAKR 83
Cdd:PLN02617  382 VYGNQAVVVSIDPRR 396
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 13-87 2.23e-05

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: 40.72  E-value: 2.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSaAVARREFVKEAAEKFGDQCIVVAIDAKRTGSD 87
Cdd:cd04723    67 DEAIRELAAAWPLGLWVDGGIRSLENAQEWLKRGASRVIVGT-ETLPSDDDEDRLAALGEQRLVLSLDFRGGQLL 140
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 8-55 1.19e-04

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: 38.41  E-value: 1.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2285271422   8 NRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSA 55
Cdd:cd04723   173 GQGPDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASA 220
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 1-82 3.19e-04

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 37.44  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2285271422   1 DITATHENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVaRREFVKEAAEKFGDqcIVVAID 80
Cdd:PRK04128   50 DLDGAFEGKPKNLDVVKNIIRETGLKVQVGGGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFEG--ITVSLD 126


                  ..
gi 2285271422  81 AK 82
Cdd:PRK04128  127 VK 128
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 13-55 7.17e-04

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: 36.30  E-value: 7.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSA 55
Cdd:pfam00977 179 LELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSA 221
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 25-80 1.20e-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: 35.65  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2285271422  25 MPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQcIVVAID 80
Cdd:cd04735   285 LPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEGREDE-INLEID 339
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 7-85 1.50e-03

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 35.49  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2285271422   7 ENRGTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQCIVVAIDAKRTG 85
Cdd:PRK13586   56 EGVGNNEMYIKEISKIGFDWIQVGGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDYDNTK 134
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 10-68 1.50e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 35.27  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2285271422  10 GTILDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAE 68
Cdd:PRK13585  179 GVNTEPVKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAIE 237
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 13-48 1.82e-03

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: 35.01  E-value: 1.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2285271422  13 LDVVRRTAEACFMPLTVGGGVRTVDDIRTLLTYGAD 48
Cdd:COG0106   178 LELYRELAAATGIPVIASGGVSSLDDLRALKELGVE 213
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 26-81 3.18e-03

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 34.42  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2285271422  26 PLTVGGGVRTVDDIRTLLTYGADKVSINSAAVARREFVKEAAEKFGDQcIVVAIDA 81
Cdd:PRK13587   78 DIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVDA 132
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
14-48 9.80e-03

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 33.21  E-value: 9.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2285271422  14 DVVRRTAEACF-MPLTVGGGVRTVDDIRTLLTYGAD 48
Cdd:COG1646   185 EMVKAVKKALEdTPLIYGGGIRSPEKAREMAEAGAD 220
 
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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