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Conserved domains on  [gi|1278428236|gb|PIZ57562|]
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hypothetical protein COY28_00105 [Candidatus Woesearchaeota archaeon CG_4_10_14_0_2_um_filter_57_5]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 3-177 1.21e-12

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member TIGR00070:

Pssm-ID: 473866  Cd Length: 183  Bit Score: 63.33  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   3 SIAQETLRLLTR-----------------PGERME---LRGEDIPFWLERlsrqGTSAIGLTGQDLYTEyllsskaRARS 62
Cdd:TIGR00070   9 RLLEDTLKLLEKaglklsredgrkliardPDEGIEvllLRPQDIPTYVEH----GAADLGITGYDVLLE-------SGAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  63 TQTLRVLasiswqasqtRFGKPALCLIGPSDATLPGLASARRPLRVSvpAKYRALGRRYLNTLELQGYTFlkqYLRGGIE 142
Cdd:TIGR00070  78 VEELLDL----------GFGKCRLVLAVPQESDIDSLEDLKEGKRIA--TKYPNLARRYFEKKGIDVEII---KLNGSVE 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1278428236 143 ATIKAGLADLAIDIVYTGDTLREMGLAVYNIILLS 177
Cdd:TIGR00070 143 LAPLLGLADAIVDIVSTGTTLRENGLRIIEVILES 177
 
Name Accession Description Interval E-value
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 3-177 1.21e-12

ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272888  Cd Length: 183  Bit Score: 63.33  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   3 SIAQETLRLLTR-----------------PGERME---LRGEDIPFWLERlsrqGTSAIGLTGQDLYTEyllsskaRARS 62
Cdd:TIGR00070   9 RLLEDTLKLLEKaglklsredgrkliardPDEGIEvllLRPQDIPTYVEH----GAADLGITGYDVLLE-------SGAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  63 TQTLRVLasiswqasqtRFGKPALCLIGPSDATLPGLASARRPLRVSvpAKYRALGRRYLNTLELQGYTFlkqYLRGGIE 142
Cdd:TIGR00070  78 VEELLDL----------GFGKCRLVLAVPQESDIDSLEDLKEGKRIA--TKYPNLARRYFEKKGIDVEII---KLNGSVE 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1278428236 143 ATIKAGLADLAIDIVYTGDTLREMGLAVYNIILLS 177
Cdd:TIGR00070 143 LAPLLGLADAIVDIVSTGTTLRENGLRIIEVILES 177
HisG pfam01634
ATP phosphoribosyltransferase;
22-175 1.64e-10

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 56.99  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  22 RGEDIPFWLERlsrqGTSAIGLTGQDLYTEyllsskararSTQTLRVLAsiswqasQTRFGKPALCLIGPSDATLPGLAS 101
Cdd:pfam01634   1 RAQDIPTYVED----GAADLGITGKDVLLE----------SGADVYELL-------DLGFGKCRLVVAVPEDSPYKSLED 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278428236 102 ARRPLRVsvpA-KYRALGRRYLNTLELQgYTFLKqyLRGGIEATIKAGLADLAIDIVYTGDTLREMGLAVYNIIL 175
Cdd:pfam01634  60 LPEGLRI---AtKYPNLTRRYFAEKGIQ-VEIIK--LSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETIL 128
PBP2_HisGL1 cd13591
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
 21-171 5.34e-09

The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270309  Cd Length: 204  Bit Score: 53.55  E-value: 5.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  21 LRGEDIPFWLErlsrQGTSAIGLTGQDLyteyLLSSKARARSTQTLRvlasiswqasqtrFGKPALCLIGP--SDATLPG 98
Cdd:cd13591    48 LRPRDIAIYVS----SGILDIGITGRDL----LSDSGANATELLDLG-------------FGRSTFRFAAPpgSTLTVAD 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278428236  99 LASARrplrvsVPAKYRALGRRYLNTLELQGYTFlkqYLRGGIEATIKAGLADLAIDIVYTGDTLREMGLAVY 171
Cdd:cd13591   107 LAGLR------VATSYPNLVRRHLADLGVDATVV---RLDGAVEISVQLGVADAIADVVETGRTLKQAGLRVF 170
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 3-175 1.85e-08

ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP phosphoribosyltransferase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439810 [Multi-domain]  Cd Length: 281  Bit Score: 52.78  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   3 SIAQETLRLLTR-------PGER-------------MELRGEDIPFWLErlsrQGTSAIGLTGQDLYTEyllsSKARARS 62
Cdd:COG0040    11 RLLEETLELLKKagiklreEDSRkliaetndpdvevLLLRPQDIPTYVE----DGAADLGITGKDVLLE----SGADVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  63 TQTLRvlasiswqasqtrFGKPALCLIGPSDATLPGLASARRpLRVsvpA-KYRALGRRYLNTLELQgYTFLKqyLRGGI 141
Cdd:COG0040    83 LLDLG-------------FGKCRLVVAVPEGSDYTSLADLRG-LRI---AtKYPNLTRRYFAEKGID-VEIVK--LNGSV 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1278428236 142 EATIKAGLADLAIDIVYTGDTLREMGLAVYNIIL 175
Cdd:COG0040   143 ELAPLLGLADAIVDIVSTGSTLRANGLKEVETIL 176
PLN02245 PLN02245
ATP phosphoribosyl transferase
 101-168 6.44e-03

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 36.70  E-value: 6.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278428236 101 SARRPLRVSVPAKYraLGRRYLNTLELQGYTFLKQylRGGIEATIKAGLADLAIDIVYTGDTLREMGL 168
Cdd:PLN02245  192 TEERPLRVVTGFTY--LGPKFMKDNGFKHVTFSTA--DGALEAAPAMGIADAILDLVSSGTTLRENNL 255
 
Name Accession Description Interval E-value
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 3-177 1.21e-12

ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272888  Cd Length: 183  Bit Score: 63.33  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   3 SIAQETLRLLTR-----------------PGERME---LRGEDIPFWLERlsrqGTSAIGLTGQDLYTEyllsskaRARS 62
Cdd:TIGR00070   9 RLLEDTLKLLEKaglklsredgrkliardPDEGIEvllLRPQDIPTYVEH----GAADLGITGYDVLLE-------SGAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  63 TQTLRVLasiswqasqtRFGKPALCLIGPSDATLPGLASARRPLRVSvpAKYRALGRRYLNTLELQGYTFlkqYLRGGIE 142
Cdd:TIGR00070  78 VEELLDL----------GFGKCRLVLAVPQESDIDSLEDLKEGKRIA--TKYPNLARRYFEKKGIDVEII---KLNGSVE 142

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1278428236 143 ATIKAGLADLAIDIVYTGDTLREMGLAVYNIILLS 177
Cdd:TIGR00070 143 LAPLLGLADAIVDIVSTGTTLRENGLRIIEVILES 177
HisG pfam01634
ATP phosphoribosyltransferase;
22-175 1.64e-10

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 56.99  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  22 RGEDIPFWLERlsrqGTSAIGLTGQDLYTEyllsskararSTQTLRVLAsiswqasQTRFGKPALCLIGPSDATLPGLAS 101
Cdd:pfam01634   1 RAQDIPTYVED----GAADLGITGKDVLLE----------SGADVYELL-------DLGFGKCRLVVAVPEDSPYKSLED 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278428236 102 ARRPLRVsvpA-KYRALGRRYLNTLELQgYTFLKqyLRGGIEATIKAGLADLAIDIVYTGDTLREMGLAVYNIIL 175
Cdd:pfam01634  60 LPEGLRI---AtKYPNLTRRYFAEKGIQ-VEIIK--LSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETIL 128
PBP2_HisGL1 cd13591
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
 21-171 5.34e-09

The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270309  Cd Length: 204  Bit Score: 53.55  E-value: 5.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  21 LRGEDIPFWLErlsrQGTSAIGLTGQDLyteyLLSSKARARSTQTLRvlasiswqasqtrFGKPALCLIGP--SDATLPG 98
Cdd:cd13591    48 LRPRDIAIYVS----SGILDIGITGRDL----LSDSGANATELLDLG-------------FGRSTFRFAAPpgSTLTVAD 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278428236  99 LASARrplrvsVPAKYRALGRRYLNTLELQGYTFlkqYLRGGIEATIKAGLADLAIDIVYTGDTLREMGLAVY 171
Cdd:cd13591   107 LAGLR------VATSYPNLVRRHLADLGVDATVV---RLDGAVEISVQLGVADAIADVVETGRTLKQAGLRVF 170
PBP2_HisGL2 cd13592
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
 21-168 5.90e-09

The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270310  Cd Length: 208  Bit Score: 53.38  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  21 LRGEDIPfwleRLSRQGTSAIGLTGQDLYTEyllsSKARARSTQTLRVLAsiswqasqtrFGKPALCLIGPSDATLPGLA 100
Cdd:cd13592    48 LRDDDIP----TFVGDGVVDLGITGENVLEE----AQLAGPNVEEVMDLG----------FGKCRLSVAVPEDGDYTGPA 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236 101 S--ARRplrvsVPAKYRALGRRYLNTlelQGYTFLKQYLRGGIEATIKAGLADLAIDIVYTGDTLREMGL 168
Cdd:cd13592   110 QlnGKR-----IATSYPNLLKRYLDE---LGVKASIVYVSGSVEVAPRLGLADAICDLVSSGATLRANGL 171
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 3-175 1.85e-08

ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP phosphoribosyltransferase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439810 [Multi-domain]  Cd Length: 281  Bit Score: 52.78  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   3 SIAQETLRLLTR-------PGER-------------MELRGEDIPFWLErlsrQGTSAIGLTGQDLYTEyllsSKARARS 62
Cdd:COG0040    11 RLLEETLELLKKagiklreEDSRkliaetndpdvevLLLRPQDIPTYVE----DGAADLGITGKDVLLE----SGADVYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  63 TQTLRvlasiswqasqtrFGKPALCLIGPSDATLPGLASARRpLRVsvpA-KYRALGRRYLNTLELQgYTFLKqyLRGGI 141
Cdd:COG0040    83 LLDLG-------------FGKCRLVVAVPEGSDYTSLADLRG-LRI---AtKYPNLTRRYFAEKGID-VEIVK--LNGSV 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1278428236 142 EATIKAGLADLAIDIVYTGDTLREMGLAVYNIIL 175
Cdd:COG0040   143 ELAPLLGLADAIVDIVSTGSTLRANGLKEVETIL 176
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 4-174 1.02e-07

The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270313  Cd Length: 205  Bit Score: 49.83  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236   4 IAQETLRLLTR---------PGER-------------MELRGEDIPFWLErlsrQGTSAIGLTGQDLYTEyllsskaraR 61
Cdd:cd13595    11 LLEEVLPLLEKagidpsellEESRklifedeegdirfILVKPSDVPTYVE----HGAADIGIVGKDVLLE---------Q 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  62 STQTLRVLasiswqasQTRFGKPALCLIGPSDATLPGLASARRplrvsVPAKYRALGRRYLNTLELQGYTFlkqYLRGGI 141
Cdd:cd13595    78 ERDVYELL--------DLGIGKCRFSVAGPPGRGLDSPLRRKR-----VATKYPNIARRYFASKGVDVEII---KLNGSV 141

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1278428236 142 EATIKAGLADLAIDIVYTGDTLREMGLAVYNII 174
Cdd:cd13595   142 ELAPLVGLADAIVDIVETGNTLKENGLEELEEI 174
PBP2_ATP-Prtase_HisG cd13525
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ...
 17-177 1.31e-07

The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic substrate-binding fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea.


Pssm-ID: 270243  Cd Length: 208  Bit Score: 49.76  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  17 ERMELRGEDIPFWLErlsrQGTSAIGLTGQDLYTEYLLSSkararsTQTLRVLasiswqasqtRFGKPALCLIGPSDATL 96
Cdd:cd13525    45 EILFGRPNDIPEFVA----DGIVDLGITGYDLVEENGFDD------VYELLDL----------GFGQCSLVLAAPPDFSW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278428236  97 PGLASARRpLRVSvpAKYRALGRRYLNTlelQGYTFLKQYLRGGIEATIKAGLADLAIDIVYTGDTLREMGLAVYNIILL 176
Cdd:cd13525   105 KGTNFLRG-KRIA--TKYPNLVRKYLAQ---KGIDFEVIKLEGSVEIAPVLGLADAIADLVSTGTTLSANGLRVIEKILD 178


                  .
gi 1278428236 177 S 177
Cdd:cd13525   179 S 179
PLN02245 PLN02245
ATP phosphoribosyl transferase
 101-168 6.44e-03

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 36.70  E-value: 6.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278428236 101 SARRPLRVSVPAKYraLGRRYLNTLELQGYTFLKQylRGGIEATIKAGLADLAIDIVYTGDTLREMGL 168
Cdd:PLN02245  192 TEERPLRVVTGFTY--LGPKFMKDNGFKHVTFSTA--DGALEAAPAMGIADAILDLVSSGTTLRENNL 255
 
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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