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Conserved domains on  [gi|1372041483|gb|AVR52653|]
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His1 [Expression vector pCPC77]

Protein Classification

Periplasmic_Binding_Protein_Type_2 and HisG_C-term domain-containing protein( domain architecture ID 10402584)

Periplasmic_Binding_Protein_Type_2 and HisG_C-term domain-containing protein

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 ...
 10-215 6.21e-101

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 cd13592:

Pssm-ID: 473866  Cd Length: 208  Bit Score: 294.13  E-value: 6.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  10 RLLFAVPKKGRLYEKCCNLLSGADIQFRRSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAE-QFD 88
Cdd:cd13592     1 RLRIAIQKKGRLSEKSLDLLAGCGIKFRRGNRLLIALAENLPIDLLFLRDDDIPTFVGDGVVDLGITGENVLEEAQlAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  89 NIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKpTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:cd13592    81 NVEEVMDLGFGKCRLSVAVPEDGDYTGPAQLNGKRIATSYPNLLKRYLDELGVK-ASIVYVSGSVEVAPRLGLADAICDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLISSK--KSKFPEMVNIIVQRLQGV 215
Cdd:cd13592   160 VSSGATLRANGLKEVETILESEAVLIGRPnpSKEKKALLDLLLRRIDGV 208
HisG_C-term TIGR03455
ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal ...
 203-297 2.90e-35

ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal third of the HisG protein. It is absent in many lineages.


:

Pssm-ID: 274587 [Multi-domain]  Cd Length: 92  Bit Score: 122.66  E-value: 2.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 203 EMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDkhsddEEDWVAISSMVNRKEIGNVMDELKK 282
Cdd:TIGR03455   3 EKIEQLLTRLQGVLAARGKVLLMMNVPRDNLDEVRAVLPGLEGPTVSPLA-----DEGWVAVHAVVDEKVVNELIDKLKA 77

                          90
                  ....*....|....*
gi 1372041483 283 AGATDILVLEISNCR 297
Cdd:TIGR03455  78 AGARDILVLPIEKCR 92
 
Name Accession Description Interval E-value
PBP2_HisGL2 cd13592
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
 10-215 6.21e-101

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: 294.13  E-value: 6.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  10 RLLFAVPKKGRLYEKCCNLLSGADIQFRRSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAE-QFD 88
Cdd:cd13592     1 RLRIAIQKKGRLSEKSLDLLAGCGIKFRRGNRLLIALAENLPIDLLFLRDDDIPTFVGDGVVDLGITGENVLEEAQlAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  89 NIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKpTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:cd13592    81 NVEEVMDLGFGKCRLSVAVPEDGDYTGPAQLNGKRIATSYPNLLKRYLDELGVK-ASIVYVSGSVEVAPRLGLADAICDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLISSK--KSKFPEMVNIIVQRLQGV 215
Cdd:cd13592   160 VSSGATLRANGLKEVETILESEAVLIGRPnpSKEKKALLDLLLRRIDGV 208
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 9-297 6.15e-91

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: 271.58  E-value: 6.15e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483   9 DRLLFAVPKkGRLYEKCCNLLSGADIQFR-RSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEqf 87
Cdd:COG0040     1 MMLRIALPK-GRLLEETLELLKKAGIKLReEDSRKLIAETNDPDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  88 DNIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLsDKPTNIRYVGGSVEASCALGVADAIVD 167
Cdd:COG0040    78 ADVYELLDLGFGKCRLVVAVPEGSDYTSLADLRGLRIATKYPNLTRRYFAEK-GIDVEIVKLNGSVELAPLLGLADAIVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 168 LVESGETMKAAGLKAIETILETSAHLISSKKS---KfPEMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRR 244
Cdd:COG0040   157 IVSTGSTLRANGLKEVETILESSARLIANRASlkdK-REKIEQLLERLEGVLEARGKVYLMMNVPKEKLEEVVALLPGLE 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1372041483 245 AATVSTLdkhsddeEDWVAISSMVNRKEIGNVMDELKKAGATDILVLEISNCR 297
Cdd:COG0040   236 SPTVSPL-------EDWVAVHAVVPEDEVWELIDKLKAAGARGILVTPIEKMI 281
HisG pfam01634
ATP phosphoribosyltransferase;
58-214 3.07e-63

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 196.43  E-value: 3.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  58 PAADIPVFVGEGNCDLGITGLDQIKEAEqfDNIEDLLDLKFGSCKLQIQVPADGEYEKPEQLV-GKKIVSSFTKLSTDYF 136
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESG--ADVYELLDLGFGKCRLVVAVPEDSPYKSLEDLPeGLRIATKYPNLTRRYF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 137 KQLsDKPTNIRYVGGSVEASCALGVADAIVDLVESGETMKAAGLKAIETILETSAHLISSKKSKF--PEMVNIIVQRLQG 214
Cdd:pfam01634  79 AEK-GIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKdkRELIEELLERLRG 157
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 11-194 3.51e-53

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: 171.58  E-value: 3.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  11 LLFAVPKkGRLYEKCCNLLSGADIQFRRS-NRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQfdN 89
Cdd:TIGR00070   1 LRIALPK-GRLLEDTLKLLEKAGLKLSREdGRKLIARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGA--D 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  90 IEDLLDLKFGSCKLQIQVPADGEYEKPEQL-VGKKIVSSFTKLSTDYFKQLsDKPTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:TIGR00070  78 VEELLDLGFGKCRLVLAVPQESDIDSLEDLkEGKRIATKYPNLARRYFEKK-GIDVEIIKLNGSVELAPLLGLADAIVDI 156

                         170       180
                  ....*....|....*....|....*.
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLI 194
Cdd:TIGR00070 157 VSTGTTLRENGLRIIEVILESSARLI 182
HisG_C-term TIGR03455
ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal ...
 203-297 2.90e-35

ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal third of the HisG protein. It is absent in many lineages.


Pssm-ID: 274587 [Multi-domain]  Cd Length: 92  Bit Score: 122.66  E-value: 2.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 203 EMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDkhsddEEDWVAISSMVNRKEIGNVMDELKK 282
Cdd:TIGR03455   3 EKIEQLLTRLQGVLAARGKVLLMMNVPRDNLDEVRAVLPGLEGPTVSPLA-----DEGWVAVHAVVDEKVVNELIDKLKA 77

                          90
                  ....*....|....*
gi 1372041483 283 AGATDILVLEISNCR 297
Cdd:TIGR03455  78 AGARDILVLPIEKCR 92
HisG_C pfam08029
HisG, C-terminal domain;
218-295 2.41e-31

HisG, C-terminal domain;


Pssm-ID: 462342 [Multi-domain]  Cd Length: 73  Bit Score: 111.70  E-value: 2.41e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372041483 218 AQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDkhsddEEDWVAISSMVNRKEIGNVMDELKKAGATDILVLEISN 295
Cdd:pfam08029   1 ARKYVYLMYNVPREKLEEVLAILPGLRSPTVSPLA-----DEGWVAVHAVVEEKEVWEVMDELKAAGAEGILVLPIEK 73
PLN02245 PLN02245
ATP phosphoribosyl transferase
 13-290 4.32e-29

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 114.51  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  13 FAVPKKGRLYEKCCNLLSGADIQFRRSN-RLDIALSTNLP-IALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQFDni 90
Cdd:PLN02245   72 LGLPSKGRMAEDTLDLLKDCQLSVKKVNpRQYVAEIPQLPnLEVWFQRPKDIVRKLLSGDLDLGIVGYDMLREYGQGN-- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  91 EDLL----DLKFGSCKLQIQVPADGEYEK----------PEQLVGK--KIVSSFTKLSTDYFKQLSDKPTNIRYVGGSVE 154
Cdd:PLN02245  150 EDLVivhdALGFGDCHLSIAIPKYGIFENinslkelaqmPQWTEERplRVVTGFTYLGPKFMKDNGFKHVTFSTADGALE 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 155 ASCALGVADAIVDLVESGETMKAAGLKAIE--TILETSAHLISSKKS--KFPEMVNI---IVQRLQGVLAA--QEYVLCN 225
Cdd:PLN02245  230 AAPAMGIADAILDLVSSGTTLRENNLKEIEggVVLESQAVLVASRRAllERKGALEVvheILERLEAHLRAegQFTVTAN 309

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372041483 226 Y--NAPKSIQAKCLTIT--PGRRAATVSTLDKHSDDEE--DWVAISSMVNRKEIGNVMDELKKAGATDILV 290
Cdd:PLN02245  310 MrgSSAEEVAERVLSQPslSGLQGPTISPVYCKRDGKVavDYYAIVICVPKKALYESVQQLRKIGGSGVLV 380
 
Name Accession Description Interval E-value
PBP2_HisGL2 cd13592
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
 10-215 6.21e-101

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: 294.13  E-value: 6.21e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  10 RLLFAVPKKGRLYEKCCNLLSGADIQFRRSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAE-QFD 88
Cdd:cd13592     1 RLRIAIQKKGRLSEKSLDLLAGCGIKFRRGNRLLIALAENLPIDLLFLRDDDIPTFVGDGVVDLGITGENVLEEAQlAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  89 NIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKpTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:cd13592    81 NVEEVMDLGFGKCRLSVAVPEDGDYTGPAQLNGKRIATSYPNLLKRYLDELGVK-ASIVYVSGSVEVAPRLGLADAICDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLISSK--KSKFPEMVNIIVQRLQGV 215
Cdd:cd13592   160 VSSGATLRANGLKEVETILESEAVLIGRPnpSKEKKALLDLLLRRIDGV 208
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 9-297 6.15e-91

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: 271.58  E-value: 6.15e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483   9 DRLLFAVPKkGRLYEKCCNLLSGADIQFR-RSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEqf 87
Cdd:COG0040     1 MMLRIALPK-GRLLEETLELLKKAGIKLReEDSRKLIAETNDPDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  88 DNIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLsDKPTNIRYVGGSVEASCALGVADAIVD 167
Cdd:COG0040    78 ADVYELLDLGFGKCRLVVAVPEGSDYTSLADLRGLRIATKYPNLTRRYFAEK-GIDVEIVKLNGSVELAPLLGLADAIVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 168 LVESGETMKAAGLKAIETILETSAHLISSKKS---KfPEMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRR 244
Cdd:COG0040   157 IVSTGSTLRANGLKEVETILESSARLIANRASlkdK-REKIEQLLERLEGVLEARGKVYLMMNVPKEKLEEVVALLPGLE 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1372041483 245 AATVSTLdkhsddeEDWVAISSMVNRKEIGNVMDELKKAGATDILVLEISNCR 297
Cdd:COG0040   236 SPTVSPL-------EDWVAVHAVVPEDEVWELIDKLKAAGARGILVTPIEKMI 281
HisG pfam01634
ATP phosphoribosyltransferase;
58-214 3.07e-63

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 196.43  E-value: 3.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  58 PAADIPVFVGEGNCDLGITGLDQIKEAEqfDNIEDLLDLKFGSCKLQIQVPADGEYEKPEQLV-GKKIVSSFTKLSTDYF 136
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESG--ADVYELLDLGFGKCRLVVAVPEDSPYKSLEDLPeGLRIATKYPNLTRRYF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 137 KQLsDKPTNIRYVGGSVEASCALGVADAIVDLVESGETMKAAGLKAIETILETSAHLISSKKSKF--PEMVNIIVQRLQG 214
Cdd:pfam01634  79 AEK-GIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKdkRELIEELLERLRG 157
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 11-194 3.51e-53

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: 171.58  E-value: 3.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  11 LLFAVPKkGRLYEKCCNLLSGADIQFRRS-NRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQfdN 89
Cdd:TIGR00070   1 LRIALPK-GRLLEDTLKLLEKAGLKLSREdGRKLIARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGA--D 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  90 IEDLLDLKFGSCKLQIQVPADGEYEKPEQL-VGKKIVSSFTKLSTDYFKQLsDKPTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:TIGR00070  78 VEELLDLGFGKCRLVLAVPQESDIDSLEDLkEGKRIATKYPNLARRYFEKK-GIDVEIIKLNGSVELAPLLGLADAIVDI 156

                         170       180
                  ....*....|....*....|....*.
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLI 194
Cdd:TIGR00070 157 VSTGTTLRENGLRIIEVILESSARLI 182
PBP2_HisGL4 cd13594
The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding ...
 11-215 1.39e-46

The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic 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: 270312  Cd Length: 207  Bit Score: 155.56  E-value: 1.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  11 LLFAVPKKGRLYEKCCNLLSGADIQFRRS-NRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQfdN 89
Cdd:cd13594     2 IRIAPPNKGRLSEPTLKLLERAGIKVLASdERALFAPTSDPDIELLFARAADIPEYVEDGAADLGITGYDLVVESGA--D 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  90 IEDLLDLKFGSCKLQIQVPADGEYEKPE-QLVGKKIVSSFTKLSTDYFKQLSdKPTNIRYVGGSVEASCALGVADAIVDL 168
Cdd:cd13594    80 VEELLDLGFGRAKLVLAVPEDSGIRSPEdDPKGKRVATEFPNITRQYFEELG-IDVEIVEVSGATEIAPHIGIADAIVDL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLISSKKSKFPE--MVNIIVQRLQGV 215
Cdd:cd13594   159 TSTGTTLRVNGLKVIDTVLESSARLIANKNSLAVEkdKIEELVTALKGV 207
PBP2_ATP-Prtase_HisG cd13525
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ...
 10-215 6.71e-45

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: 151.45  E-value: 6.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  10 RLLFAVPKKGRLYEKCCNLLSGADIQFRRSNRLDIALST-NLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEaEQFD 88
Cdd:cd13525     1 MLRIAVPKKGRLSDDATELLENAGYKVELTLGRRLTAKTkVPDVEILFGRPNDIPEFVADGIVDLGITGYDLVEE-NGFD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  89 NIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKPTNIRyVGGSVEASCALGVADAIVDL 168
Cdd:cd13525    80 DVYELLDLGFGQCSLVLAAPPDFSWKGTNFLRGKRIATKYPNLVRKYLAQKGIDFEVIK-LEGSVEIAPVLGLADAIADL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1372041483 169 VESGETMKAAGLKAIETILETSAHLISSKKSKFP---EMVNIIVQRLQGV 215
Cdd:cd13525   159 VSTGTTLSANGLRVIEKILDSSARLIANRGSFGKfkqDKIDELVERIEGV 208
PBP2_HisGL3 cd13593
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ...
 13-215 1.99e-41

The catalytic domain of hexameric long form HisGL3; 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: 270311  Cd Length: 220  Bit Score: 142.75  E-value: 1.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  13 FAVPKKGRLYEKCCNLLSGADIQFRRSN-RLDIALSTNLP-IALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQfdNI 90
Cdd:cd13593     4 LGIPSKGSLAEATLELLKKAGLKVSRGNpRQYFASIDDLPeVEVLLLRAQEIVRYVADGDLDLGITGYDWVRESGA--DV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  91 EDLLDLKFGSCKLQIQVP---------ADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKPTNIRYVGGSVEASCALGV 161
Cdd:cd13593    82 VVVADLGYGPVRLVLAVPedwidvstmADLAAFRAEDGRGLRIATEYPNLTRRFFAEKGGVKVQIVFSWGATEAKPPEGV 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1372041483 162 ADAIVDLVESGETMKAAGLKAIETI-LETSAHLISSKKS-KFPEMVNIIVQ---RLQGV 215
Cdd:cd13593   162 ADAIVDLTETGTTLRANRLKIIDDGvLESQAVLIANKRAlKDPWKREKIEDlleLLEAA 220
PBP2_HisGL1 cd13591
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
 11-215 2.24e-39

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: 136.75  E-value: 2.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  11 LLFAVPKKGRLYEKCCNLLSGADIQFRR-SNRLDIALSTNlPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQfdN 89
Cdd:cd13591     2 LRIAVPNKGSLAEPAAELLVEAGYRQRRdGKELVVRDPDN-EVEFFFLRPRDIAIYVSSGILDIGITGRDLLSDSGA--N 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  90 IEDLLDLKFGSCKLQIQVPAdGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKPTNIRyVGGSVEASCALGVADAIVDLV 169
Cdd:cd13591    79 ATELLDLGFGRSTFRFAAPP-GSTLTVADLAGLRVATSYPNLVRRHLADLGVDATVVR-LDGAVEISVQLGVADAIADVV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1372041483 170 ESGETMKAAGLKAI-ETILETSAHLISSKKSKFP-EMVNIIVQRLQGV 215
Cdd:cd13591   157 ETGRTLKQAGLRVFgEPILKSEAVLIRRSGAQTNkPAQQQLVRRLQGV 204
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 11-215 2.46e-38

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: 134.19  E-value: 2.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  11 LLFAVPKkGRLYEKCCNLLSGADIQFR----RSNRLDIALSTNlPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQ 86
Cdd:cd13595     2 LTIALPK-GRLLEEVLPLLEKAGIDPSelleESRKLIFEDEEG-DIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQER 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  87 fdNIEDLLDLKFGSCKLQIQVPADGEYEKPeqLVGKKIVSSFTKLSTDYFKQLsDKPTNIRYVGGSVEASCALGVADAIV 166
Cdd:cd13595    80 --DVYELLDLGIGKCRFSVAGPPGRGLDSP--LRRKRVATKYPNIARRYFASK-GVDVEIIKLNGSVELAPLVGLADAIV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1372041483 167 DLVESGETMKAAGLKAIETILETSAHLISSKKS---KFPEMVNIIvQRLQGV 215
Cdd:cd13595   155 DIVETGNTLKENGLEELEEIMDISARLIVNRASyktKRDEIKELI-ERLREV 205
HisG_C-term TIGR03455
ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal ...
 203-297 2.90e-35

ATP phosphoribosyltransferase, C-terminal domain; This domain corresponds to the C-terminal third of the HisG protein. It is absent in many lineages.


Pssm-ID: 274587 [Multi-domain]  Cd Length: 92  Bit Score: 122.66  E-value: 2.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 203 EMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDkhsddEEDWVAISSMVNRKEIGNVMDELKK 282
Cdd:TIGR03455   3 EKIEQLLTRLQGVLAARGKVLLMMNVPRDNLDEVRAVLPGLEGPTVSPLA-----DEGWVAVHAVVDEKVVNELIDKLKA 77

                          90
                  ....*....|....*
gi 1372041483 283 AGATDILVLEISNCR 297
Cdd:TIGR03455  78 AGARDILVLPIEKCR 92
HisG_C pfam08029
HisG, C-terminal domain;
218-295 2.41e-31

HisG, C-terminal domain;


Pssm-ID: 462342 [Multi-domain]  Cd Length: 73  Bit Score: 111.70  E-value: 2.41e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372041483 218 AQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDkhsddEEDWVAISSMVNRKEIGNVMDELKKAGATDILVLEISN 295
Cdd:pfam08029   1 ARKYVYLMYNVPREKLEEVLAILPGLRSPTVSPLA-----DEGWVAVHAVVEEKEVWEVMDELKAAGAEGILVLPIEK 73
PLN02245 PLN02245
ATP phosphoribosyl transferase
 13-290 4.32e-29

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 114.51  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  13 FAVPKKGRLYEKCCNLLSGADIQFRRSN-RLDIALSTNLP-IALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQFDni 90
Cdd:PLN02245   72 LGLPSKGRMAEDTLDLLKDCQLSVKKVNpRQYVAEIPQLPnLEVWFQRPKDIVRKLLSGDLDLGIVGYDMLREYGQGN-- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483  91 EDLL----DLKFGSCKLQIQVPADGEYEK----------PEQLVGK--KIVSSFTKLSTDYFKQLSDKPTNIRYVGGSVE 154
Cdd:PLN02245  150 EDLVivhdALGFGDCHLSIAIPKYGIFENinslkelaqmPQWTEERplRVVTGFTYLGPKFMKDNGFKHVTFSTADGALE 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372041483 155 ASCALGVADAIVDLVESGETMKAAGLKAIE--TILETSAHLISSKKS--KFPEMVNI---IVQRLQGVLAA--QEYVLCN 225
Cdd:PLN02245  230 AAPAMGIADAILDLVSSGTTLRENNLKEIEggVVLESQAVLVASRRAllERKGALEVvheILERLEAHLRAegQFTVTAN 309

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1372041483 226 Y--NAPKSIQAKCLTIT--PGRRAATVSTLDKHSDDEE--DWVAISSMVNRKEIGNVMDELKKAGATDILV 290
Cdd:PLN02245  310 MrgSSAEEVAERVLSQPslSGLQGPTISPVYCKRDGKVavDYYAIVICVPKKALYESVQQLRKIGGSGVLV 380
 
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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