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Conserved domains on  [gi|39654305|pdb|1O64|B]
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Chain B, ATP phosphoribosyltransferase

Protein Classification

ATP phosphoribosyltransferase( domain architecture ID 10194437)

ATP phosphoribosyltransferase, the first enzyme in the histidine biosynthetic pathway, catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 2-198 4.63e-95

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: 275.95  E-value: 4.63e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIPKGRLEEKVMTYLKKTGVIFERESSILR------EGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETS 75
Cdd:cd13595   1 MLTIALPKGRLLEEVLPLLEKAGIDPSELLEESRklifedEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       76 LIQPFFIPTNISRMVLAGPKGRGI--PEGEKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETG 153
Cdd:cd13595  81 VYELLDLGIGKCRFSVAGPPGRGLdsPLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1O64_B      154 RTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEV 198
Cdd:cd13595 161 NTLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLREV 205
 
Name Accession Description Interval E-value
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 2-198 4.63e-95

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: 275.95  E-value: 4.63e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIPKGRLEEKVMTYLKKTGVIFERESSILR------EGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETS 75
Cdd:cd13595   1 MLTIALPKGRLLEEVLPLLEKAGIDPSELLEESRklifedEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       76 LIQPFFIPTNISRMVLAGPKGRGI--PEGEKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETG 153
Cdd:cd13595  81 VYELLDLGIGKCRFSVAGPPGRGLdsPLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1O64_B      154 RTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEV 198
Cdd:cd13595 161 NTLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLREV 205
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 3-176 7.63e-81

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: 238.98  E-value: 7.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B          3 LKLAIPKGRLEEKVMTYLKKTGVIFERESS----ILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQ 78
Cdd:TIGR00070   1 LRIALPKGRLLEDTLKLLEKAGLKLSREDGrkliARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGADVEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         79 PFFIPTNISRMVLAGPKGRGIPEGE-----KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETG 153
Cdd:TIGR00070  81 LLDLGFGKCRLVLAVPQESDIDSLEdlkegKRIATKYPNLARRYFEKKGIDVEIIKLNGSVELAPLLGLADAIVDIVSTG 160

                         170       180
                  ....*....|....*....|...
1O64_B        154 RTLKENNLEILDEIFVIRTHVVV 176
Cdd:TIGR00070 161 TTLRENGLRIIEVILESSARLIA 183
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 3-200 1.56e-79

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: 239.22  E-value: 1.56e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        3 LKLAIPKGRLEEKVMTYLKKTGVIFERESS---ILREGK-DIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQ 78
Cdd:COG0040   3 LRIALPKGRLLEETLELLKKAGIKLREEDSrklIAETNDpDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESGADVYE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       79 PFFIPTNISRMVLAGPKGRGIPEGE----KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGR 154
Cdd:COG0040  83 LLDLGFGKCRLVVAVPEGSDYTSLAdlrgLRIATKYPNLTRRYFAEKGIDVEIVKLNGSVELAPLLGLADAIVDIVSTGS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
1O64_B      155 TLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEVIE 200
Cdd:COG0040 163 TLRANGLKEVETILESSARLIANRASLKDKREKIEQLLERLEGVLE 208
HisG pfam01634
ATP phosphoribosyltransferase;
46-197 1.70e-61

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 189.11  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         46 RPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQPffIPTNIS--RMVLAGPKGRGIPEGE-----KRIATKFPNVTQRYC 118
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESGADVYEL--LDLGFGkcRLVVAVPEDSPYKSLEdlpegLRIATKYPNLTRRYF 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1O64_B        119 ESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQE 197
Cdd:pfam01634  79 AEKGIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKDKRELIEELLERLRG 157
PLN02245 PLN02245
ATP phosphoribosyl transferase
 3-200 8.55e-11

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 60.58  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         3 LKLAIP-KGRLEEKVMTYLKkTGVIFERESSILREGKDI-------VCFMvRPFDVPTYLVHGVADIGFCGTDVLLE--- 71
Cdd:PLN02245  70 IRLGLPsKGRMAEDTLDLLK-DCQLSVKKVNPRQYVAEIpqlpnleVWFQ-RPKDIVRKLLSGDLDLGIVGYDMLREygq 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        72 KETSLI------------QPFFIPT-----NISRM--VLAGPkgRGIPEGEKRIATKFPNVTQRYCESKGW-HCRIIPLK 131
Cdd:PLN02245 148 GNEDLVivhdalgfgdchLSIAIPKygifeNINSLkeLAQMP--QWTEERPLRVVTGFTYLGPKFMKDNGFkHVTFSTAD 225

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1O64_B       132 GSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVnpVSYR---TKREEVvsfLEKLQEVIE 200
Cdd:PLN02245 226 GALEAAPAMGIADAILDLVSSGTTLRENNLKEIEGGVVLESQAVL--VASRralLERKGA---LEVVHEILE 292
 
Name Accession Description Interval E-value
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 2-198 4.63e-95

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: 275.95  E-value: 4.63e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIPKGRLEEKVMTYLKKTGVIFERESSILR------EGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETS 75
Cdd:cd13595   1 MLTIALPKGRLLEEVLPLLEKAGIDPSELLEESRklifedEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       76 LIQPFFIPTNISRMVLAGPKGRGI--PEGEKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETG 153
Cdd:cd13595  81 VYELLDLGIGKCRFSVAGPPGRGLdsPLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETG 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1O64_B      154 RTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEV 198
Cdd:cd13595 161 NTLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLREV 205
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 3-176 7.63e-81

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: 238.98  E-value: 7.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B          3 LKLAIPKGRLEEKVMTYLKKTGVIFERESS----ILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQ 78
Cdd:TIGR00070   1 LRIALPKGRLLEDTLKLLEKAGLKLSREDGrkliARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGADVEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         79 PFFIPTNISRMVLAGPKGRGIPEGE-----KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETG 153
Cdd:TIGR00070  81 LLDLGFGKCRLVLAVPQESDIDSLEdlkegKRIATKYPNLARRYFEKKGIDVEIIKLNGSVELAPLLGLADAIVDIVSTG 160

                         170       180
                  ....*....|....*....|...
1O64_B        154 RTLKENNLEILDEIFVIRTHVVV 176
Cdd:TIGR00070 161 TTLRENGLRIIEVILESSARLIA 183
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 3-200 1.56e-79

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: 239.22  E-value: 1.56e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        3 LKLAIPKGRLEEKVMTYLKKTGVIFERESS---ILREGK-DIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQ 78
Cdd:COG0040   3 LRIALPKGRLLEETLELLKKAGIKLREEDSrklIAETNDpDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESGADVYE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       79 PFFIPTNISRMVLAGPKGRGIPEGE----KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGR 154
Cdd:COG0040  83 LLDLGFGKCRLVVAVPEGSDYTSLAdlrgLRIATKYPNLTRRYFAEKGIDVEIVKLNGSVELAPLLGLADAIVDIVSTGS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
1O64_B      155 TLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEVIE 200
Cdd:COG0040 163 TLRANGLKEVETILESSARLIANRASLKDKREKIEQLLERLEGVLE 208
HisG pfam01634
ATP phosphoribosyltransferase;
46-197 1.70e-61

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 189.11  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         46 RPFDVPTYLVHGVADIGFCGTDVLLEKETSLIQPffIPTNIS--RMVLAGPKGRGIPEGE-----KRIATKFPNVTQRYC 118
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESGADVYEL--LDLGFGkcRLVVAVPEDSPYKSLEdlpegLRIATKYPNLTRRYF 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1O64_B        119 ESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQE 197
Cdd:pfam01634  79 AEKGIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKDKRELIEELLERLRG 157
PBP2_ATP-Prtase_HisG cd13525
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ...
 2-198 1.19e-39

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: 135.28  E-value: 1.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIP-KGRLEEKVMTYLKKTGVIFE----RESSILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSL 76
Cdd:cd13525   1 MLRIAVPkKGRLSDDATELLENAGYKVEltlgRRLTAKTKVPDVEILFGRPNDIPEFVADGIVDLGITGYDLVEENGFDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       77 IQPF-FIPTNISRMVLAGP-----KGRGIPEGeKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDIT 150
Cdd:cd13525  81 VYELlDLGFGQCSLVLAAPpdfswKGTNFLRG-KRIATKYPNLVRKYLAQKGIDFEVIKLEGSVEIAPVLGLADAIADLV 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1O64_B      151 ETGRTLKENNLEILDEIFVIRTHVVVNPVSY-RTKREEVVSFLEKLQEV 198
Cdd:cd13525 160 STGTTLSANGLRVIEKILDSSARLIANRGSFgKFKQDKIDELVERIEGV 208
PBP2_HisGL4 cd13594
The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding ...
 2-188 8.14e-35

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: 122.81  E-value: 8.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIP-KGRLEEKVMTYLKKTGV-IFERESSIL---REGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSL 76
Cdd:cd13594   1 MIRIAPPnKGRLSEPTLKLLERAGIkVLASDERALfapTSDPDIELLFARAADIPEYVEDGAADLGITGYDLVVESGADV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       77 IQPFFIPTNISRMVLAGPKGRGI------PEGeKRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDIT 150
Cdd:cd13594  81 EELLDLGFGRAKLVLAVPEDSGIrspeddPKG-KRVATEFPNITRQYFEELGIDVEIVEVSGATEIAPHIGIADAIVDLT 159

                       170       180       190
                ....*....|....*....|....*....|....*...
1O64_B      151 ETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEV 188
Cdd:cd13594 160 STGTTLRVNGLKVIDTVLESSARLIANKNSLAVEKDKI 197
PBP2_HisGL3 cd13593
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ...
 2-196 1.80e-33

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: 119.64  E-value: 1.80e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIP-KGRLEEKVMTYLKKTGVIFERESS-----ILREGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETS 75
Cdd:cd13593   1 MLRLGIPsKGSLAEATLELLKKAGLKVSRGNPrqyfaSIDDLPEVEVLLLRAQEIVRYVADGDLDLGITGYDWVRESGAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       76 LIQPFFIPTNISRMVLAGP------------------KGRGipegeKRIATKFPNVTQRYCESKGW-HCRIIPLKGSVEL 136
Cdd:cd13593  81 VVVVADLGYGPVRLVLAVPedwidvstmadlaafraeDGRG-----LRIATEYPNLTRRFFAEKGGvKVQIVFSWGATEA 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1O64_B      137 APIAGLSDLIVDITETGRTLKENNLEILDEI-FVIRTHVVVNPVSYRT--KREEVVSFLEKLQ 196
Cdd:cd13593 156 KPPEGVADAIVDLTETGTTLRANRLKIIDDGvLESQAVLIANKRALKDpwKREKIEDLLELLE 218
PBP2_HisGL2 cd13592
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
 3-198 7.36e-31

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: 112.31  E-value: 7.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        3 LKLAIPK-GRLEEKVMTYLKKTGVIFERESSILR---EGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEketSLIQ 78
Cdd:cd13592   2 LRIAIQKkGRLSEKSLDLLAGCGIKFRRGNRLLIalaENLPIDLLFLRDDDIPTFVGDGVVDLGITGENVLEE---AQLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       79 PFFIPTNIS------RMVLAGPKGRGIPEGE----KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVD 148
Cdd:cd13592  79 GPNVEEVMDlgfgkcRLSVAVPEDGDYTGPAqlngKRIATSYPNLLKRYLDELGVKASIVYVSGSVEVAPRLGLADAICD 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1O64_B      149 ITETGRTLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEV 198
Cdd:cd13592 159 LVSSGATLRANGLKEVETILESEAVLIGRPNPSKEKKALLDLLLRRIDGV 208
PBP2_HisGL1 cd13591
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
 2-198 2.47e-28

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: 105.93  E-value: 2.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        2 LLKLAIP-KGRLEEKVMTYLKKTGVIFERESSILR---EGKDIVCFMVRPFDVPTYLVHGVADIGFCGTDVLLEKETSLI 77
Cdd:cd13591   1 MLRIAVPnKGSLAEPAAELLVEAGYRQRRDGKELVvrdPDNEVEFFFLRPRDIAIYVSSGILDIGITGRDLLSDSGANAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B       78 QPFFIPTNISRMVLAGPKGRGIPEGE---KRIATKFPNVTQRYCESKGWHCRIIPLKGSVELAPIAGLSDLIVDITETGR 154
Cdd:cd13591  81 ELLDLGFGRSTFRFAAPPGSTLTVADlagLRVATSYPNLVRRHLADLGVDATVVRLDGAVEISVQLGVADAIADVVETGR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1O64_B      155 TLKENNLEILDEIFVIRTHVVVNPVSYRTKREEVVSFLEKLQEV 198
Cdd:cd13591 161 TLKQAGLRVFGEPILKSEAVLIRRSGAQTNKPAQQQLVRRLQGV 204
PLN02245 PLN02245
ATP phosphoribosyl transferase
 3-200 8.55e-11

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 60.58  E-value: 8.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B         3 LKLAIP-KGRLEEKVMTYLKkTGVIFERESSILREGKDI-------VCFMvRPFDVPTYLVHGVADIGFCGTDVLLE--- 71
Cdd:PLN02245  70 IRLGLPsKGRMAEDTLDLLK-DCQLSVKKVNPRQYVAEIpqlpnleVWFQ-RPKDIVRKLLSGDLDLGIVGYDMLREygq 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1O64_B        72 KETSLI------------QPFFIPT-----NISRM--VLAGPkgRGIPEGEKRIATKFPNVTQRYCESKGW-HCRIIPLK 131
Cdd:PLN02245 148 GNEDLVivhdalgfgdchLSIAIPKygifeNINSLkeLAQMP--QWTEERPLRVVTGFTYLGPKFMKDNGFkHVTFSTAD 225

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1O64_B       132 GSVELAPIAGLSDLIVDITETGRTLKENNLEILDEIFVIRTHVVVnpVSYR---TKREEVvsfLEKLQEVIE 200
Cdd:PLN02245 226 GALEAAPAMGIADAILDLVSSGTTLRENNLKEIEGGVVLESQAVL--VASRralLERKGA---LEVVHEILE 292
 
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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