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Conserved domains on  [gi|489277935|ref|WP_003185607|]
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MULTISPECIES: ATP phosphoribosyltransferase [Bacillus]

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 ...
 5-204 3.19e-114

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: 324.10  E-value: 3.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPKGRIFEEAADMLRKAGYQLPEEFDDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:cd13595    2 LTIALPKGRLLEEVLPLLEKAGIDPSELLEESRKLIFEDEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  85 YEVLDLNISKCRLAVAGLPETAAD--TVAPRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVSTGQ 162
Cdd:cd13595   82 YELLDLGIGKCRFSVAGPPGRGLDspLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETGN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489277935 163 TLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRLS 204
Cdd:cd13595  162 TLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLR 203
 
Name Accession Description Interval E-value
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 5-204 3.19e-114

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: 324.10  E-value: 3.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPKGRIFEEAADMLRKAGYQLPEEFDDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:cd13595    2 LTIALPKGRLLEEVLPLLEKAGIDPSELLEESRKLIFEDEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  85 YEVLDLNISKCRLAVAGLPETAAD--TVAPRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVSTGQ 162
Cdd:cd13595   82 YELLDLGIGKCRFSVAGPPGRGLDspLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETGN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489277935 163 TLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRLS 204
Cdd:cd13595  162 TLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLR 203
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 5-213 6.30e-102

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: 295.84  E-value: 6.30e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPKGRIFEEAADMLRKAGYQLPEEfdDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:COG0040    3 LRIALPKGRLLEETLELLKKAGIKLREE--DSRKLIAETNDPDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESGADV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  85 YEVLDLNISKCRLAVAGLPETAADTVAP----RVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVST 160
Cdd:COG0040   81 YELLDLGFGKCRLVVAVPEGSDYTSLADlrglRIATKYPNLTRRYFAEKGIDVEIVKLNGSVELAPLLGLADAIVDIVST 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489277935 161 GQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRLSLIVEGEKAK 213
Cdd:COG0040  161 GSTLRANGLKEVETILESSARLIANRASLKDKREKIEQLLERLEGVLEARGKV 213
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 5-184 3.15e-85

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: 250.16  E-value: 3.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935    5 LTIAMPKGRIFEEAADMLRKAGYQLPEEfdDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:TIGR00070   1 LRIALPKGRLLEDTLKLLEKAGLKLSRE--DGRKLIARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGADV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   85 YEVLDLNISKCRLAVAGLPETAADTVAP-----RVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVS 159
Cdd:TIGR00070  79 EELLDLGFGKCRLVLAVPQESDIDSLEDlkegkRIATKYPNLARRYFEKKGIDVEIIKLNGSVELAPLLGLADAIVDIVS 158

                         170       180
                  ....*....|....*....|....*
gi 489277935  160 TGQTLRENGLVETEKICDITSRLIV 184
Cdd:TIGR00070 159 TGTTLRENGLRIIEVILESSARLIA 183
HisG pfam01634
ATP phosphoribosyltransferase;
54-203 1.04e-74

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 222.24  E-value: 1.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   54 KPMDVTTYVEHGVADVGIAGKDVLLEEERDVYEVLDLNISKCRLAVAGLPETAADTVAP-----RVATKYPNVASSYFRE 128
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESGADVYELLDLGFGKCRLVVAVPEDSPYKSLEDlpeglRIATKYPNLTRRYFAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489277935  129 QGEQVEIIKLNGSIELAPLIGLAGRIVDIVSTGQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRL 203
Cdd:pfam01634  81 KGIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKDKRELIEELLERL 155
PLN02245 PLN02245
ATP phosphoribosyl transferase
 3-173 1.76e-21

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 91.01  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   3 KELTIAMP-KGRIFEEAADMLRKAgyQLPEEFDDSRKLIIQVPE-ENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLE- 79
Cdd:PLN02245  68 TQIRLGLPsKGRMAEDTLDLLKDC--QLSVKKVNPRQYVAEIPQlPNLEVWFQRPKDIVRKLLSGDLDLGIVGYDMLREy 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  80 --EERDVYEVLD-LNISKCRLAVA-----------GLPETAAD----TVAP-RVATKYPNVASSYFREQG-EQVEIIKLN 139
Cdd:PLN02245 146 gqGNEDLVIVHDaLGFGDCHLSIAipkygifeninSLKELAQMpqwtEERPlRVVTGFTYLGPKFMKDNGfKHVTFSTAD 225

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489277935 140 GSIELAPLIGLAGRIVDIVSTGQTLRENGLVETE 173
Cdd:PLN02245 226 GALEAAPAMGIADAILDLVSSGTTLRENNLKEIE 259
 
Name Accession Description Interval E-value
PBP2_HisGs cd13595
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
 5-204 3.19e-114

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: 324.10  E-value: 3.19e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPKGRIFEEAADMLRKAGYQLPEEFDDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:cd13595    2 LTIALPKGRLLEEVLPLLEKAGIDPSELLEESRKLIFEDEEGDIRFILVKPSDVPTYVEHGAADIGIVGKDVLLEQERDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  85 YEVLDLNISKCRLAVAGLPETAAD--TVAPRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVSTGQ 162
Cdd:cd13595   82 YELLDLGIGKCRFSVAGPPGRGLDspLRRKRVATKYPNIARRYFASKGVDVEIIKLNGSVELAPLVGLADAIVDIVETGN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489277935 163 TLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRLS 204
Cdd:cd13595  162 TLKENGLEELEEIMDISARLIVNRASYKTKRDEIKELIERLR 203
HisG COG0040
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
 5-213 6.30e-102

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: 295.84  E-value: 6.30e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPKGRIFEEAADMLRKAGYQLPEEfdDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:COG0040    3 LRIALPKGRLLEETLELLKKAGIKLREE--DSRKLIAETNDPDVEVLLLRPQDIPTYVEDGAADLGITGKDVLLESGADV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  85 YEVLDLNISKCRLAVAGLPETAADTVAP----RVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVST 160
Cdd:COG0040   81 YELLDLGFGKCRLVVAVPEGSDYTSLADlrglRIATKYPNLTRRYFAEKGIDVEIVKLNGSVELAPLLGLADAIVDIVST 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489277935 161 GQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRLSLIVEGEKAK 213
Cdd:COG0040  161 GSTLRANGLKEVETILESSARLIANRASLKDKREKIEQLLERLEGVLEARGKV 213
hisG TIGR00070
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
 5-184 3.15e-85

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: 250.16  E-value: 3.15e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935    5 LTIAMPKGRIFEEAADMLRKAGYQLPEEfdDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERDV 84
Cdd:TIGR00070   1 LRIALPKGRLLEDTLKLLEKAGLKLSRE--DGRKLIARDPDEGIEVLLLRPQDIPTYVEHGAADLGITGYDVLLESGADV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   85 YEVLDLNISKCRLAVAGLPETAADTVAP-----RVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVS 159
Cdd:TIGR00070  79 EELLDLGFGKCRLVLAVPQESDIDSLEDlkegkRIATKYPNLARRYFEKKGIDVEIIKLNGSVELAPLLGLADAIVDIVS 158

                         170       180
                  ....*....|....*....|....*
gi 489277935  160 TGQTLRENGLVETEKICDITSRLIV 184
Cdd:TIGR00070 159 TGTTLRENGLRIIEVILESSARLIA 183
HisG pfam01634
ATP phosphoribosyltransferase;
54-203 1.04e-74

ATP phosphoribosyltransferase;


Pssm-ID: 460274  Cd Length: 157  Bit Score: 222.24  E-value: 1.04e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   54 KPMDVTTYVEHGVADVGIAGKDVLLEEERDVYEVLDLNISKCRLAVAGLPETAADTVAP-----RVATKYPNVASSYFRE 128
Cdd:pfam01634   1 RAQDIPTYVEDGAADLGITGKDVLLESGADVYELLDLGFGKCRLVVAVPEDSPYKSLEDlpeglRIATKYPNLTRRYFAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489277935  129 QGEQVEIIKLNGSIELAPLIGLAGRIVDIVSTGQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRL 203
Cdd:pfam01634  81 KGIQVEIIKLSGSVELAPALGLADAIVDIVETGTTLRANGLKEIETILESSARLIANRASLKDKRELIEELLERL 155
PBP2_ATP-Prtase_HisG cd13525
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ...
 5-203 2.66e-54

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: 172.26  E-value: 2.66e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMP-KGRIFEEAADMLRKAGYQLpeEFDDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEE-R 82
Cdd:cd13525    2 LRIAVPkKGRLSDDATELLENAGYKV--ELTLGRRLTAKTKVPDVEILFGRPNDIPEFVADGIVDLGITGYDLVEENGfD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  83 DVYEVLDLNISKCRLAVAGLPETAADTVA----PRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIV 158
Cdd:cd13525   80 DVYELLDLGFGQCSLVLAAPPDFSWKGTNflrgKRIATKYPNLVRKYLAQKGIDFEVIKLEGSVEIAPVLGLADAIADLV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489277935 159 STGQTLRENGLVETEKICDITSRLIVNPVSY-RMKDAVIDEMASRL 203
Cdd:cd13525  160 STGTTLSANGLRVIEKILDSSARLIANRGSFgKFKQDKIDELVERI 205
PBP2_HisGL4 cd13594
The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding ...
 5-199 6.82e-48

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: 155.94  E-value: 6.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMP-KGRIFEEAADMLRKAGyqLPEEFDDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERD 83
Cdd:cd13594    2 IRIAPPnKGRLSEPTLKLLERAG--IKVLASDERALFAPTSDPDIELLFARAADIPEYVEDGAADLGITGYDLVVESGAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  84 VYEVLDLNISKCRLAVAgLPETAADTVAP------RVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDI 157
Cdd:cd13594   80 VEELLDLGFGRAKLVLA-VPEDSGIRSPEddpkgkRVATEFPNITRQYFEELGIDVEIVEVSGATEIAPHIGIADAIVDL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489277935 158 VSTGQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEM 199
Cdd:cd13594  159 TSTGTTLRVNGLKVIDTVLESSARLIANKNSLAVEKDKIEEL 200
PBP2_HisGL2 cd13592
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
 5-203 9.87e-46

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: 150.45  E-value: 9.87e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMPK-GRIFEEAADMLRKAGYQLPEEfddSRKLIIQVpeENLR--FILAKPMDVTTYVEHGVADVGIAGKDVLLEEE 81
Cdd:cd13592    2 LRIAIQKkGRLSEKSLDLLAGCGIKFRRG---NRLLIALA--ENLPidLLFLRDDDIPTFVGDGVVDLGITGENVLEEAQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  82 ---RDVYEVLDLNISKCRLAVAgLPE-----TAADTVAPRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGR 153
Cdd:cd13592   77 lagPNVEEVMDLGFGKCRLSVA-VPEdgdytGPAQLNGKRIATSYPNLLKRYLDELGVKASIVYVSGSVEVAPRLGLADA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489277935 154 IVDIVSTGQTLRENGLVETEKICDITSRLIVNPVSYRMKDAVIDEMASRL 203
Cdd:cd13592  156 ICDLVSSGATLRANGLKEVETILESEAVLIGRPNPSKEKKALLDLLLRRI 205
PBP2_HisGL1 cd13591
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
 5-203 4.67e-38

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: 130.59  E-value: 4.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMP-KGRIFEEAADMLRKAGYQLPEefdDSRKLIIQVPEENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEERD 83
Cdd:cd13591    2 LRIAVPnKGSLAEPAAELLVEAGYRQRR---DGKELVVRDPDNEVEFFFLRPRDIAIYVSSGILDIGITGRDLLSDSGAN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  84 VYEVLDLNISKCRLAVAGLPE---TAADTVAPRVATKYPNVASSYFREQGEQVEIIKLNGSIELAPLIGLAGRIVDIVST 160
Cdd:cd13591   79 ATELLDLGFGRSTFRFAAPPGstlTVADLAGLRVATSYPNLVRRHLADLGVDATVVRLDGAVEISVQLGVADAIADVVET 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489277935 161 GQTLRENGL-VETEKICDITSRLIVNPVSYRMKDAvIDEMASRL 203
Cdd:cd13591  159 GRTLKQAGLrVFGEPILKSEAVLIRRSGAQTNKPA-QQQLVRRL 201
PBP2_HisGL3 cd13593
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ...
 5-203 5.81e-35

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: 123.11  E-value: 5.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   5 LTIAMP-KGRIFEEAADMLRKAGYQLpeEFDDSRKLIIQVPE-ENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLEEER 82
Cdd:cd13593    2 LRLGIPsKGSLAEATLELLKKAGLKV--SRGNPRQYFASIDDlPEVEVLLLRAQEIVRYVADGDLDLGITGYDWVRESGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  83 DVYEVLDLNISKCRLAVAgLPE------TAADTVAP--------RVATKYPNVASSYFREQG-EQVEIIKLNGSIELAPL 147
Cdd:cd13593   80 DVVVVADLGYGPVRLVLA-VPEdwidvsTMADLAAFraedgrglRIATEYPNLTRRFFAEKGgVKVQIVFSWGATEAKPP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489277935 148 IGLAGRIVDIVSTGQTLRENGLVEtekICDI----TSRLIVNPVSYR--MKDAVIDEMASRL 203
Cdd:cd13593  159 EGVADAIVDLTETGTTLRANRLKI---IDDGvlesQAVLIANKRALKdpWKREKIEDLLELL 217
PLN02245 PLN02245
ATP phosphoribosyl transferase
 3-173 1.76e-21

ATP phosphoribosyl transferase


Pssm-ID: 215136 [Multi-domain]  Cd Length: 403  Bit Score: 91.01  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935   3 KELTIAMP-KGRIFEEAADMLRKAgyQLPEEFDDSRKLIIQVPE-ENLRFILAKPMDVTTYVEHGVADVGIAGKDVLLE- 79
Cdd:PLN02245  68 TQIRLGLPsKGRMAEDTLDLLKDC--QLSVKKVNPRQYVAEIPQlPNLEVWFQRPKDIVRKLLSGDLDLGIVGYDMLREy 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489277935  80 --EERDVYEVLD-LNISKCRLAVA-----------GLPETAAD----TVAP-RVATKYPNVASSYFREQG-EQVEIIKLN 139
Cdd:PLN02245 146 gqGNEDLVIVHDaLGFGDCHLSIAipkygifeninSLKELAQMpqwtEERPlRVVTGFTYLGPKFMKDNGfKHVTFSTAD 225

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489277935 140 GSIELAPLIGLAGRIVDIVSTGQTLRENGLVETE 173
Cdd:PLN02245 226 GALEAAPAMGIADAILDLVSSGTTLRENNLKEIE 259
 
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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