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Conserved domains on  [gi|487749743|ref|WP_001831685|]
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MULTISPECIES: phosphoribosylformylglycinamidine cyclo-ligase [Staphylococcus]

Protein Classification

phosphoribosylformylglycinamidine cyclo-ligase( domain architecture ID 11414961)

phosphoribosylformylglycinamidine cyclo-ligase catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, in the fifth step in de novo purine biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-339 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 592.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   1 MSKAYEESGVNIQAGYEAVERITSHVERTLRKEVLGGLGGFGATFDLSQLKMKAPVLVSGTDGVGTKLKLAIDYGKHDTI 80
Cdd:COG0150    3 MSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  81 GIDAVAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGA 160
Cdd:COG0150   83 GIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 161 VEKEDYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQLHDQF--NGQTFLETFLAPTKLYVKPILELKKHIDI 238
Cdd:COG0150  163 VEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAVDV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 239 KAMSHITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRA 318
Cdd:COG0150  243 HGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKA 322
                        330       340
                 ....*....|....*....|.
gi 487749743 319 MDTTAYEIGEIIKDDDTPIHL 339
Cdd:COG0150  323 AGETAYVIGEVVAGEGEGVVL 343
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-339 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 592.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   1 MSKAYEESGVNIQAGYEAVERITSHVERTLRKEVLGGLGGFGATFDLSQLKMKAPVLVSGTDGVGTKLKLAIDYGKHDTI 80
Cdd:COG0150    3 MSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  81 GIDAVAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGA 160
Cdd:COG0150   83 GIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 161 VEKEDYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQLHDQF--NGQTFLETFLAPTKLYVKPILELKKHIDI 238
Cdd:COG0150  163 VEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAVDV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 239 KAMSHITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRA 318
Cdd:COG0150  243 HGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKA 322
                        330       340
                 ....*....|....*....|.
gi 487749743 319 MDTTAYEIGEIIKDDDTPIHL 339
Cdd:COG0150  323 AGETAYVIGEVVAGEGEGVVL 343
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
36-330 6.89e-174

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 484.29  E-value: 6.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  36 GGLGGFGATFDLSQLKMKAPVLVSGTDGVGTKLKLAIDYGKHDTIGIDAVAMCVNDILTTGAEPLYFLDYIATNKVVPST 115
Cdd:cd02196    1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 116 IEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEKEDYIDGSNVEEGQAIIGLASSGIHSNGYSLVR 195
Cdd:cd02196   81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 196 KMIKESGVQLHDQF--NGQTFLETFLAPTKLYVKPILELKKHIDIKAMSHITGGGFYENIPRALPKGLSAKIDTQSFPTL 273
Cdd:cd02196  161 KILFEEGLDYDDPEpgLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487749743 274 EVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRAMDTTAYEIGEII 330
Cdd:cd02196  241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
4-331 9.89e-156

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 439.85  E-value: 9.89e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743    4 AYEESGVNIQAGYEAVERITSHVERTLRKEVLGGLGGFGATFDLSQlKMKAPVLVSGTDGVGTKLKLAIDYGKHDTIGID 83
Cdd:TIGR00878   2 TYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   84 AVAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEK 163
Cdd:TIGR00878  81 LVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  164 EDYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQL---HDQFNGQTFLETFLAPTKLYVKPILELKKHIDIKA 240
Cdd:TIGR00878 161 DEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDyedTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVHG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  241 MSHITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRAMD 320
Cdd:TIGR00878 241 LAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYG 320
                         330
                  ....*....|.
gi 487749743  321 TTAYEIGEIIK 331
Cdd:TIGR00878 321 EKAWVIGEVKK 331
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
5-333 3.63e-129

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 374.14  E-value: 3.63e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   5 YEESGVNIQAGYEAVERItshvertlrKEVLGGLGGFGATFDLSQlkmkaPVLVSGTDGVGTKLKLAIDYGKHDTIGIDA 84
Cdd:PLN02557  61 YKDAGVDIDAGSELVRRI---------AKMAPGIGGFGGLFPFGD-----SYLVAGTDGVGTKLKLAFETGIHDTIGIDL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  85 VAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEKE 164
Cdd:PLN02557 127 VAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVKKD 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 165 DYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQLHDQFNGQ--TFLETFLAPTKLYVKPILELKKHIDIKAMS 242
Cdd:PLN02557 207 AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGAsvTIGEALMAPTVIYVKQVLDIISKGGVKGIA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 243 HITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQttlTTLRAMDTT 322
Cdd:PLN02557 287 HITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAAD---RILEEGAYP 363
                        330
                 ....*....|.
gi 487749743 323 AYEIGEIIKDD 333
Cdd:PLN02557 364 AYRIGEVINGE 374
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
173-334 2.31e-32

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 118.22  E-value: 2.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  173 EEGQAIIGLASSGIHSNGYSLVRKMIKESGVqlhdqfNGQTFLETFLAPTKLYVKPILELKKHiDIKAMSHITGGGFYEN 252
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGL------AAVQLGDPLLEPTLIYVKLLLAALGG-LVKAMHDITGGGLAGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  253 IPRALPK-GLSAKIDTQSFPtleVFNWLQkqgniSTNEMYNIFNMGIGYtIIVDKKDVQTTLTTLRAMDTTAYEIGEIIK 331
Cdd:pfam02769  74 LAEMAPAsGVGAEIDLDKVP---IFEELM-----LPLEMLLSENQGRGL-VVVAPEEAEAVLAILEKEGLEAAVIGEVTA 144

                  ...
gi 487749743  332 DDD 334
Cdd:pfam02769 145 GGR 147
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-339 0e+00

Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole (AIR) synthetase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439920 [Multi-domain]  Cd Length: 343  Bit Score: 592.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   1 MSKAYEESGVNIQAGYEAVERITSHVERTLRKEVLGGLGGFGATFDLSQLKMKAPVLVSGTDGVGTKLKLAIDYGKHDTI 80
Cdd:COG0150    3 MSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDTI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  81 GIDAVAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGA 160
Cdd:COG0150   83 GIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 161 VEKEDYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQLHDQF--NGQTFLETFLAPTKLYVKPILELKKHIDI 238
Cdd:COG0150  163 VEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAVDV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 239 KAMSHITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRA 318
Cdd:COG0150  243 HGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALLKA 322
                        330       340
                 ....*....|....*....|.
gi 487749743 319 MDTTAYEIGEIIKDDDTPIHL 339
Cdd:COG0150  323 AGETAYVIGEVVAGEGEGVVL 343
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
36-330 6.89e-174

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 484.29  E-value: 6.89e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  36 GGLGGFGATFDLSQLKMKAPVLVSGTDGVGTKLKLAIDYGKHDTIGIDAVAMCVNDILTTGAEPLYFLDYIATNKVVPST 115
Cdd:cd02196    1 GGIGGFAGLFDLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 116 IEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEKEDYIDGSNVEEGQAIIGLASSGIHSNGYSLVR 195
Cdd:cd02196   81 AAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 196 KMIKESGVQLHDQF--NGQTFLETFLAPTKLYVKPILELKKHIDIKAMSHITGGGFYENIPRALPKGLSAKIDTQSFPTL 273
Cdd:cd02196  161 KILFEEGLDYDDPEpgLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487749743 274 EVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRAMDTTAYEIGEII 330
Cdd:cd02196  241 PIFKWIQKAGNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
4-331 9.89e-156

phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine cyclo-ligase; AIRS; AIR synthase This enzyme is found as a homodimeric monofunctional protein in prokaryotes and as part of a larger, multifunctional protein, sometimes with two copies of this enzyme in tandem, in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273316 [Multi-domain]  Cd Length: 332  Bit Score: 439.85  E-value: 9.89e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743    4 AYEESGVNIQAGYEAVERITSHVERTLRKEVLGGLGGFGATFDLSQlKMKAPVLVSGTDGVGTKLKLAIDYGKHDTIGID 83
Cdd:TIGR00878   2 TYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   84 AVAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEK 163
Cdd:TIGR00878  81 LVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  164 EDYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQL---HDQFNGQTFLETFLAPTKLYVKPILELKKHIDIKA 240
Cdd:TIGR00878 161 DEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDyedTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVHG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  241 MSHITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQTTLTTLRAMD 320
Cdd:TIGR00878 241 LAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYG 320
                         330
                  ....*....|.
gi 487749743  321 TTAYEIGEIIK 331
Cdd:TIGR00878 321 EKAWVIGEVKK 331
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
5-333 3.63e-129

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 374.14  E-value: 3.63e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   5 YEESGVNIQAGYEAVERItshvertlrKEVLGGLGGFGATFDLSQlkmkaPVLVSGTDGVGTKLKLAIDYGKHDTIGIDA 84
Cdd:PLN02557  61 YKDAGVDIDAGSELVRRI---------AKMAPGIGGFGGLFPFGD-----SYLVAGTDGVGTKLKLAFETGIHDTIGIDL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  85 VAMCVNDILTTGAEPLYFLDYIATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIAGFAVGAVEKE 164
Cdd:PLN02557 127 VAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVKKD 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 165 DYIDGSNVEEGQAIIGLASSGIHSNGYSLVRKMIKESGVQLHDQFNGQ--TFLETFLAPTKLYVKPILELKKHIDIKAMS 242
Cdd:PLN02557 207 AVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLPGAsvTIGEALMAPTVIYVKQVLDIISKGGVKGIA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 243 HITGGGFYENIPRALPKGLSAKIDTQSFPTLEVFNWLQKQGNISTNEMYNIFNMGIGYTIIVDKKDVQttlTTLRAMDTT 322
Cdd:PLN02557 287 HITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEAAD---RILEEGAYP 363
                        330
                 ....*....|.
gi 487749743 323 AYEIGEIIKDD 333
Cdd:PLN02557 364 AYRIGEVINGE 374
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
173-334 2.31e-32

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 118.22  E-value: 2.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  173 EEGQAIIGLASSGIHSNGYSLVRKMIKESGVqlhdqfNGQTFLETFLAPTKLYVKPILELKKHiDIKAMSHITGGGFYEN 252
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGL------AAVQLGDPLLEPTLIYVKLLLAALGG-LVKAMHDITGGGLAGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  253 IPRALPK-GLSAKIDTQSFPtleVFNWLQkqgniSTNEMYNIFNMGIGYtIIVDKKDVQTTLTTLRAMDTTAYEIGEIIK 331
Cdd:pfam02769  74 LAEMAPAsGVGAEIDLDKVP---IFEELM-----LPLEMLLSENQGRGL-VVVAPEEAEAVLAILEKEGLEAAVIGEVTA 144

                  ...
gi 487749743  332 DDD 334
Cdd:pfam02769 145 GGR 147
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
56-328 6.11e-32

AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 100027 [Multi-domain]  Cd Length: 222  Bit Score: 119.04  E-value: 6.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  56 VLVSGTDGVGTKLKLaidygKHDTIGIDAVAMCVNDILTTGAEPLYFLDYIAT-NKVVPSTIEQIVKGISDGCEQTNTAL 134
Cdd:cd00396    1 SLAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLsNGLEVDILEDVVDGVAEACNQLGVPI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 135 IGGETAEMGEMyHEGEYDIAGFAVGAVEKEDYIDGSNVEEGQAIIGLAssgihsngyslvrkmikesgvqlhdqfngqtf 214
Cdd:cd00396   76 VGGHTSVSPGT-MGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG-------------------------------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743 215 letflaptklyVKPILELKKHIDIKAMSHITGGGFYENIPRALPK-GLSAKIDTQSFPTLEVFNWLQKQgnisTNEMYNI 293
Cdd:cd00396  123 -----------VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQAsGVGAEIDLEAIPLDEVVRWLCVE----HIEEALL 187
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 487749743 294 FNMGIGYTIIVDKKDVQTTLTTLRAMDTTAYEIGE 328
Cdd:cd00396  188 FNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
57-161 2.09e-25

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 98.29  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   57 LVSGTDGVGTKLKLAidygKHDTIGIDAVAMCVNDILTTGAEPLYFLDYIAT--NKVVPSTIEQIVKGISDGCEQTNTAL 134
Cdd:pfam00586   5 VAVTTDGHGTPSLVD----PYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALpgGPEVEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*..
gi 487749743  135 IGGETAEMGEmyhEGEYDIAGFAVGAV 161
Cdd:pfam00586  81 VGGDTSFDPE---GGKPTISVTAVGIV 104
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
80-179 2.09e-09

Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 57.78  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  80 IGIDAVAMCVNDILTTGAEPLYFLDYIatnkVVP-----STIEQIVKGISDGCEQTNTALIGGETaemgEMYHEGEYD-- 152
Cdd:COG0309   62 IGKLAVHGTVNDLAVSGAKPLYLSVSL----ILEegfplEDLERIVESMAEAAREAGVSIVTGDT----KVVERGGVDgp 133
                         90       100
                 ....*....|....*....|....*...
gi 487749743 153 -IAGFAVGAVEKEDYIDGSNVEEGQAII 179
Cdd:COG0309  134 fINTTGIGVVPKGRLISPSGARPGDKII 161
hypE TIGR02124
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
80-248 1.42e-07

hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.


Pssm-ID: 273984 [Multi-domain]  Cd Length: 320  Bit Score: 52.26  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   80 IGIDAVAMCVNDILTTGAEPLYFLDYIATNKVVP-STIEQIVKGISDGCEQTNTALIGGETAEMGemyhEGEYD---IAG 155
Cdd:TIGR02124  53 IGKLAVCGTVNDVAVSGAKPLYLSCGFILEEGFPiEDLERIVKSMAEAARKAGVKIVTGDTKVVE----KGKADgifINT 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  156 FAVGAVEKEDYIDGSNVEEGQAIIGLASSGIHsnGYSLvrkMIKESGVQLhdqfngQTFLETFLAPTKLYVKPILELKKh 235
Cdd:TIGR02124 129 TGIGVIPSGIPISAHNLQPGDKIIVSGTIGDH--GAAI---LAVREGLGF------ETNLESDCAPLNGLVETLLNAGP- 196
                         170
                  ....*....|...
gi 487749743  236 iDIKAMSHITGGG 248
Cdd:TIGR02124 197 -AVHAMRDATRGG 208
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
29-179 1.63e-07

AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100037 [Multi-domain]  Cd Length: 298  Bit Score: 52.21  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  29 TLRKEVLGGLGGfGATFDLSQLKMKapVLVSGTDGVgtklklaidYGKHDTIGIDAVAMCVNDILTTGAEPLYFLDYI-- 106
Cdd:cd06061   20 ADRDEVLVGPGG-GEDAAVVDFGGK--VLVVSTDPI---------TGAGKDAGWLAVHIAANDIATSGARPRWLLVTLll 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487749743 107 ---ATNKvvpsTIEQIVKGISDGCEQTNTALIGGETAemgemYHEG-EYDIAG-FAVGAVEKEDYIDGSNVEEGQAII 179
Cdd:cd06061   88 ppgTDEE----ELKAIMREINEAAKELGVSIVGGHTE-----VTPGvTRPIISvTAIGKGEKDKLVTPSGAKPGDDIV 156
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
84-185 1.10e-06

ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).


Pssm-ID: 100030 [Multi-domain]  Cd Length: 291  Bit Score: 49.47  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  84 AVAMCVNDILTTGAEPLYFLDYIATNKVVP-STIEQIVKGISDGCEQTNTALIGGETAEMGEMYhegeydIAGFAVGAVE 162
Cdd:cd02194   63 ALAVNLSDLAAMGARPLGFLLSLGLPPDTDeEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVTALGEVE 136
                         90       100
                 ....*....|....*....|....*...
gi 487749743 163 KEDYIDGSNVEEGQAI-----IGLASSG 185
Cdd:cd02194  137 KGKPLRRSGAKPGDLLyvtgtLGDAAAG 164
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
80-179 1.01e-05

HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100033 [Multi-domain]  Cd Length: 293  Bit Score: 46.67  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  80 IGIDAVAMCVNDILTTGAEPLYFLDYIatnkVVP-----STIEQIVKGISDGCEQTNTALIGGETAEMGemyhEGEYD-- 152
Cdd:cd02197   58 IGKLAVCGTVNDLAMMGAKPLYLSLGF----ILEegfplEDLERIVKSMAEAAREAGVKIVTGDTKVVP----KGKADgi 129
                         90       100
                 ....*....|....*....|....*...
gi 487749743 153 -IAGFAVGAVEKEDYIDGSNVEEGQAII 179
Cdd:cd02197  130 fINTTGIGVIPRGVIISPSNIRPGDKII 157
FGAM_synth_II TIGR01736
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ...
84-179 3.63e-04

phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273781 [Multi-domain]  Cd Length: 715  Bit Score: 42.29  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743   84 AVAMCVNDILTTGAEPLYFLDYI----ATNKVVPSTIEQIVKGISDGCEQTNTALIGGETAemgeMYHEGEY-DIAG--- 155
Cdd:TIGR01736 455 AVAEAYRNLAAVGAEPLAAVDCLnfgnPERPEVYWQFVEAVKGLGDACRALGTPVVGGNVS----LYNETNGvPIAPtpt 530
                          90       100
                  ....*....|....*....|....*.
gi 487749743  156 -FAVGAVEKEDYIDGSNV-EEGQAII 179
Cdd:TIGR01736 531 iGMVGLVEDVEKLLTSNFkKEGDAIY 556
PurM-like3 cd02192
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ...
89-179 7.44e-04

AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100028 [Multi-domain]  Cd Length: 283  Bit Score: 40.66  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  89 VNDILTTGAEPLYFLDYIATNKvvPSTIEQIVKGISDGCEQTNTALIGGETaemgemYHEGEYDIAGFAVGAVEKEDYID 168
Cdd:cd02192   76 VSDIAAMGGRPLAMVDALWSPS--AEAAAQVLEGMRDAAEKFGVPIVGGHT------HPDSPYNALSVAILGRARKDLLI 147
                         90
                 ....*....|.
gi 487749743 169 GSNVEEGQAII 179
Cdd:cd02192  148 SFGAKPGDRLI 158
PRK14090 PRK14090
phosphoribosylformylglycinamidine synthase subunit PurL;
89-219 9.12e-04

phosphoribosylformylglycinamidine synthase subunit PurL;


Pssm-ID: 184499 [Multi-domain]  Cd Length: 601  Bit Score: 40.99  E-value: 9.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749743  89 VNDILTTGAEPLYFLDYIATNKVvpstIEQIVKGISDGCEQTNTALIGGETAEMGEMYHEGEYDIagFAVGAVEKEDYID 168
Cdd:PRK14090  90 IRDVLAMGARPTAIFDSLHMSRI----IDGIIEGIADYGNSIGVPTVGGELRISSLYAHNPLVNV--LAAGVVRNDMLVD 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 487749743 169 GSNVEEGQAII--GLAS--SGIHSNGYS---LVRKMIKESGVQLHDQFNGQTFLETFL 219
Cdd:PRK14090 164 SKASRPGQVIVifGGATgrDGIHGASFAsedLTGEKATKLSIQVGDPFAEKMLIEAFL 221
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
80-139 1.78e-03

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 39.81  E-value: 1.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749743  80 IGIDAVAMCVNDILTTGAEPLYFLDYIATNKVVP-STIEQIVKGISDGCEQTNTALIGGET 139
Cdd:PRK05731  62 LGYKALAVNLSDLAAMGARPAAFLLALALPKDLDeAWLEALADGLFELADRYGAELIGGDT 122
 
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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