NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|166229475|sp|A0KM24|]
View 

RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; AltName: Full=AIR synthase; AltName: Full=AIRS; AltName: Full=Phosphoribosyl-aminoimidazole synthetase

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
3-344 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: 622.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   3 DKTSLSYKDAGVDIDAGNALVERIKGVSKRTRRPEVLGGLGGFGALCQIPA-GYKEPVLVSGTDGVGTKLRLAIDLKKHD 81
Cdd:COG0150    1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAkGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  82 TVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCV 161
Cdd:COG0150   81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 162 GVVEKSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKADVQQPL--GDTTLANALLEPTRIYVKPVLKLIKEC 239
Cdd:COG0150  161 GVVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 240 EIHALSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPADQLEKALTLL 319
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*
gi 166229475 320 KTEGENAWHIGYITKAAdgEEQVII 344
Cdd:COG0150  321 KAAGETAYVIGEVVAGE--GEGVVL 343
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
3-344 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: 622.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   3 DKTSLSYKDAGVDIDAGNALVERIKGVSKRTRRPEVLGGLGGFGALCQIPA-GYKEPVLVSGTDGVGTKLRLAIDLKKHD 81
Cdd:COG0150    1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAkGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  82 TVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCV 161
Cdd:COG0150   81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 162 GVVEKSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKADVQQPL--GDTTLANALLEPTRIYVKPVLKLIKEC 239
Cdd:COG0150  161 GVVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 240 EIHALSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPADQLEKALTLL 319
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*
gi 166229475 320 KTEGENAWHIGYITKAAdgEEQVII 344
Cdd:COG0150  321 KAAGETAYVIGEVVAGE--GEGVVL 343
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
7-334 0e+00

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: 515.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475    7 LSYKDAGVDIDAGNALVERIKGVSKRTRRPEVLGGLGGFGALCQIPAGYKEPVLVSGTDGVGTKLRLAIDLKKHDTVGID 86
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGDKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   87 LVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCVGVVEK 166
Cdd:TIGR00878  81 LVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  167 SEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKA---DVQQPLGDTTLANALLEPTRIYVKPVLKLIKECEIHA 243
Cdd:TIGR00878 161 DEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGldyEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVHG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  244 LSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPADQLEKALTLLKTEG 323
Cdd:TIGR00878 241 LAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYG 320
                         330
                  ....*....|.
gi 166229475  324 ENAWHIGYITK 334
Cdd:TIGR00878 321 EKAWVIGEVKK 331
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
53-333 1.76e-179

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: 498.54  E-value: 1.76e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  53 AGYKEPVLVSGTDGVGTKLRLAIDLKKHDTVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQ 132
Cdd:cd02196   15 GGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAEGCRQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 133 SGCALVGGETAEMPGMYEGEDYDIAGFCVGVVEKSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVS--KADVQQ 210
Cdd:cd02196   95 AGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVRKILFEEglDYDDPE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 211 PLGDTTLANALLEPTRIYVKPVLKLIKECEIHALSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTR 290
Cdd:cd02196  175 PGLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIPPIFKWIQKAGNVSE 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 166229475 291 HEMYRTFNCGVGMIIALPADQLEKALTLLKTEGENAWHIGYIT 333
Cdd:cd02196  255 EEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
6-332 1.65e-131

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 380.31  E-value: 1.65e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   6 SLSYKDAGVDIDAGNALVERIKGVSkrtrrPEVLGGLGGfgalcqIPAGykEPVLVSGTDGVGTKLRLAIDLKKHDTVGI 85
Cdd:PLN02557  58 GLTYKDAGVDIDAGSELVRRIAKMA-----PGIGGFGGL------FPFG--DSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  86 DLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCVGVVE 165
Cdd:PLN02557 125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 166 KSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKADV--QQPLGDTTLANALLEPTRIYVKPVLKLIKECEIHA 243
Cdd:PLN02557 205 KDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLkdQLPGASVTIGEALMAPTVIYVKQVLDIISKGGVKG 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 244 LSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPAdqlEKALTLLKTEG 323
Cdd:PLN02557 285 IAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSP---EAADRILEEGA 361

                 ....*....
gi 166229475 324 ENAWHIGYI 332
Cdd:PLN02557 362 YPAYRIGEV 370
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
176-342 4.39e-36

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: 127.85  E-value: 4.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  176 GEGDALIALAASGPHSNGFSLVRKILEVSKadvqqpLGDTTLANALLEPTRIYVKPVLKLIKEcEIHALSHITGGGFWEN 255
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG------LAAVQLGDPLLEPTLIYVKLLLAALGG-LVKAMHDITGGGLAGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  256 IPRVLPA-NTQAVIDEqswQWPAVFSWLQqagnvTRHEMYRTFNCGVGMIIALPADQlEKALTLLKTEGENAWHIGYITK 334
Cdd:pfam02769  74 LAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGEVTA 144

                  ....*...
gi 166229475  335 AADGEEQV 342
Cdd:pfam02769 145 GGRLTVIV 152
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
3-344 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: 622.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   3 DKTSLSYKDAGVDIDAGNALVERIKGVSKRTRRPEVLGGLGGFGALCQIPA-GYKEPVLVSGTDGVGTKLRLAIDLKKHD 81
Cdd:COG0150    1 MSMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAkGYKEPVLVSGTDGVGTKLKIAQALDKHD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  82 TVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCV 161
Cdd:COG0150   81 TIGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 162 GVVEKSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKADVQQPL--GDTTLANALLEPTRIYVKPVLKLIKEC 239
Cdd:COG0150  161 GVVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVpeLGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 240 EIHALSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPADQLEKALTLL 319
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*
gi 166229475 320 KTEGENAWHIGYITKAAdgEEQVII 344
Cdd:COG0150  321 KAAGETAYVIGEVVAGE--GEGVVL 343
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
7-334 0e+00

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: 515.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475    7 LSYKDAGVDIDAGNALVERIKGVSKRTRRPEVLGGLGGFGALCQIPAGYKEPVLVSGTDGVGTKLRLAIDLKKHDTVGID 86
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGDKYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGID 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   87 LVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCVGVVEK 166
Cdd:TIGR00878  81 LVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  167 SEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKA---DVQQPLGDTTLANALLEPTRIYVKPVLKLIKECEIHA 243
Cdd:TIGR00878 161 DEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGldyEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVHG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  244 LSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPADQLEKALTLLKTEG 323
Cdd:TIGR00878 241 LAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAYG 320
                         330
                  ....*....|.
gi 166229475  324 ENAWHIGYITK 334
Cdd:TIGR00878 321 EKAWVIGEVKK 331
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
53-333 1.76e-179

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: 498.54  E-value: 1.76e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  53 AGYKEPVLVSGTDGVGTKLRLAIDLKKHDTVGIDLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQ 132
Cdd:cd02196   15 GGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAEGCRQ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 133 SGCALVGGETAEMPGMYEGEDYDIAGFCVGVVEKSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVS--KADVQQ 210
Cdd:cd02196   95 AGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVRKILFEEglDYDDPE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 211 PLGDTTLANALLEPTRIYVKPVLKLIKECEIHALSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTR 290
Cdd:cd02196  175 PGLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIPPIFKWIQKAGNVSE 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 166229475 291 HEMYRTFNCGVGMIIALPADQLEKALTLLKTEGENAWHIGYIT 333
Cdd:cd02196  255 EEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
6-332 1.65e-131

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 380.31  E-value: 1.65e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   6 SLSYKDAGVDIDAGNALVERIKGVSkrtrrPEVLGGLGGfgalcqIPAGykEPVLVSGTDGVGTKLRLAIDLKKHDTVGI 85
Cdd:PLN02557  58 GLTYKDAGVDIDAGSELVRRIAKMA-----PGIGGFGGL------FPFG--DSYLVAGTDGVGTKLKLAFETGIHDTIGI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  86 DLVAMCVNDLIVQGAEPLFFLDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYEGEDYDIAGFCVGVVE 165
Cdd:PLN02557 125 DLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFAVGSVK 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 166 KSEIIDGSKVGEGDALIALAASGPHSNGFSLVRKILEVSKADV--QQPLGDTTLANALLEPTRIYVKPVLKLIKECEIHA 243
Cdd:PLN02557 205 KDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLkdQLPGASVTIGEALMAPTVIYVKQVLDIISKGGVKG 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 244 LSHITGGGFWENIPRVLPANTQAVIDEQSWQWPAVFSWLQQAGNVTRHEMYRTFNCGVGMIIALPAdqlEKALTLLKTEG 323
Cdd:PLN02557 285 IAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSP---EAADRILEEGA 361

                 ....*....
gi 166229475 324 ENAWHIGYI 332
Cdd:PLN02557 362 YPAYRIGEV 370
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
59-330 5.40e-53

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: 174.12  E-value: 5.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  59 VLVSGTDGVGTKLRlaidlKKHDTVGIDLVAMCVNDLIVQGAEPLFFLDYYATGK-LDVDTAAAVVTGIGAGCEQSGCAL 137
Cdd:cd00396    1 SLAMSTDGINPPLA-----INPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 138 VGGETAEMPGMYeGEDYDIAGFCVGVVEKSEIIDGSKVGEGDALIALAasgphsngfslvrkilevskadvqqplgdttl 217
Cdd:cd00396   76 VGGHTSVSPGTM-GHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG-------------------------------- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 218 analleptriyVKPVLKLIKECEIHALSHITGGGFWENIPRVLPA-NTQAVIDEQSWQWPAVFSWLQqagnVTRHEMYRT 296
Cdd:cd00396  123 -----------VDAVLELVAAGDVHAMHDITDGGLLGTLPELAQAsGVGAEIDLEAIPLDEVVRWLC----VEHIEEALL 187
                        250       260       270
                 ....*....|....*....|....*....|....
gi 166229475 297 FNCGVGMIIALPADQLEKALTLLKTEGENAWHIG 330
Cdd:cd00396  188 FNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIG 221
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
176-342 4.39e-36

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: 127.85  E-value: 4.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  176 GEGDALIALAASGPHSNGFSLVRKILEVSKadvqqpLGDTTLANALLEPTRIYVKPVLKLIKEcEIHALSHITGGGFWEN 255
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSG------LAAVQLGDPLLEPTLIYVKLLLAALGG-LVKAMHDITGGGLAGA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  256 IPRVLPA-NTQAVIDEqswQWPAVFSWLQqagnvTRHEMYRTFNCGVGMIIALPADQlEKALTLLKTEGENAWHIGYITK 334
Cdd:pfam02769  74 LAEMAPAsGVGAEIDL---DKVPIFEELM-----LPLEMLLSENQGRGLVVVAPEEA-EAVLAILEKEGLEAAVIGEVTA 144

                  ....*...
gi 166229475  335 AADGEEQV 342
Cdd:pfam02769 145 GGRLTVIV 152
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
60-164 1.79e-23

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: 92.89  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475   60 LVSGTDGVGTKLRLAidlkKHDTVGIDLVAMCVNDLIVQGAEPLFFLDYYATGK--LDVDTAAAVVTGIGAGCEQSGCAL 137
Cdd:pfam00586   5 VAVTTDGHGTPSLVD----PYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*..
gi 166229475  138 VGGETAEMPgmyEGEDYDIAGFCVGVV 164
Cdd:pfam00586  81 VGGDTSFDP---EGGKPTISVTAVGIV 104
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
86-332 4.79e-08

Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100031 [Multi-domain]  Cd Length: 287  Bit Score: 53.68  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  86 DLVAMcvndlivqGAEPLFFLDY----YATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMyegedydIAGFCV 161
Cdd:cd02195   83 DIYAM--------GAKPLSALAIvtlpRKLPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEP-------KYGLSV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 162 -GVVEKSEII--DGSKVGegDALI---------ALAASgphsngfslvrKILEVSKADVQQPLGDTTLANalleptriyv 229
Cdd:cd02195  148 tGLVHPNKILrnSGAKPG--DVLIltkplgtgiLFAAE-----------MAGLARGEDIDAALESMARLN---------- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 230 KPVLKLIKECEIHALSHITGGGFW---ENIPRvlPANTQAVIDEQSwqwpavFSWLQQAGnvtrhemyrtfncgvGMIIA 306
Cdd:cd02195  205 RAAAELLRKYGAHACTDVTGFGLLghlLEMAR--ASGVSAEIDLDK------LPLLQTSG---------------GLLAA 261
                        250       260
                 ....*....|....*....|....*.
gi 166229475 307 LPADQLEKALTLLKTEGENAWHIGYI 332
Cdd:cd02195  262 VPPEDAAALLALLKAGGPPAAIIGEV 287
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
87-225 5.21e-07

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: 50.63  E-value: 5.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  87 LVAMCVNDLIVQGAEPLFFL-DYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMYegedydIAGFCVGVVE 165
Cdd:cd02194   63 ALAVNLSDLAAMGARPLGFLlSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVTALGEVE 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166229475 166 KSEII--DGSKVGEgdaliALAASGPH---SNGFSLVRKILEVSKADVQQplgdttLANALLEPT 225
Cdd:cd02194  137 KGKPLrrSGAKPGD-----LLYVTGTLgdaAAGLALLLGGLKLPEELYEE------LIERHLRPE 190
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
88-332 1.23e-06

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: 49.52  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  88 VAMCVNDLIVQGAEPLFFL-DYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETaempGMYEGEDYDIAG-FCVGVVE 165
Cdd:cd06061   64 VHIAANDIATSGARPRWLLvTLLLPPGTDEEELKAIMREINEAAKELGVSIVGGHT----EVTPGVTRPIISvTAIGKGE 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 166 KSEIIDGSKVGEGDALI-----ALAASGphsngfslvrkILEVSKAD-VQQPLGDTTLANALLEPTRIYVKPVLKLIKEC 239
Cdd:cd06061  140 KDKLVTPSGAKPGDDIVmtkgaGIEGTA-----------ILANDFEEeLKKRLSEEELREAAKLFYKISVVKEALIAAEA 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 240 EIHALSHITGGGFWENIPRVLPA-NTQAVIDEQSwqwpavFSWLQQAGNVTRH---EMYRTFNCGVgMIIALPADQLEKA 315
Cdd:cd06061  209 GVTAMHDATEGGILGALWEVAEAsGVGLRIEKDK------IPIRQETKEICEAlgiDPLRLISSGT-LLITVPPEKGDEL 281
                        250
                 ....*....|....*..
gi 166229475 316 LTLLKTEGENAWHIGYI 332
Cdd:cd06061  282 VDALEEAGIPASVIGKI 298
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
89-275 9.78e-05

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 43.67  E-value: 9.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  89 AMCVN--DLIVQGAEPLFF-LDYYATGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAempgmyEGEDYDIAGFCVGVVE 165
Cdd:PRK05731  66 ALAVNlsDLAAMGARPAAFlLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT------RGPDLSISVTAIGDVP 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 166 KSEII--DGSKVGEgdaliALAASGPHSN---GFSLVRKILEVSKADVQQplgdttLANALLEPT-RIYVKPVLK----- 234
Cdd:PRK05731 140 GGRALrrSGAKPGD-----LVAVTGTLGDsaaGLALLLNGLRVPDADAAA------LISRHLRPQpRVGLGQALAglasa 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 166229475 235 -------LIKEC-EIHALSHItGGGFWENIPRVLPANTQAVIDEQSWQW 275
Cdd:PRK05731 209 aidisdgLAADLgHIAEASGV-GADIDLDALPISPALREAAEGEDALRW 256
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
86-338 2.34e-04

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 42.37  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  86 DLVAMcvndlivqGAEPLFFLdyyA-----TGKLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMPGMyegedydIAGFC 160
Cdd:COG0709   89 DVYAM--------GGRPLTAL---AivgfpIDKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEP-------KYGLA 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 161 V-GVVEKSEIIDGSKVGEGDALI---------ALAASgphsngfslvrKILEVSKADVQQPLGDTTLANalleptriyvK 230
Cdd:COG0709  151 VtGLVHPDKVLRNAGARPGDVLIltkplgtgiLTTAI-----------KAGLADGEDIAAAIASMTTLN----------K 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475 231 PVLKLIKECEIHALSHITGGGF------------------WENIPR-----------VLPANTQ-------AVIDEQSWQ 274
Cdd:COG0709  210 AAAELARLYGVHACTDVTGFGLlghllemargsgvsaeidLDAVPLlpgalelaeqgIVPGGTYrnrasygAKVEFAEGL 289
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166229475 275 WPAVFSWL---QQAGnvtrhemyrtfncgvGMIIALPADQLEKALTLLKTEGENAWHIGYITKAADG 338
Cdd:COG0709  290 DEAQRDLLfdpQTSG---------------GLLIAVPPEAAEELLAALRAAGYAAAIIGEVTAGEGG 341
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
92-182 2.82e-04

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: 42.05  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166229475  92 VNDLIVQGAEPLFFLDYY--ATGkLDVDTAAAVVTGIGAGCEQSGCALVGGETAEMP-----GMYegedydIAGFCVGVV 164
Cdd:cd02197   67 VNDLAMMGAKPLYLSLGFilEEG-FPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPkgkadGIF------INTTGIGVI 139
                         90
                 ....*....|....*...
gi 166229475 165 EKSEIIDGSKVGEGDALI 182
Cdd:cd02197  140 PRGVIISPSNIRPGDKII 157
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH