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Conserved domains on  [gi|518291517|ref|WP_019461725|]
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MULTISPECIES: phosphoribosylformylglycinamidine cyclo-ligase [Roseomonas]

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]; ...
1-346 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: 567.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   1 MASLTYRDAGVDIEAGDALVDAIKPLARSTDRSGTMGGLGGFGALFDLKAAGFKDPVLVSSTDGVGTKLRLAIDSGHHDG 80
Cdd:COG0150    2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  81 VGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVG 160
Cdd:COG0150   82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 161 AAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPfASGRTLGEALLEPTRIYVKSVLAVHRAG 240
Cdd:COG0150  162 VVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP-ELGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 241 LLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLL 320
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*.
gi 518291517 321 QEAGETVARIGRIEtapEGDEASVRV 346
Cdd:COG0150  321 KAAGETAYVIGEVV---AGEGEGVVL 343
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-346 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: 567.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   1 MASLTYRDAGVDIEAGDALVDAIKPLARSTDRSGTMGGLGGFGALFDLKAAGFKDPVLVSSTDGVGTKLRLAIDSGHHDG 80
Cdd:COG0150    2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  81 VGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVG 160
Cdd:COG0150   82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 161 AAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPfASGRTLGEALLEPTRIYVKSVLAVHRAG 240
Cdd:COG0150  162 VVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP-ELGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 241 LLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLL 320
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*.
gi 518291517 321 QEAGETVARIGRIEtapEGDEASVRV 346
Cdd:COG0150  321 KAAGETAYVIGEVV---AGEGEGVVL 343
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
47-334 2.15e-169

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: 473.50  E-value: 2.15e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  47 DLKAAGFKDPVLVSSTDGVGTKLRLAIDSGHHDGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAE 126
Cdd:cd02196   11 DLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 127 GCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVGAAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGL 206
Cdd:cd02196   91 GCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVRKILFEEGLDY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 207 KDPAPfASGRTLGEALLEPTRIYVKSVLAVHRAGLLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARM 286
Cdd:cd02196  171 DDPEP-GLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIPPIFKWIQKA 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 518291517 287 GGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLLQEAGETVARIGRIE 334
Cdd:cd02196  250 GNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
4-334 5.78e-152

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: 430.99  E-value: 5.78e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517    4 LTYRDAGVDIEAGDALVDAIKPLARSTDRSGTMGGLGGFGALFDLKAaGFKDPVLVSSTDGVGTKLRLAIDSGHHDGVGI 83
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   84 DLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVGAAE 163
Cdd:TIGR00878  80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  164 RTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPFASGRTLGEALLEPTRIYVKSVLAVHRAGLLK 243
Cdd:TIGR00878 160 KDEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  244 AAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLLQEA 323
Cdd:TIGR00878 240 GLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAY 319
                         330
                  ....*....|.
gi 518291517  324 GETVARIGRIE 334
Cdd:TIGR00878 320 GEKAWVIGEVK 330
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
3-333 1.13e-124

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 363.36  E-value: 1.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   3 SLTYRDAGVDIEAGDALVDAIKPLArstdrsgtmgglggfgalFDLKAAG----FKDPVLVSSTDGVGTKLRLAIDSGHH 78
Cdd:PLN02557  58 GLTYKDAGVDIDAGSELVRRIAKMA------------------PGIGGFGglfpFGDSYLVAGTDGVGTKLKLAFETGIH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  79 DGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFS 158
Cdd:PLN02557 120 DTIGIDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 159 VGAAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPfASGRTLGEALLEPTRIYVKSVLAVHR 238
Cdd:PLN02557 200 VGSVKKDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTVIYVKQVLDIIS 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 239 AGLLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSvgeATR 318
Cdd:PLN02557 279 KGGVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEA---ADR 355
                        330
                 ....*....|....*
gi 518291517 319 LLQEAGETVARIGRI 333
Cdd:PLN02557 356 ILEEGAYPAYRIGEV 370
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
174-339 2.55e-31

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: 115.52  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  174 GAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGlkdpapfasGRTLGEALLEPTRIYVKSVLAVhRAGLLKAAAHITGGGL 253
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGLA---------AVQLGDPLLEPTLIYVKLLLAA-LGGLVKAMHDITGGGL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  254 PGNLPRVLPAGTV-AVVDAAAwtpPPVFAWLArmggvVPEEMLRVFNCGLGMVLVVAENsVGEATRLLQEAGETVARIGR 332
Cdd:pfam02769  71 AGALAEMAPASGVgAEIDLDK---VPIFEELM-----LPLEMLLSENQGRGLVVVAPEE-AEAVLAILEKEGLEAAVIGE 141

                  ....*..
gi 518291517  333 IETAPEG 339
Cdd:pfam02769 142 VTAGGRL 148
 
Name Accession Description Interval E-value
PurM COG0150
Phosphoribosylaminoimidazole (AIR) synthetase [Nucleotide transport and metabolism]; ...
1-346 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: 567.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   1 MASLTYRDAGVDIEAGDALVDAIKPLARSTDRSGTMGGLGGFGALFDLKAAGFKDPVLVSSTDGVGTKLRLAIDSGHHDG 80
Cdd:COG0150    2 SMSLTYKDAGVDIDAGNAAVERIKPAVKRTFRPGVLGGLGGFGGLFDLPAKGYKEPVLVSGTDGVGTKLKIAQALDKHDT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  81 VGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVG 160
Cdd:COG0150   82 IGIDLVAMCVNDILVQGAEPLFFLDYIATGKLDPEVAAAVVKGIAEGCRQAGCALIGGETAEMPGMYAPGEYDLAGFAVG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 161 AAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPfASGRTLGEALLEPTRIYVKSVLAVHRAG 240
Cdd:COG0150  162 VVEKDKIIDGSRVKAGDVLIGLASSGLHSNGYSLVRKILEVAGLDLDDPVP-ELGRTLGEALLEPTRIYVKPVLALLKAV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 241 LLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLL 320
Cdd:COG0150  241 DVHGMAHITGGGLPENLPRVLPEGLGAVIDRGSWPVPPIFDWLQELGNVSEEEMYRTFNMGIGMVLVVPPEDADAALALL 320
                        330       340
                 ....*....|....*....|....*.
gi 518291517 321 QEAGETVARIGRIEtapEGDEASVRV 346
Cdd:COG0150  321 KAAGETAYVIGEVV---AGEGEGVVL 343
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
47-334 2.15e-169

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: 473.50  E-value: 2.15e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  47 DLKAAGFKDPVLVSSTDGVGTKLRLAIDSGHHDGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAE 126
Cdd:cd02196   11 DLGLGGYKDPVLVSGTDGVGTKLKLAQEMGKHDTIGIDLVAMCVNDILCQGAEPLFFLDYIATGKLDPEVAAEIVKGIAE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 127 GCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVGAAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGL 206
Cdd:cd02196   91 GCRQAGCALLGGETAEMPGVYAEGEYDLAGFAVGVVEKDKIIDGSKIKPGDVLIGLPSSGLHSNGYSLVRKILFEEGLDY 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 207 KDPAPfASGRTLGEALLEPTRIYVKSVLAVHRAGLLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARM 286
Cdd:cd02196  171 DDPEP-GLGKTLGEELLTPTRIYVKPILPLLEKVLVKGMAHITGGGLPENLPRVLPEGLGAVIDLGSWEIPPIFKWIQKA 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 518291517 287 GGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLLQEAGETVARIGRIE 334
Cdd:cd02196  250 GNVSEEEMYRTFNMGIGMVLIVSEEDADEVLEILEKLGEKAYVIGEVV 297
purM TIGR00878
phosphoribosylaminoimidazole synthetase; Alternate name: phosphoribosylformylglycinamidine ...
4-334 5.78e-152

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: 430.99  E-value: 5.78e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517    4 LTYRDAGVDIEAGDALVDAIKPLARSTDRSGTMGGLGGFGALFDLKAaGFKDPVLVSSTDGVGTKLRLAIDSGHHDGVGI 83
Cdd:TIGR00878   1 VTYADAGVDIDAGNEAVKRIKSLVKKTRRPEVMGGLGGFAGLFDLGD-KYKEPVLVSGTDGVGTKLLVAEAMNKHDTIGI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   84 DLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFSVGAAE 163
Cdd:TIGR00878  80 DLVAMNVNDLLVQGAEPLFFLDYLAVGKLDPEVASQIVKGIAEGCKQAGCALVGGETAEMPGMYRGGHYDLAGTAVGVVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  164 RTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPFASGRTLGEALLEPTRIYVKSVLAVHRAGLLK 243
Cdd:TIGR00878 160 KDEIITGEKVKPGDVLIGLGSSGIHSNGLSLVRKVLEDIAGLDYEDTPEEFGKTLGEELLEPTRIYVKPILELIKSVIVH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  244 AAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSVGEATRLLQEA 323
Cdd:TIGR00878 240 GLAHITGGGLLENIPRRLPDGLKAVIDMSSWPQPPIFKWIQEAGNVEEEEMYRTFNMGVGFVVIVPEEEVDKALALLNAY 319
                         330
                  ....*....|.
gi 518291517  324 GETVARIGRIE 334
Cdd:TIGR00878 320 GEKAWVIGEVK 330
PLN02557 PLN02557
phosphoribosylformylglycinamidine cyclo-ligase
3-333 1.13e-124

phosphoribosylformylglycinamidine cyclo-ligase


Pssm-ID: 178172 [Multi-domain]  Cd Length: 379  Bit Score: 363.36  E-value: 1.13e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   3 SLTYRDAGVDIEAGDALVDAIKPLArstdrsgtmgglggfgalFDLKAAG----FKDPVLVSSTDGVGTKLRLAIDSGHH 78
Cdd:PLN02557  58 GLTYKDAGVDIDAGSELVRRIAKMA------------------PGIGGFGglfpFGDSYLVAGTDGVGTKLKLAFETGIH 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  79 DGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYGKGDYDLAGFS 158
Cdd:PLN02557 120 DTIGIDLVAMSVNDIVTSGAKPLFFLDYFATSHLDVDLAEKVIKGIVDGCQQSDCALLGGETAEMPGFYAEGEYDLSGFA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 159 VGAAERTDLLPKPDVGAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGLKDPAPfASGRTLGEALLEPTRIYVKSVLAVHR 238
Cdd:PLN02557 200 VGSVKKDAVIDGKNIVAGDVLIGLPSSGVHSNGFSLVRRVLAKSGLSLKDQLP-GASVTIGEALMAPTVIYVKQVLDIIS 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 239 AGLLKAAAHITGGGLPGNLPRVLPAGTVAVVDAAAWTPPPVFAWLARMGGVVPEEMLRVFNCGLGMVLVVAENSvgeATR 318
Cdd:PLN02557 279 KGGVKGIAHITGGGFTDNIPRVFPKGLGAKIRTGSWEVPPLFKWLQEAGNIEDAEMRRTFNMGIGMVLVVSPEA---ADR 355
                        330
                 ....*....|....*
gi 518291517 319 LLQEAGETVARIGRI 333
Cdd:PLN02557 356 ILEEGAYPAYRIGEV 370
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
57-332 8.06e-33

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: 121.73  E-value: 8.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  57 VLVSSTDGVGTKLRLaidsgHHDGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGK-LEVAQASAVVAGIAEGCRQAGCAL 135
Cdd:cd00396    1 SLAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNgLEVDILEDVVDGVAEACNQLGVPI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 136 VGGETAEMPGMyGKGDYDLAGFSVGaaertdllpkpdvgagdvllgllssgvhsngyslvrrIVEggnaglKDPAPFASG 215
Cdd:cd00396   76 VGGHTSVSPGT-MGHKLSLAVFAIG-------------------------------------VVE------KDRVIDSSG 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 216 RTLGEALLEPTRIYVKSVLAvhrAGLLKAAAHITGGGLPGNLPRVLPA-GTVAVVDAAAWTPPPVFAWLARMGGvvpeEM 294
Cdd:cd00396  112 ARPGDVLILTGVDAVLELVA---AGDVHAMHDITDGGLLGTLPELAQAsGVGAEIDLEAIPLDEVVRWLCVEHI----EE 184
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 518291517 295 LRVFNCGLGMVLVVAENSVGEATRLLQEAGETVARIGR 332
Cdd:cd00396  185 ALLFNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVIGR 222
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
174-339 2.55e-31

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: 115.52  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  174 GAGDVLLGLLSSGVHSNGYSLVRRIVEGGNAGlkdpapfasGRTLGEALLEPTRIYVKSVLAVhRAGLLKAAAHITGGGL 253
Cdd:pfam02769   1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGLA---------AVQLGDPLLEPTLIYVKLLLAA-LGGLVKAMHDITGGGL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  254 PGNLPRVLPAGTV-AVVDAAAwtpPPVFAWLArmggvVPEEMLRVFNCGLGMVLVVAENsVGEATRLLQEAGETVARIGR 332
Cdd:pfam02769  71 AGALAEMAPASGVgAEIDLDK---VPIFEELM-----LPLEMLLSENQGRGLVVVAPEE-AEAVLAILEKEGLEAAVIGE 141

                  ....*..
gi 518291517  333 IETAPEG 339
Cdd:pfam02769 142 VTAGGRL 148
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
58-162 9.89e-22

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: 88.66  E-value: 9.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517   58 LVSSTDGVGTKLrlaIDSGHHdGVGIDLVAMCVNDLVVQGAEPLFFLDYFATGK--LEVAQASAVVAGIAEGCRQAGCAL 135
Cdd:pfam00586   5 VAVTTDGHGTPS---LVDPYH-FPGAKAVAGNLSDIAAMGARPLAFLDSLALPGgpEVEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*..
gi 518291517  136 VGGETAEMPGMygkGDYDLAGFSVGAA 162
Cdd:pfam00586  81 VGGDTSFDPEG---GKPTISVTAVGIV 104
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
85-334 2.12e-05

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: 45.62  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  85 LVAMCVNDLVVQGAEPLFFL-DYFATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGMYgkgdydLAGFSVGAAE 163
Cdd:cd02194   63 ALAVNLSDLAAMGARPLGFLlSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELV------ISVTALGEVE 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 164 RTDLLPKPDVGAGDVllgLLSSGVHsnGYS-LVRRIVEGGNAGLKDPAPFASgrtlgEALLEPT-RIyvksvlavhRAGL 241
Cdd:cd02194  137 KGKPLRRSGAKPGDL---LYVTGTL--GDAaAGLALLLGGLKLPEELYEELI-----ERHLRPEpRL---------ELGR 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 242 LKAAAHITGG-----GLPGNLPRVLPAGTV-AVVDAAAwtPPPVFAWLARMGGVVPEEMlrVFNCG--LGMVLVVAENSV 313
Cdd:cd02194  198 ALAEGLATAMidisdGLLADLGHIAEASGVgAVIDLDK--LPLSPALRAAELGEDALEL--ALSGGedYELLFTVPPENA 273
                        250       260
                 ....*....|....*....|.
gi 518291517 314 GEAtrlLQEAGETVARIGRIE 334
Cdd:cd02194  274 EAA---AAKLGVPVTVIGRVT 291
PurM-like3 cd02192
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ...
90-332 3.22e-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: 41.81  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  90 VNDLVVQGAEPLFFLDYFATGKLEVAQAsaVVAGIAEGCRQAGCALVGGETAemPGmygkGDYDLAGFSVGAAERTDLLP 169
Cdd:cd02192   76 VSDIAAMGGRPLAMVDALWSPSAEAAAQ--VLEGMRDAAEKFGVPIVGGHTH--PD----SPYNALSVAILGRARKDLLI 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 170 KPDVGAGDVLLGLlssgvhsngYSLVRRIveGGNAGLK-DPAPFASGRTLgealleptRIYVKSVLAVHRAGLLKAAAHI 248
Cdd:cd02192  148 SFGAKPGDRLILA---------IDLDGRV--HPSPPPNwDATTMKSPALL--------RRQIALLPELAERGLVHAAKDI 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 249 TGGGLPGNLPRVLPA-GTVAVVDAAAWTPPPVFAWlarmggvvpEEMLRVFNcGLGMVLVVAENSVGEATRLLQEAGETV 327
Cdd:cd02192  209 SNPGIIGTLGMLLEAsGVGAEIDLDAIPRPEGVDL---------ERWLKCFP-GFGFLLTARPENADEVVAVFAAVGITA 278

                 ....*
gi 518291517 328 ARIGR 332
Cdd:cd02192  279 AVIGE 283
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
90-151 5.28e-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: 41.28  E-value: 5.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518291517  90 VNDLVVQGAEPLFFLDYF--ATGkLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGmyGKGD 151
Cdd:cd02197   67 VNDLAMMGAKPLYLSLGFilEEG-FPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPK--GKAD 127
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
84-346 7.90e-04

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 40.83  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517  84 DLVAMcvndlvvqGAEPLFFLDY--FATGKLEVAQASAVVAGIAEGCRQAGCALVGGETAEMPGM-YgkgdydlaGFSV- 159
Cdd:COG0709   89 DVYAM--------GGRPLTALAIvgFPIDKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEPkY--------GLAVt 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 160 GAAERTDLLPKPDVGAGDVL-----LGllsSGVHSngyslvrriveggnAGLKdpAPFASGRTLGEAlleptriyVKSVL 234
Cdd:COG0709  153 GLVHPDKVLRNAGARPGDVLiltkpLG---TGILT--------------TAIK--AGLADGEDIAAA--------IASMT 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518291517 235 AVHRAG---LLKAAAH----ITGGGLPGNLPRVL-PAGTVAVVDAAAwTP--PPVFAwLARMG----------------- 287
Cdd:COG0709  206 TLNKAAaelARLYGVHactdVTGFGLLGHLLEMArGSGVSAEIDLDA-VPllPGALE-LAEQGivpggtyrnrasygakv 283
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518291517 288 ---GVVPEEMLRVF----NCGlGMVLVVAENSVGEATRLLQEAGETVARIGRIEtapEGDEASVRV 346
Cdd:COG0709  284 efaEGLDEAQRDLLfdpqTSG-GLLIAVPPEAAEELLAALRAAGYAAAIIGEVT---AGEGGAIEV 345
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
87-140 4.28e-03

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 38.66  E-value: 4.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518291517  87 AMCVN--DLVVQGAEPLFFLDYFAT-GKLEVAQASAVVAGIAEGCRQAGCALVGGET 140
Cdd:PRK05731  66 ALAVNlsDLAAMGARPAAFLLALALpKDLDEAWLEALADGLFELADRYGAELIGGDT 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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