|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
1-276 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 563.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:PRK04180 15 MLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHFVEAQILEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:PRK04180 95 LGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQINGEIRRLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:PRK04180 175 SMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRARAIVEAT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIK--LLMANRG 276
Cdd:PRK04180 255 THYDDPEVLAEVSKGLGEAMVGIDIDELPpeERLQERG 292
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
1-276 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 555.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:COG0214 15 MLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRIGHFVEAQILEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:COG0214 95 LGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHMRTINSEIRRLQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:COG0214 175 GMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKRARAIVEAT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIK--LLMANRG 276
Cdd:COG0214 255 THYDDPEVLAEVSEGLGEAMKGIDISTLPeeERLQERG 292
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
1-276 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 507.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:cd04727 6 MLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEAQILEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:cd04727 86 LGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGEIRKLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:cd04727 166 SMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARAIVEAV 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIKL--LMANRG 276
Cdd:cd04727 246 THYDDPEILAEVSEGLGEAMVGIDIASLKEeeRMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
1-268 |
6.13e-165 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 458.47 E-value: 6.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:TIGR00343 8 MLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFVEAQILEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:TIGR00343 88 LGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKINEEIRQIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SM-REDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKA 239
Cdd:TIGR00343 168 NMlEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKLAKAIVEA 247
|
250 260
....*....|....*....|....*....
gi 1445269322 240 VTNYKDAKMIAKLSENLGEAMVGINEQEI 268
Cdd:TIGR00343 248 TTHYDNPEKLAEVSKDLGEAMKGISISSI 276
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
1-196 |
5.90e-144 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 402.24 E-value: 5.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:pfam01680 11 MLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIGHFVEAQILEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:pfam01680 91 LGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRTINGEIRRLQ 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFA 196
Cdd:pfam01680 171 NMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
1-276 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 563.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:PRK04180 15 MLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKARIGHFVEAQILEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:PRK04180 95 LGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRQINGEIRRLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:PRK04180 175 SMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSGDPEKRARAIVEAT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIK--LLMANRG 276
Cdd:PRK04180 255 THYDDPEVLAEVSKGLGEAMVGIDIDELPpeERLQERG 292
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
1-276 |
0e+00 |
|
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxS is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 439984 Cd Length: 293 Bit Score: 555.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:COG0214 15 MLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKVRIGHFVEAQILEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:COG0214 95 LGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVRHMRTINSEIRRLQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:COG0214 175 GMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSEDPEKRARAIVEAT 254
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIK--LLMANRG 276
Cdd:COG0214 255 THYDDPEVLAEVSEGLGEAMKGIDISTLPeeERLQERG 292
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
1-276 |
0e+00 |
|
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 507.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:cd04727 6 MLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEAQILEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:cd04727 86 LGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGEIRKLQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:cd04727 166 SMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARAIVEAV 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 1445269322 241 TNYKDAKMIAKLSENLGEAMVGINEQEIKL--LMANRG 276
Cdd:cd04727 246 THYDDPEILAEVSEGLGEAMVGIDIASLKEeeRMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
1-268 |
6.13e-165 |
|
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a singlet oxygen resistance protein. Subsequent work showed that it is a protein of pyridoxine (vitamin B6) biosynthesis, and that pyridoxine quenches the highly toxic singlet form of oxygen produced by light in the presence of certain chemicals. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 129443 Cd Length: 287 Bit Score: 458.47 E-value: 6.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:TIGR00343 8 MLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFVEAQILEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:TIGR00343 88 LGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKINEEIRQIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 161 SM-REDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKA 239
Cdd:TIGR00343 168 NMlEEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKLAKAIVEA 247
|
250 260
....*....|....*....|....*....
gi 1445269322 240 VTNYKDAKMIAKLSENLGEAMVGINEQEI 268
Cdd:TIGR00343 248 TTHYDNPEKLAEVSKDLGEAMKGISISSI 276
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
1-196 |
5.90e-144 |
|
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine/pyridoxal 5-phosphate biosynthesis. This family was formerly known as UPF0019.
Pssm-ID: 460291 Cd Length: 206 Bit Score: 402.24 E-value: 5.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 1 MLKGGVIMDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMIHGIQEAVSIPVMAKCRIGHFVEAQVLEA 80
Cdd:pfam01680 11 MLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIGHFVEAQILEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 81 IEIDYIDESEVLSPADDVYHINKRDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHMRMMNSAIRKLT 160
Cdd:pfam01680 91 LGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMRTINGEIRRLQ 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1445269322 161 SMREDELFEEAKTLRVPFDLVKYVAQNGKLPVVNFA 196
Cdd:pfam01680 171 NMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
181-264 |
1.06e-05 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 45.85 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 181 VKYVAQNGKLPVVNFAagGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAVTN----YKDAKMIAKLSENL 256
Cdd:CHL00162 181 LQIIIENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAMKLAVQAgrlaYLAGRMPKKKYAQA 258
|
....*...
gi 1445269322 257 GEAMVGIN 264
Cdd:CHL00162 259 SSPIEGIS 266
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
186-240 |
1.73e-05 |
|
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.
Pssm-ID: 428589 Cd Length: 247 Bit Score: 44.93 E-value: 1.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1445269322 186 QNGKLPVVNFAagGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:pfam05690 172 EEADVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAV 224
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
181-246 |
2.02e-05 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 2.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 181 VKYVAQNGKLPVVNFAagGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAVTNYKDA 246
Cdd:PRK11840 241 IRLIVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEAGRLA 304
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
177-221 |
2.48e-05 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 44.40 E-value: 2.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1445269322 177 PFDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGS 221
Cdd:cd04730 144 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 186
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
179-238 |
2.52e-05 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 44.05 E-value: 2.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 179 DLVKYVAQNGKLPVVnfAAGGVaTPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVK 238
Cdd:cd00564 140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
189-240 |
1.30e-04 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 42.36 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1445269322 189 KLPVVNFAagGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:PRK00208 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAV 224
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
189-240 |
1.68e-04 |
|
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).
Pssm-ID: 240079 Cd Length: 248 Bit Score: 42.09 E-value: 1.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1445269322 189 KLPVVNFAagGVATPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAV 240
Cdd:cd04728 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFKLAV 224
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
169-223 |
1.88e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 41.67 E-value: 1.88e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 169 EEAKTLRVP-FDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGSGI 223
Cdd:PRK01130 152 EETKKPEEPdFALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
8-221 |
3.55e-04 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 40.65 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 8 MDVTTPEQARIAEDSGACAVMALERIPADIRAAGGVSRMSDPAMihgiqEAVSIPVMAKCRIGHFVEAQ-----VLEAIE 82
Cdd:cd04722 10 PSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVA-----AETDLPLGVQLAINDAAAAVdiaaaAARAAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 83 IDYI--DESEVLSPADDVYHINK-----RDFAVPFVCGAKDLGEALRRINEGASMIRTKGEPGTGDVIQAVRHmrmmnsa 155
Cdd:cd04722 85 ADGVeiHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPI------- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 156 irkltsmrEDELFEEAKtlrvpfdlvkyvaqnGKLPVVNFAAGGVATPADAALMMQLGAEGVFVGS 221
Cdd:cd04722 158 --------ADLLLILAK---------------RGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
169-223 |
4.04e-04 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 40.64 E-value: 4.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 169 EEAKTLRVP-FDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGSGI 223
Cdd:cd04729 156 EETAKTEDPdFELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
177-221 |
4.87e-04 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 40.86 E-value: 4.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1445269322 177 PFDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGS 221
Cdd:COG2070 146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
177-247 |
8.87e-04 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 40.39 E-value: 8.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1445269322 177 PFDLVKYVAQNGKLPVVnfAAGGVaTPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAVTNYKDAK 247
Cdd:PRK07028 150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGKPVK 217
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
184-244 |
1.00e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 39.40 E-value: 1.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1445269322 184 VAQNGKLPVVnfAAGGVaTPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASIVKAVTNYK 244
Cdd:PRK00043 155 RAAVGDIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
169-236 |
1.67e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 38.72 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1445269322 169 EEAKTLRVPFDLVKYVAQNGKLPVVnfAAGGVaTPADAALMMQLGAEGVFVGSGIFKSGDPAKRAASI 236
Cdd:cd04726 138 AQAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
176-224 |
2.73e-03 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis
Pssm-ID: 439876 Cd Length: 236 Bit Score: 38.10 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1445269322 176 VPFDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGSGIF 224
Cdd:COG0106 176 PNLELYRELAAATGIPVI--ASGGVSSLDDLRALKELGVEGAIVGKALY 222
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
180-253 |
2.82e-03 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 38.52 E-value: 2.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 180 LVKYVAQ--NGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGSGIFKSGdPAKrAASIVKAVTNYKDAKMIAKLS 253
Cdd:COG0167 225 MVREVAQavGGDIPII--GVGGISTAEDALEFILAGASAVQVGTALFYEG-PGL-VRRIIRGLEAYLEEKGFSSIS 296
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
16-229 |
3.46e-03 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 38.15 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 16 ARIAEDSGA--------CavmaleriPAD--IRAAGGVSRMSDP----AMIHGIQEAVSIPVMAKCRIGhfveaqvleai 81
Cdd:COG0042 80 ARIAEELGAdeidinmgC--------PVKkvTKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG----------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 82 eidyIDESevlspaddvyHINKRDFAvpfvcgakdlgealRRINE-GASMI----RTK--GEPGTGDviqavrhmrmmns 154
Cdd:COG0042 141 ----WDDD----------DENALEFA--------------RIAEDaGAAALtvhgRTReqRYKGPAD------------- 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1445269322 155 airkltsmredelfeeaktlrvpFDLVKYVAQNGKLPVVnfAAGGVATPADAALMMQL-GAEGVFVGSGIFksGDP 229
Cdd:COG0042 180 -----------------------WDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGAL--GNP 228
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
181-225 |
3.47e-03 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 37.96 E-value: 3.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1445269322 181 VKYVAQNGKLPVVnfAAGGVATPADAALMMQLGAEGVFVGSGIFK 225
Cdd:PRK13585 185 VKELVDSVDIPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
16-83 |
5.20e-03 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 37.47 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1445269322 16 ARIAEDSGACAVmaleripaDI----------RAAGGVSRMSDP----AMIHGIQEAVSIPVMAKCRIGHFVEAQVLEAI 81
Cdd:cd02801 73 AKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGWDDEEETLELA 144
|
..
gi 1445269322 82 EI 83
Cdd:cd02801 145 KA 146
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