|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
3-294 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 599.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 3 QTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKA 82
Cdd:PRK04180 2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 83 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVR 162
Cdd:PRK04180 82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 163 HMRKVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSD 242
Cdd:PRK04180 162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 586857 243 NPAKFAKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:PRK04180 242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
3-294 |
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: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 3 QTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKA 82
Cdd:COG0214 2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 83 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVR 162
Cdd:COG0214 82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 163 HMRKVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSD 242
Cdd:COG0214 162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 586857 243 NPAKFAKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:COG0214 242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
11-293 |
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: 541.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 11 RGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIGHIVEA 90
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 91 RVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 170
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 171 VRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKA 250
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 586857 251 IVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERG 293
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
9-294 |
0e+00 |
|
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: 516.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 9 VKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIGHIV 88
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 89 EARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVN 168
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 169 AQVRKVVAMS-EDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKF 247
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 586857 248 AKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
6-211 |
4.24e-148 |
|
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: 413.41 E-value: 4.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 6 TERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIG 85
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 86 HIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMR 165
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586857 166 KVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFA 211
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04180 |
PRK04180 |
pyridoxal 5'-phosphate synthase lyase subunit PdxS; |
3-294 |
0e+00 |
|
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
Pssm-ID: 179769 Cd Length: 293 Bit Score: 599.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 3 QTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKA 82
Cdd:PRK04180 2 ETGTERVKRGFAEMLKGGVIMDVVNAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIEEIMDAVSIPVMAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 83 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVR 162
Cdd:PRK04180 82 RIGHFVEAQILEALGVDYIDESEVLTPADEEYHIDKWDFTVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 163 HMRKVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSD 242
Cdd:PRK04180 162 HMRQINGEIRRLTSMSEDELYTAAKELQAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 586857 243 NPAKFAKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:PRK04180 242 DPEKRARAIVEATTHYDDPEVLAEVSKGLGEAMVGIDIDELPPEERLQERGW 293
|
|
| PdxS |
COG0214 |
Pyridoxal 5'-phosphate synthase subunit PdxS [Coenzyme transport and metabolism]; Pyridoxal 5 ... |
3-294 |
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: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 3 QTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKA 82
Cdd:COG0214 2 ETGTERVKRGLAEMLKGGVIMDVTNPEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMEAVSIPVMAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 83 RIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVR 162
Cdd:COG0214 82 RIGHFVEAQILEALGVDFIDESEVLTPADEEYHIDKHAFKVPFVCGARNLGEALRRIGEGAAMIRTKGEAGTGNVVEAVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 163 HMRKVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSD 242
Cdd:COG0214 162 HMRTINSEIRRLQGMDEEELMAAAKELGAPYELVKEVAELGRLPVVNFAAGGIATPADAALMMQLGADGVFVGSGIFKSE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 586857 243 NPAKFAKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:COG0214 242 DPEKRARAIVEATTHYDDPEVLAEVSEGLGEAMKGIDISTLPEEERLQERGW 293
|
|
| pdxS |
cd04727 |
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ... |
11-293 |
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: 541.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 11 RGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIGHIVEA 90
Cdd:cd04727 1 RGFAQMLKGGVIMDVTNAEQARIAEEAGAVAVMALERVPADIRAAGGVARMADPKMIKEIMDAVSIPVMAKVRIGHFVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 91 RVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQ 170
Cdd:cd04727 81 QILEALGVDMIDESEVLTPADEEHHIDKHKFKVPFVCGARNLGEALRRISEGAAMIRTKGEAGTGNVVEAVRHMRAVNGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 171 VRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKA 250
Cdd:cd04727 161 IRKLQSMSEEELYAVAKEIQAPYELVKETAKLGRLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSENPEKRARA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 586857 251 IVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERG 293
Cdd:cd04727 241 IVEAVTHYDDPEILAEVSEGLGEAMVGIDIASLKEEERMQERG 283
|
|
| TIGR00343 |
TIGR00343 |
pyridoxal 5'-phosphate synthase, synthase subunit Pdx1; This protein had been believed to be a ... |
9-294 |
0e+00 |
|
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: 516.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 9 VKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIGHIV 88
Cdd:TIGR00343 1 LKKGLAQMLKGGVIMDVVNPEQAKIAEEAGAVAVMALERVPADIRASGGVARMSDPKMIKEIMDAVSIPVMAKVRIGHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 89 EARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVN 168
Cdd:TIGR00343 81 EAQILEALGVDYIDESEVLTPADWTFHIDKKKFKVPFVCGARDLGEALRRINEGAAMIRTKGEAGTGNIVEAVRHMRKIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 169 AQVRKVVAMS-EDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKF 247
Cdd:TIGR00343 161 EEIRQIQNMLeEEDLAAVAKELRVPVELLLEVLKLGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSSNPEKL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 586857 248 AKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW 294
Cdd:TIGR00343 241 AKAIVEATTHYDNPEKLAEVSKDLGEAMKGISISSISEAERLQERGW 287
|
|
| SOR_SNZ |
pfam01680 |
SOR/SNZ family; Members of this family are enzymes involved in a new pathway of pyridoxine ... |
6-211 |
4.24e-148 |
|
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: 413.41 E-value: 4.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 6 TERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIG 85
Cdd:pfam01680 1 TFRVKRGLAQMLKGGVIMDVTNAEQAKIAEEAGAVAVMALERVPADIRKAGGVARMSDPKMIKEIMDAVSIPVMAKARIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 86 HIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMR 165
Cdd:pfam01680 81 HFVEAQILEALGVDYIDESEVLTPADEEHHIDKHNFKVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVVEAVRHMR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 586857 166 KVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFA 211
Cdd:pfam01680 161 TINGEIRRLQNMDEEELYAFAKELGAPYELVKEVAELGRLPVVNFA 206
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
28-236 |
5.11e-11 |
|
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: 60.68 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 28 AEQAKIAEEAGAVAVMALERVPADIRAAGgvarmADPTIVEEVMNAVSIPVMAKARIGHIVE-----ARVLEAMGVDYID 102
Cdd:cd04722 15 VELAKAAAEAGADAIIVGTRSSDPEEAET-----DDKEVLKEVAAETDLPLGVQLAINDAAAavdiaAAAARAAGADGVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 103 ESEVLTPADEEFHLNKNE-----YTVPFVCGCRDLGEATRRIAE--GASMLRTKGEPGTGNIVEAVRHmrkvnaqvrkvv 175
Cdd:cd04722 90 IHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEeaGVDEVGLGNGGGGGGGRDAVPI------------ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586857 176 amsedelmteaknlgapyELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGS 236
Cdd:cd04722 158 ------------------ADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
194-253 |
1.14e-06 |
|
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: 48.28 E-value: 1.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 194 ELLLQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVE 253
Cdd:cd00564 140 ELLREIAELVEIPVV--AIGGI-TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| thiG |
CHL00162 |
thiamin biosynthesis protein G; Validated |
199-251 |
1.60e-06 |
|
thiamin biosynthesis protein G; Validated
Pssm-ID: 214380 Cd Length: 267 Bit Score: 48.55 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 586857 199 IKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:CHL00162 184 IIENAKIPVIIDA--GIGTPSEASQAMELGASGVLLNTAVAQAKNPEQMAKAM 234
|
|
| ThiG |
pfam05690 |
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ... |
188-254 |
6.90e-06 |
|
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: 46.47 E-value: 6.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586857 188 NLGAPYELLLQIKKDG-KLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:pfam05690 158 GLGLLNPYNLKIIIEEaDVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFklaVEA 226
|
|
| PRK11840 |
PRK11840 |
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional |
192-254 |
8.48e-06 |
|
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
Pssm-ID: 236998 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 8.48e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586857 192 PYELLLqIKKDGKLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:PRK11840 238 PYTIRL-IVEGATVPVLVDA--GVGTASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMklaVEA 300
|
|
| ThiG |
cd04728 |
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ... |
204-254 |
8.50e-06 |
|
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: 45.94 E-value: 8.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 586857 204 KLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:cd04728 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFklaVEA 226
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
191-255 |
1.12e-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: 45.55 E-value: 1.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586857 191 APYELLLQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSgIF----KSDNPAKFAKAIVEAT 255
Cdd:cd04730 143 GTFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT-RFlateESGASPAYKQALLAAT 208
|
|
| thiG |
PRK00208 |
thiazole synthase; Reviewed |
204-254 |
1.14e-05 |
|
thiazole synthase; Reviewed
Pssm-ID: 234687 Cd Length: 250 Bit Score: 45.82 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 586857 204 KLPVVNFAagGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI---VEA 254
Cdd:PRK00208 175 DVPVIVDA--GIGTPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFklaVEA 226
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
28-248 |
1.55e-05 |
|
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: 45.47 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 28 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVARMADP----TIVEEVMNAVSIPVMAKARIGhivearvl 93
Cdd:COG0042 77 AEAARIAEELGADEI--------DInmgcpvkkvtKGGAGAALLRDPelvaEIVKAVVEAVDVPVTVKIRLG-------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 94 eamgvdyIDESevltpadeefHLNkneytvpfvcgCRDLGeatrRIAE--GASML----RTKGEpgtgniveavrhMRKV 167
Cdd:COG0042 141 -------WDDD----------DEN-----------ALEFA----RIAEdaGAAALtvhgRTREQ------------RYKG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 168 NAQvrkvvamsedelmteaknlgapYELLLQIKKDGKLPVVnfAAGGVATPADAALMMQL-GADGVFVGSGIFKsdNPAK 246
Cdd:COG0042 177 PAD----------------------WDAIARVKEAVSIPVI--GNGDIFSPEDAKRMLEEtGCDGVMIGRGALG--NPWL 230
|
..
gi 586857 247 FA 248
Cdd:COG0042 231 FR 232
|
|
| IGPS |
cd00331 |
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
211-251 |
6.00e-05 |
|
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.
Pssm-ID: 238203 Cd Length: 217 Bit Score: 43.22 E-value: 6.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 586857 211 AAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd00331 177 SESGISTPEDVKRLAEAGADAVLIGESLMRAPDPGAALREL 217
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
193-238 |
7.21e-05 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 43.21 E-value: 7.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 586857 193 YELLLQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 238
Cdd:PRK01130 162 FALLKELLKAVGCPVI--AEGRINTPEQAKKALELGAHAVVVGGAI 205
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
194-255 |
1.10e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.48 E-value: 1.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586857 194 ELLLQIKKDGK-LPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEAT 255
Cdd:PRK00043 149 EGLREIRAAVGdIPIV--AIGGI-TPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAF 208
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
193-238 |
1.40e-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: 42.18 E-value: 1.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 586857 193 YELLLQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGSGI 238
Cdd:cd04729 166 FELLKELRKALGIPVI--AEGRINSPEQAAKALELGADAVVVGSAI 209
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
185-251 |
3.27e-04 |
|
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: 41.03 E-value: 3.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586857 185 EAKNLGAPYELLLQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd04726 139 QAAGGWWPEDDLKKVKKLLGVKVA--VAGGI-TPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
28-249 |
3.85e-04 |
|
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: 40.94 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 28 AEQAKIAEEAGAVAVmalervpaDI----------RAAGGVARMADP----TIVEEVMNAVSIPVMAKARIGHivearvl 93
Cdd:cd02801 70 AEAAKIVEELGADGI--------DLnmgcpspkvtKGGAGAALLKDPelvaEIVRAVREAVPIPVTVKIRLGW------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 94 eamgvdyidesevltpadeefhlNKNEYTVPFVCGCRDlgeatrriaEGASML----RTKGEPGTGNiveavrhmrkvna 169
Cdd:cd02801 135 -----------------------DDEEETLELAKALED---------AGASALtvhgRTREQRYSGP------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 170 qvrkvvamsedelmteaknlgAPYELLLQIKKDGKLPVvnFAAGGVATPADAALMMQL-GADGVFVGSGIFKsdNPAKFA 248
Cdd:cd02801 170 ---------------------ADWDYIAEIKEAVSIPV--IANGDIFSLEDALRCLEQtGVDGVMIGRGALG--NPWLFR 224
|
.
gi 586857 249 K 249
Cdd:cd02801 225 E 225
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
194-254 |
3.99e-04 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 40.77 E-value: 3.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586857 194 ELLLQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK07695 139 EELSDIARALSIPVI--AIGGI-TPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAES 196
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
192-254 |
4.64e-04 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 41.54 E-value: 4.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586857 192 PYELLLQIKKDGKLPVVnfAAGGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK07028 150 PLELLKEVSEEVSIPIA--VAGGL-DAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
|
|
| trpC |
PRK00278 |
indole-3-glycerol phosphate synthase TrpC; |
214-254 |
7.59e-04 |
|
indole-3-glycerol phosphate synthase TrpC;
Pssm-ID: 234710 Cd Length: 260 Bit Score: 40.14 E-value: 7.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 586857 214 GVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEA 254
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMRADDPGAALRELLGA 259
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
192-236 |
1.13e-03 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 39.71 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 586857 192 PYELLLQIKKDGKLPVVnfAAGGVATPADAALMMQLGADGVFVGS 236
Cdd:COG2070 146 TFALVPEVRDAVDIPVI--AAGGIADGRGIAAALALGADGVQMGT 188
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
28-248 |
1.60e-03 |
|
Dihydrouridine synthase (Dus); 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 archae. 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. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 39.62 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 28 AEQAKIAEEAGAVAVMALERVPAD--IRAAGGVARMADP----TIVEEVMNAVSIPVMAKARIGhivearvleamgvdyI 101
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKkvTRGGGGAALLRNPdlvaQIVKAVVKAVGIPVTVKIRIG---------------W 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 102 DESevltpadeefHLNKNEYtVPFVCGCrdlgeatrriaeGASMLrtkgepgtgniveaVRHMRkvnaqvrkvvamsede 181
Cdd:pfam01207 134 DDS----------HENAVEI-AKIVEDA------------GAQAL--------------TVHGR---------------- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586857 182 lmTEAKNLGAP--YELLLQIKKDGKLPVvnFAAGGVATPADA-ALMMQLGADGVFVGSGIFKsdNPAKFA 248
Cdd:pfam01207 161 --TRAQNYEGTadWDAIKQVKQAVSIPV--IANGDITDPEDAqRCLAYTGADGVMIGRGALG--NPWLFA 224
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
213-251 |
6.79e-03 |
|
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.
Pssm-ID: 238244 Cd Length: 211 Bit Score: 37.07 E-value: 6.79e-03
10 20 30
....*....|....*....|....*....|....*....
gi 586857 213 GGVaTPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAI 251
Cdd:cd00429 173 GGI-NLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
204-240 |
7.78e-03 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 37.19 E-value: 7.78e-03
10 20 30
....*....|....*....|....*....|....*..
gi 586857 204 KLPVVnfAAGGVATPADAALMMQLGADGVFVGSGIFK 240
Cdd:PRK13585 193 DIPVI--ASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
200-237 |
8.73e-03 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 37.11 E-value: 8.73e-03
10 20 30
....*....|....*....|....*....|....*...
gi 586857 200 KKDGKLPVVnfaAGGVATPADAALMMQLGADGVFVGSG 237
Cdd:cd00381 131 KKYPNVDVI---AGNVVTAEAARDLIDAGADGVKVGIG 165
|
|
| |
