NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|270346531|pdb|3H2O|A]
View 

Chain A, Dihydropteroate synthase

Protein Classification

dihydropteroate synthase( domain architecture ID 11416730)

dihydropteroate synthase catalyzes the formation of 7,8-dihydropteroate from para-aminobenzoic acid and 6-hydroxymethyl-7,8-dihydropterin-pyrophosphate, a key step in the folate biosynthetic pathway

CATH:  3.20.20.20
EC:  2.5.1.15
Gene Ontology:  GO:0009396|GO:0004156|GO:0046656|GO:0046872
PubMed:  19899766|22383850
SCOP:  4003341

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 21-295 1.07e-156

Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis


:

Pssm-ID: 440063  Cd Length: 274  Bit Score: 437.95  E-value: 1.07e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       21 MKWDYDLRCgeytlnlnEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEI 100
Cdd:COG0294   1 MTLGRTLDL--------SRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEEL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      101 KRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNY 173
Cdd:COG0294  73 ARVVPVIEALRAEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFDPEMAEVAAEYGVPVVLMHMRgtpqtmqRNPHY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      174 RNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEE 253
Cdd:COG0294 153 DDVVAEVRDFLEERIEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRALGYPVLVGVSRKSFIGALLGRPPEE 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
3H2O_A      254 RLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAKMMDAMIGKG 295
Cdd:COG0294 233 RLAGTLAAAALAAARGADIVRVHDVAETVDALKVADAIRRAR 274
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 21-295 1.07e-156

Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440063  Cd Length: 274  Bit Score: 437.95  E-value: 1.07e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       21 MKWDYDLRCgeytlnlnEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEI 100
Cdd:COG0294   1 MTLGRTLDL--------SRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEEL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      101 KRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNY 173
Cdd:COG0294  73 ARVVPVIEALRAEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFDPEMAEVAAEYGVPVVLMHMRgtpqtmqRNPHY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      174 RNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEE 253
Cdd:COG0294 153 DDVVAEVRDFLEERIEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRALGYPVLVGVSRKSFIGALLGRPPEE 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
3H2O_A      254 RLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAKMMDAMIGKG 295
Cdd:COG0294 233 RLAGTLAAAALAAARGADIVRVHDVAETVDALKVADAIRRAR 274
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 40-289 1.97e-129

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


Pssm-ID: 238380  Cd Length: 257  Bit Score: 368.47  E-value: 1.97e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       40 TLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPIS 119
Cdd:cd00739   1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGELDVLIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      120 IDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNYRNLMADMIADLYDSIKIAK 192
Cdd:cd00739  81 VDTFRAEVARAALEAGADIINDVSGGSDDPAMLEVAAEYGAPLVLMHMRgtpktmqENPYYEDVVDEVLSFLEARLEAAE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      193 DAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEF 272
Cdd:cd00739 161 SAGVARNRIILDPGIGFGKTPEHNLELLRRLDELKQLGLPVLVGASRKSFIGALLGREPKDRDWGTLALSALAAANGADI 240

                       250
                ....*....|....*..
3H2O_A      273 VRVHDVKEMSRMAKMMD 289
Cdd:cd00739 241 VRVHDVKATRDALKVAD 257
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 41-291 7.30e-127

dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273657  Cd Length: 257  Bit Score: 361.96  E-value: 7.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A         41 LIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISI 120
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALRDQPDVPISV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        121 DTYKAEVAKQAIEAGAHIINDIWGAKaEPKIAEVAAHYDVPIILMHNR-------DNMNYRNLMADMIADLYDSIKIAKD 193
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQ-DPAMLEVAAEYGVPLVLMHMRgtprtmqENPHYEDVVEEVLRFLEARAEELVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        194 AGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFV 273
Cdd:TIGR01496 160 AGVAAERIILDPGIGFGKTPEHNLELLKHLEEFVALGYPLLVGASRKSFIGALLGTPPEERLEGTLAASAYAVQKGADIV 239

                         250
                  ....*....|....*...
3H2O_A        274 RVHDVKEMSRMAKMMDAM 291
Cdd:TIGR01496 240 RVHDVKETRDALKVLEAL 257
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 43-276 7.66e-106

Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.


Pssm-ID: 395651 [Multi-domain]  Cd Length: 243  Bit Score: 308.06  E-value: 7.66e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A         43 MGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDT 122
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEADVPISVDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        123 YKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDN--------MNYRNLMADMIADLYDSIKIAKDA 194
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDGDPEMAELAAEYGAAVVVMHMDGTpktmqeneQQYEDVVEEVERFLRARVAAAEEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        195 GVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNV-LGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFV 273
Cdd:pfam00809 161 GVPPEDIILDPGIGFGKTEEHNLELLRTLDELRViLGVPVLLGVSRKSFIGRGLPLGGEERDAGTAAFLALAIAAGADIV 240


                  ...
3H2O_A        274 RVH 276
Cdd:pfam00809 241 RVH 243
folP PRK11613
dihydropteroate synthase; Provisional
 27-280 1.74e-82

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 250.05  E-value: 1.74e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        27 LRCGEYTLNLNEKTlIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPM 106
Cdd:PRK11613   3 LFAQGTTLDLSHPH-VMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       107 IQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIwGAKAEPKIAEVAAHYDVPIILMH---NRDNM----NYRNLMAD 179
Cdd:PRK11613  82 VEAIAQRFEVWISVDTSKPEVIRESAKAGAHIINDI-RSLSEPGALEAAAETGLPVCLMHmqgNPKTMqeapKYDDVFAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       180 MIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTG 259
Cdd:PRK11613 161 VNRYFIEQIARCEAAGIAKEKLLLDPGFGFGKNLSHNYQLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSL 240

                        250       260
                 ....*....|....*....|.
3H2O_A       260 ATVCLGIEKGCEFVRVHDVKE 280
Cdd:PRK11613 241 ACAVIAAMQGAQIIRVHDVKE 261
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 21-295 1.07e-156

Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440063  Cd Length: 274  Bit Score: 437.95  E-value: 1.07e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       21 MKWDYDLRCgeytlnlnEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEI 100
Cdd:COG0294   1 MTLGRTLDL--------SRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEEL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      101 KRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNY 173
Cdd:COG0294  73 ARVVPVIEALRAEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFDPEMAEVAAEYGVPVVLMHMRgtpqtmqRNPHY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      174 RNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEE 253
Cdd:COG0294 153 DDVVAEVRDFLEERIEAAEAAGIARERIILDPGIGFGKTLEHNLELLRRLDELRALGYPVLVGVSRKSFIGALLGRPPEE 232

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
3H2O_A      254 RLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAKMMDAMIGKG 295
Cdd:COG0294 233 RLAGTLAAAALAAARGADIVRVHDVAETVDALKVADAIRRAR 274
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 40-289 1.97e-129

DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.


Pssm-ID: 238380  Cd Length: 257  Bit Score: 368.47  E-value: 1.97e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       40 TLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPIS 119
Cdd:cd00739   1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGELDVLIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      120 IDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNYRNLMADMIADLYDSIKIAK 192
Cdd:cd00739  81 VDTFRAEVARAALEAGADIINDVSGGSDDPAMLEVAAEYGAPLVLMHMRgtpktmqENPYYEDVVDEVLSFLEARLEAAE 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      193 DAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEF 272
Cdd:cd00739 161 SAGVARNRIILDPGIGFGKTPEHNLELLRRLDELKQLGLPVLVGASRKSFIGALLGREPKDRDWGTLALSALAAANGADI 240

                       250
                ....*....|....*..
3H2O_A      273 VRVHDVKEMSRMAKMMD 289
Cdd:cd00739 241 VRVHDVKATRDALKVAD 257
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 41-291 7.30e-127

dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 273657  Cd Length: 257  Bit Score: 361.96  E-value: 7.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A         41 LIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISI 120
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKALRDQPDVPISV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        121 DTYKAEVAKQAIEAGAHIINDIWGAKaEPKIAEVAAHYDVPIILMHNR-------DNMNYRNLMADMIADLYDSIKIAKD 193
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQ-DPAMLEVAAEYGVPLVLMHMRgtprtmqENPHYEDVVEEVLRFLEARAEELVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        194 AGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFV 273
Cdd:TIGR01496 160 AGVAAERIILDPGIGFGKTPEHNLELLKHLEEFVALGYPLLVGASRKSFIGALLGTPPEERLEGTLAASAYAVQKGADIV 239

                         250
                  ....*....|....*...
3H2O_A        274 RVHDVKEMSRMAKMMDAM 291
Cdd:TIGR01496 240 RVHDVKETRDALKVLEAL 257
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
 40-289 5.18e-109

Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). DHPS, a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS. Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.


Pssm-ID: 238242 [Multi-domain]  Cd Length: 258  Bit Score: 316.52  E-value: 5.18e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       40 TLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPIS 119
Cdd:cd00423   1 TLIMGILNVTPDSFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLRALAGEPDVPIS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      120 IDTYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNR-------DNMNYRNLMADMIADLYDSIKIAK 192
Cdd:cd00423  81 VDTFNAEVAEAALKAGADIINDVSGGRGDPEMAPLAAEYGAPVVLMHMDgtpqtmqNNPYYADVVDEVVEFLEERVEAAT 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      193 DAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVL-GYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCE 271
Cdd:cd00423 161 EAGIPPEDIILDPGIGFGKTEEHNLELLRRLDAFRELpGLPLLLGVSRKSFLGDLLSVGPKDRLAGTAAFLAAAILNGAD 240

                       250
                ....*....|....*...
3H2O_A      272 FVRVHDVKEMSRMAKMMD 289
Cdd:cd00423 241 IVRVHDVKELRDAIKVAE 258
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 43-276 7.66e-106

Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) that catalyzes a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin.


Pssm-ID: 395651 [Multi-domain]  Cd Length: 243  Bit Score: 308.06  E-value: 7.66e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A         43 MGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDT 122
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEADVPISVDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        123 YKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDN--------MNYRNLMADMIADLYDSIKIAKDA 194
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDGDPEMAELAAEYGAAVVVMHMDGTpktmqeneQQYEDVVEEVERFLRARVAAAEEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        195 GVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNV-LGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFV 273
Cdd:pfam00809 161 GVPPEDIILDPGIGFGKTEEHNLELLRTLDELRViLGVPVLLGVSRKSFIGRGLPLGGEERDAGTAAFLALAIAAGADIV 240


                  ...
3H2O_A        274 RVH 276
Cdd:pfam00809 241 RVH 243
folP PRK11613
dihydropteroate synthase; Provisional
 27-280 1.74e-82

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 250.05  E-value: 1.74e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        27 LRCGEYTLNLNEKTlIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPM 106
Cdd:PRK11613   3 LFAQGTTLDLSHPH-VMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       107 IQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIwGAKAEPKIAEVAAHYDVPIILMH---NRDNM----NYRNLMAD 179
Cdd:PRK11613  82 VEAIAQRFEVWISVDTSKPEVIRESAKAGAHIINDI-RSLSEPGALEAAAETGLPVCLMHmqgNPKTMqeapKYDDVFAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       180 MIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTG 259
Cdd:PRK11613 161 VNRYFIEQIARCEAAGIAKEKLLLDPGFGFGKNLSHNYQLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSL 240

                        250       260
                 ....*....|....*....|.
3H2O_A       260 ATVCLGIEKGCEFVRVHDVKE 280
Cdd:PRK11613 241 ACAVIAAMQGAQIIRVHDVKE 261
PRK13753 PRK13753
dihydropteroate synthase; Provisional
 39-276 1.02e-34

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 127.12  E-value: 1.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        39 KTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKEMRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKlPI 118
Cdd:PRK13753   1 MVTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMH-RV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       119 SIDTYKAEVAKQAIEAGAHIINDIWGAkAEPKIAEVAAHYDVPIILMHN--RDNMNYR-------NLMADMIADLYDSIK 189
Cdd:PRK13753  80 SIDSFQPETQRYALKRGVGYLNDIQGF-PDPALYPDIAEADCRLVVMHSaqRDGIATRtghlrpeDALDEIVRFFEARVS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       190 IAKDAGVRDENIILDPGIGF--AKTPEQNLEAMRNLEQL-NVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGI 266
Cdd:PRK13753 159 ALRRSGVAADRLILDPGMGFflSPAPETSLHVLSNLQKLkSALGLPLLVSVSRKSFLGATVGLPVKDLGPASLAAELHAI 238

                        250
                 ....*....|
3H2O_A       267 EKGCEFVRVH 276
Cdd:PRK13753 239 GNGADYVRTH 248
MetH2 COG1410
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ...
 63-242 2.79e-06

Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441020 [Multi-domain]  Cd Length: 1141  Bit Score: 48.80  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        63 DAAVRHAKEMRDEGAHIIDIG-GESTRPGfakvsvEEEIKRVVPMIQAvskEVKLPISIDTYKAEVakqaIEAGAH---- 137
Cdd:COG1410  358 DEALEVAREQVEAGAQILDVNvDEPGRDE------VAAMVRFLNLLAS---EVRVPLMIDSSKPEV----IEAGLKcyqg 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       138 --IINDIWGAKAEPK---IAEVAAHYDVPIIlmhnrdnmnyrnLMA---DMIADLYDS-IKIAK--------DAGVRDEN 200
Cdd:COG1410  425 kpIVNSISLEEGEERfeeVAPLAKKYGAAVV------------VLAideEGQADTAERkLEIAEriydlaveEYGFPPED 492

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
3H2O_A       201 IILDP-------GIgfaktPEQN------LEAMRNLEQlNVLGYPVLLGTSRKSF 242
Cdd:COG1410  493 IIFDPlvftvatGI-----EEHRnyavetIEAIRLIKE-ELPGAKTSLGVSNVSF 541
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 48-195 5.52e-04

Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.


Pssm-ID: 188630 [Multi-domain]  Cd Length: 281  Bit Score: 40.61  E-value: 5.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       48 VTPdsFSDGGSYNEvDAAVRHAKEMRDEGAHIIDIGGeSTrpG-FAKVSVEEEIKrvvpMIQAVSKEV--KLPI-----S 119
Cdd:cd00408   6 VTP--FTADGEVDL-DALRRLVEFLIEAGVDGLVVLG-TT--GeAPTLTDEERKE----VIEAVVEAVagRVPViagvgA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      120 IDTYKA-EVAKQAIEAGAH---IINDIWGAKAEPKIA----EVAAHYDVPIILmHNRDNMNYRNLMADMIADL--YDSIK 189
Cdd:cd00408  76 NSTREAiELARHAEEAGADgvlVVPPYYNKPSQEGIVahfkAVADASDLPVIL-YNIPGRTGVDLSPETIARLaeHPNIV 154


                ....*.
3H2O_A      190 IAKDAG 195
Cdd:cd00408 155 GIKDSS 160
PRK04165 PRK04165
acetyl-CoA decarbonylase/synthase complex subunit gamma; Provisional
 107-234 1.03e-03

acetyl-CoA decarbonylase/synthase complex subunit gamma; Provisional


Pssm-ID: 235235 [Multi-domain]  Cd Length: 450  Bit Score: 40.23  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       107 IQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDIWGAKAE--PKIAEVAAHYDVPIIlmhnrdnmnyrnLMADMIADL 184
Cdd:PRK04165 147 VKKVAETTDLPLILCSEDPAVLKAALEVVADRKPLLYAATKEnyEEMAELAKEYNCPLV------------VKAPNLEEL 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
3H2O_A       185 YDSIKIAKDAGVRDenIILDPGigfAKTPEQNLEAMRNLEQLNV------LGYPVL 234
Cdd:PRK04165 215 KELVEKLQAAGIKD--LVLDPG---TENIKETLDDFVQIRRAAIkkgdrpLGYPII 265
PRK07535 PRK07535
methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated
 69-242 1.85e-03

methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase; Validated


Pssm-ID: 181022 [Multi-domain]  Cd Length: 261  Bit Score: 39.06  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A        69 AKEMRDEGAHIIDIGgestrpgfAKVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEvakqAIEAG--AH----IINDI 142
Cdd:PRK07535  31 ALKQAEAGADYLDVN--------AGTAVEEEPETMEWLVETVQEVVDVPLCIDSPNPA----AIEAGlkVAkgppLINSV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       143 wgaKAEPKIAEV----AAHYDVPIILMHNRDN-----MNYRNLMADMIadlydsIKIAKDAGVRDENIILDPGIGFAKTP 213
Cdd:PRK07535  99 ---SAEGEKLEVvlplVKKYNAPVVALTMDDTgipkdAEDRLAVAKEL------VEKADEYGIPPEDIYIDPLVLPLSAA 169

                        170       180       190
                 ....*....|....*....|....*....|....*.
3H2O_A       214 EQN----LEAMRNLEQLnvlgYP---VLLGTSRKSF 242
Cdd:PRK07535 170 QDAgpevLETIRRIKEL----YPkvhTTCGLSNISF 201
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 66-139 4.18e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 38.58  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A         66 VRHAKEMRDEGAHII---DIGGeSTRPGFAKVsveeeikrvvpMIQAVSKEVKLPI----------SIDTYKAevakqAI 132
Cdd:PRK12999  694 VDLAKELEKAGAHILaikDMAG-LLKPAAAYE-----------LVSALKEEVDLPIhlhthdtsgnGLATYLA-----AA 756


                  ....*..
3H2O_A        133 EAGAHII 139
Cdd:PRK12999  757 EAGVDIV 763
MeTr cd00740
MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent ...
 63-242 8.28e-03

MeTr subgroup of pterin binding enzymes. This family includes cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH). Cobalamin-dependent methyltransferases catalyze the transfer of a methyl group via a methyl- cob(III)amide intermediate. These include MeTr, a functional heterodimer, and the folate binding domain of MetH.


Pssm-ID: 238381 [Multi-domain]  Cd Length: 252  Bit Score: 36.99  E-value: 8.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A       63 DAAVRHAKEMRDEGAHIIDIG-GESTRPGfakvsvEEEIKRVVPMIQAVSkevKLPISIDTYKAEVAKQAIE--AGAHII 139
Cdd:cd00740  26 DEALDVARQQVEGGAQILDLNvDYGGLDG------VSAMKWLLNLLATEP---TVPLMLDSTNWEVIEAGLKccQGKCVV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3H2O_A      140 NDIW---GAKAEPKIAEVAAHYDVPIILMhnrdNMNYRNlmadMIADLYDSIKIAKDA--------GVRDENIILDPGIG 208
Cdd:cd00740  97 NSINledGEERFLKVARLAKEHGAAVVVL----AFDEQG----QAKTRDKKVEIAERAyealtefvGFPPEDIIFDPLIL 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3H2O_A      209 FAKT--PEQNLEAMRNLEQLNVL-----GYPVLLGTSRKSF 242
Cdd:cd00740 169 PIATgiEEHRPYALETIDAIRMIkerlpAVKISLGVSNVSF 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH