NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|937547929|gb|ALI57150|]
View 

dihydropteroate synthase, partial [Pneumocystis carinii]

Protein Classification

pterin-binding domain-containing protein( domain architecture ID 1161)

pterin-binding domain-containing protein, similar to dihydropteroate synthase (DHPS) and cobalamin-dependent methyltransferases such as methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) and methionine synthase (MetH)

CATH:  3.20.20.20
Gene Ontology:  GO:0005488
SCOP:  3000643

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 super family cl43091
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 1-82 1.37e-34

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


The actual alignment was detected with superfamily member COG0294:

Pssm-ID: 440063  Cd Length: 274  Bit Score: 118.23  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:COG0294   19 NVTPDSFSDGGRYnDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALRAEF-DVPISVDTYKA 97


                 ...
gi 937547929  80 EVA 82
Cdd:COG0294   98 EVA 100
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 1-82 1.37e-34

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 118.23  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:COG0294   19 NVTPDSFSDGGRYnDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALRAEF-DVPISVDTYKA 97


                 ...
gi 937547929  80 EVA 82
Cdd:COG0294   98 EVA 100
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 1-82 1.62e-33

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: 115.40  E-value: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:cd00739    8 NVTPDSFSDGGRFlSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGEL-DVLISVDTFRA 86


                 ...
gi 937547929  80 EVA 82
Cdd:cd00739   87 EVA 89
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 1-82 1.34e-30

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: 107.73  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929    1 NLTPDSFFDGG-IHSCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKyLLKTYPDILISIDTFRS 79
Cdd:TIGR01496   7 NVTPDSFSDGGrFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIK-ALRDQPDVPISVDTYRA 85


                  ...
gi 937547929   80 EVA 82
Cdd:TIGR01496  86 EVA 88
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 1-82 2.37e-27

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: 98.90  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929    1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:pfam00809   5 NVTPDSFSDGGRFlDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEA-DVPISVDTTKA 83


                  ...
gi 937547929   80 EVA 82
Cdd:pfam00809  84 EVA 86
folP PRK11613
dihydropteroate synthase; Provisional
 1-81 2.18e-24

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 92.12  E-value: 2.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:PRK11613  22 NVTPDSFSDGGTHnSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAIAQRF-EVWISVDTSKP 100


                 ..
gi 937547929  80 EV 81
Cdd:PRK11613 101 EV 102
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 1-82 1.37e-34

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 118.23  E-value: 1.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:COG0294   19 NVTPDSFSDGGRYnDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEALRAEF-DVPISVDTYKA 97


                 ...
gi 937547929  80 EVA 82
Cdd:COG0294   98 EVA 100
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 1-82 1.62e-33

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: 115.40  E-value: 1.62e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:cd00739    8 NVTPDSFSDGGRFlSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEALRGEL-DVLISVDTFRA 86


                 ...
gi 937547929  80 EVA 82
Cdd:cd00739   87 EVA 89
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 1-82 1.34e-30

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: 107.73  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929    1 NLTPDSFFDGG-IHSCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKyLLKTYPDILISIDTFRS 79
Cdd:TIGR01496   7 NVTPDSFSDGGrFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIK-ALRDQPDVPISVDTYRA 85


                  ...
gi 937547929   80 EVA 82
Cdd:TIGR01496  86 EVA 88
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 1-82 2.37e-27

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: 98.90  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929    1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:pfam00809   5 NVTPDSFSDGGRFlDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAALRDEA-DVPISVDTTKA 83


                  ...
gi 937547929   80 EVA 82
Cdd:pfam00809  84 EVA 86
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
 1-82 9.63e-27

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: 97.73  E-value: 9.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKyLLKTYPDILISIDTFRS 79
Cdd:cd00423    8 NVTPDSFSDGGKFlSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLR-ALAGEPDVPISVDTFNA 86


                 ...
gi 937547929  80 EVA 82
Cdd:cd00423   87 EVA 89
folP PRK11613
dihydropteroate synthase; Provisional
 1-81 2.18e-24

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 92.12  E-value: 2.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGGIH-SCDSVLIDVKKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPAIKYLLKTYpDILISIDTFRS 79
Cdd:PRK11613  22 NVTPDSFSDGGTHnSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAIAQRF-EVWISVDTSKP 100


                 ..
gi 937547929  80 EV 81
Cdd:PRK11613 101 EV 102
PRK13753 PRK13753
dihydropteroate synthase; Provisional
 1-80 8.60e-05

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 38.91  E-value: 8.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937547929   1 NLTPDSFFDGG--IHSCDSVLIDVkKFINAGATIVDIGGQSTRPGSRIIPLEEEIFRVIPaikyLLKTYPDIL--ISIDT 76
Cdd:PRK13753   9 NLTEDSFFDESrrLDPAGAVTAAI-EMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAP----LLDALSDQMhrVSIDS 83


                 ....
gi 937547929  77 FRSE 80
Cdd:PRK13753  84 FQPE 87
 
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