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dihydropteroate synthase, partial [Thiocystis violacea]

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

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List of domain hits

 Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 9-146 1.34e-72

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


:

Pssm-ID: 440063  Cd Length: 274  Bit Score: 218.38  E-value: 1.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894   9 TARFRIELSRPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH 88
Cdd:COG0294     2 TLGRTLDLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  89 AV-TLGVPVSVDTSRPELMRAALEAGADIVNDVRALRR-PGALEAVAEHpSAGVCLMHMR 146
Cdd:COG0294    82 LRaEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFdPEMAEVAAEY-GVPVVLMHMR 140
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 9-146 1.34e-72

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 218.38  E-value: 1.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894   9 TARFRIELSRPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH 88
Cdd:COG0294     2 TLGRTLDLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  89 AV-TLGVPVSVDTSRPELMRAALEAGADIVNDVRALRR-PGALEAVAEHpSAGVCLMHMR 146
Cdd:COG0294    82 LRaEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFdPEMAEVAAEY-GVPVVLMHMR 140
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 19-146 7.73e-56

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: 175.10  E-value: 7.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  19 PRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVS 97
Cdd:cd00739     1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEAlRGELDVLIS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1956496894  98 VDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEHPSAGVCLMHMR 146
Cdd:cd00739    81 VDTFRAEVARAALEAGADIINDVSGGSDDPAMLEVAAEYGAPLVLMHMR 129
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 20-146 1.03e-53

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: 169.75  E-value: 1.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  20 RVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVSV 98
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKAlRDQPDVPISV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1956496894  99 DTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEHpSAGVCLMHMR 146
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEY-GVPLVLMHMR 127
folP PRK11613
dihydropteroate synthase; Provisional
 14-146 5.12e-50

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 161.07  E-value: 5.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  14 IELSRPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTL 92
Cdd:PRK11613   10 LDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAiAQRF 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1956496894  93 GVPVSVDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEhPSAGVCLMHMR 146
Cdd:PRK11613   90 EVWISVDTSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAE-TGLPVCLMHMQ 142
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 22-146 2.73e-49

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: 158.22  E-value: 2.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  22 MAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVSVDT 100
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAAlRDEADVPISVDT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1956496894 101 SRPELMRAALEAGADIVNDVRALRR-PGALEAVAEHpSAGVCLMHMR 146
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDGdPEMAELAAEY-GAAVVVMHMD 126
 
Name Accession Description Interval E-value
FolP COG0294
Dihydropteroate synthase [Coenzyme transport and metabolism]; Dihydropteroate synthase is part ...
 9-146 1.34e-72

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


Pssm-ID: 440063  Cd Length: 274  Bit Score: 218.38  E-value: 1.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894   9 TARFRIELSRPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH 88
Cdd:COG0294     2 TLGRTLDLSRPLVMGILNVTPDSFSDGGRYNDPDAALAHAEEMVEEGADIIDIGGESTRPGAEPVSAEEELARVVPVIEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  89 AV-TLGVPVSVDTSRPELMRAALEAGADIVNDVRALRR-PGALEAVAEHpSAGVCLMHMR 146
Cdd:COG0294    82 LRaEFDVPISVDTYKAEVARAALEAGADIINDVSGLRFdPEMAEVAAEY-GVPVVLMHMR 140
DHPS cd00739
DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional ...
 19-146 7.73e-56

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: 175.10  E-value: 7.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  19 PRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVS 97
Cdd:cd00739     1 TQIMGILNVTPDSFSDGGRFLSLDKAVAHAEKMIAEGADIIDIGGESTRPGADPVSVEEELERVIPVLEAlRGELDVLIS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1956496894  98 VDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEHPSAGVCLMHMR 146
Cdd:cd00739    81 VDTFRAEVARAALEAGADIINDVSGGSDDPAMLEVAAEYGAPLVLMHMR 129
DHPS TIGR01496
dihydropteroate synthase; This model represents dihydropteroate synthase, the enzyme that ...
 20-146 1.03e-53

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: 169.75  E-value: 1.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  20 RVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVSV 98
Cdd:TIGR01496   1 QIMGIVNVTPDSFSDGGRFLSVDKAVAHAERMLEEGADIIDVGGESTRPGADRVSPEEELNRVVPVIKAlRDQPDVPISV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1956496894  99 DTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEHpSAGVCLMHMR 146
Cdd:TIGR01496  81 DTYRAEVARAALEAGADIINDVSGGQDPAMLEVAAEY-GVPLVLMHMR 127
Pterin_binding cd00423
Pterin binding enzymes. This family includes dihydropteroate synthase (DHPS) and ...
 19-146 6.63e-51

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: 162.44  E-value: 6.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  19 PRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVS 97
Cdd:cd00423     1 TLIMGILNVTPDSFSDGGKFLSLDKALEHARRMVEEGADIIDIGGESTRPGAEPVSVEEELERVIPVLRAlAGEPDVPIS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1956496894  98 VDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEHPSAGVCLMHMR 146
Cdd:cd00423    81 VDTFNAEVAEAALKAGADIINDVSGGRGDPEMAPLAAEYGAPVVLMHMD 129
folP PRK11613
dihydropteroate synthase; Provisional
 14-146 5.12e-50

dihydropteroate synthase; Provisional


Pssm-ID: 183230  Cd Length: 282  Bit Score: 161.07  E-value: 5.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  14 IELSRPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTL 92
Cdd:PRK11613   10 LDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELDRVIPVVEAiAQRF 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1956496894  93 GVPVSVDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAEhPSAGVCLMHMR 146
Cdd:PRK11613   90 EVWISVDTSKPEVIRESAKAGAHIINDIRSLSEPGALEAAAE-TGLPVCLMHMQ 142
Pterin_bind pfam00809
Pterin binding enzyme; This family includes a variety of pterin binding enzymes that all adopt ...
 22-146 2.73e-49

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: 158.22  E-value: 2.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  22 MAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRH-AVTLGVPVSVDT 100
Cdd:pfam00809   1 MGILNVTPDSFSDGGRFLDLDKALAHARRMVEEGADIIDIGGESTRPGAERVDGEEEMERVLPVLAAlRDEADVPISVDT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1956496894 101 SRPELMRAALEAGADIVNDVRALRR-PGALEAVAEHpSAGVCLMHMR 146
Cdd:pfam00809  81 TKAEVAEAALKAGADIINDISGGDGdPEMAELAAEY-GAAVVVMHMD 126
PRK13753 PRK13753
dihydropteroate synthase; Provisional
 18-134 4.45e-13

dihydropteroate synthase; Provisional


Pssm-ID: 184303  Cd Length: 279  Bit Score: 64.34  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  18 RPRVMAIVNVTPDSFSDGGRYVDLDAARARCEQLLREGADILDIGGESTRPGSRAPELDEELERVLPLVRHAVTLGVPVS 97
Cdd:PRK13753    1 MVTVFGILNLTEDSFFDESRRLDPAGAVTAAIEMLRVGSDVVDVGPAASHPDARPVSPADEIRRIAPLLDALSDQMHRVS 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1956496894  98 VDTSRPELMRAALEAGADIVNDVRALRRPGALEAVAE 134
Cdd:PRK13753   81 IDSFQPETQRYALKRGVGYLNDIQGFPDPALYPDIAE 117
DHDPS cd00950
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ...
 27-115 8.29e-06

Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.


Pssm-ID: 188637 [Multi-domain]  Cd Length: 284  Bit Score: 44.02  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  27 VTPdsFSDGGRyVDLDAARARCEQLLREGADILDIG---GEStrpgsraPEL-DEELERVLPLVRHAVTLGVPV-----S 97
Cdd:cd00950     9 VTP--FKDDGS-VDFDALERLIEFQIENGTDGLVVCgttGES-------PTLsDEEHEAVIEAVVEAVNGRVPViagtgS 78

                          90
                  ....*....|....*....
gi 1956496894  98 VDTSRP-ELMRAALEAGAD 115
Cdd:cd00950    79 NNTAEAiELTKRAEKAGAD 97
MetH2 COG1410
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ...
 40-120 4.84e-05

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: 41.86  E-value: 4.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894   40 DLDAARARCEQLLREGADILDIG-GEstrpgsraPELDEE--LERVLPLVRHAVTlgVPVSVDTSRPELMRAALEA--GA 114
Cdd:COG1410    356 DYDEALEVAREQVEAGAQILDVNvDE--------PGRDEVaaMVRFLNLLASEVR--VPLMIDSSKPEVIEAGLKCyqGK 425


                   ....*.
gi 1956496894  115 DIVNDV 120
Cdd:COG1410    426 PIVNSI 431
DHDPS-like cd00408
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ...
 21-115 1.63e-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: 40.22  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  21 VMAIVnVTPdsFSDGGRyVDLDAARARCEQLLREGADILDIGGeSTrpgSRAPEL-DEELERVLPLVRHAVTLGVPVSVD 99
Cdd:cd00408     1 VIPAL-VTP--FTADGE-VDLDALRRLVEFLIEAGVDGLVVLG-TT---GEAPTLtDEERKEVIEAVVEAVAGRVPVIAG 72

                          90       100
                  ....*....|....*....|..
gi 1956496894 100 TSRP------ELMRAALEAGAD 115
Cdd:cd00408    73 VGANstreaiELARHAEEAGAD 94
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 42-117 8.39e-03

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 35.35  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956496894  42 DAARARCEQLLREGADILDI--GGESTRPGSRAPEL---DEELERVlplVRHAVTLGVPVSVDTSRPELMRAALEAGADI 116
Cdd:cd01299   120 EEVRAAVREQLRRGADQIKImaTGGVLSPGDPPPDTqfsEEELRAI---VDEAHKAGLYVAAHAYGAEAIRRAIRAGVDT 196


                  .
gi 1956496894 117 V 117
Cdd:cd01299   197 I 197
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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