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1F76

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004152molecular_functiondihydroorotate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006221biological_processpyrimidine nucleotide biosynthetic process
A0006222biological_processUMP biosynthetic process
A0009220biological_processpyrimidine ribonucleotide biosynthetic process
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0044205biological_process'de novo' UMP biosynthetic process
A0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
B0004152molecular_functiondihydroorotate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006221biological_processpyrimidine nucleotide biosynthetic process
B0006222biological_processUMP biosynthetic process
B0009220biological_processpyrimidine ribonucleotide biosynthetic process
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
B0044205biological_process'de novo' UMP biosynthetic process
B0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
D0004152molecular_functiondihydroorotate dehydrogenase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
D0006221biological_processpyrimidine nucleotide biosynthetic process
D0006222biological_processUMP biosynthetic process
D0009220biological_processpyrimidine ribonucleotide biosynthetic process
D0010181molecular_functionFMN binding
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
D0044205biological_process'de novo' UMP biosynthetic process
D0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
E0004152molecular_functiondihydroorotate dehydrogenase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
E0006221biological_processpyrimidine nucleotide biosynthetic process
E0006222biological_processUMP biosynthetic process
E0009220biological_processpyrimidine ribonucleotide biosynthetic process
E0010181molecular_functionFMN binding
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
E0044205biological_process'de novo' UMP biosynthetic process
E0106430molecular_functiondihydroorotate dehydrogenase (quinone) activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN A 1337
ChainResidue
AALA61
ATHR245
ATHR247
ASER267
AGLY268
ALEU271
AVAL295
AGLY296
AGLY297
ATYR318
ASER319
AALA62
AORO1338
AHOH1352
AHOH1404
AHOH1675
AGLY63
ALYS66
ATHR86
AASN111
AASN139
AASN172
ALYS217

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ORO A 1338
ChainResidue
ALYS66
AASN111
AMSE113
AGLY114
APHE115
AASN172
ASER175
AASN177
AASN246
ATHR247
AFMN1337

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ORO A 1339
ChainResidue
AMSE1
ALEU37
AVAL38
AARG39
AGLN40
APRO326
AHOH1517
AHOH1528
AHOH1677

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 1437
ChainResidue
BALA61
BALA62
BGLY63
BLYS66
BTHR86
BASN111
BASN139
BASN172
BLYS217
BTHR245
BASN246
BTHR247
BSER267
BGLY268
BVAL295
BGLY296
BGLY297
BTYR318
BSER319
BFMT1439
BFMT1440
BHOH1441
BHOH1463

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN D 1537
ChainResidue
DALA61
DALA62
DGLY63
DLYS66
DTHR86
DASN111
DASN139
DASN172
DLYS217
DTHR245
DASN246
DTHR247
DSER267
DGLY268
DVAL295
DGLY296
DGLY297
DTYR318
DSER319
DFMT1538
DFMT1539
DHOH1542
DHOH1561
DHOH1564

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ORO D 1540
ChainResidue
DMSE1
DLEU37
DVAL38
DGLN40
DPRO326
DHOH1617

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FMN E 1637
ChainResidue
ELYS66
ETHR86
ELEU100
EASN111
EASN139
EASN172
ELYS217
ETHR245
EASN246
ETHR247
ESER267
EGLY268
ELEU271
EVAL295
EGLY296
EGLY297
ETYR318
ESER319
EFMT1638
EFMT1640
EHOH1641
EHOH1653
EHOH1693
EALA61
EALA62
EGLY63

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT B 1438
ChainResidue
BASN111
BASN177
BASN246
BTHR247
BFMT1439
BFMT1440

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 1439
ChainResidue
BPHE115
BASN172
BSER175
BASN246
BFMN1437
BFMT1438
BFMT1440

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT B 1440
ChainResidue
BLYS66
BMSE113
BGLY114
BPHE115
BSER175
BASN177
BFMN1437
BFMT1438
BFMT1439

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT D 1538
ChainResidue
DASN172
DSER175
DASN246
DFMN1537
DFMT1539

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT D 1539
ChainResidue
DLYS66
DMSE113
DGLY114
DPHE115
DSER175
DASN177
DFMN1537
DFMT1538
DHOH1557

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT E 1638
ChainResidue
ELYS66
EMSE113
EGLY114
EPHE115
EASN177
EFMN1637
EFMT1639
EFMT1640

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT E 1639
ChainResidue
EASN111
EASN177
ETHR247
EGLY265
EFMT1638
EFMT1640

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT E 1640
ChainResidue
EASN172
ESER175
EPRO176
EASN246
EFMN1637
EFMT1638
EFMT1639

Functional Information from PROSITE/UniProt
site_idPS00911
Number of Residues20
DetailsDHODEHASE_1 Dihydroorotate dehydrogenase signature 1. GsieiGTVTprpQpGNdkPR
ChainResidueDetails
AGLY80-ARG99

site_idPS00912
Number of Residues21
DetailsDHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGvGGIdSviaAreKIaAGA
ChainResidueDetails
AILE292-ALA312

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER175
BSER175
DSER175
ESER175

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:12220493
ChainResidueDetails
AALA62
BTHR86
BASN139
BLYS217
BTHR245
BGLY268
BGLY297
BTYR318
DALA62
DTHR86
DASN139
ATHR86
DLYS217
DTHR245
DGLY268
DGLY297
DTYR318
EALA62
ETHR86
EASN139
ELYS217
ETHR245
AASN139
EGLY268
EGLY297
ETYR318
ALYS217
ATHR245
AGLY268
AGLY297
ATYR318
BALA62

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING:
ChainResidueDetails
ALYS66
BASN246
DLYS66
DASN111
DASN172
DASN177
DASN246
ELYS66
EASN111
EASN172
EASN177
AASN111
EASN246
AASN172
AASN177
AASN246
BLYS66
BASN111
BASN172
BASN177

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER175
ATHR178
APHE115
ALYS217

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER175
BTHR178
BPHE115
BLYS217

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
DSER175
DTHR178
DPHE115
DLYS217

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ESER175
ETHR178
EPHE115
ELYS217

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ASER175

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
BSER175

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
DSER175

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1h7x
ChainResidueDetails
ESER175

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PDB entries from 2024-09-04

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