NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|237757300|ref|NP_001153773|]
View 

dihydropyrimidine dehydrogenase [NADP(+)] isoform 2 [Homo sapiens]

Protein Classification

photosystem I iron-sulfur center; ferredoxin family protein( domain architecture ID 10631146)

photosystem I iron-sulfur center is an apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI) and is essential for photochemical activity; ferredoxin-like protein that may be a iron-sulfur cluster-containing protein which mediates electron transfer;contains a DUF3470 domain at the C-terminus

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
 56-162 2.75e-45

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


:

Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 144.60  E-value: 2.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300   56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691   2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80

                          90       100
                  ....*....|....*....|....*..
gi 237757300  136 CVGGCNLYATEEGPINIGGLQQFATET 162
Cdd:pfam14691  81 CEGACVLGKKGFEPVAIGRLERFAADW 107
 
Name Accession Description Interval E-value
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
 56-162 2.75e-45

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 144.60  E-value: 2.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300   56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691   2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80

                          90       100
                  ....*....|....*....|....*..
gi 237757300  136 CVGGCNLYATEEGPINIGGLQQFATET 162
Cdd:pfam14691  81 CEGACVLGKKGFEPVAIGRLERFAADW 107
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 53-162 5.52e-37

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 132.23  E-value: 5.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  53 EKLENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749  17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 237757300 133 SDLCVGGCNLYATEEgPINIGGLQQFATET 162
Cdd:PRK11749  96 ERLCEGACVRGKKGE-PVAIGRLERYITDW 124
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 57-162 1.11e-28

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 109.45  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493    3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79

                         90       100
                 ....*....|....*....|....*.
gi 237757300 137 VGGCNLyATEEGPINIGGLQQFATET 162
Cdd:COG0493   80 EGACVR-GIVDEPVAIGALERFIADK 104
 
Name Accession Description Interval E-value
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
 56-162 2.75e-45

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 144.60  E-value: 2.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300   56 ENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:pfam14691   2 IKNFEEV-ALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80

                          90       100
                  ....*....|....*....|....*..
gi 237757300  136 CVGGCNLYATEEGPINIGGLQQFATET 162
Cdd:pfam14691  81 CEGACVLGKKGFEPVAIGRLERFAADW 107
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 53-162 5.52e-37

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 132.23  E-value: 5.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  53 EKLENNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPT 132
Cdd:PRK11749  17 EERAQNFDEV-APGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQ 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 237757300 133 SDLCVGGCNLYATEEgPINIGGLQQFATET 162
Cdd:PRK11749  96 ERLCEGACVRGKKGE-PVAIGRLERYITDW 124
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 57-162 1.11e-28

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 109.45  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTsdLC 136
Cdd:COG0493    3 KDFREV-YPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPA--PC 79

                         90       100
                 ....*....|....*....|....*.
gi 237757300 137 VGGCNLyATEEGPINIGGLQQFATET 162
Cdd:COG0493   80 EGACVR-GIVDEPVAIGALERFIADK 104
PRK12831 PRK12831
putative oxidoreductase; Provisional
 58-162 3.03e-23

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 95.08  E-value: 3.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  58 NFDDIkhtTLG--ERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDL 135
Cdd:PRK12831  22 NFEEV---CLGynEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQ 98

                         90       100
                 ....*....|....*....|....*..
gi 237757300 136 CVGGCNLYATEEgPINIGGLQQFATET 162
Cdd:PRK12831  99 CEGKCVLGIKGE-PVAIGKLERFVADW 124
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 57-159 4.05e-21

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 89.42  E-value: 4.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  57 NNFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLC 136
Cdd:PRK12778 310 NRFEEV-NLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQC 388

                         90       100
                 ....*....|....*....|...
gi 237757300 137 VGGCNLYATEEGPINIGGLQQFA 159
Cdd:PRK12778 389 ESKCIHGKMGEEAVAIGYLERFV 411
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 58-162 1.29e-15

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 73.27  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  58 NFDDIkHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCV 137
Cdd:PRK12810  26 DFKEF-YEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102

                         90       100
                 ....*....|....*....|....*
gi 237757300 138 GGCNLyATEEGPINIGGLQQFATET 162
Cdd:PRK12810 103 GACTL-NINFGPVTIKNIERYIIDK 126
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 72-158 4.78e-14

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 68.81  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300   72 ALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnLYATEEGPIN 151
Cdd:PRK12775  326 ALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEAQC-IIAKKHESVG 404


                  ....*..
gi 237757300  152 IGGLQQF 158
Cdd:PRK12775  405 IGRLERF 411
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 53-162 4.87e-12

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 63.12  E-value: 4.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  53 EKLENNFDDIkHTTLGERGALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCP 131
Cdd:PRK12809 185 SERKTHFGEI-YCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCP 263

                         90       100       110
                 ....*....|....*....|....*....|.
gi 237757300 132 TSDLCVGGCNLyATEEGPINIGGLQQFATET 162
Cdd:PRK12809 264 QDRLCEGACTL-KDHSGAVSIGNLERYITDT 293
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 30-162 1.68e-11

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 61.69  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  30 STSAKKLDKKHW--KRNPDKNCFNCEKleNNFDDIKHTTLGERgALREAMRCLKCAD-APCQKSCPTNLDIKSFITSIAN 106
Cdd:PRK12769 179 PAMSKVEQMQATppRGEPDKLAIEARK--TGFDEIYLPFRADQ-AQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKA 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 237757300 107 KNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLyATEEGPINIGGLQQFATET 162
Cdd:PRK12769 256 GNIDAAVELSHQTNSLPEITGRVCPQDRLCEGACTL-RDEYGAVTIGNIERYISDQ 310
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 86-159 1.10e-09

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 56.04  E-value: 1.10e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237757300  86 PCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNlYATEEGPINIGGLQQFA 159
Cdd:PRK12771  48 PCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCN-RGQVDDAVGINAVERFL 118
PRK13984 PRK13984
putative oxidoreductase; Provisional
 72-130 3.73e-09

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 54.77  E-value: 3.73e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 237757300  72 ALREAMRCLKCAdaPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVC 130
Cdd:PRK13984 180 AMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVC 236
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 82-159 5.89e-08

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 51.27  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  82 CAD--APCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSdlCVGGCNLYATEEgPINIGGLQQFA 159
Cdd:PRK12814  97 CGDclGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHGVDE-PVSICALKRYA 173
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 75-161 8.79e-07

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 47.90  E-value: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237757300  75 EAMRCLKCADAPCQ------------KSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCnl 142
Cdd:PRK12779 186 EVMRDKQCDDKPCElgvlvqgkaepkGGCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-- 263

                         90
                 ....*....|....*....
gi 237757300 143 yATEEGPINIGGLQQFATE 161
Cdd:PRK12779 264 -THTKRPIEIGQLEWYLPQ 281
 
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