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Conserved domains on  [gi|2052594783|gb|QWQ31552|]
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hypothetical protein KOY49_00795 [Candidatus Minimicrobia vallesae]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-260 2.41e-46

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd04738:

Pssm-ID: 473867  Cd Length: 327  Bit Score: 157.28  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIElnRSKVKSMPT 80
Cdd:cd04738    54 LAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLK--KRRPRGGPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAviADKSTkdefgpvvPEEYIIRDVKKAVSYIVenSLASVIEINISCPN-AGKEPFIYADTLESLLS----ELDSV 155
Cdd:cd04738   132 GVNIG--KNKDT--------PLEDAVEDYVIGVRKLG--PYADYLVVNVSSPNtPGLRDLQGKEALRELLTavkeERNKL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 156 ERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdLKDPLTDDiRGGLSGEPTRTHSLELIGYTYKN 234
Cdd:cd04738   200 GKKVPLLVKIaPDL-SDEELEDIADVALEHGVDGIIATNTTISRPGL-LRSPLANE-TGGLSGAPLKERSTEVLRELYKL 276

                         250       260
                  ....*....|....*....|....*.
gi 2052594783 235 YGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:cd04738   277 TGGKIPIIGVGGISSGEDAYEKIRAG 302
 
Name Accession Description Interval E-value
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 1-260 2.41e-46

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 157.28  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIElnRSKVKSMPT 80
Cdd:cd04738    54 LAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLK--KRRPRGGPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAviADKSTkdefgpvvPEEYIIRDVKKAVSYIVenSLASVIEINISCPN-AGKEPFIYADTLESLLS----ELDSV 155
Cdd:cd04738   132 GVNIG--KNKDT--------PLEDAVEDYVIGVRKLG--PYADYLVVNVSSPNtPGLRDLQGKEALRELLTavkeERNKL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 156 ERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdLKDPLTDDiRGGLSGEPTRTHSLELIGYTYKN 234
Cdd:cd04738   200 GKKVPLLVKIaPDL-SDEELEDIADVALEHGVDGIIATNTTISRPGL-LRSPLANE-TGGLSGAPLKERSTEVLRELYKL 276

                         250       260
                  ....*....|....*....|....*.
gi 2052594783 235 YGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:cd04738   277 TGGKIPIIGVGGISSGEDAYEKIRAG 302
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 1-248 3.87e-46

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 156.00  E-value: 3.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGF-DKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDyiELNRSKVKSMP 79
Cdd:COG0167    17 LASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLE--RLLPAKRYDVP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  80 TVVSVAviadKSTKDEFgpvvpeEYIIRdvkkavsyIVENSLASVIEINISCPNA---GKEPFIYADTLESLLSELDSVe 156
Cdd:COG0167    95 VIVNIG----GNTVEDY------VELAR--------RLADAGADYLELNISCPNTpggGRALGQDPEALAELLAAVKAA- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 157 RNVPFWIKMPHlyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGK-VDLKDPLTDDIRGGLSGEPTRTHSLELIGYTYKNY 235
Cdd:COG0167   156 TDKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTTLGRAIdLETRRPVLANEAGGLSGPALKPIALRMVREVAQAV 233

                         250
                  ....*....|...
gi 2052594783 236 GDKLTVIGVGGVF 248
Cdd:COG0167   234 GGDIPIIGVGGIS 246
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
1-262 1.82e-43

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 150.31  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVksmpt 80
Cdd:PRK05286   64 LAAGFDKNGEAIDALGALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAVIADKSTKDEFGpvvPEEYII--RDVKKAVSYIVenslasvieINISCPN-AGKEPFIYADTLESLLSEL----D 153
Cdd:PRK05286  139 PLGINIGKNKDTPLEDA---VDDYLIclEKLYPYADYFT---------VNISSPNtPGLRDLQYGEALDELLAALkeaqA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 154 SVERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRgkVDLKDPLTDDIRGGLSGEPTRTHSLELIGYTY 232
Cdd:PRK05286  207 ELHGYVPLLVKIaPDL-SDEELDDIADLALEHGIDGVIATNTTLSR--DGLKGLPNADEAGGLSGRPLFERSTEVIRRLY 283

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2052594783 233 KNYGDKLTVIGVGGVFRPKTHTLRLRQG--LV 262
Cdd:PRK05286  284 KELGGRLPIIGVGGIDSAEDAYEKIRAGasLV 315
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
2-248 3.66e-30

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 113.98  E-value: 3.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   2 SAGFDKN-VQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPntKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPt 80
Cdd:pfam01180  18 ASGFDKFgEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLAELLKRRKEYPRPD- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 vvsVAVIADKSTKDEfgpvvpEEYIirdvkkAVSYIVENsLASVIEINISCPNA-GKEPFIYADTLESLLSELDSVERNV 159
Cdd:pfam01180  95 ---LGINLSKAGMTV------DDYV------EVARKIGP-FADYIELNVSCPNTpGLRALQTDPELAAILLKVVKEVSKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 160 PFWIKM-PHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYG 236
Cdd:pfam01180 159 PVLVKLaPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKteKPILANGTGGLSGPPIKPIALKVIRELYQRTG 238

                         250
                  ....*....|..
gi 2052594783 237 DKLTVIGVGGVF 248
Cdd:pfam01180 239 PEIPIIGVGGIE 250
pyrD_sub2 TIGR01036
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ...
 1-247 5.32e-25

dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273408  Cd Length: 335  Bit Score: 101.40  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQ-LSPLMEdVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLekisDYIELNrskVKSMP 79
Cdd:TIGR01036  61 LAAGFDKDGEaIDALGA-MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGA----DVLVER---LKRAR 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  80 --TVVSVAVIADKSTKDEFGpvvPEEYIIrDVKKAVSYivenslASVIEINISCPN-AGKEPFIYADTLESLLS----EL 152
Cdd:TIGR01036 133 ykGPIGINIGKNKDTPSEDA---KEDYAA-CLRKLGPL------ADYLVVNVSSPNtPGLRDLQYKAELRDLLTavkqEQ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 153 DSVER--NVPFWIKM-PHLYDlKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdlKDPLTDDIRGGLSGEPTRTHSLELIG 229
Cdd:TIGR01036 203 DGLRRvhRVPVLVKIaPDLTE-SDLEDIADSLVELGIDGVIATNTTVSRSLV--QGPKNSDETGGLSGKPLQDKSTEIIR 279

                         250
                  ....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:TIGR01036 280 RLYAELQGRLPIIGVGGI 297
 
Name Accession Description Interval E-value
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 1-260 2.41e-46

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 157.28  E-value: 2.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIElnRSKVKSMPT 80
Cdd:cd04738    54 LAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADAVAKRLK--KRRPRGGPL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAviADKSTkdefgpvvPEEYIIRDVKKAVSYIVenSLASVIEINISCPN-AGKEPFIYADTLESLLS----ELDSV 155
Cdd:cd04738   132 GVNIG--KNKDT--------PLEDAVEDYVIGVRKLG--PYADYLVVNVSSPNtPGLRDLQGKEALRELLTavkeERNKL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 156 ERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdLKDPLTDDiRGGLSGEPTRTHSLELIGYTYKN 234
Cdd:cd04738   200 GKKVPLLVKIaPDL-SDEELEDIADVALEHGVDGIIATNTTISRPGL-LRSPLANE-TGGLSGAPLKERSTEVLRELYKL 276

                         250       260
                  ....*....|....*....|....*.
gi 2052594783 235 YGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:cd04738   277 TGGKIPIIGVGGISSGEDAYEKIRAG 302
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 1-248 3.87e-46

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 156.00  E-value: 3.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGF-DKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDyiELNRSKVKSMP 79
Cdd:COG0167    17 LASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPEDSGLINRMGLNNPGVDAFLE--RLLPAKRYDVP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  80 TVVSVAviadKSTKDEFgpvvpeEYIIRdvkkavsyIVENSLASVIEINISCPNA---GKEPFIYADTLESLLSELDSVe 156
Cdd:COG0167    95 VIVNIG----GNTVEDY------VELAR--------RLADAGADYLELNISCPNTpggGRALGQDPEALAELLAAVKAA- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 157 RNVPFWIKMPHlyDLKQFDSLLKVIVEHNIRGVTVANLIKDRGK-VDLKDPLTDDIRGGLSGEPTRTHSLELIGYTYKNY 235
Cdd:COG0167   156 TDKPVLVKLAP--DLTDIVEIARAAEEAGADGVIAINTTLGRAIdLETRRPVLANEAGGLSGPALKPIALRMVREVAQAV 233

                         250
                  ....*....|...
gi 2052594783 236 GDKLTVIGVGGVF 248
Cdd:COG0167   234 GGDIPIIGVGGIS 246
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
1-262 1.82e-43

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 150.31  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVksmpt 80
Cdd:PRK05286   64 LAAGFDKNGEAIDALGALGFGFVEVGTVTPRPQPGNPKPRLFRLPEDEALINRMGFNNDGADALAERLKKAYRGI----- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAVIADKSTKDEFGpvvPEEYII--RDVKKAVSYIVenslasvieINISCPN-AGKEPFIYADTLESLLSEL----D 153
Cdd:PRK05286  139 PLGINIGKNKDTPLEDA---VDDYLIclEKLYPYADYFT---------VNISSPNtPGLRDLQYGEALDELLAALkeaqA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 154 SVERNVPFWIKM-PHLyDLKQFDSLLKVIVEHNIRGVTVANLIKDRgkVDLKDPLTDDIRGGLSGEPTRTHSLELIGYTY 232
Cdd:PRK05286  207 ELHGYVPLLVKIaPDL-SDEELDDIADLALEHGIDGVIATNTTLSR--DGLKGLPNADEAGGLSGRPLFERSTEVIRRLY 283

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2052594783 233 KNYGDKLTVIGVGGVFRPKTHTLRLRQG--LV 262
Cdd:PRK05286  284 KELGGRLPIIGVGGIDSAEDAYEKIRAGasLV 315
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 2-247 3.49e-32

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 119.38  E-value: 3.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   2 SAGFD-KNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYA-------GMPNYGLEKISDYIELNRS 73
Cdd:cd02810    15 AAGPLlKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGESYPEQlgilnsfGLPNLGLDVWLQDIAKAKK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  74 KVKSMPTVVSVAviadKSTKDEfgpvvpeeyIIRDVKKavsyiVENSLASVIEINISCPNAGKEPFIY--ADTLESLLSE 151
Cdd:cd02810    95 EFPGQPLIASVG----GSSKED---------YVELARK-----IERAGAKALELNLSCPNVGGGRQLGqdPEAVANLLKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 152 LDSvERNVPFWIKMPHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRgKVDLKDPLT--DDIRGGLSGEPTRTHSLELIG 229
Cdd:cd02810   157 VKA-AVDIPLLVKLSPYFDLEDIVELAKAAERAGADGLTAINTISGR-VVDLKTVGPgpKRGTGGLSGAPIRPLALRWVA 234

                         250
                  ....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:cd02810   235 RLAARLQLDIPIIGVGGI 252
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
2-248 3.66e-30

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 113.98  E-value: 3.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   2 SAGFDKN-VQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPntKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPt 80
Cdd:pfam01180  18 ASGFDKFgEEALKWLALGKFGAIEIKSVTPYPQPGNPTPRVFRLP--EGVLNRMGLNNPGLDAVLAELLKRRKEYPRPD- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 vvsVAVIADKSTKDEfgpvvpEEYIirdvkkAVSYIVENsLASVIEINISCPNA-GKEPFIYADTLESLLSELDSVERNV 159
Cdd:pfam01180  95 ---LGINLSKAGMTV------DDYV------EVARKIGP-FADYIELNVSCPNTpGLRALQTDPELAAILLKVVKEVSKV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 160 PFWIKM-PHLYDLKQFDSLLKVIVEHNIRGVTVANLIKDRGKVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYG 236
Cdd:pfam01180 159 PVLVKLaPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKteKPILANGTGGLSGPPIKPIALKVIRELYQRTG 238

                         250
                  ....*....|..
gi 2052594783 237 DKLTVIGVGGVF 248
Cdd:pfam01180 239 PEIPIIGVGGIE 250
pyrD_sub2 TIGR01036
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ...
 1-247 5.32e-25

dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273408  Cd Length: 335  Bit Score: 101.40  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQ-LSPLMEdVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLekisDYIELNrskVKSMP 79
Cdd:TIGR01036  61 LAAGFDKDGEaIDALGA-MGFGFLEIGTVTPKPQPGNPRPRLFRLIEDEALINRMGFNNHGA----DVLVER---LKRAR 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  80 --TVVSVAVIADKSTKDEFGpvvPEEYIIrDVKKAVSYivenslASVIEINISCPN-AGKEPFIYADTLESLLS----EL 152
Cdd:TIGR01036 133 ykGPIGINIGKNKDTPSEDA---KEDYAA-CLRKLGPL------ADYLVVNVSSPNtPGLRDLQYKAELRDLLTavkqEQ 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 153 DSVER--NVPFWIKM-PHLYDlKQFDSLLKVIVEHNIRGVTVANLIKDRGKVdlKDPLTDDIRGGLSGEPTRTHSLELIG 229
Cdd:TIGR01036 203 DGLRRvhRVPVLVKIaPDLTE-SDLEDIADSLVELGIDGVIATNTTVSRSLV--QGPKNSDETGGLSGKPLQDKSTEIIR 279

                         250
                  ....*....|....*...
gi 2052594783 230 YTYKNYGDKLTVIGVGGV 247
Cdd:TIGR01036 280 RLYAELQGRLPIIGVGGI 297
PLN02826 PLN02826
dihydroorotate dehydrogenase
 1-260 1.74e-22

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 95.19  E-value: 1.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783   1 MSAGFDKNVQLSPLMEDVGFGFASGGSVTMEPRKGNLRPWFHRLPNTKSVVVYAGMPNYGLEKISDYIELNRSKVKSMPT 80
Cdd:PLN02826   89 LAAGFDKNAEAVEGLLGLGFGFVEIGSVTPLPQPGNPKPRVFRLREEGAIINRYGFNSEGIVAVAKRLGAQHGKRKLDET 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  81 VVSVAVIADKSTKDEFGPVV--------------PEEYI--IRDVKKAVSYIVenslasvieINISCPNA-------GKE 137
Cdd:PLN02826  169 SSSSFSSDDVKAGGKAGPGIlgvnlgknktsedaAADYVqgVRALSQYADYLV---------INVSSPNTpglrklqGRK 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 138 PFiyADTLESLLSELDSVERN----VPFWIKM-PHLY--DLKQfdsLLKVIVEHNIRGVTVANLIKDRGKVDLKDPLTDD 210
Cdd:PLN02826  240 QL--KDLLKKVLAARDEMQWGeegpPPLLVKIaPDLSkeDLED---IAAVALALGIDGLIISNTTISRPDSVLGHPHADE 314

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2052594783 211 IrGGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGVFRPKTHTLRLRQG 260
Cdd:PLN02826  315 A-GGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAG 363
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 25-247 1.98e-14

Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240092  Cd Length: 294  Bit Score: 71.20  E-value: 1.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  25 GGSVTMEPRKGNLRPWFHRLPNtkSVVVYAGMPNYGLEKISDYIELNRSKVK--SMPTVVSVAVIADKstkdefgpvvpe 102
Cdd:cd04741    39 TRSSTLAGRPGNPEPRYYAFPL--GSINSLGLPNLGLDYYLEYIRTISDGLPgsAKPFFISVTGSAED------------ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 103 eyIIRDVKKAVSyiVENSLASVIEINISCPN-AGKEPFIYA-DTLESLLSELDSVERnVPFWIKMPHLYDLKQFDSLLKV 180
Cdd:cd04741   105 --IAAMYKKIAA--HQKQFPLAMELNLSCPNvPGKPPPAYDfDATLEYLTAVKAAYS-IPVGVKTPPYTDPAQFDTLAEA 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2052594783 181 IVEHN--IRGVTVANLI-------KDRGKVDLKdplTDDIRGGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGV 247
Cdd:cd04741   180 LNAFAcpISFITATNTLgnglvldPERETVVLK---PKTGFGGLAGAYLHPLALGNVRTFRRLLPSEIQIIGVGGV 252
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 27-247 7.93e-12

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 64.20  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  27 SVTMEPRKGNLRPWFHRLP----NTksvvvyAGMPNYGLEKISDYIELNRSKVKSMPTVVSVAVIAdkstkdefgpvvPE 102
Cdd:PRK02506   44 SATLEPRPGNPEPRYADTPlgsiNS------MGLPNLGFDYYLDYVLELQKKGPNKPHFLSVVGLS------------PE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 103 EyIIRDVKKavsyIVENSLASVIEINISCPN-AGKEPFIYA-DTLESLLSELDSVeRNVPFWIKMPHLYDLKQFDSLLKV 180
Cdd:PRK02506  106 E-THTILKK----IQASDFNGLVELNLSCPNvPGKPQIAYDfETTEQILEEVFTY-FTKPLGVKLPPYFDIVHFDQAAAI 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2052594783 181 IVEHNIRGVTVANLIKDRGKVDLKDPlTDDIR-----GGLSGEPTRTHSLELIGYTYKNYGDKLTVIGVGGV 247
Cdd:PRK02506  180 FNKFPLAFVNCINSIGNGLVIDPEDE-TVVIKpkngfGGIGGDYIKPTALANVRAFYQRLNPSIQIIGTGGV 250
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 27-247 1.10e-11

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 63.60  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  27 SVTMEPRKGNLRPwfhRLPNTKSVVVYA-GMPNYGLEKISDYIELNRSKVKSmPTVVSVAviadKSTKDEFGPVVpeeyi 105
Cdd:TIGR01037  43 SIGLEPRPGYRNP---TIVETPCGMLNAiGLQNPGVEAFLEELKPVREEFPT-PLIASVY----GSSVEEFAEVA----- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 106 iRDVKKAVSYIVenslasVIEINISCPNA-------GKEPFIYADTLESLLSELDsvernVPFWIKM-PHLYDLKQFDsl 177
Cdd:TIGR01037 110 -EKLEKAPPYVD------AYELNLSCPHVkgggiaiGQDPELSADVVKAVKDKTD-----VPVFAKLsPNVTDITEIA-- 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052594783 178 lKVIVEHNIRGVTVANLIkdRG-KVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYGdkLTVIGVGGV 247
Cdd:TIGR01037 176 -KAAEEAGADGLTLINTL--RGmKIDIKtgKPILANKTGGLSGPAIKPIALRMVYDVYKMVD--IPIIGVGGI 243
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 27-248 5.17e-11

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 61.41  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  27 SVTMEPRKGNLRPwfhRLPNTKSVVVYA-GMPNYGLEK-ISDYIELNRSKVKsmPTVVSVAviadKSTKDEFgpvvpeey 104
Cdd:cd04740    42 SITLEPREGNPPP---RVVETPGGMLNAiGLQNPGVEAfLEELLPWLREFGT--PVIASIA----GSTVEEF-------- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 105 iirdvkKAVSYIVENSLASVIEINISCPNAGKEPFIYADTLESLLSELDSVER--NVPFWIKM-PHLYDLKQfdsLLKVI 181
Cdd:cd04740   105 ------VEVAEKLADAGADAIELNISCPNVKGGGMAFGTDPEAVAEIVKAVKKatDVPVIVKLtPNVTDIVE---IARAA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2052594783 182 VEHNIRGVTVANLIKDrGKVDLKD--PLTDDIRGGLSGEPTRTHSLELIGYTYKNYgdKLTVIGVGGVF 248
Cdd:cd04740   176 EEAGADGLTLINTLKG-MAIDIETrkPILGNVTGGLSGPAIKPIALRMVYQVYKAV--EIPIIGVGGIA 241
PRK07259 PRK07259
dihydroorotate dehydrogenase;
27-247 1.10e-10

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 60.55  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783  27 SVTMEPRKGNlrpwfhrlPNTKSVVVYAGM------PNYGLEKISDYIElnrSKVKSMPTVVsVAVIADKStkdefgpvv 100
Cdd:PRK07259   44 STTLEPREGN--------PTPRIAETPGGMlnaiglQNPGVDAFIEEEL---PWLEEFDTPI-IANVAGST--------- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052594783 101 PEEYIirdvkKAVSYIVENSLASVIEINISCPNA-------GKEPfiyaDTLESLLSELDSVErNVPFWIKM-PHLYDLK 172
Cdd:PRK07259  103 EEEYA-----EVAEKLSKAPNVDAIELNISCPNVkhggmafGTDP----ELAYEVVKAVKEVV-KVPVIVKLtPNVTDIV 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2052594783 173 QfdsLLKVIVEHNIRGVTVANLIKdrG-KVDLK--DPLTDDIRGGLSGEPTRTHSLELIGYTYKNYgdKLTVIGVGGV 247
Cdd:PRK07259  173 E---IAKAAEEAGADGLSLINTLK--GmAIDIKtrKPILANVTGGLSGPAIKPIALRMVYQVYQAV--DIPIIGMGGI 243
 
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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