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Conserved domains on  [gi|311227136|gb|ADP79991|]
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dihydroorotate oxidase [Frankia inefficax]

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

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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 ...
 6-303 3.22e-82

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 cd04741:

Pssm-ID: 473867  Cd Length: 294  Bit Score: 250.32  E-value: 3.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPAMA 84
Cdd:cd04741    5 GLTISPPLMNAAGPwCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIRTIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  85 RAAHDAGKPLILSVAGF---SVDDYARSAAAAAPTGVdLLELNLACPNVwdGGTQKRIACFDEGQTAAVLAavdavlrDA 161
Cdd:cd04741   85 DGLPGSAKPFFISVTGSaedIAAMYKKIAAHQKQFPL-AMELNLSCPNV--PGKPPPAYDFDATLEYLTAV-------KA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 162 PTRVPYGVKISPFSDPEALAGLAAVLASAVaagGGPRYVCASNTFPNGLAFDDAG-RPVIGVE--LAGLAGPALRPVALG 238
Cdd:cd04741  155 AYSIPVGVKTPPYTDPAQFDTLAEALNAFA---CPISFITATNTLGNGLVLDPEReTVVLKPKtgFGGLAGAYLHPLALG 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311227136 239 QVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWNRdgDPAVFGVIAAEWAEAL 303
Cdd:cd04741  232 NVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKE--GPKVFARIEKELEDIW 294
 
Name Accession Description Interval E-value
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-303 3.22e-82

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: 250.32  E-value: 3.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPAMA 84
Cdd:cd04741    5 GLTISPPLMNAAGPwCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIRTIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  85 RAAHDAGKPLILSVAGF---SVDDYARSAAAAAPTGVdLLELNLACPNVwdGGTQKRIACFDEGQTAAVLAavdavlrDA 161
Cdd:cd04741   85 DGLPGSAKPFFISVTGSaedIAAMYKKIAAHQKQFPL-AMELNLSCPNV--PGKPPPAYDFDATLEYLTAV-------KA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 162 PTRVPYGVKISPFSDPEALAGLAAVLASAVaagGGPRYVCASNTFPNGLAFDDAG-RPVIGVE--LAGLAGPALRPVALG 238
Cdd:cd04741  155 AYSIPVGVKTPPYTDPAQFDTLAEALNAFA---CPISFITATNTLGNGLVLDPEReTVVLKPKtgFGGLAGAYLHPLALG 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311227136 239 QVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWNRdgDPAVFGVIAAEWAEAL 303
Cdd:cd04741  232 NVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKE--GPKVFARIEKELEDIW 294
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 4-305 6.00e-57

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: 185.28  E-value: 6.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYH--AGDGFSLNALGLPNRGLAYYVEQL 80
Cdd:COG0167    6 LAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFrlPEDSGLINRMGLNNPGVDAFLERL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  81 pamaRAAHDAGKPLILSVAGFSVDDYARSAAAAAPTGVDLLELNLACPNVWDGGTQkriacFdeGQTAAVLAAVDAVLRD 160
Cdd:COG0167   86 ----LPAKRYDVPVIVNIGGNTVEDYVELARRLADAGADYLELNISCPNTPGGGRA-----L--GQDPEALAELLAAVKA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 161 ApTRVPYGVKISP-FSDPEALAGLAAVlasavaagGGPRYVCASNTFpNGLAFD-DAGRPVIGVELAGLAGPALRPVALG 238
Cdd:COG0167  155 A-TDKPVLVKLAPdLTDIVEIARAAEE--------AGADGVIAINTT-LGRAIDlETRRPVLANEAGGLSGPALKPIALR 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 239 QVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWnRDGdPAVFGVIAAEWAEALAD 305
Cdd:COG0167  225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALF-YEG-PGLVRRIIRGLEAYLEE 289
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-303 1.51e-48

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 163.78  E-value: 1.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGTC---KSLDDVQDLARsaAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQ- 79
Cdd:PRK07259   6 LPGLKLKNPVMPASGTFgfgGEYARFYDLNG--LGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIEEe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  80 LPAMAraahDAGKPLILSVAGFSVDDYARSAAAAAPTG-VDLLELNLACPNVWDGGtqkriACFdeGQTAAVLAAVDAVL 158
Cdd:PRK07259  84 LPWLE----EFDTPIIANVAGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKHGG-----MAF--GTDPELAYEVVKAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 159 RDApTRVPYGVKISPFSDpealaglAAVLASAVAAGGGPRYVCASNTFPnGLAFD-DAGRPVIGVELAGLAGPALRPVAL 237
Cdd:PRK07259 153 KEV-VKVPVIVKLTPNVT-------DIVEIAKAAEEAGADGLSLINTLK-GMAIDiKTRKPILANVTGGLSGPAIKPIAL 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 238 GQVRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATA-YWnrdgDPAVFGVIAAEWAEAL 303
Cdd:PRK07259 224 RMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTAnFY----DPYAFPKIIEGLEAYL 284
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-303 4.03e-39

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 139.02  E-value: 4.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136    4 LCGIDLEHPVMNAAGTCKSLDDVQD-LARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPA 82
Cdd:pfam01180   6 IPGLDFKNPIGLASGFDKFGEEALKwLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAELLK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   83 MARAAHDAGKPLILSVAGFSVDDYARSAAAAAPTgVDLLELNLACPNVwDGGTQKriacfdegQTAAVLAAVDAVLRDAP 162
Cdd:pfam01180  86 RRKEYPRPDLGINLSKAGMTVDDYVEVARKIGPF-ADYIELNVSCPNT-PGLRAL--------QTDPELAAILLKVVKEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  163 TRVPYGVKISP-FSDPEALAGLAAVLASAvaaggGPRYVCASNTFPNGLAFD-DAGRPVIGVELAGLAGPALRPVALGQV 240
Cdd:pfam01180 156 SKVPVLVKLAPdLTDIVIIDIADVALGED-----GLDGINATNTTVRGMRIDlKTEKPILANGTGGLSGPPIKPIALKVI 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311227136  241 RQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAywNRDGDPAVFGVIAAEWAEAL 303
Cdd:pfam01180 231 RELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTA--LIFGGPFIFPKIIDELPELL 291
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 4-286 1.33e-35

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: 130.24  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136    4 LCGIDLEHPVMNAAGTCKSLDDVQDL-ARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLpa 82
Cdd:TIGR01037   5 LFGIRFKNPLILASGIMGSGVESLRRiDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEEL-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   83 mARAAHDAGKPLILSVAGFSVDDYARSAAA--AAPTGVDLLELNLACPNVWDGGtqkriacFDEGQTAAVLAAVDAVLRD 160
Cdd:TIGR01037  83 -KPVREEFPTPLIASVYGSSVEEFAEVAEKleKAPPYVDAYELNLSCPHVKGGG-------IAIGQDPELSADVVKAVKD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  161 ApTRVPYGVKISPfsdpealAGLAAVLASAVAAGGGPRYVCASNTFpNGLAFD-DAGRPVIGVELAGLAGPALRPVALGQ 239
Cdd:TIGR01037 155 K-TDVPVFAKLSP-------NVTDITEIAKAAEEAGADGLTLINTL-RGMKIDiKTGKPILANKTGGLSGPAIKPIALRM 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 311227136  240 VRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATA-YWNRD 286
Cdd:TIGR01037 226 VYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAvYYRGF 271
 
Name Accession Description Interval E-value
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 6-303 3.22e-82

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: 250.32  E-value: 3.22e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPAMA 84
Cdd:cd04741    5 GLTISPPLMNAAGPwCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRYYAFPLGSINSLGLPNLGLDYYLEYIRTIS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  85 RAAHDAGKPLILSVAGF---SVDDYARSAAAAAPTGVdLLELNLACPNVwdGGTQKRIACFDEGQTAAVLAavdavlrDA 161
Cdd:cd04741   85 DGLPGSAKPFFISVTGSaedIAAMYKKIAAHQKQFPL-AMELNLSCPNV--PGKPPPAYDFDATLEYLTAV-------KA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 162 PTRVPYGVKISPFSDPEALAGLAAVLASAVaagGGPRYVCASNTFPNGLAFDDAG-RPVIGVE--LAGLAGPALRPVALG 238
Cdd:cd04741  155 AYSIPVGVKTPPYTDPAQFDTLAEALNAFA---CPISFITATNTLGNGLVLDPEReTVVLKPKtgFGGLAGAYLHPLALG 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311227136 239 QVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWNRdgDPAVFGVIAAEWAEAL 303
Cdd:cd04741  232 NVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKE--GPKVFARIEKELEDIW 294
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 4-305 6.00e-57

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: 185.28  E-value: 6.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYH--AGDGFSLNALGLPNRGLAYYVEQL 80
Cdd:COG0167    6 LAGLKFPNPVGLASGFfDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFrlPEDSGLINRMGLNNPGVDAFLERL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  81 pamaRAAHDAGKPLILSVAGFSVDDYARSAAAAAPTGVDLLELNLACPNVWDGGTQkriacFdeGQTAAVLAAVDAVLRD 160
Cdd:COG0167   86 ----LPAKRYDVPVIVNIGGNTVEDYVELARRLADAGADYLELNISCPNTPGGGRA-----L--GQDPEALAELLAAVKA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 161 ApTRVPYGVKISP-FSDPEALAGLAAVlasavaagGGPRYVCASNTFpNGLAFD-DAGRPVIGVELAGLAGPALRPVALG 238
Cdd:COG0167  155 A-TDKPVLVKLAPdLTDIVEIARAAEE--------AGADGVIAINTT-LGRAIDlETRRPVLANEAGGLSGPALKPIALR 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 239 QVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWnRDGdPAVFGVIAAEWAEALAD 305
Cdd:COG0167  225 MVREVAQAVGGDIPIIGVGGISTAEDALEFILAGASAVQVGTALF-YEG-PGLVRRIIRGLEAYLEE 289
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-303 1.51e-48

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 163.78  E-value: 1.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGTC---KSLDDVQDLARsaAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQ- 79
Cdd:PRK07259   6 LPGLKLKNPVMPASGTFgfgGEYARFYDLNG--LGAIVTKSTTLEPREGNPTPRIAETPGGMLNAIGLQNPGVDAFIEEe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  80 LPAMAraahDAGKPLILSVAGFSVDDYARSAAAAAPTG-VDLLELNLACPNVWDGGtqkriACFdeGQTAAVLAAVDAVL 158
Cdd:PRK07259  84 LPWLE----EFDTPIIANVAGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVKHGG-----MAF--GTDPELAYEVVKAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 159 RDApTRVPYGVKISPFSDpealaglAAVLASAVAAGGGPRYVCASNTFPnGLAFD-DAGRPVIGVELAGLAGPALRPVAL 237
Cdd:PRK07259 153 KEV-VKVPVIVKLTPNVT-------DIVEIAKAAEEAGADGLSLINTLK-GMAIDiKTRKPILANVTGGLSGPAIKPIAL 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 238 GQVRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATA-YWnrdgDPAVFGVIAAEWAEAL 303
Cdd:PRK07259 224 RMVYQVYQAV--DIPIIGMGGISSAEDAIEFIMAGASAVQVGTAnFY----DPYAFPKIIEGLEAYL 284
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 4-303 5.95e-48

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: 162.33  E-value: 5.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGTC---KSLDDVQDLarSAAAAIVVGSITVAARTGNSGAT-YHAGDGFsLNALGLPNRGLAYYV-E 78
Cdd:cd04740    4 LAGLRLKNPVILASGTFgfgEELSRVADL--GKLGAIVTKSITLEPREGNPPPRvVETPGGM-LNAIGLQNPGVEAFLeE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  79 QLPAMAraahDAGKPLILSVAGFSVDDYARSAAAAAPTGVDLLELNLACPNVWDGGTQkriacFdeGQTAAVLAAVDAVL 158
Cdd:cd04740   81 LLPWLR----EFGTPVIASIAGSTVEEFVEVAEKLADAGADAIELNISCPNVKGGGMA-----F--GTDPEAVAEIVKAV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 159 RDApTRVPYGVKISPfsdpealAGLAAVLASAVAAGGGPRYVCASNTFPnGLAFD-DAGRPVIGVELAGLAGPALRPVAL 237
Cdd:cd04740  150 KKA-TDVPVIVKLTP-------NVTDIVEIARAAEEAGADGLTLINTLK-GMAIDiETRKPILGNVTGGLSGPAIKPIAL 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311227136 238 GQVRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATAywNRDgDPAVFGVIAAEWAEAL 303
Cdd:cd04740  221 RMVYQVYKAV--EIPIIGVGGIASGEDALEFLMAGASAVQVGTA--NFV-DPEAFKEIIEGLEAYL 281
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 6-305 6.47e-48

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 162.43  E-value: 6.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPAMA 84
Cdd:PRK02506   8 GFKFDNCLMNAAGVyCMTKEELEEVEASAAGAFVTKSATLEPRPGNPEPRYADTPLGSINSMGLPNLGFDYYLDYVLELQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  85 RAahDAGKPLILSVAGFSVDD-YARSAAAAAPTGVDLLELNLACPNVwDGGTQkrIAcFDEGQTaavlaavdavlRDAPT 163
Cdd:PRK02506  88 KK--GPNKPHFLSVVGLSPEEtHTILKKIQASDFNGLVELNLSCPNV-PGKPQ--IA-YDFETT-----------EQILE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 164 RV------PYGVKISPFSDPEALAGLAAVLASAVAAgggprYVCASNTFPNGLAFD-DAGRPVI----GveLAGLAGPAL 232
Cdd:PRK02506 151 EVftyftkPLGVKLPPYFDIVHFDQAAAIFNKFPLA-----FVNCINSIGNGLVIDpEDETVVIkpknG--FGGIGGDYI 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311227136 233 RPVALGQVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWnRDGdPAVFGVIAAEWAEALAD 305
Cdd:PRK02506 224 KPTALANVRAFYQRLNPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALH-KEG-PAVFERLTKELKAIMAE 294
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 6-298 1.77e-41

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: 145.19  E-value: 1.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHPVMNAAGT-CKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYHAGDGFS---------LNALGLPNRGLAY 75
Cdd:cd02810    5 GLKLKNPFGVAAGPlLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARLPPEGesypeqlgiLNSFGLPNLGLDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  76 YVEqlpaMARAAHDA--GKPLILSVAGFSVDDYARSAAAAAPTGVDLLELNLACPNVwdggTQKRIACFDEGQTAAVLAA 153
Cdd:cd02810   85 WLQ----DIAKAKKEfpGQPLIASVGGSSKEDYVELARKIERAGAKALELNLSCPNV----GGGRQLGQDPEAVANLLKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 154 VDavlrdAPTRVPYGVKISPFSDPEALAGLAAVLAsavaaGGGPRYVCASNTFpNGLAFDDAGRPVIGVELA-GLAGPAL 232
Cdd:cd02810  157 VK-----AAVDIPLLVKLSPYFDLEDIVELAKAAE-----RAGADGLTAINTI-SGRVVDLKTVGPGPKRGTgGLSGAPI 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311227136 233 RPVALGQVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWNRdgDPAVFGVIAAE 298
Cdd:cd02810  226 RPLALRWVARLAARLQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWD--GPDVIRKIKKE 289
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-303 4.03e-39

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 139.02  E-value: 4.03e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136    4 LCGIDLEHPVMNAAGTCKSLDDVQD-LARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLPA 82
Cdd:pfam01180   6 IPGLDFKNPIGLASGFDKFGEEALKwLALGKFGAIEIKSVTPYPQPGNPTPRVFRLPEGVLNRMGLNNPGLDAVLAELLK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   83 MARAAHDAGKPLILSVAGFSVDDYARSAAAAAPTgVDLLELNLACPNVwDGGTQKriacfdegQTAAVLAAVDAVLRDAP 162
Cdd:pfam01180  86 RRKEYPRPDLGINLSKAGMTVDDYVEVARKIGPF-ADYIELNVSCPNT-PGLRAL--------QTDPELAAILLKVVKEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  163 TRVPYGVKISP-FSDPEALAGLAAVLASAvaaggGPRYVCASNTFPNGLAFD-DAGRPVIGVELAGLAGPALRPVALGQV 240
Cdd:pfam01180 156 SKVPVLVKLAPdLTDIVIIDIADVALGED-----GLDGINATNTTVRGMRIDlKTEKPILANGTGGLSGPPIKPIALKVI 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311227136  241 RQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAywNRDGDPAVFGVIAAEWAEAL 303
Cdd:pfam01180 231 RELYQRTGPEIPIIGVGGIESGEDALEKILAGASAVQIGTA--LIFGGPFIFPKIIDELPELL 291
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 4-286 1.33e-35

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: 130.24  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136    4 LCGIDLEHPVMNAAGTCKSLDDVQDL-ARSAAAAIVVGSITVAARTGNSGATYHAGDGFSLNALGLPNRGLAYYVEQLpa 82
Cdd:TIGR01037   5 LFGIRFKNPLILASGIMGSGVESLRRiDRSGAGAVVTKSIGLEPRPGYRNPTIVETPCGMLNAIGLQNPGVEAFLEEL-- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   83 mARAAHDAGKPLILSVAGFSVDDYARSAAA--AAPTGVDLLELNLACPNVWDGGtqkriacFDEGQTAAVLAAVDAVLRD 160
Cdd:TIGR01037  83 -KPVREEFPTPLIASVYGSSVEEFAEVAEKleKAPPYVDAYELNLSCPHVKGGG-------IAIGQDPELSADVVKAVKD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  161 ApTRVPYGVKISPfsdpealAGLAAVLASAVAAGGGPRYVCASNTFpNGLAFD-DAGRPVIGVELAGLAGPALRPVALGQ 239
Cdd:TIGR01037 155 K-TDVPVFAKLSP-------NVTDITEIAKAAEEAGADGLTLINTL-RGMKIDiKTGKPILANKTGGLSGPAIKPIALRM 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 311227136  240 VRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATA-YWNRD 286
Cdd:TIGR01037 226 VYDVYKMV--DIPIIGVGGITSFEDALEFLMAGASAVQVGTAvYYRGF 271
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 92-295 3.95e-20

Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. 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 the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239244  Cd Length: 299  Bit Score: 88.11  E-value: 3.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  92 KPLILSV-AGFSVDDYARSAAAAAPTGVDLLELNLACPNvwdGGTQKRI--ACfdeGQTAAVLAAVDAVLRDApTRVPYG 168
Cdd:cd02940  100 KILIASImCEYNKEDWTELAKLVEEAGADALELNFSCPH---GMPERGMgaAV---GQDPELVEEICRWVREA-VKIPVI 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 169 VKISP-FSDPEALAGLAAVlasavaagGGPRYVCASNTFPNGLAFD-DAGRPVIGVEL----AGLAGPALRPVALGQVRQ 242
Cdd:cd02940  173 AKLTPnITDIREIARAAKE--------GGADGVSAINTVNSLMGVDlDGTPPAPGVEGkttyGGYSGPAVKPIALRAVSQ 244

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311227136 243 LRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYWNRDgdpavFGVI 295
Cdd:cd02940  245 IARAPEPGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQG-----FTIV 292
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 4-281 1.24e-17

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: 81.78  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   4 LCGIDLEHPVMNAAGTCKSLDDVQDLARSAAAAIVVGSITVAARTGNSGATYhagdgFSL-------NALGLPNRGLAYY 76
Cdd:cd04738   43 VFGLTFPNPVGLAAGFDKNAEAIDALLALGFGFVEVGTVTPRPQPGNPKPRL-----FRLpedealiNRMGFNNDGADAV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  77 VEQLpamaRAAHDAGKPLILSVAGF-------SVDDYARSAAAAAPTGvDLLELNLACPNVWDGGT-QKRIAcFDEGQTa 148
Cdd:cd04738  118 AKRL----KKRRPRGGPLGVNIGKNkdtpledAVEDYVIGVRKLGPYA-DYLVVNVSSPNTPGLRDlQGKEA-LRELLT- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 149 avlaAVDAVLRDAPTRVPYGVKISPFSDPEALAGLAAVLASAVAAGggpryVCASNTfpnGLAFDDAGRPVIGVELAGLA 228
Cdd:cd04738  191 ----AVKEERNKLGKKVPLLVKIAPDLSDEELEDIADVALEHGVDG-----IIATNT---TISRPGLLRSPLANETGGLS 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 311227136 229 GPALRPVALGQVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATA 281
Cdd:cd04738  259 GAPLKERSTEVLRELYKLTGGKIPIIGVGGISSGEDAYEKIRAGASLVQLYTG 311
PLN02826 PLN02826
dihydroorotate dehydrogenase
 213-303 2.68e-09

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 57.44  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 213 DDAGRPVIGVELAGLAGPALRPVALGQVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATAYwnRDGDPAVF 292
Cdd:PLN02826 304 DSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGKIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAF--AYEGPALI 381

                         90
                 ....*....|.
gi 311227136 293 GVIAAEWAEAL 303
Cdd:PLN02826 382 PRIKAELAACL 392
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
226-281 8.55e-09

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 56.11  E-value: 8.55e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 226 GLAGPALRPVALGQVRQLRRLLP-ASVEIVGAGGVTTGRDVADFLRAGANAVQVATA 281
Cdd:PRK08318 228 GYCGPAVKPIALNMVAEIARDPEtRGLPISGIGGIETWRDAAEFILLGAGTVQVCTA 284
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 116-280 2.25e-07

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 51.76  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 116 TGVDLLELNLACPNvwdgGTQKRIACFDEGQTAAVLAAVDAVLRDAPTrVPYGVKISP----FSDPEALAGLAavlasav 191
Cdd:PLN02495 139 TGVDALEINFSCPH----GMPERKMGAAVGQDCDLLEEVCGWINAKAT-VPVWAKMTPnitdITQPARVALKS------- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 192 aaggGPRYVCASNTFPNGLAFD-DAGRPVIGVE----LAGLAGPALRPVALGQVRQLRRLL----PASVEIVGAGGVTTG 262
Cdd:PLN02495 207 ----GCEGVAAINTIMSVMGINlDTLRPEPCVEgystPGGYSSKAVRPIALAKVMAIAKMMksefPEDRSLSGIGGVETG 282

                        170
                 ....*....|....*...
gi 311227136 263 RDVADFLRAGANAVQVAT 280
Cdd:PLN02495 283 GDAAEFILLGADTVQVCT 300
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
202-281 7.73e-07

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 49.78  E-value: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 202 ASNTfpnGLAFDDAGRPVIGVELAGLAGPALRPVALGQVRQLRRLLPASVEIVGAGGVTTGRDVADFLRAGANAVQVATA 281
Cdd:PRK05286 244 ATNT---TLSRDGLKGLPNADEAGGLSGRPLFERSTEVIRRLYKELGGRLPIIGVGGIDSAEDAYEKIRAGASLVQIYSG 320
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 240-283 6.80e-04

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 40.16  E-value: 6.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 311227136 240 VRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATAYW 283
Cdd:cd04730  148 VPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMGTRFL 189
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 240-282 1.68e-03

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 39.32  E-value: 1.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 311227136 240 VRQLRRLLpaSVEIVGAGGVTTGRDVADFLRAGANAVQVATAY 282
Cdd:COG2070  150 VPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMGTRF 190
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 6-281 3.67e-03

Dihydroorotate dehydrogenase (DHOD) like proteins. 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. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.


Pssm-ID: 240090  Cd Length: 325  Bit Score: 38.36  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136   6 GIDLEHP-VMNAAGTCKSLDDVQDLARSAAAAIVVGS-----ITVAARTGNSGATYhaGDGFSLNALGLP-----NRGLA 74
Cdd:cd04739    8 GLSLKNPlVASASPLSRNLDNIRRLEDAGAGAIVLPSlfeeqIEREAQELDRFLTY--GSSFAEALSYFPeygryNLGPE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136  75 YYVEQLPAMARAAhdaGKPLILSVAGFSVD---DYARSAAAAaptGVDLLELNL----ACPNVWDGGTQKRIAcfdegqt 147
Cdd:cd04739   86 EYLELIRRAKRAV---SIPVIASLNGVSAGgwvDYARQIEEA---GADALELNIyalpTDPDISGAEVEQRYL------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311227136 148 aavlaAVDAVLRDApTRVPYGVKISPFSdpealagLAAVLASAVAAGGGPRYVCASNTFPNGlAFD-DAGRPVIGVEL-- 224
Cdd:cd04739  153 -----DILRAVKSA-VTIPVAVKLSPFF-------SALAHMAKQLDAAGADGLVLFNRFYQP-DIDlETLEVVPNLLLss 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311227136 225 AGLAGPALRPVALgqvrqLRRLLPASveIVGAGGVTTGRDVADFLRAGANAVQVATA 281
Cdd:cd04739  219 PAEIRLPLRWIAI-----LSGRVKAS--LAASGGVHDAEDVVKYLLAGADVVMTTSA 268
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 250-282 5.26e-03

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 37.88  E-value: 5.26e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 311227136  250 SVEIVGAGGVTTGRDVADFLRAGANAVQVATAY 282
Cdd:pfam03060 193 DIPVIAAGGIWDRRGVAAALALGASGVQMGTRF 225
 
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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