NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|518606586|ref|WP_019776793|]
View 

enoyl-[acyl-carrier-protein] reductase FabK [Streptococcus sobrinus]

Protein Classification

nitronate monooxygenase( domain architecture ID 11496426)

nitronate monooxygenase is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and nitroalkanes to the corresponding carbonyl compounds and nitrite

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
enACPred_II TIGR03151
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ...
 2-310 2.41e-165

putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.


:

Pssm-ID: 132195  Cd Length: 307  Bit Score: 462.30  E-value: 2.41e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586    2 KTRITELLNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLSPFADDIV 81
Cdd:TIGR03151   1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIMLLSPFVDELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   82 DLVIEEGVKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGKLTTMTLVRQVVDAI 161
Cdd:TIGR03151  81 DLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMESGGHIGELTTMALVPQVVDAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  162 DIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAIKNKLSSAYA 241
Cdd:TIGR03151 161 SIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKECNVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKNKLTRKYQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518606586  242 QAEKdfltGKLKKEEIEELGAGALRNAVVDGDVQNGSVMAGQIAGLVRKEETCEEILKDLYYGAAKVIE 310
Cdd:TIGR03151 241 ELEK----EGASPEEFEKLGAGALRRAVVEGDVENGSVMAGQIAGLIKEIKPAKEIIEDIMSEAKEVIK 305
 
Name Accession Description Interval E-value
enACPred_II TIGR03151
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ...
 2-310 2.41e-165

putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.


Pssm-ID: 132195  Cd Length: 307  Bit Score: 462.30  E-value: 2.41e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586    2 KTRITELLNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLSPFADDIV 81
Cdd:TIGR03151   1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIMLLSPFVDELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   82 DLVIEEGVKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGKLTTMTLVRQVVDAI 161
Cdd:TIGR03151  81 DLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMESGGHIGELTTMALVPQVVDAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  162 DIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAIKNKLSSAYA 241
Cdd:TIGR03151 161 SIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKECNVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKNKLTRKYQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518606586  242 QAEKdfltGKLKKEEIEELGAGALRNAVVDGDVQNGSVMAGQIAGLVRKEETCEEILKDLYYGAAKVIE 310
Cdd:TIGR03151 241 ELEK----EGASPEEFEKLGAGALRRAVVEGDVENGSVMAGQIAGLIKEIKPAKEIIEDIMSEAKEVIK 305
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 9-310 1.10e-119

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 346.33  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   9 LNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLS--PFADDIVDLVIE 86
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPanPRFEELLEVVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  87 EGVKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGK--LTTMTLVRQVVDAIDIP 164
Cdd:COG2070   81 EGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGAdeVSTFALVPEVRDAVDIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 165 VVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAIKNKLSSAYAQAE 244
Cdd:COG2070  161 VIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518606586 245 KdfltgKLKKEEIEELGAGA-LRNAVVDGDVQNGSVMAGQIAGLVRKEETCEEILKDLYYGAAKVIE 310
Cdd:COG2070  241 A-----ECLYPILEALTAGKrLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAALA 302
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 11-232 9.74e-88

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: 262.80  E-value: 9.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  11 IKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLS--PFADDIVDLVIEEG 88
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSsnPDFEALLEVALEEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  89 VKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIG--KLTTMTLVRQVVDAIDIPVV 166
Cdd:cd04730   81 VPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGtfDIGTFALVPEVRDAVDIPVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518606586 167 GAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAI 232
Cdd:cd04730  161 AAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARGL 226
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 2-301 6.48e-65

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: 207.75  E-value: 6.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586    2 KTRITELLNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLSPFADDI- 80
Cdd:pfam03060   1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   81 -------------------------VDLVIEEGVKVVTTGAGNPGKYME-RFHDAGITVIPVVPSVALAKRMEKLGADAV 134
Cdd:pfam03060  81 anyakilgnnalgynieegvpdygkVLVDLDEGVNVVSFGFGLPPNDVVfRLHFAGVALIPTISSAKEARIAEARGADAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  135 IAEGMEAGGHIGKLT-----TMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDK 209
Cdd:pfam03060 161 IVQGPEAGGHQGTPEygdkgLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  210 LLKAKDIDTVVSANVVGHPVRAIKNKLSSAYAQAEKDFLTgklKKEEIEElgAGALRNAVVD-GDVQNGSVMAGQIAGLV 288
Cdd:pfam03060 241 ITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLA---YPEAHEM--TKPIRAAAVRgGNREEGLLWAGQGIYRL 315

                         330
                  ....*....|...
gi 518606586  289 RKEETCEEILKDL 301
Cdd:pfam03060 316 DRIISVKELIESL 328
PRK07259 PRK07259
dihydroorotate dehydrogenase;
49-192 8.95e-07

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 49.76  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  49 EVVKAnidkVKSITDKPFgvnIMLLSPFADDIVDLvieeGVKVVTTGAgnpgkymerfhdAGITVIPVVPSVA------- 121
Cdd:PRK07259 147 EVVKA----VKEVVKVPV---IVKLTPNVTDIVEI----AKAAEEAGA------------DGLSLINTLKGMAidiktrk 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518606586 122 --LAKRMEKLGADAV--IAEGMeagghigklttmtlVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:PRK07259 204 piLANVTGGLSGPAIkpIALRM--------------VYQVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGT 264
 
Name Accession Description Interval E-value
enACPred_II TIGR03151
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ...
 2-310 2.41e-165

putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.


Pssm-ID: 132195  Cd Length: 307  Bit Score: 462.30  E-value: 2.41e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586    2 KTRITELLNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLSPFADDIV 81
Cdd:TIGR03151   1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIMLLSPFVDELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   82 DLVIEEGVKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGKLTTMTLVRQVVDAI 161
Cdd:TIGR03151  81 DLVIEEKVPVVTTGAGNPGKYIPRLKENGVKVIPVVASVALAKRMEKAGADAVIAEGMESGGHIGELTTMALVPQVVDAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  162 DIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAIKNKLSSAYA 241
Cdd:TIGR03151 161 SIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFLCAKECNVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKNKLTRKYQ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518606586  242 QAEKdfltGKLKKEEIEELGAGALRNAVVDGDVQNGSVMAGQIAGLVRKEETCEEILKDLYYGAAKVIE 310
Cdd:TIGR03151 241 ELEK----EGASPEEFEKLGAGALRRAVVEGDVENGSVMAGQIAGLIKEIKPAKEIIEDIMSEAKEVIK 305
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 9-310 1.10e-119

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 346.33  E-value: 1.10e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   9 LNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLS--PFADDIVDLVIE 86
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPanPRFEELLEVVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  87 EGVKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGK--LTTMTLVRQVVDAIDIP 164
Cdd:COG2070   81 EGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRGAdeVSTFALVPEVRDAVDIP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 165 VVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAIKNKLSSAYAQAE 244
Cdd:COG2070  161 VIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLE 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518606586 245 KdfltgKLKKEEIEELGAGA-LRNAVVDGDVQNGSVMAGQIAGLVRKEETCEEILKDLYYGAAKVIE 310
Cdd:COG2070  241 A-----ECLYPILEALTAGKrLRAAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAALA 302
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 11-232 9.74e-88

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: 262.80  E-value: 9.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  11 IKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLS--PFADDIVDLVIEEG 88
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSsnPDFEALLEVALEEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  89 VKVVTTGAGNPGKYMERFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIG--KLTTMTLVRQVVDAIDIPVV 166
Cdd:cd04730   81 VPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGtfDIGTFALVPEVRDAVDIPVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518606586 167 GAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDKLLKAKDIDTVVSANVVGHPVRAI 232
Cdd:cd04730  161 AAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARGL 226
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 2-301 6.48e-65

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: 207.75  E-value: 6.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586    2 KTRITELLNIKYPIFQGGMAWVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSITDKPFGVNIMLLSPFADDI- 80
Cdd:pfam03060   1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPKPDLADPa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   81 -------------------------VDLVIEEGVKVVTTGAGNPGKYME-RFHDAGITVIPVVPSVALAKRMEKLGADAV 134
Cdd:pfam03060  81 anyakilgnnalgynieegvpdygkVLVDLDEGVNVVSFGFGLPPNDVVfRLHFAGVALIPTISSAKEARIAEARGADAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  135 IAEGMEAGGHIGKLT-----TMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRFVVAKESNAHQNFKDK 209
Cdd:pfam03060 161 IVQGPEAGGHQGTPEygdkgLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  210 LLKAKDIDTVVSANVVGHPVRAIKNKLSSAYAQAEKDFLTgklKKEEIEElgAGALRNAVVD-GDVQNGSVMAGQIAGLV 288
Cdd:pfam03060 241 ITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLA---YPEAHEM--TKPIRAAAVRgGNREEGLLWAGQGIYRL 315

                         330
                  ....*....|...
gi 518606586  289 RKEETCEEILKDL 301
Cdd:pfam03060 316 DRIISVKELIESL 328
NPD_PKS cd04743
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD ...
 12-268 5.03e-14

2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members 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: 240094  Cd Length: 320  Bit Score: 71.39  E-value: 5.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  12 KYPIFQGGMAWVAD-GDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKS-ITDKPFGVNIMLLSPFA--DDIVDLVIEE 87
Cdd:cd04743    2 RYPIVQGPMTRVSDvAEFAVAVAEGGGLPFIALALMRGEQVKALLEETAElLGDKPWGVGILGFVDTElrAAQLAVVRAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  88 GVKVVTTGAGNPGKYMErFHDAGITVIPVVPSVALAKRMEKLGADAVIAEGMEAGGHIGKLTTMTLVRQVVDA------- 160
Cdd:cd04743   82 KPTFALIAGGRPDQARA-LEAIGISTYLHVPSPGLLKQFLENGARKFIFEGRECGGHVGPRSSFVLWESAIDAllaangp 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 161 ---IDIPVVGAGGVADGNGAAAVFMLGAE--------AIQVGTRFVVAKESNAH----QNFKDKLLKAKDIDTVVSANvv 225
Cdd:cd04743  161 dkaGKIHLLFAGGIHDERSAAMVSALAAPlaergakvGVLMGTAYLFTEEAVSAgailPTFQDQAIAATRTALLETGP-- 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 518606586 226 GHPVRAIKNKLSSAYAQAEKDFL----TGKLKKEEIEELGAGALRNA 268
Cdd:cd04743  239 GHATRCVVSPFVDEFRATRRRMAregvSGEEIKERLEALNVGRLRLA 285
PRK07259 PRK07259
dihydroorotate dehydrogenase;
49-192 8.95e-07

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 49.76  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  49 EVVKAnidkVKSITDKPFgvnIMLLSPFADDIVDLvieeGVKVVTTGAgnpgkymerfhdAGITVIPVVPSVA------- 121
Cdd:PRK07259 147 EVVKA----VKEVVKVPV---IVKLTPNVTDIVEI----AKAAEEAGA------------DGLSLINTLKGMAidiktrk 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518606586 122 --LAKRMEKLGADAV--IAEGMeagghigklttmtlVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:PRK07259 204 piLANVTGGLSGPAIkpIALRM--------------VYQVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGT 264
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 49-192 1.67e-06

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: 48.70  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  49 EVVKANIDKVKSITDKPFGVNimlLSPFADDIVDL--VIEEGvkvvttGAgnpgkymerfhDaGITVIPVVPSVALAKRM 126
Cdd:cd04740  140 EAVAEIVKAVKKATDVPVIVK---LTPNVTDIVEIarAAEEA------GA-----------D-GLTLINTLKGMAIDIET 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518606586 127 EKlgadAVIAEGMeaGGHIG---KLTTMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:cd04740  199 RK----PILGNVT--GGLSGpaiKPIALRMVYQVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGT 261
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 120-192 1.76e-06

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: 48.53  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 120 VALAKRMEKLGADAVIA-----------------EGMEAGGHIGK-LTTMTL--VRQVVDA--IDIPVVGAGGVADGNGA 177
Cdd:COG0167  172 VEIARAAEEAGADGVIAinttlgraidletrrpvLANEAGGLSGPaLKPIALrmVREVAQAvgGDIPIIGVGGISTAEDA 251

                         90
                 ....*....|....*
gi 518606586 178 AAVFMLGAEAIQVGT 192
Cdd:COG0167  252 LEFILAGASAVQVGT 266
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 47-192 2.93e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 47.20  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  47 PKEVVKANIDKVKSITDKPFGVNIMLLSP--FADDIVDLVIEEGVKVVTTGAGNPGKY----------MERFHDAGITVI 114
Cdd:cd04722   41 AETDDKEVLKEVAAETDLPLGVQLAINDAaaAVDIAAAAARAAGADGVEIHGAVGYLAredlelirelREAVPDVKVVVK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 115 PVVPSVALAKRMEKLGADAVIAEGMEAGGHIGKL--TTMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:cd04722  121 LSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAvpIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 49-192 2.41e-04

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: 42.03  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586   49 EVVKAnidkVKSITDKPFGVNimlLSPFADDIVDL--VIEEGvkvvttGAGnpgkymerfhdaGITVIPVVPSVALAKRM 126
Cdd:TIGR01037 147 DVVKA----VKDKTDVPVFAK---LSPNVTDITEIakAAEEA------GAD------------GLTLINTLRGMKIDIKT 201

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518606586  127 EKlgadAVIAEgmEAGGHIG---KLTTMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:TIGR01037 202 GK----PILAN--KTGGLSGpaiKPIALRMVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGT 264
NPD_FabD cd04742
2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) ...
 10-218 1.04e-03

2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) S-malonyltransferase FabD. NPD is part of the nitroalkaneoxidizing enzyme family, that catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDPs are members 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: 240093  Cd Length: 418  Bit Score: 40.31  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  10 NIKYPIFQGGMA-WVADGDLAGAVSNAGGLGIIGGGNAPKEVVKANIDKVKSIT--DKPFGVNiMLLSPFADD----IVD 82
Cdd:cd04742   11 GLRYAYVAGAMArGIASAELVVAMGKAGMLGFFGAGGLPLDEVEQAIERIQAALgnGEPYGVN-LIHSPDEPEleegLVD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  83 LVIEEGVKVVTTGAgnpgkYME------RFHDAGIT------------VIPVV--PSVALA-------KRMEKLGADAVI 135
Cdd:cd04742   90 LFLRHGVRVVEASA-----FMQltpalvRYRAKGLRrdadgrvqianrIIAKVsrPEVAEAfmspapeRILKKLLAEGKI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 136 AEG---------------MEA--GGHI--GKLTT-MTLVRQVVDAI--------DIPVVGAGGVADGNGAAAVFMLGAEA 187
Cdd:cd04742  165 TEEqaelarrvpvadditVEAdsGGHTdnRPLSVlLPTIIRLRDELaarygyrrPIRVGAAGGIGTPEAAAAAFALGADF 244

                        250       260       270
                 ....*....|....*....|....*....|.
gi 518606586 188 IQVGTRFVVAKESNAHQNFKDKLLKAKDIDT 218
Cdd:cd04742  245 IVTGSINQCTVEAGTSDAVKDLLQKAGVQDT 275
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 120-192 1.16e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 39.89  E-value: 1.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518606586 120 VALAKRMEKLGADA-----VIAEGMEAGGHIGKlttmtlVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:PRK13585 152 VEAAKRFEELGAGSilftnVDVEGLLEGVNTEP------VKELVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGS 223
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 120-194 3.11e-03

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 38.23  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586  120 VALAKRMEKLGADAVI-----AEGMEAGGHIgklttmTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRF 194
Cdd:pfam00977 149 VEWAKELEELGAGEILltdidRDGTLSGPDL------ELTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 120-192 4.29e-03

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 37.95  E-value: 4.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518606586  120 VALAKRMEKLGADAVI-----AEGMEAGghigklTTMTLVRQVVDAIDIPVVGAGGVADGNGAAAVFMLGAEAIQVGT 192
Cdd:TIGR00007 148 EELAKRLEELGLEGIIytdisRDGTLSG------PNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGK 219
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 162-194 5.18e-03

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: 38.07  E-value: 5.18e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 518606586 162 DIPVVGAGGVADGNGAAAVFMLGAEAIQVGTRF 194
Cdd:cd04741  243 EIQIIGVGGVLDGRGAFRMRLAGASAVQVGTAL 275
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 119-180 5.27e-03

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 37.94  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518606586 119 SVALAKRMEKLGADAV-IAEG-------MEAGGHIGKLTTMTLVRQVVDAIDIPVVGAGGVADGNGAAAV 180
Cdd:cd02803  230 AIEIAKALEEAGVDALhVSGGsyespppIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEI 299
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 117-173 5.48e-03

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 37.84  E-value: 5.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518606586 117 VPSVALAKRMEKLGADAVI-----AEGMEAGGHIGklttmtLVRQVVDAIDIPVVGAGGVAD 173
Cdd:cd04732  146 VSLEELAKRFEELGVKAIIytdisRDGTLSGPNFE------LYKELAAATGIPVIASGGVSS 201
 
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