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Conserved domains on  [gi|976710542|gb|KVG05150|]
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2-nitropropane dioxygenase [Burkholderia vietnamiensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 26-337 5.09e-86

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


:

Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 266.59  E-value: 5.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  26 LGCAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLIPASTPRELlDAQLDACI 105
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPRF-EELLEVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 106 ELRVPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHV-RGDRPLVELLPQVVRATRL 184
Cdd:COG2070   80 EEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRgADEVSTFALVPEVRDAVDI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 185 PVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIVDARDGDTLLTDVFHinwprGARVRVLPSSVTR 264
Cdd:COG2070  160 PVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFT-----GRPARALRNSFTR 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976710542 265 ----GERGDPFGDARVVIGDEEGRpiylfstdspLRTMTGDFEAMALYAGTGVGRIRAIEPAGDVLRRIALDAAARL 337
Cdd:COG2070  235 egldLEAECLYPILEALTAGKRLR----------AAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
DUF6306 super family cl45217
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 368-482 4.33e-36

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


The actual alignment was detected with superfamily member pfam19825:

Pssm-ID: 437657  Cd Length: 129  Bit Score: 130.36  E-value: 4.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  368 RAGARVASETAAEIDDdPDLHRLIAHIRQDEAHWCSVLVDAIRTLGATPTRATGAFYQKAMAIDDLGERMAFLNRGQRWV 447
Cdd:pfam19825  15 RAGARVALKSAKAAAE-PAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFLNRGQAWV 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 976710542  448 VRRLQALLPTLANPDLHHALSLMLVAHEKNVGAVD 482
Cdd:pfam19825  94 VRKLETLTPRVRDDELHADLEAMLAAHRHNIARAA 128
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 26-337 5.09e-86

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 266.59  E-value: 5.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  26 LGCAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLIPASTPRELlDAQLDACI 105
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPRF-EELLEVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 106 ELRVPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHV-RGDRPLVELLPQVVRATRL 184
Cdd:COG2070   80 EEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRgADEVSTFALVPEVRDAVDI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 185 PVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIVDARDGDTLLTDVFHinwprGARVRVLPSSVTR 264
Cdd:COG2070  160 PVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFT-----GRPARALRNSFTR 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976710542 265 ----GERGDPFGDARVVIGDEEGRpiylfstdspLRTMTGDFEAMALYAGTGVGRIRAIEPAGDVLRRIALDAAARL 337
Cdd:COG2070  235 egldLEAECLYPILEALTAGKRLR----------AAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 28-252 4.74e-78

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: 243.93  E-value: 4.74e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  28 CAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLIPASTPrELLDAQLDACIEL 107
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSSN-PDFEALLEVALEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 108 RVPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHVRG-DRPLVELLPQVVRATRLPV 186
Cdd:cd04730   80 GVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTfDIGTFALVPEVRDAVDIPV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976710542 187 LAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIVDARDGDTLLTDVFHINWPRG 252
Cdd:cd04730  160 IAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARG 225
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 21-332 2.81e-45

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: 161.14  E-value: 2.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542   21 PVCDLLGCAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLI--------PAST 92
Cdd:pfam03060   3 LLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFlpkpdladPAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542   93 PRELL---------------DAQLDACIELRVPVVAL-FWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIV 156
Cdd:pfam03060  83 YAKILgnnalgynieegvpdYGKVLVDLDEGVNVVSFgFGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADALIV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  157 QGHEAGGHV----RGDRPLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIV 232
Cdd:pfam03060 163 QGPEAGGHQgtpeYGDKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQKIT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  233 DARDGDTLLTDVFhinwpRGARVRVLPSSVTRGERGDPFGDARVVIGDEEGRPIYLFSTDSplrtmtGDFEAMALYAGTG 312
Cdd:pfam03060 243 EAGEDDTLVTSPF-----SGRPARALANGFLEELEEPKIATLAYPEAHEMTKPIRAAAVRG------GNREEGLLWAGQG 311

                         330       340
                  ....*....|....*....|
gi 976710542  313 VGRIRAIEPAGDVLRRIALD 332
Cdd:pfam03060 312 IYRLDRIISVKELIESLTEE 331
DUF6306 pfam19825
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 368-482 4.33e-36

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


Pssm-ID: 437657  Cd Length: 129  Bit Score: 130.36  E-value: 4.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  368 RAGARVASETAAEIDDdPDLHRLIAHIRQDEAHWCSVLVDAIRTLGATPTRATGAFYQKAMAIDDLGERMAFLNRGQRWV 447
Cdd:pfam19825  15 RAGARVALKSAKAAAE-PAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFLNRGQAWV 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 976710542  448 VRRLQALLPTLANPDLHHALSLMLVAHEKNVGAVD 482
Cdd:pfam19825  94 VRKLETLTPRVRDDELHADLEAMLAAHRHNIARAA 128
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 170-215 9.61e-06

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: 46.81  E-value: 9.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 976710542  170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAF 215
Cdd:TIGR00007 176 PNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
170-214 4.00e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.67  E-value: 4.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTA 214
Cdd:PRK01130 160 PDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGA 204
 
Name Accession Description Interval E-value
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 26-337 5.09e-86

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 266.59  E-value: 5.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  26 LGCAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLIPASTPRELlDAQLDACI 105
Cdd:COG2070    1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPRF-EELLEVVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 106 ELRVPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHV-RGDRPLVELLPQVVRATRL 184
Cdd:COG2070   80 EEGVPVVSTSAGLPADLIERLKEAGIKVIPIVTSVREARKAEKAGADAVVAEGAEAGGHRgADEVSTFALVPEVRDAVDI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 185 PVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIVDARDGDTLLTDVFHinwprGARVRVLPSSVTR 264
Cdd:COG2070  160 PVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPAHEAYKQALVDAKEEDTVLTRSFT-----GRPARALRNSFTR 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976710542 265 ----GERGDPFGDARVVIGDEEGRpiylfstdspLRTMTGDFEAMALYAGTGVGRIRAIEPAGDVLRRIALDAAARL 337
Cdd:COG2070  235 egldLEAECLYPILEALTAGKRLR----------AAAAEGDLEKGLLWAGQGAGLIRDILPAAELVARLVAEAEAAL 301
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 28-252 4.74e-78

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: 243.93  E-value: 4.74e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  28 CAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLIPASTPrELLDAQLDACIEL 107
Cdd:cd04730    1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSSN-PDFEALLEVALEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 108 RVPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHVRG-DRPLVELLPQVVRATRLPV 186
Cdd:cd04730   80 GVPVVSFSFGPPAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAEAGGHRGTfDIGTFALVPEVRDAVDIPV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976710542 187 LAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIVDARDGDTLLTDVFHINWPRG 252
Cdd:cd04730  160 IAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASPAYKQALLAATAEDTVLTRAFSGRPARG 225
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 21-332 2.81e-45

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: 161.14  E-value: 2.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542   21 PVCDLLGCAWPIVLAGMGGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAATAQPFGVNLI--------PAST 92
Cdd:pfam03060   3 LLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFlpkpdladPAAN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542   93 PRELL---------------DAQLDACIELRVPVVAL-FWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIV 156
Cdd:pfam03060  83 YAKILgnnalgynieegvpdYGKVLVDLDEGVNVVSFgFGLPPNDVVFRLHFAGVALIPTISSAKEARIAEARGADALIV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  157 QGHEAGGHV----RGDRPLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESFAHPYHQQRIV 232
Cdd:pfam03060 163 QGPEAGGHQgtpeYGDKGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESGAHDAHKQKIT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  233 DARDGDTLLTDVFhinwpRGARVRVLPSSVTRGERGDPFGDARVVIGDEEGRPIYLFSTDSplrtmtGDFEAMALYAGTG 312
Cdd:pfam03060 243 EAGEDDTLVTSPF-----SGRPARALANGFLEELEEPKIATLAYPEAHEMTKPIRAAAVRG------GNREEGLLWAGQG 311

                         330       340
                  ....*....|....*....|
gi 976710542  313 VGRIRAIEPAGDVLRRIALD 332
Cdd:pfam03060 312 IYRLDRIISVKELIESLTEE 331
DUF6306 pfam19825
Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. ...
 368-482 4.33e-36

Domain of unknown function (DUF6306); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 137 and 172 amino acids in length. Protein in this family belong to the ferritin clan.


Pssm-ID: 437657  Cd Length: 129  Bit Score: 130.36  E-value: 4.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  368 RAGARVASETAAEIDDdPDLHRLIAHIRQDEAHWCSVLVDAIRTLGATPTRATGAFYQKAMAIDDLGERMAFLNRGQRWV 447
Cdd:pfam19825  15 RAGARVALKSAKAAAE-PAYAELMQDVRKDEARWCAMLSRAIRRLDGAPSRRTGAFHGKAMAIAEPWERLAFLNRGQAWV 93

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 976710542  448 VRRLQALLPTLANPDLHHALSLMLVAHEKNVGAVD 482
Cdd:pfam19825  94 VRKLETLTPRVRDDELHADLEAMLAAHRHNIARAA 128
NPD_PKS cd04743
2-Nitropropane dioxygenase (NPD)-like domain, associated with polyketide synthases (PKS). NPD ...
 30-242 1.17e-10

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: 62.53  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  30 WPIVLAGMGGVA-RAELASAVSAAGGFGFLGmvrepVALIRRE-----VERVRAATA-QPFGVNLIpASTPRELLDAQLD 102
Cdd:cd04743    3 YPIVQGPMTRVSdVAEFAVAVAEGGGLPFIA-----LALMRGEqvkalLEETAELLGdKPWGVGIL-GFVDTELRAAQLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 103 ACIELRvPVVALFWDVMPDVVRRLRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHEAGGHV--RGDRPLVELLPQVVR 180
Cdd:cd04743   77 VVRAIK-PTFALIAGGRPDQARALEAIGISTYLHVPSPGLLKQFLENGARKFIFEGRECGGHVgpRSSFVLWESAIDALL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 181 ATRLP-------VLAAGGIADGADVAAAMALGAQ--------GAVIGTAFIATHESFAH----PYHQQRIVDARDGDTLL 241
Cdd:cd04743  156 AANGPdkagkihLLFAGGIHDERSAAMVSALAAPlaergakvGVLMGTAYLFTEEAVSAgailPTFQDQAIAATRTALLE 235


                 .
gi 976710542 242 T 242
Cdd:cd04743  236 T 236
NPD_FabD cd04742
2-Nitropropane dioxygenase (NPD)-like domain, associated with the (acyl-carrier-protein) ...
 27-258 2.82e-07

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: 52.64  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  27 GCAWPIVLAGM-GGVARAELASAVSAAGGFGFLGMVREPVALIRREVERVRAAT--AQPFGVNLIPASTPRELLDAQLDA 103
Cdd:cd04742   11 GLRYAYVAGAMaRGIASAELVVAMGKAGMLGFFGAGGLPLDEVEQAIERIQAALgnGEPYGVNLIHSPDEPELEEGLVDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 104 CIELRVPVV--ALFWDVMPDVVR-------RLRDAGVRVVHQV----------------------------GSLDDAQAA 146
Cdd:cd04742   91 FLRHGVRVVeaSAFMQLTPALVRyrakglrRDADGRVQIANRIiakvsrpevaeafmspaperilkkllaeGKITEEQAE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 147 DAAG---AHALIVQGhEAGGHVRGdRPLVELLPQVVR-----------ATRLPVLAAGGIADGADVAAAMALGAQGAVIG 212
Cdd:cd04742  171 LARRvpvADDITVEA-DSGGHTDN-RPLSVLLPTIIRlrdelaarygyRRPIRVGAAGGIGTPEAAAAAFALGADFIVTG 248

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 976710542 213 TAFIATHESFAHPYHQQRIVDARDGDTLLT---DVFHInwprGARVRVL 258
Cdd:cd04742  249 SINQCTVEAGTSDAVKDLLQKAGVQDTAYApaaDMFEL----GAKVQVL 293
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 120-216 2.44e-06

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 49.36  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 120 PDVVRRLRDAGVRVVhqvgslddaqaadaagahalIVQGHeaGG-HVRGDRPLVELLPQVVRAT--RLPVLAAGGIADGA 196
Cdd:COG1304  236 PEDARRAVDAGVDGI--------------------DVSNH--GGrQLDGGPPTIDALPEIRAAVggRIPVIADGGIRRGL 293

                         90       100
                 ....*....|....*....|
gi 976710542 197 DVAAAMALGAQGAVIGTAFI 216
Cdd:COG1304  294 DVAKALALGADAVGLGRPFL 313
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 170-215 3.97e-06

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: 47.86  E-value: 3.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAF 215
Cdd:cd04732  177 PNFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKAL 222
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 170-215 9.61e-06

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: 46.81  E-value: 9.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 976710542  170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAF 215
Cdd:TIGR00007 176 PNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 172-215 1.82e-05

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 46.18  E-value: 1.82e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 976710542 172 VELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAF 215
Cdd:COG0106  178 LELYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKAL 221
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 42-213 4.00e-05

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: 44.50  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542  42 RAELASAVSAAGGFGFLGMVREPVALIRREVER-VRAATAQPFGVNL-------IPASTPRELLDAQLDAC-IELRVPVV 112
Cdd:cd04722   18 AKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKeVAAETDLPLGVQLaindaaaAVDIAAAAARAAGADGVeIHGAVGYL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976710542 113 ALFWDVMPDVVRRlRDAGVRVVHQVGSLDDAQAADAAGAHALIVQGHE---AGGHVRGDRPLVELLPQVVRATRLPVLAA 189
Cdd:cd04722   98 AREDLELIRELRE-AVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAG 176

                        170       180
                 ....*....|....*....|....
gi 976710542 190 GGIADGADVAAAMALGAQGAVIGT 213
Cdd:cd04722  177 GGINDPEDAAEALALGADGVIVGS 200
FMN_dh pfam01070
FMN-dependent dehydrogenase;
172-216 7.68e-05

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 44.83  E-value: 7.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 976710542  172 VELLPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIGTAFI 216
Cdd:pfam01070 260 IDALPEIVAAVggRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFL 306
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 173-216 2.16e-04

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 43.20  E-value: 2.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 976710542 173 ELLPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIGTAFI 216
Cdd:cd02809  215 DALPEIVAAVggRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFL 260
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 170-215 2.84e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The 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. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 42.26  E-value: 2.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAF 215
Cdd:cd04723  176 PDLELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
170-214 4.00e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.67  E-value: 4.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTA 214
Cdd:PRK01130 160 PDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGA 204
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
 172-212 4.33e-04

PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.


Pssm-ID: 240078  Cd Length: 283  Bit Score: 42.23  E-value: 4.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 976710542 172 VELLPQVVRATRLPVL--AAGGIADGADVAAAMALGAQGAVIG 212
Cdd:cd04727  183 YELVKETAKLGRLPVVnfAAGGVATPADAALMMQLGADGVFVG 225
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 172-214 4.62e-04

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 42.51  E-value: 4.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 976710542 172 VELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTA 214
Cdd:cd04736  278 IEALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRA 320
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 170-214 5.04e-04

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 41.41  E-value: 5.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTA 214
Cdd:cd04729  164 PDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 170-218 5.16e-04

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 42.14  E-value: 5.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 976710542 170 PLVELLPQVVRA-------TRLPVLAAGGIADGADVAAAMALGAQGAVIGTAFIAT 218
Cdd:cd02808  265 PTELGLARAHQAlvknglrDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIA 320
PRK04180 PRK04180
pyridoxal 5'-phosphate synthase lyase subunit PdxS;
173-212 7.29e-04

pyridoxal 5'-phosphate synthase lyase subunit PdxS;


Pssm-ID: 179769  Cd Length: 293  Bit Score: 41.66  E-value: 7.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 976710542 173 ELLPQVVRATRLPVL--AAGGIADGADVAAAMALGAQGAVIG 212
Cdd:PRK04180 193 ELVKEVAELGRLPVVnfAAGGIATPADAALMMQLGADGVFVG 234
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 154-212 9.72e-04

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448 [Multi-domain]  Cd Length: 383  Bit Score: 41.50  E-value: 9.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 976710542 154 LIVQGHeAGGHVRGDRPLVELLPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIG 212
Cdd:cd03332  278 VVVSNH-GGRQVDGSIAALDALPEIVEAVgdRLTVLFDSGVRTGADIMKALALGAKAVLIG 337
PLN02535 PLN02535
glycolate oxidase
 172-216 1.58e-03

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 40.59  E-value: 1.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 976710542 172 VELLPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIGTAFI 216
Cdd:PLN02535 265 ISVLEEVVQAVggRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 170-217 2.28e-03

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 39.56  E-value: 2.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMAL---GAQGAVIGTAFIA 217
Cdd:PRK14024 177 PNLELLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKALYA 227
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 172-215 2.42e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 39.66  E-value: 2.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 976710542 172 VELLPQVVRATRLPVLAAGGIADGADVAAAMALGA-QGAVIGTAF 215
Cdd:PRK00748 179 VEATRELAAAVPIPVIASGGVSSLDDIKALKGLGAvEGVIVGRAL 223
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 178-214 2.64e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 39.51  E-value: 2.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 976710542 178 VVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTA 214
Cdd:PRK13585 188 LVDSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSA 224
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 170-222 3.16e-03

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 39.04  E-value: 3.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 976710542 170 PLVELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAfiATHESF 222
Cdd:PRK13587 179 PNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA--AHQASF 229
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 177-233 4.58e-03

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: 39.07  E-value: 4.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 976710542 177 QVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAfiatheSFAHPYHQQRIVD 233
Cdd:cd04740  225 QVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTA------NFVDPEAFKEIIE 275
lldD PRK11197
L-lactate dehydrogenase; Provisional
 175-216 5.29e-03

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 39.24  E-value: 5.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 976710542 175 LPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIGTAFI 216
Cdd:PRK11197 290 LPAIADAVkgDITILADSGIRNGLDVVRMIALGADTVLLGRAFV 333
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 173-237 6.80e-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: 38.23  E-value: 6.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 976710542 173 ELLPQVVRATRLPVLAAGGIADGADVAAAMALGAQGAVIGTAFIATHESF---AHPYHQQRIV---DARDG 237
Cdd:cd04732   63 ELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVkelLKEYGGERIVvglDAKDG 133
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 172-212 9.47e-03

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 38.17  E-value: 9.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 976710542 172 VELLPQVVRAT--RLPVLAAGGIADGADVAAAMALGAQGAVIG 212
Cdd:PLN02493 266 ISALEEVVKATqgRIPVFLDGGVRRGTDVFKALALGASGIFIG 308
 
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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