NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446610776|ref|WP_000688122|]
View 

MULTISPECIES: GMP reductase [Staphylococcus]

Protein Classification

guanosine monophosphate reductase( domain architecture ID 11481014)

Guanosine monophosphate reductase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-325 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


:

Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 719.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   1 MKIFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHM 80
Cdd:PRK05458   2 MKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKDM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  81 QNSGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAG 160
Cdd:PRK05458  82 HEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 161 ADATKVGIGPGRVCITKIKTGFGTGGWQLAALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPG 240
Cdd:PRK05458 162 ADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 241 ETVELDGKQYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSIF 320
Cdd:PRK05458 242 KTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSIF 321


                 ....*
gi 446610776 321 NGDRD 325
Cdd:PRK05458 322 NGDKI 326
 
Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-325 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 719.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   1 MKIFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHM 80
Cdd:PRK05458   2 MKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKDM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  81 QNSGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAG 160
Cdd:PRK05458  82 HEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 161 ADATKVGIGPGRVCITKIKTGFGTGGWQLAALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPG 240
Cdd:PRK05458 162 ADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 241 ETVELDGKQYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSIF 320
Cdd:PRK05458 242 KTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSIF 321


                 ....*
gi 446610776 321 NGDRD 325
Cdd:PRK05458 322 NGDKI 326
GMP_reduct_2 TIGR01306
guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP ...
 3-323 0e+00

guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP reductase. The other (TIGR01305) is found in eukaryotic and some proteobacterial lineages, including E. coli, while this family is found in a variety of bacterial lineages. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 130373  Cd Length: 321  Bit Score: 656.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776    3 IFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHMQN 82
Cdd:TIGR01306   1 VFDYEDIQLIPNKCIVNSRSECDTSVTLGKHKFKLPVVPANMQTIIDEKLAEQLAENGYFYIMHRFDEESRIPFIKDMQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   83 SGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGAD 162
Cdd:TIGR01306  81 RGLFASISVGVKACEYEFVTQLAEEALTPEYITIDIAHGHSNSVINMIKHIKTHLPDSFVIAGNVGTPEAVRELENAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  163 ATKVGIGPGRVCITKIKTGFGTGGWQLAALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGET 242
Cdd:TIGR01306 161 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHEESPGET 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  243 VELDGKQYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSIFNG 322
Cdd:TIGR01306 241 VEKDGKLYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLSDTLIEMQQDLQSSISYAGGKDLDSLRTVDYVIVKNSIFNG 320


                  .
gi 446610776  323 D 323
Cdd:TIGR01306 321 D 321
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 4-316 3.35e-115

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 336.03  E-value: 3.35e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   4 FDYEDIQLIPNKCIVEsRSECDTTIQFGPK-KFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRF----DEEARIPFIK 78
Cdd:cd00381    2 LTFDDVLLVPGYSTVL-PSEVDLSTKLTKNiTLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNmsieEQAEEVRKVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  79 hmqnSGLFASISVGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELEN 158
Cdd:cd00381   81 ----GRLLVGAAVGTREDDKERAEALVEAGV--DVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLID 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 159 AGADATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAH 235
Cdd:cd00381  155 AGADGVKVGIGPGSICTTRIVTGVGVP--QATAVADVAAAARDygvPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 236 EESPGETVELDGKQYKEYFGSASEFQKGEH------------KNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKD 303
Cdd:cd00381  233 DESPGEYIEINGKRYKEYRGMGSLGAMKKGggdryfgeeakkLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKS 312

                        330
                 ....*....|...
gi 446610776 304 LKSLRTVDYVIVR 316
Cdd:cd00381  313 LKELQEKARFVRI 325
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 2-319 6.87e-98

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 292.11  E-value: 6.87e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   2 KIFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHMQ 81
Cdd:COG0516    1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  82 NSGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSviNMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGA 161
Cdd:COG0516   81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 162 DATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK--PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESP 239
Cdd:COG0516  159 DLTKVGIGPGSICTTRVVIGLGIP--QLSAAMDTVTEARMaiAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 240 GETVELDGKQYKEYFGSASefqKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSI 319
Cdd:COG0516  237 GEVILYQGRSVKRYRGMGS---DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRITSA 313
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 91-309 3.66e-72

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 230.35  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   91 VGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGADATKVGIGP 170
Cdd:pfam00478 215 VGVGDDTLERAEALVEAGV--DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGP 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  171 GRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGETVELDG 247
Cdd:pfam00478 293 GSICTTRVVAGVGVP--QLTAIYDVAEAAKKygvPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQG 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446610776  248 KQYKEYFGSASE-----------FQKGEHKN-----VEGKkmfVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRT 309
Cdd:pfam00478 371 RRYKSYRGMGSLgamkkgskdryFQEDDDKKlvpegVEGR---VPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE 445
 
Name Accession Description Interval E-value
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 1-325 0e+00

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 719.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   1 MKIFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHM 80
Cdd:PRK05458   2 MKVFDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFKLPVVPANMQTIIDEKIAEWLAENGYFYIMHRFDPEARIPFIKDM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  81 QNSGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAG 160
Cdd:PRK05458  82 HEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 161 ADATKVGIGPGRVCITKIKTGFGTGGWQLAALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPG 240
Cdd:PRK05458 162 ADATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 241 ETVELDGKQYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSIF 320
Cdd:PRK05458 242 KTVEIDGKLYKEYFGSASEFQKGEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRKVDYVIVKNSIF 321


                 ....*
gi 446610776 321 NGDRD 325
Cdd:PRK05458 322 NGDKI 326
GMP_reduct_2 TIGR01306
guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP ...
 3-323 0e+00

guanosine monophosphate reductase, bacterial; A deep split separates two families of GMP reductase. The other (TIGR01305) is found in eukaryotic and some proteobacterial lineages, including E. coli, while this family is found in a variety of bacterial lineages. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 130373  Cd Length: 321  Bit Score: 656.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776    3 IFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHMQN 82
Cdd:TIGR01306   1 VFDYEDIQLIPNKCIVNSRSECDTSVTLGKHKFKLPVVPANMQTIIDEKLAEQLAENGYFYIMHRFDEESRIPFIKDMQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   83 SGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGAD 162
Cdd:TIGR01306  81 RGLFASISVGVKACEYEFVTQLAEEALTPEYITIDIAHGHSNSVINMIKHIKTHLPDSFVIAGNVGTPEAVRELENAGAD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  163 ATKVGIGPGRVCITKIKTGFGTGGWQLAALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGET 242
Cdd:TIGR01306 161 ATKVGIGPGKVCITKIKTGFGTGGWQLAALRWCAKAARKPIIADGGIRTHGDIAKSIRFGASMVMIGSLFAGHEESPGET 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  243 VELDGKQYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSIFNG 322
Cdd:TIGR01306 241 VEKDGKLYKEYFGSASEFQKGEHKNVEGKKMFVEHKGSLSDTLIEMQQDLQSSISYAGGKDLDSLRTVDYVIVKNSIFNG 320


                  .
gi 446610776  323 D 323
Cdd:TIGR01306 321 D 321
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 4-316 3.35e-115

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 336.03  E-value: 3.35e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   4 FDYEDIQLIPNKCIVEsRSECDTTIQFGPK-KFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRF----DEEARIPFIK 78
Cdd:cd00381    2 LTFDDVLLVPGYSTVL-PSEVDLSTKLTKNiTLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNmsieEQAEEVRKVK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  79 hmqnSGLFASISVGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELEN 158
Cdd:cd00381   81 ----GRLLVGAAVGTREDDKERAEALVEAGV--DVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLID 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 159 AGADATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAH 235
Cdd:cd00381  155 AGADGVKVGIGPGSICTTRIVTGVGVP--QATAVADVAAAARDygvPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGT 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 236 EESPGETVELDGKQYKEYFGSASEFQKGEH------------KNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKD 303
Cdd:cd00381  233 DESPGEYIEINGKRYKEYRGMGSLGAMKKGggdryfgeeakkLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKS 312

                        330
                 ....*....|...
gi 446610776 304 LKSLRTVDYVIVR 316
Cdd:cd00381  313 LKELQEKARFVRI 325
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 2-319 6.87e-98

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 292.11  E-value: 6.87e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   2 KIFDYEDIQLIPNKCIVESRSECDTTIQFGPKKFKLPVVPANMQTVMNEKLAKWFAENDYFYIMHRFDEEARIPFIKHMQ 81
Cdd:COG0516    1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  82 NSGLFASISVGVKKAEFDFIEKLAQEKLIPEYITIDIAHGHSDSviNMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGA 161
Cdd:COG0516   81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 162 DATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK--PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESP 239
Cdd:COG0516  159 DLTKVGIGPGSICTTRVVIGLGIP--QLSAAMDTVTEARMaiAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQP 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 240 GETVELDGKQYKEYFGSASefqKGEHKNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRTVDYVIVRNSI 319
Cdd:COG0516  237 GEVILYQGRSVKRYRGMGS---DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRITSA 313
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 91-309 3.66e-72

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 230.35  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   91 VGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGADATKVGIGP 170
Cdd:pfam00478 215 VGVGDDTLERAEALVEAGV--DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGP 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  171 GRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGETVELDG 247
Cdd:pfam00478 293 GSICTTRVVAGVGVP--QLTAIYDVAEAAKKygvPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQG 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446610776  248 KQYKEYFGSASE-----------FQKGEHKN-----VEGKkmfVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLRT 309
Cdd:pfam00478 371 RRYKSYRGMGSLgamkkgskdryFQEDDDKKlvpegVEGR---VPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE 445
PRK05096 PRK05096
guanosine 5'-monophosphate oxidoreductase; Provisional
 5-321 7.76e-57

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235343 [Multi-domain]  Cd Length: 346  Bit Score: 187.46  E-value: 7.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   5 DYEDIQLIPNKCIVESRSECDTTIQFgpkKFK--------LPVVPANMQTVMNEKLAKWFAENDYFYIMHRF-DEEARIP 75
Cdd:PRK05096  10 GFKDVLIRPKRSTLKSRSDVELERQF---TFKhsgqswsgVPIIAANMDTVGTFEMAKALASFDILTAVHKHySVEEWAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  76 FIKHMQNSGL-FASISVGVKKAEFDFIEK-LAQEKLIpEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGV 153
Cdd:PRK05096  87 FVNNSSADVLkHVMVSTGTSDADFEKTKQiLALSPAL-NFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVTGEMV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 154 RELENAGADATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGS 230
Cdd:PRK05096 166 EELILSGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAVIECADAAHGlggQIVSDGGCTVPGDVAKAFGGGADFVMLGG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 231 LFAAHEESPGETVELDGKQYKEYFGSASEFQKGEH-------KNVEGKKMFVEHKGSLMDTLKEMQQDLQSSISYAGGKD 303
Cdd:PRK05096 244 MLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHvggvaeyRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASR 323

                        330       340
                 ....*....|....*....|...
gi 446610776 304 LKSL--RTVdYVIV---RNSIFN 321
Cdd:PRK05096 324 LKELtkRTT-FIRVqeqENRVFN 345
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
 81-309 1.43e-53

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 181.78  E-value: 1.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776   81 QNSGLFASISVGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAG 160
Cdd:TIGR01302 209 ENGRLIVGAAVGTREFDKERAEALVKAGV--DVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAG 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  161 ADATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEE 237
Cdd:TIGR01302 287 ADGLRVGIGPGSICTTRIVAGVGVP--QITAVYDVAEYAAQsgiPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTE 364

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  238 SPGETVELDGKQYKEY----------FGSASEFQKGEHKN-------VEGKkmfVEHKGSLMDTLKEMQQDLQSSISYAG 300
Cdd:TIGR01302 365 SPGEYEIINGRRYKQYrgmgslgamtKGSSDRYLQDENKTkkfvpegVEGA---VPYKGSVLELLPQLVGGLKSGMGYVG 441


                  ....*....
gi 446610776  301 GKDLKSLRT 309
Cdd:TIGR01302 442 ARSIDELRE 450
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 81-312 1.38e-46

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 163.99  E-value: 1.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  81 QNSGLFASISVGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAG 160
Cdd:PTZ00314 226 SNGQLLVGAAISTRPEDIERAAALIEAGV--DVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAG 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 161 ADATKVGIGPGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEE 237
Cdd:PTZ00314 304 ADGLRIGMGSGSICITQEVCAVGRP--QASAVYHVARYARErgvPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEE 381

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 238 SPGETVELDGKQYKEYFGSAS---EFQKGEHKN-------------VEGkkmFVEHKGSLMDTLKEMQQDLQSSISYAGG 301
Cdd:PTZ00314 382 APGEYFFKDGVRLKVYRGMGSleaMLSKESGERyldenetikvaqgVSG---SVVDKGSVAKLIPYLVKGVKHGMQYIGA 458

                        250
                 ....*....|.
gi 446610776 302 KDLKSLRTVDY 312
Cdd:PTZ00314 459 HSIPELHEKLY 469
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 43-308 3.70e-45

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 158.66  E-value: 3.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  43 NMQTVMNEKLAKWFAENDYFY---IMHRFDEEARIPFIKHMQNSGLFASISVGVKKAEFDFIEKLAQEKLipEYITIDIA 119
Cdd:PRK06843  97 NTNGDTNEQKPEIFTAKQHLEksdAYKNAEHKEDFPNACKDLNNKLRVGAAVSIDIDTIERVEELVKAHV--DILVIDSA 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 120 HGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGADATKVGIGPGRVCITKIKTGFGTGgwQLAAL------- 192
Cdd:PRK06843 175 HGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVP--QITAIcdvyevc 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 193 ---NICskaarkpLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGETVELDGKQYKEY--FGSASEFQKGEH-- 265
Cdd:PRK06843 253 kntNIC-------IIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYvgMGSISAMKRGSKsr 325

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446610776 266 ----KNVEGKKM-------FVEHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLR 308
Cdd:PRK06843 326 yfqlENNEPKKLvpegiegMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLK 379
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
114-308 8.49e-39

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 142.74  E-value: 8.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 114 ITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGADATKVGIGPGRVCITKIKTGFGTGgwQLAALN 193
Cdd:PRK07807 243 LVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRP--QFSAVL 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 194 ICSKAAR---KPLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGET-VELDGKQYKEYFGSASE---------- 259
Cdd:PRK07807 321 ECAAAARelgAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASAravaartagd 400

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 260 ----------FQKGehknVEGKKMFV-EHKGSLMDTLKEMQQDLQSSISYAGGKDLKSLR 308
Cdd:PRK07807 401 safdrarkalFEEG----ISTSRMYLdPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFH 456
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 90-299 1.95e-30

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 120.16  E-value: 1.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  90 SVGVKKAEFDFIEKLAQEKLipEYITIDIAHGHSDSVINMIKHIKNHIPDSFVIAGNVGTPEGVRELENAGADATKVGIG 169
Cdd:PLN02274 242 AIGTRESDKERLEHLVKAGV--DVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMG 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 170 PGRVCITKIKTGFGTGgwQLAALNICSKAARK---PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGETVELD 246
Cdd:PLN02274 320 SGSICTTQEVCAVGRG--QATAVYKVASIAAQhgvPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQD 397

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446610776 247 GKQYKEY--FGSASEFQKGEH----------KNVEGKKMFVEHKGS-------LMDTLKEMQQDL-QSSISYA 299
Cdd:PLN02274 398 GVRVKKYrgMGSLEAMTKGSDqrylgdtaklKIAQGVSGAVADKGSvlkfvpyTMQAVKQGFQDLgASSLQSA 470
PRK07107 PRK07107
IMP dehydrogenase;
116-285 9.12e-23

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 98.23  E-value: 9.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 116 IDIAHGHSDSVINMIKHIKNHIPDSFVI-AGNVGTPEGVRELENAGADATKVGIGPGRVCITKIKTGFGTGgwQLAALnI 194
Cdd:PRK07107 260 IDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRG--QATAL-I 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 195 CSKAARK----------PLIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESPGETVELDGKQYKEYFGSAS----EF 260
Cdd:PRK07107 337 EVAKARDeyfeetgvyiPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGSnrarNW 416

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446610776 261 QKGEH------KNVEGKKMFVEHKGSLMDTL 285
Cdd:PRK07107 417 QRYDLggdkklSFEEGVDSYVPYAGSLKDNV 447
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 91-230 1.80e-07

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: 50.66  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  91 VGVKKAEFDFIEKLAQEKLIPE---YITIDIAHGHSDS-VINMIKHIKNHIPD-SFVIAGNVGTPEGVRELENAGADATK 165
Cdd:cd04722   62 VQLAINDAAAAVDIAAAAARAAgadGVEIHGAVGYLAReDLELIRELREAVPDvKVVVKLSPTGELAAAAAEEAGVDEVG 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446610776 166 VGIGPGRVCItkiKTGFGTGGWQLAALNIcskAARKPLIADGGIRTHGDIAKSIRFGASMVMIGS 230
Cdd:cd04722  142 LGNGGGGGGG---RDAVPIADLLLILAKR---GSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 149-229 3.89e-07

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: 50.90  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 149 TPEGVRELENAGADATKVGigpgrvcitkiktgfGTGGWQL-------AALNICSKAA--RKPLIADGGIRTHGDIAKSI 219
Cdd:COG1304  235 SPEDARRAVDAGVDGIDVS---------------NHGGRQLdggpptiDALPEIRAAVggRIPVIADGGIRRGLDVAKAL 299

                         90
                 ....*....|
gi 446610776 220 RFGASMVMIG 229
Cdd:COG1304  300 ALGADAVGLG 309
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 133-239 2.87e-06

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: 48.28  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  133 IKNHIPDSFVIAGnVGTPEGVRELENAGADATkvgigpgrvcitkIKTGFGTGGWQ----------LAALNICSKAARKP 202
Cdd:pfam03060 130 FRLHFAGVALIPT-ISSAKEARIAEARGADAL-------------IVQGPEAGGHQgtpeygdkglFRLVPQVPDAVDIP 195

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446610776  203 LIADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESP 239
Cdd:pfam03060 196 VIAAGGIWDRRGVAAALALGASGVQMGTRFLLTKESG 232
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 129-239 4.48e-06

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: 47.09  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 129 MIKHIKNHipDSFVIAgNVGTPEGVRELENAGADAtkvgigpgrVCITKIKTGfGTGGWQLAA----LNICSKAARKPLI 204
Cdd:cd04730   94 VVERLKAA--GIKVIP-TVTSVEEARKAEAAGADA---------LVAQGAEAG-GHRGTFDIGtfalVPEVRDAVDIPVI 160

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446610776 205 ADGGIRTHGDIAKSIRFGASMVMIGSLFAAHEESP 239
Cdd:cd04730  161 AAGGIADGRGIAAALALGADGVQMGTRFLATEESG 195
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 130-229 2.37e-05

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: 45.13  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 130 IKHIKNHIPDSFVIAGnVGTPEGVRELENAGADATKV---GigpGRvcitkiktgfgtggwQL-------AALNICSKAA 199
Cdd:cd02809  164 LAWLRSQWKGPLILKG-ILTPEDALRAVDAGADGIVVsnhG---GR---------------QLdgapatiDALPEIVAAV 224

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446610776 200 --RKPLIADGGIRTHGDIAKSIRFGASMVMIG 229
Cdd:cd02809  225 ggRIEVLLDGGIRRGTDVLKALALGADAVLIG 256
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 147-239 4.31e-05

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 44.33  E-value: 4.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 147 VGTPEGVRELENAGADAtkvgigpgrVCITkiktGFGTGG--------------WQLAALNIcskaarkPLIADGGIRTH 212
Cdd:COG2070  111 VTSVREARKAEKAGADA---------VVAE----GAEAGGhrgadevstfalvpEVRDAVDI-------PVIAAGGIADG 170

                         90       100
                 ....*....|....*....|....*..
gi 446610776 213 GDIAKSIRFGASMVMIGSLFAAHEESP 239
Cdd:COG2070  171 RGIAAALALGADGVQMGTRFLATEESP 197
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 202-245 4.38e-05

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 44.41  E-value: 4.38e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446610776 202 PLIADGGIRTHGDIAKSIRFGASMV-MIGSLFAAHEESPGETVEL 245
Cdd:cd02811  257 PLIASGGIRNGLDIAKALALGADLVgMAGPFLKAALEGEEAVIET 301
FMN_dh pfam01070
FMN-dependent dehydrogenase;
130-237 5.23e-05

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 44.44  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  130 IKHIKNHIPDSFVIAGnVGTPEGVRELENAGADatkvGI-----GpGRVCITKIKTgfgtggwqLAALNICSKAARK--P 202
Cdd:pfam01070 210 LAWLRERWKGPLVVKG-ILSPEDAKRAVEAGVD----GIvvsnhG-GRQLDGAPAT--------IDALPEIVAAVGGriP 275

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446610776  203 LIADGGIRTHGDIAKSIRFGASMVMIG-----SLFAAHEE 237
Cdd:pfam01070 276 VLVDGGIRRGTDVLKALALGADAVLLGrpflyGLAAGGEA 315
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 185-245 1.19e-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: 43.28  E-value: 1.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446610776 185 GGWQLA-------ALNICSKAARKPLIADGGIRTHGDIAKSIRFGASMVMIG-----SLFAAHEESPGETVEL 245
Cdd:cd04736  267 GGRQLDdaiapieALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGratlyGLAARGEAGVSEVLRL 339
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 130-244 1.66e-03

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 39.04  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 130 IKHIKNHIPDSFVIAGNVGTPEGVRELENAGADAtkVGIGPgrvcI--TKIKTGFGTGgWQLAALNICSKAARKPLIADG 207
Cdd:cd00564   85 VAEARALLGPDLIIGVSTHSLEEALRAEELGADY--VGFGP----VfpTPTKPGAGPP-LGLELLREIAELVEIPVVAIG 157

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446610776 208 GIrTHGDIAKSIRFGASMV-MIGSLFAAheESPGETVE 244
Cdd:cd00564  158 GI-TPENAAEVLAAGADGVaVISAITGA--DDPAAAAR 192
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 122-230 6.63e-03

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: 37.17  E-value: 6.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776 122 HSDSVINMIKHIKNHIpDSFVIAgNVGTPEGVRELENAGAD---ATKVGIGPGRVCITkiktgfgTGGWQLaaLNICSKA 198
Cdd:cd04729  107 DGETLAELIKRIHEEY-NCLLMA-DISTLEEALNAAKLGFDiigTTLSGYTEETAKTE-------DPDFEL--LKELRKA 175

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446610776 199 ARKPLIADGGIRTHGDIAKSIRFGASMVMIGS 230
Cdd:cd04729  176 LGIPVIAEGRINSPEQAAKALELGADAVVVGS 207
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 99-229 9.42e-03

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. 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: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 37.42  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446610776  99 DFIEKLAQEKLIPEyitiDIAHghsdsvinmIKHIKNhIPdsfVIAGNVGTPEGVRELENAGADATKVGIGPGRvcitKI 178
Cdd:cd04737  198 SEIYAAAKQKLSPA----DIEF---------IAKISG-LP---VIVKGIQSPEDADVAINAGADGIWVSNHGGR----QL 256

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446610776 179 KTGFGTggwqLAALNICSKAA--RKPLIADGGIRTHGDIAKSIRFGASMVMIG 229
Cdd:cd04737  257 DGGPAS----FDSLPEIAEAVnhRVPIIFDSGVRRGEHVFKALASGADAVAVG 305
 
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