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Conserved domains on  [gi|1632590678|ref|WP_136758997|]
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N-acetylmannosamine-6-phosphate 2-epimerase [Escherichia coli]

Protein Classification

N-acetylmannosamine-6-phosphate 2-epimerase( domain architecture ID 10011628)

N-acetylmannosamine-6-phosphate 2-epimerase converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P)

EC:  5.1.3.9
Gene Ontology:  GO:0005975|GO:0006051|GO:0009385|GO:0019262
PubMed:  34607125|34437902

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
6-227 1.02e-115

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


:

Pssm-ID: 234907  Cd Length: 221  Bit Score: 329.42  E-value: 1.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   6 DSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITATLRE 85
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  86 VDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARyPSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETAghVL 165
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPDGETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETK--KP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632590678 166 AENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:PRK01130  158 EEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDAL 219
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
6-227 1.02e-115

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 329.42  E-value: 1.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   6 DSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITATLRE 85
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  86 VDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARyPSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETAghVL 165
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPDGETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETK--KP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632590678 166 AENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:PRK01130  158 EEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDAL 219
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
2-227 1.17e-114

Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 442247  Cd Length: 226  Bit Score: 327.06  E-value: 1.17e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   2 KTVLDSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITA 81
Cdd:COG3010     1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  82 TLREVDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARyPSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETA 161
Cdd:COG3010    81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632590678 162 GHVLaeNDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:COG3010   160 GTDG--PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDAL 223
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 2-223 3.42e-104

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: 300.26  E-value: 3.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   2 KTVLDSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITA 81
Cdd:cd04729     1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  82 TLREVDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARYpSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETA 161
Cdd:cd04729    81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632590678 162 GhvLAENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRF 223
Cdd:cd04729   160 K--TEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 30-227 4.04e-61

Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.


Pssm-ID: 427732  Cd Length: 192  Bit Score: 189.95  E-value: 4.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  30 MSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITATLREVDELMTVEPEIIALDATARPRPgg 109
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 110 QTLEELVTQIRARYpsVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETAGhvlAENDCGFLREVLAAvSVPVVAEGN 189
Cdd:pfam04131  79 VTIEDFIKRIKEKG--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP---AEPDFQLVKTLSEA-GCFVIAEGR 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1632590678 190 VDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:pfam04131 153 YNTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAI 190
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
6-227 1.02e-115

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 329.42  E-value: 1.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   6 DSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITATLRE 85
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  86 VDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARyPSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETAghVL 165
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPDGETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETK--KP 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632590678 166 AENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:PRK01130  158 EEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDAL 219
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
2-227 1.17e-114

Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 442247  Cd Length: 226  Bit Score: 327.06  E-value: 1.17e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   2 KTVLDSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITA 81
Cdd:COG3010     1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  82 TLREVDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARyPSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETA 161
Cdd:COG3010    81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETK 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1632590678 162 GHVLaeNDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:COG3010   160 GTDG--PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDAL 223
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 2-223 3.42e-104

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: 300.26  E-value: 3.42e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678   2 KTVLDSLKGKLIVSCQALENEPLHSPFIMSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITA 81
Cdd:cd04729     1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  82 TLREVDELMTVEPEIIALDATARPRPGGQTLEELVTQIRARYpSVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETA 161
Cdd:cd04729    81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1632590678 162 GhvLAENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGGAITRPQQITTRF 223
Cdd:cd04729   160 K--TEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 30-227 4.04e-61

Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.


Pssm-ID: 427732  Cd Length: 192  Bit Score: 189.95  E-value: 4.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  30 MSRMALAAAQGGAAGIRANSVADISAIKEIVSLPMIGIIKRDYPGSEVFITATLREVDELMTVEPEIIALDATARPRPgg 109
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 110 QTLEELVTQIRARYpsVLLMADIATVEEAVTAERLGFDCVGTTLYGYTAETAGhvlAENDCGFLREVLAAvSVPVVAEGN 189
Cdd:pfam04131  79 VTIEDFIKRIKEKG--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP---AEPDFQLVKTLSEA-GCFVIAEGR 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1632590678 190 VDTPERAARCLTLGAHTVVVGGAITRPQQITTRFIAAI 227
Cdd:pfam04131 153 YNTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAI 190
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 113-226 6.32e-09

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: 54.41  E-value: 6.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 113 EELVTQIRARypSVLLMADIATVEEAVTAERLGFDCVgtTLYGYTAetAGHVLAENDCGF--LREVLAAVSVPVVAEGNV 190
Cdd:cd04730    92 AEVVERLKAA--GIKVIPTVTSVEEARKAEAAGADAL--VAQGAEA--GGHRGTFDIGTFalVPEVRDAVDIPVIAAGGI 165

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1632590678 191 DTPERAARCLTLGAHTVVVGgaitrpqqitTRFIAA 226
Cdd:cd04730   166 ADGRGIAAALALGADGVQMG----------TRFLAT 191
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 121-220 8.96e-08

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 51.94  E-value: 8.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 121 ARYPSVLLMADIATVEE----AVTAERLGFDCVGTtlygytaetagHV------LAENDCGFLREVLAAVSVPVVAEGNV 190
Cdd:PRK07028  103 ARKYGVRLMADLINVPDpvkrAVELEELGVDYINV-----------HVgidqqmLGKDPLELLKEVSEEVSIPIAVAGGL 171

                          90       100       110
                  ....*....|....*....|....*....|
gi 1632590678 191 DtPERAARCLTLGAHTVVVGGAITRPQQIT 220
Cdd:PRK07028  172 D-AETAAKAVAAGADIVIVGGNIIKSADVT 200
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 134-228 1.44e-07

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 50.18  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 134 TVEEAVTAERLGFDCVGttlYGYTAETAGHVLAENDCG--FLREVLAAVSVPVVAEGNVdTPERAARCLTLGAHTVVVGG 211
Cdd:COG0352   109 SLEEALRAEEAGADYVG---FGPVFPTPTKPGAPPPLGleGLAWWAELVEIPVVAIGGI-TPENAAEVLAAGADGVAVIS 184

                          90       100
                  ....*....|....*....|
gi 1632590678 212 AITR---PQQITTRFIAAIS 228
Cdd:COG0352   185 AIWGapdPAAAARELRAALE 204
PRK07695 PRK07695
thiazole tautomerase TenI;
116-213 3.27e-07

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 49.25  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 116 VTQIRARYPSVLLMADIATVEEAVTAERLGFDCVgttLYGYTAETAGH--VLAendCGF--LREVLAAVSVPVVAEGNVd 191
Cdd:PRK07695   86 VRSVREKFPYLHVGYSVHSLEEAIQAEKNGADYV---VYGHVFPTDCKkgVPA---RGLeeLSDIARALSIPVIAIGGI- 158

                          90       100
                  ....*....|....*....|..
gi 1632590678 192 TPERAARCLTLGAHTVVVGGAI 213
Cdd:PRK07695  159 TPENTRDVLAAGVSGIAVMSGI 180
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 134-225 4.88e-07

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: 48.67  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 134 TVEEAVTAERLGFDCVG------TTlygyTAETAGHVLaenDCGFLREVLAAVSVPVVAEGNVdTPERAARCLTLGAHTV 207
Cdd:cd00564   104 SLEEALRAEELGADYVGfgpvfpTP----TKPGAGPPL---GLELLREIAELVEIPVVAIGGI-TPENAAEVLAAGADGV 175

                          90       100
                  ....*....|....*....|.
gi 1632590678 208 VVGGAITR---PQQITTRFIA 225
Cdd:cd00564   176 AVISAITGaddPAAAARELLA 196
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 55-211 8.54e-06

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


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 45.27  E-value: 8.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678  55 AIKEIVSLPMIGIIKRDYPGSEVFITATLREVDELmtvepEIIALDATARPRPGGQTleELVTQIRARYPSVLLMADIA- 133
Cdd:cd04722    51 EVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGA-----DGVEIHGAVGYLAREDL--ELIRELREAVPDVKVVVKLSp 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1632590678 134 -TVEEAVTAERLGFDCVGTTLYGYTaeTAGHVLAENDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTLGAHTVVVGG 211
Cdd:cd04722   124 tGELAAAAAEEAGVDEVGLGNGGGG--GGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 126-226 1.04e-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: 45.49  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 126 VLLMADIATVEEAVTAERLGFD---CVGttlygytAETAGHVLAENDCGF--LREVLAAVSVPVVAEGNVDTPERAARCL 200
Cdd:COG2070   105 IKVIPIVTSVREARKAEKAGADavvAEG-------AEAGGHRGADEVSTFalVPEVRDAVDIPVIAAGGIADGRGIAAAL 177

                          90       100
                  ....*....|....*....|....*.
gi 1632590678 201 TLGAHTVVVGgaitrpqqitTRFIAA 226
Cdd:COG2070   178 ALGADGVQMG----------TRFLAT 193
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 131-216 6.82e-05

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 42.48  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 131 DIATVEEAVTAERLGFDCVgtTLYGYTAETAGHVLAenDCGFLREVLAAVSVPVVAEGNVDTPERAARCLTL-GAHTVVV 209
Cdd:cd02801   137 EEETLELAKALEDAGASAL--TVHGRTREQRYSGPA--DWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQtGVDGVMI 212


                  ....*...
gi 1632590678 210 G-GAITRP 216
Cdd:cd02801   213 GrGALGNP 220
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 174-216 1.12e-04

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 42.39  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1632590678 174 REVLAAVSVPVVAEGNVDTPERAARCL-TLGAHTVVVG-GAITRP 216
Cdd:COG0042   184 ARVKEAVSIPVIGNGDIFSPEDAKRMLeETGCDGVMIGrGALGNP 228
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 134-216 3.10e-04

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 41.16  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 134 TVEEAVTAERLGFDCVgtTLYGYTAETAGHVLAENDcgFLREVLAAVSVPVVAEGNVDTPERAARCLT-LGAHTVVVG-G 211
Cdd:pfam01207 140 AVEIAKIVEDAGAQAL--TVHGRTRAQNYEGTADWD--AIKQVKQAVSIPVIANGDITDPEDAQRCLAyTGADGVMIGrG 215


                  ....*
gi 1632590678 212 AITRP 216
Cdd:pfam01207 216 ALGNP 220
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 126-233 5.22e-03

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


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 37.49  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 126 VLLMADIATVEEAVTAERLGFDCVgtTLYGYtaETAGH--VLAENDCGFLR---EVLAAVSVPVVAEGNVDTPERAARCL 200
Cdd:pfam03060 137 VALIPTISSAKEARIAEARGADAL--IVQGP--EAGGHqgTPEYGDKGLFRlvpQVPDAVDIPVIAAGGIWDRRGVAAAL 212

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1632590678 201 TLGAHTVvvggaitrpqQITTRFIAAISLPSSD 233
Cdd:pfam03060 213 ALGASGV----------QMGTRFLLTKESGAHD 235
thiE PRK00043
thiamine phosphate synthase;
134-227 9.78e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 35.93  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1632590678 134 TVEEAVTAERLGFD--CVG----TTlygyTAETAGHVLAENdcgFLREVLAAVS-VPVVAEGNVdTPERAARCLTLGAHT 206
Cdd:PRK00043  113 TLEEAAAALAAGADyvGVGpifpTP----TKKDAKAPQGLE---GLREIRAAVGdIPIVAIGGI-TPENAPEVLEAGADG 184

                          90       100
                  ....*....|....*....|....
gi 1632590678 207 VVVGGAITR---PQQITTRFIAAI 227
Cdd:PRK00043  185 VAVVSAITGaedPEAAARALLAAF 208
 
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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