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Conserved domains on  [gi|503617618|ref|WP_013851694|]
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N-acetylmannosamine-6-phosphate 2-epimerase [Streptococcus pasteurianus]

Protein Classification

N-acetylmannosamine-6-phosphate 2-epimerase( domain architecture ID 10789899)

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
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
7-233 1.24e-106

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


:

Pssm-ID: 442247  Cd Length: 226  Bit Score: 306.64  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   7 LLQQLKGGVVISCQALPGEPMYSekGGVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITP 86
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHS--PEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  87 TMDEIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQsYPEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQ 166
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHE-EPGALVMADISTLEEALAAAELGADIVGTTLSGYTGETK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503617618 167 DLAIesNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:COG3010  160 GTDG--PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALK 224
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
7-233 1.24e-106

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 306.64  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   7 LLQQLKGGVVISCQALPGEPMYSekGGVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITP 86
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHS--PEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  87 TMDEIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQsYPEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQ 166
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHE-EPGALVMADISTLEEALAAAELGADIVGTTLSGYTGETK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503617618 167 DLAIesNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:COG3010  160 GTDG--PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALK 224
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
10-233 3.62e-102

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 295.13  E-value: 3.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  10 QLKGGVVISCQALPGEPMYSEKggVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITPTMD 89
Cdd:PRK01130   2 QLKGGLIVSCQALPGEPLHSPE--IMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  90 EIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQSyPEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQDla 169
Cdd:PRK01130  80 EVDALAAAGADIIALDATLRPRPDGETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKK-- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503617618 170 IESNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:PRK01130 157 PEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALK 220
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 7-228 3.62e-95

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: 277.53  E-value: 3.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   7 LLQQLKGGVVISCQALPGEPMYSekGGVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITP 86
Cdd:cd04729    3 LLEQLKGGLIVSCQALPGEPLHS--PEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  87 TMDEIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQSYpEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQ 166
Cdd:cd04729   81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503617618 167 DlaIESNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPF 228
Cdd:cd04729  160 K--TEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 48-233 1.77e-64

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: 198.81  E-value: 1.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   48 VGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITPTMDEIDALVETKVDIIALDATTSSRPngQTLEEFVIQIRQS 127
Cdd:pfam04131  14 VGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP--VTIEDFIKRIKEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  128 YpeQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQDlaiESNDFEIIRKAVGVlETPVIAEGNINTPSKVRRVLQL 207
Cdd:pfam04131  92 G--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP---AEPDFQLVKTLSEA-GCFVIAEGRYNTPELAKKAIEI 165

                         170       180
                  ....*....|....*....|....*.
gi 503617618  208 GVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:pfam04131 166 GADAVTVGSAITRLEHITQWFNNAIK 191
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 174-218 3.16e-03

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


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 37.56  E-value: 3.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 503617618  174 DFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAI 218
Cdd:TIGR00007 177 NFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
7-233 1.24e-106

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 306.64  E-value: 1.24e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   7 LLQQLKGGVVISCQALPGEPMYSekGGVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITP 86
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHS--PEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  87 TMDEIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQsYPEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQ 166
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHE-EPGALVMADISTLEEALAAAELGADIVGTTLSGYTGETK 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503617618 167 DLAIesNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:COG3010  160 GTDG--PDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALK 224
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
10-233 3.62e-102

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 295.13  E-value: 3.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  10 QLKGGVVISCQALPGEPMYSEKggVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITPTMD 89
Cdd:PRK01130   2 QLKGGLIVSCQALPGEPLHSPE--IMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  90 EIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQSyPEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQDla 169
Cdd:PRK01130  80 EVDALAAAGADIIALDATLRPRPDGETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKK-- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503617618 170 IESNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:PRK01130 157 PEEPDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALK 220
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 7-228 3.62e-95

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: 277.53  E-value: 3.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   7 LLQQLKGGVVISCQALPGEPMYSekGGVMPLFAKAAAQAGAVGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITP 86
Cdd:cd04729    3 LLEQLKGGLIVSCQALPGEPLHS--PEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  87 TMDEIDALVETKVDIIALDATTSSRPNGQTLEEFVIQIRQSYpEQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQ 166
Cdd:cd04729   81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503617618 167 DlaIESNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAITRPLVIAKPF 228
Cdd:cd04729  160 K--TEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 48-233 1.77e-64

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: 198.81  E-value: 1.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618   48 VGIRANGIRDITEIKEAVDLPIIGIIKKNYENADVFITPTMDEIDALVETKVDIIALDATTSSRPngQTLEEFVIQIRQS 127
Cdd:pfam04131  14 VGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRP--VTIEDFIKRIKEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  128 YpeQLLMADCSTMDEMIVADKLDFDFIGTTLVGYTKQSQDlaiESNDFEIIRKAVGVlETPVIAEGNINTPSKVRRVLQL 207
Cdd:pfam04131  92 G--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP---AEPDFQLVKTLSEA-GCFVIAEGRYNTPELAKKAIEI 165

                         170       180
                  ....*....|....*....|....*.
gi 503617618  208 GVHTVVVGSAITRPLVIAKPFIEATN 233
Cdd:pfam04131 166 GADAVTVGSAITRLEHITQWFNNAIK 191
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 58-216 3.84e-09

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: 54.51  E-value: 3.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  58 ITEIKEAVDLPIIGIIKKNYENADVFITPTMDEidalvETKVDIIALDATTSSRPNGQTleEFVIQIRQSYPEQLLMADC 137
Cdd:cd04722   49 LKEVAAETDLPLGVQLAINDAAAAVDIAAAAAR-----AAGADGVEIHGAVGYLAREDL--ELIRELREAVPDVKVVVKL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618 138 STMDE--MIVADKLDFDFIGTTLVGYTKQSQDLAIESNDFEIIRKAVgvLETPVIAEGNINTPSKVRRVLQLGVHTVVVG 215
Cdd:cd04722  122 SPTGElaAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRG--SKVPVIAGGGINDPEDAAEALALGADGVIVG 199


                 .
gi 503617618 216 S 216
Cdd:cd04722  200 S 200
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 121-220 7.04e-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: 48.28  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618 121 VIQIRQSYPEQLLM-ADCSTMDEMIVADKLDFDFIGttlVG--YTKQSQDLAIESNDFEIIRKAVGVLETPVIAEGNInT 197
Cdd:cd00564   85 VAEARALLGPDLIIgVSTHSLEEALRAEELGADYVG---FGpvFPTPTKPGAGPPLGLELLREIAELVEIPVVAIGGI-T 160

                         90       100
                 ....*....|....*....|...
gi 503617618 198 PSKVRRVLQLGVHTVVVGSAITR 220
Cdd:cd00564  161 PENAAEVLAAGADGVAVISAITG 183
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 56-217 2.95e-04

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


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 40.93  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618  56 RDITEIKEAVDLPI-IGIIKKNYEnadvfiTPTMDEIDALVETKVDIIALdATTSSRPNGQTLEEFVIQIrqsypeqllM 134
Cdd:cd04730   43 AEIRKIRALTDKPFgVNLLVPSSN------PDFEALLEVALEEGVPVVSF-SFGPPAEVVERLKAAGIKV---------I 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618 135 ADCSTMDEMIVADKLDFDFI-----------GTTLVGytkqsqdlaiesnDFEIIRKAVGVLETPVIAEGNINTPSKVRR 203
Cdd:cd04730  107 PTVTSVEEARKAEAAGADALvaqgaeagghrGTFDIG-------------TFALVPEVRDAVDIPVIAAGGIADGRGIAA 173

                        170
                 ....*....|....
gi 503617618 204 VLQLGVHTVVVGSA 217
Cdd:cd04730  174 ALALGADGVQMGTR 187
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 161-217 4.79e-04

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 40.20  E-value: 4.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503617618 161 YTKQSQDLAIESNDFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSA 217
Cdd:PRK13587 167 YTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 118-229 7.86e-04

Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.


Pssm-ID: 240085 [Multi-domain]  Cd Length: 343  Bit Score: 39.90  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618 118 EEFVIQIRQSYPEQLlmADCSTMDEMI-VADKLD----FDFIGT------TLVGYTKQSQDLAIESNDF----EIIRKAV 182
Cdd:cd04734  207 PDFIVGIRISGDEDT--EGGLSPDEALeIAARLAaeglIDYVNVsagsyyTLLGLAHVVPSMGMPPGPFlplaARIKQAV 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 503617618 183 GVletPVIAEGNINTPSKVRRVLQLGvHTVVVGsaITRPLvIAKPFI 229
Cdd:cd04734  285 DL---PVFHAGRIRDPAEAEQALAAG-HADMVG--MTRAH-IADPHL 324
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 174-229 1.38e-03

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: 38.63  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503617618 174 DFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQL-GVHTVVVGSAItrplvIAKPFI 229
Cdd:cd02801  171 DWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQtGVDGVMIGRGA-----LGNPWL 222
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 174-218 2.62e-03

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


Pssm-ID: 240083  Cd Length: 234  Bit Score: 37.84  E-value: 2.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 503617618 174 DFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAI 218
Cdd:cd04732  178 NFELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKAL 222
PRK07695 PRK07695
thiazole tautomerase TenI;
121-231 3.04e-03

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 37.69  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503617618 121 VIQIRQSYPEqlLMADCS--TMDEMIVADKLDFDFIgttLVGYT-KQSQDLAIESNDFEIIRKAVGVLETPVIAEGNInT 197
Cdd:PRK07695  86 VRSVREKFPY--LHVGYSvhSLEEAIQAEKNGADYV---VYGHVfPTDCKKGVPARGLEELSDIARALSIPVIAIGGI-T 159

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503617618 198 PSKVRRVLQLGVHTVVVGSAI---TRPLVIAKPFIEA 231
Cdd:PRK07695 160 PENTRDVLAAGVSGIAVMSGIfssANPYSKAKRYAES 196
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 174-218 3.16e-03

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


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 37.56  E-value: 3.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 503617618  174 DFEIIRKAVGVLETPVIAEGNINTPSKVRRVLQLGVHTVVVGSAI 218
Cdd:TIGR00007 177 NFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 188-218 5.89e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 37.19  E-value: 5.89e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 503617618 188 PVIAEGNINTPSKVRRVLQLGVHTVVVGSAI 218
Cdd:cd04735  286 PLIAVGSINTPDDALEALETGADLVAIGRGL 316
 
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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