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Conserved domains on  [gi|499552406|ref|WP_011233189|]
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MULTISPECIES: N-acetylmannosamine-6-phosphate 2-epimerase [Salmonella]

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)

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;
15-226 9.10e-109

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


:

Pssm-ID: 234907  Cd Length: 221  Bit Score: 311.70  E-value: 9.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  15 GGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDSPVRITPFLDDVDAL 94
Cdd:PRK01130   5 GGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKEVDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  95 AQAGAAIIAVDGTARQRP--VAVEALLARIHH-HHLLAMADCSSVDDGLACQRLGADIIGTTMSGYTTPD-TPEEPDLPL 170
Cdd:PRK01130  85 AAAGADIIALDATLRPRPdgETLAELVKRIKEyPGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETkKPEEPDFAL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499552406 171 VKALHDA-GCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWYNDALKK 226
Cdd:PRK01130 165 LKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
15-226 9.10e-109

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 311.70  E-value: 9.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  15 GGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDSPVRITPFLDDVDAL 94
Cdd:PRK01130   5 GGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKEVDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  95 AQAGAAIIAVDGTARQRP--VAVEALLARIHH-HHLLAMADCSSVDDGLACQRLGADIIGTTMSGYTTPD-TPEEPDLPL 170
Cdd:PRK01130  85 AAAGADIIALDATLRPRPdgETLAELVKRIKEyPGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETkKPEEPDFAL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499552406 171 VKALHDA-GCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWYNDALKK 226
Cdd:PRK01130 165 LKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
1-227 8.87e-106

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 304.33  E-value: 8.87e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   1 MSLLEQLdkniaaSGGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDS 80
Cdd:COG3010    1 NELLEQL------KGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  81 PVRITPFLDDVDALAQAGAAIIAVDGTARQRP--VAVEALLARIHHH-HLLAMADCSSVDDGLACQRLGADIIGTTMSGY 157
Cdd:COG3010   75 DVYITPTLEEVDALAEAGADIIALDATRRPRPdgETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGY 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499552406 158 TTPDTP-EEPDLPLVKAL-HDAGCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWYNDALKKA 227
Cdd:COG3010  155 TGETKGtDGPDLELLKELvAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
1-220 2.53e-100

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: 290.25  E-value: 2.53e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   1 MSLLEQLdkniaaSGGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDS 80
Cdd:cd04729    1 MKLLEQL------KGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  81 PVRITPFLDDVDALAQAGAAIIAVDGTARQRPVA--VEALLARIHHH-HLLAMADCSSVDDGLACQRLGADIIGTTMSGY 157
Cdd:cd04729   75 EVYITPTIEEVDALAAAGADIIALDATDRPRPDGetLAELIKRIHEEyNCLLMADISTLEEALNAAKLGFDIIGTTLSGY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499552406 158 TTPDT-PEEPDLPLVKALHDA-GCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWY 220
Cdd:cd04729  155 TEETAkTEDPDFELLKELRKAlGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
46-226 2.05e-97

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: 282.02  E-value: 2.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   46 GAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDSPVRITPFLDDVDALAQAGAAIIAVDGTARQRPVAVEALLARIHHH 125
Cdd:pfam04131  12 GAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRPVTIEDFIKRIKEK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  126 HLLAMADCSSVDDGLACQRLGADIIGTTMSGYTTPDTPEEPDLPLVKALHDAGCRVIAEGRYNSPTLAAEAIRYGAWAVT 205
Cdd:pfam04131  92 GCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAEPDFQLVKTLSEAGCFVIAEGRYNTPELAKKAIEIGADAVT 171
                         170       180
                  ....*....|....*....|.
gi 499552406  206 VGSAITRLEHICGWYNDALKK 226
Cdd:pfam04131 172 VGSAITRLEHITQWFNNAIKS 192
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
15-226 9.10e-109

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 311.70  E-value: 9.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  15 GGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDSPVRITPFLDDVDAL 94
Cdd:PRK01130   5 GGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKEVDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  95 AQAGAAIIAVDGTARQRP--VAVEALLARIHH-HHLLAMADCSSVDDGLACQRLGADIIGTTMSGYTTPD-TPEEPDLPL 170
Cdd:PRK01130  85 AAAGADIIALDATLRPRPdgETLAELVKRIKEyPGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETkKPEEPDFAL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499552406 171 VKALHDA-GCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWYNDALKK 226
Cdd:PRK01130 165 LKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
1-227 8.87e-106

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 304.33  E-value: 8.87e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   1 MSLLEQLdkniaaSGGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDS 80
Cdd:COG3010    1 NELLEQL------KGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  81 PVRITPFLDDVDALAQAGAAIIAVDGTARQRP--VAVEALLARIHHH-HLLAMADCSSVDDGLACQRLGADIIGTTMSGY 157
Cdd:COG3010   75 DVYITPTLEEVDALAEAGADIIALDATRRPRPdgETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGY 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499552406 158 TTPDTP-EEPDLPLVKAL-HDAGCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWYNDALKKA 227
Cdd:COG3010  155 TGETKGtDGPDLELLKELvAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
1-220 2.53e-100

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: 290.25  E-value: 2.53e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   1 MSLLEQLdkniaaSGGLIVSCQPVPGSPLDKPEIVAAMALAAEQAGAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDS 80
Cdd:cd04729    1 MKLLEQL------KGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  81 PVRITPFLDDVDALAQAGAAIIAVDGTARQRPVA--VEALLARIHHH-HLLAMADCSSVDDGLACQRLGADIIGTTMSGY 157
Cdd:cd04729   75 EVYITPTIEEVDALAAAGADIIALDATDRPRPDGetLAELIKRIHEEyNCLLMADISTLEEALNAAKLGFDIIGTTLSGY 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499552406 158 TTPDT-PEEPDLPLVKALHDA-GCRVIAEGRYNSPTLAAEAIRYGAWAVTVGSAITRLEHICGWY 220
Cdd:cd04729  155 TEETAkTEDPDFELLKELRKAlGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
46-226 2.05e-97

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: 282.02  E-value: 2.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406   46 GAVAVRIEGIDNLRVARSLVSVPIIGIIKRDLDDSPVRITPFLDDVDALAQAGAAIIAVDGTARQRPVAVEALLARIHHH 125
Cdd:pfam04131  12 GAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRPVTIEDFIKRIKEK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  126 HLLAMADCSSVDDGLACQRLGADIIGTTMSGYTTPDTPEEPDLPLVKALHDAGCRVIAEGRYNSPTLAAEAIRYGAWAVT 205
Cdd:pfam04131  92 GCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAEPDFQLVKTLSEAGCFVIAEGRYNTPELAKKAIEIGADAVT 171
                         170       180
                  ....*....|....*....|.
gi 499552406  206 VGSAITRLEHICGWYNDALKK 226
Cdd:pfam04131 172 VGSAITRLEHITQWFNNAIKS 192
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
58-208 1.55e-04

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: 41.42  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  58 LRVARSLVSVPIIGIIKRDLDDSPVRITpflddVDALAQAGAAIIAVDGTARQRPVA----VEALLARIHHHHLLAMADC 133
Cdd:cd04722   49 LKEVAAETDLPLGVQLAINDAAAAVDIA-----AAAARAAGADGVEIHGAVGYLAREdlelIRELREAVPDVKVVVKLSP 123
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499552406 134 SSVDDGLACQRLGADIIGTTMSGYTTPDTPEEP--DLPLVKALHDAGCRVIAEGRYNSPTLAAEAIRYGAWAVTVGS 208
Cdd:cd04722  124 TGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPiaDLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
90-212 5.41e-03

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 37.31  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  90 DVDALAQAGAAIIAVDGTARQRPVAvEALLARiHHHHLLAMADCSSVDDGLA----CQRLGADIIGT------TMSGYTT 159
Cdd:PRK07028  73 EVEMAAKAGADIVCILGLADDSTIE-DAVRAA-RKYGVRLMADLINVPDPVKraveLEELGVDYINVhvgidqQMLGKDP 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499552406 160 pdtpeepdLPLVKALHDA-GCRVIAEGRYNSPTlAAEAIRYGAWAVTVGSAITR 212
Cdd:PRK07028 151 --------LELLKEVSEEvSIPIAVAGGLDAET-AAKAVAAGADIVIVGGNIIK 195
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
46-209 5.69e-03

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: 36.69  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406  46 GAVAVRIEGIDN-LRVARSLVSVPI-IGIIkrdlddSPVRITPFLDDVDALAQAGAAIIAvdgTARQRPvavEALLARIH 123
Cdd:cd04730   32 GAGYLTPEALRAeIRKIRALTDKPFgVNLL------VPSSNPDFEALLEVALEEGVPVVS---FSFGPP---AEVVERLK 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499552406 124 HHHLLAMADCSSVDDGLACQRLGADII---GTTMSGYTTpdTPEEPDLPLVKALHDA-GCRVIAEGRYNSPTLAAEAIRY 199
Cdd:cd04730  100 AAGIKVIPTVTSVEEARKAEAAGADALvaqGAEAGGHRG--TFDIGTFALVPEVRDAvDIPVIAAGGIADGRGIAAALAL 177
                        170
                 ....*....|
gi 499552406 200 GAWAVTVGSA 209
Cdd:cd04730  178 GADGVQMGTR 187
 
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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