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Conserved domains on  [gi|547476676|ref|WP_022094877|]
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MULTISPECIES: N-acetylmannosamine-6-phosphate 2-epimerase [Collinsella]

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];
4-228 3.16e-119

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


:

Pssm-ID: 442247  Cd Length: 226  Bit Score: 338.23  E-value: 3.16e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   4 DPLIQSLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITP 81
Cdd:COG3010    1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDsdVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  82 TLRHARACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEE-GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIDC 160
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547476676 161 TmaDGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:COG3010  161 T--DGPDLELLKELVAAL-GVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
4-228 3.16e-119

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 338.23  E-value: 3.16e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   4 DPLIQSLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITP 81
Cdd:COG3010    1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDsdVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  82 TLRHARACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEE-GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIDC 160
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547476676 161 TmaDGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:COG3010  161 T--DGPDLELLKELVAAL-GVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
9-228 4.42e-102

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 294.75  E-value: 4.42e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   9 SLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITPTLRHA 86
Cdd:PRK01130   2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDseVYITPTLKEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  87 RACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEE-GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIdcTMADG 165
Cdd:PRK01130  82 DALAAAGADIIALDATLRPRPDGETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEET--KKPEE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547476676 166 PDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:PRK01130 160 PDFALLKELLKAV-GCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 4-222 1.04e-92

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: 270.99  E-value: 1.04e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   4 DPLIQSLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITP 81
Cdd:cd04729    1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDseVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  82 TLRHARACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEEG-VLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIDC 160
Cdd:cd04729   81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547476676 161 TMadGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWF 222
Cdd:cd04729  161 TE--DPDFELLKELRKAL-GIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 32-228 6.62e-54

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: 171.46  E-value: 6.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   32 MAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITPTLRHARACVAAGADIVAIDATDRPRPdg 109
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDspVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  110 KTVEDTFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVSTTLShgvAAIDCTMADGPDLPLLRQATEEfpGLPIICEGRV 189
Cdd:pfam04131  79 VTIEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLS---GYTGGENPAEPDFQLVKTLSEA--GCFVIAEGRY 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 547476676  190 HTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:pfam04131 154 NTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
4-228 3.16e-119

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 338.23  E-value: 3.16e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   4 DPLIQSLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITP 81
Cdd:COG3010    1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDsdVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  82 TLRHARACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEE-GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIDC 160
Cdd:COG3010   81 TLEEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547476676 161 TmaDGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:COG3010  161 T--DGPDLELLKELVAAL-GVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
9-228 4.42e-102

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 294.75  E-value: 4.42e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   9 SLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITPTLRHA 86
Cdd:PRK01130   2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDseVYITPTLKEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  87 RACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEE-GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIdcTMADG 165
Cdd:PRK01130  82 DALAAAGADIIALDATLRPRPDGETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEET--KKPEE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547476676 166 PDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:PRK01130 160 PDFALLKELLKAV-GCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 4-222 1.04e-92

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: 270.99  E-value: 1.04e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   4 DPLIQSLKGKLVVSVQAYMGEPLRTPETMAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITP 81
Cdd:cd04729    1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDseVYITP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  82 TLRHARACVAAGADIVAIDATDRPRPDGKTVEDTFRPLHEEG-VLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAAIDC 160
Cdd:cd04729   81 TIEEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAK 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547476676 161 TMadGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAITHPTSITSWF 222
Cdd:cd04729  161 TE--DPDFELLKELRKAL-GIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 32-228 6.62e-54

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: 171.46  E-value: 6.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676   32 MAQMSRACELGGAAAIRCQGLADIAAIKGRCEVPVIGLWKDGHEG--VYITPTLRHARACVAAGADIVAIDATDRPRPdg 109
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDspVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  110 KTVEDTFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVSTTLShgvAAIDCTMADGPDLPLLRQATEEfpGLPIICEGRV 189
Cdd:pfam04131  79 VTIEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLS---GYTGGENPAEPDFQLVKTLSEA--GCFVIAEGRY 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 547476676  190 HTPEEARAAIDAGAWAVVVGTAITHPTSITSWFKAALEA 228
Cdd:pfam04131 154 NTPELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 18-211 5.68e-07

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: 48.63  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  18 VQAYMGePLRTPETMAQMSRACELG--GAAAIRCQGLAD-IAAIKGRCEVPV-IGLWKDGHEgvyiTPTLRHARACVAAG 93
Cdd:cd04730    6 IQAPMA-GVSTPELAAAVSNAGGLGfiGAGYLTPEALRAeIRKIRALTDKPFgVNLLVPSSN----PDFEALLEVALEEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  94 ADIVAIDATDrprpdgktVEDTFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVSTTLS----HGVAAIDCTMAdgpdlp 169
Cdd:cd04730   81 VPVVSFSFGP--------PAEVVERLKAAGIKVIPTVTSVEEARKAEAAGADALVAQGAeaggHRGTFDIGTFA------ 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 547476676 170 LLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTA 211
Cdd:cd04730  147 LVPEVRDAV-DIPVIAAGGIADGRGIAAALALGADGVQMGTR 187
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 92-219 1.68e-06

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 48.09  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  92 AGADIVAIDATdrprPDGKTVEDTFRPLHEEGVLLMADCATIED-IRRAVD---MGFDLVSTtlsHgvAAIDCTMADGPD 167
Cdd:PRK07028  80 AGADIVCILGL----ADDSTIEDAVRAARKYGVRLMADLINVPDpVKRAVEleeLGVDYINV---H--VGIDQQMLGKDP 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 547476676 168 LPLLRQATEEFPgLPIICEGRVHtPEEARAAIDAGAWAVVVGTAITHPTSIT 219
Cdd:PRK07028 151 LELLKEVSEEVS-IPIAVAGGLD-AETAAKAVAAGADIVIVGGNIIKSADVT 200
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 85-228 1.29e-04

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: 41.71  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  85 HARACVAAGADIVAIDATDRPRPDgktvedtFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVS-----TTLSHgvaaid 159
Cdd:COG0352   69 RVDLALALGADGVHLGQEDLPVAE-------ARALLGPDLIIGVSCHSLEEALRAEEAGADYVGfgpvfPTPTK------ 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547476676 160 cTMADGP-DLPLLRQATEEFPgLPIICEGRVhTPEEARAAIDAGAWAVVVGTAITH---PTSITSWFKAALEA 228
Cdd:COG0352  136 -PGAPPPlGLEGLAWWAELVE-IPVVAIGGI-TPENAAEVLAAGADGVAVISAIWGapdPAAAARELRAALEA 205
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 132-203 2.80e-04

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 41.31  E-value: 2.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547476676 132 TIED----IRRAVDMGFDLVSTTL--SHGVAAIDCTMADGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGA 203
Cdd:COG1902  234 TLEEsvelAKALEEAGVDYLHVSSggYEPDAMIPTIVPEGYQLPFAARIRKAV-GIPVIAVGGITTPEQAEAALASGD 310
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 86-214 3.29e-04

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 40.26  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  86 ARACVAAGADIVAIDAtdrpRPDGKTVEDTFRPLHEEGVLLMAD---CATIEDIRRAVDMGFDLVsttLSHgvAAIDCTM 162
Cdd:cd04726   70 AEMAFKAGADIVTVLG----AAPLSTIKKAVKAAKKYGKEVQVDligVEDPEKRAKLLKLGVDIV---ILH--RGIDAQA 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 547476676 163 ADGPDLPLLRQATEEFPGLPIICEGRVhTPEEARAAIDAGAWAVVVGTAITH 214
Cdd:cd04726  141 AGGWWPEDDLKKVKKLLGVKVAVAGGI-TPDTLPEFKKAGADIVIVGRAITG 191
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
162-212 6.46e-04

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 39.76  E-value: 6.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 547476676 162 MADGPDLP-LLRQATEEFPGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAI 212
Cdd:COG1646  177 GAGEPVDPeMVKAVKKALEDTPLIYGGGIRSPEKAREMAEAGADTIVVGNAI 228
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 84-211 6.87e-04

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 39.71  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  84 RHARACVAAGADIVAIDATDRPrpdgktveDTFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVsttlshgvaaidctMA 163
Cdd:COG2070   73 ELLEVVLEEGVPVVSTSAGLPA--------DLIERLKEAGIKVIPIVTSVREARKAEKAGADAV--------------VA 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676 164 DGPD------------LPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTA 211
Cdd:COG2070  131 EGAEagghrgadevstFALVPEVRDAV-DIPVIAAGGIADGRGIAAALALGADGVQMGTR 189
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 140-203 1.61e-03

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 38.27  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547476676 140 VDMGFDLVSTTLSHGVAAIDCTMADGPDLPLLRQATEEFPGLpIICEGRVHTPEEARAAIDAGA 203
Cdd:cd00452   15 AEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEA-LIGAGTVLTPEQADAAIAAGA 77
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 128-202 2.17e-03

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: 38.36  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676 128 ADCATIEDIRRAVDM-----GFDLVSTT--------LSHGVAAIDcTMADGPDLPL---LRQATeefpGLPIICEGRVHT 191
Cdd:cd04734  222 EGGLSPDEALEIAARlaaegLIDYVNVSagsyytllGLAHVVPSM-GMPPGPFLPLaarIKQAV----DLPVFHAGRIRD 296

                         90
                 ....*....|.
gi 547476676 192 PEEARAAIDAG 202
Cdd:cd04734  297 PAEAEQALAAG 307
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 85-213 2.93e-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: 37.50  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676  85 HARACVAAGADIVAIDATDRPrpdgktvEDTFRPLHEEGVLLMADCATIEDIRRAVDMGFDLVsttlshGVAAIDCT--- 161
Cdd:cd00564   64 RVDLALAVGADGVHLGQDDLP-------VAEARALLGPDLIIGVSTHSLEEALRAEELGADYV------GFGPVFPTptk 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 547476676 162 -MADGP-DLPLLRQATEEFPgLPIICEGRVhTPEEARAAIDAGAWAVVVGTAIT 213
Cdd:cd00564  131 pGAGPPlGLELLREIAELVE-IPVVAIGGI-TPENAAEVLAAGADGVAVISAIT 182
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 136-208 4.57e-03

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: 37.43  E-value: 4.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547476676 136 IRRAVDMGFDLVSTTLSHGVAAIDCTMADgpdLPLLRQATeefpGLPIICEGrVHTPEEARAAIDAGAWAVVV 208
Cdd:cd02809  135 LRRAEAAGYKALVLTVDTPVLGRRLTWDD---LAWLRSQW----KGPLILKG-ILTPEDALRAVDAGADGIVV 199
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
162-212 6.90e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 36.71  E-value: 6.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 547476676 162 MADGPDLP-LLRQATEEFPGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAI 212
Cdd:PRK04169 165 GAGDPVPPeMVKAVKKALDITPLIYGGGIRSPEQARELMAAGADTIVVGNII 216
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 144-212 7.13e-03

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


Pssm-ID: 439876  Cd Length: 236  Bit Score: 36.55  E-value: 7.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547476676 144 FDLVSTTLSHGVAAIDCT------MADGPDLPLLRQATEEFpGLPIICEGRVHTPEEARAAIDAGAWAVVVGTAI 212
Cdd:COG0106  148 EELAKRFEDAGVAAILYTdisrdgTLQGPNLELYRELAAAT-GIPVIASGGVSSLDDLRALKELGVEGAIVGKAL 221
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 123-207 7.67e-03

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 37.12  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547476676 123 GVLLMADCATIEDIRRAVDMGFDLVSTTLSHGVAA--------IDCTMAD-----GPDLPLLRQATEEFPGLPIICEGRV 189
Cdd:PRK13558   9 GVLFVGDDPEAGPVDCDLDEDGRLDVTQIRDFVAArdrveageIDCVVADhepdgFDGLALLEAVRQTTAVPPVVVVPTA 88

                         90
                 ....*....|....*...
gi 547476676 190 HTPEEARAAIDAGAWAVV 207
Cdd:PRK13558  89 GDEAVARRAVDADAAAYV 106
 
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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