NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|695830318|ref|WP_032743838|]
View 

MULTISPECIES: N-acetylmannosamine-6-phosphate 2-epimerase [Bifidobacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
11-231 5.39e-126

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


:

Pssm-ID: 442247  Cd Length: 226  Bit Score: 355.56  E-value: 5.39e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  11 LIDSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTL 88
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDypDSDVYITPTL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  89 RHARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSE-GAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTE 167
Cdd:COG3010   83 EEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695830318 168 GPDYELLAQMLERHPhVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:COG3010  163 GPDLELLKELVAALG-VPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
11-231 5.39e-126

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 355.56  E-value: 5.39e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  11 LIDSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTL 88
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDypDSDVYITPTL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  89 RHARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSE-GAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTE 167
Cdd:COG3010   83 EEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695830318 168 GPDYELLAQMLERHPhVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:COG3010  163 GPDLELLKELVAALG-VPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
13-231 4.23e-118

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 335.58  E-value: 4.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  13 DSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTLRH 90
Cdd:PRK01130   1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDypDSEVYITPTLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  91 ARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSE-GAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTEGP 169
Cdd:PRK01130  81 VDALAAAGADIIALDATLRPRPDGETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKKPEEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695830318 170 DYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:PRK01130 161 DFALLKELLK-AVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 11-225 3.43e-102

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: 295.25  E-value: 3.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  11 LIDSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTL 88
Cdd:cd04729    3 LLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDypDSEVYITPTI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  89 RHARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSEG-AILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTE 167
Cdd:cd04729   83 EEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAKTE 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695830318 168 GPDYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWF 225
Cdd:cd04729  163 DPDFELLKELRK-ALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 37-231 3.22e-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: 190.34  E-value: 3.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318   37 MAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTLRHARACIMAGADIVALDATDRPRPdg 114
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDlpDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  115 LTLQQTARQLKSEGAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTEgPDYELLAQMLErhPHVPVICEGRIHT 194
Cdd:pfam04131  79 VTIEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAE-PDFQLVKTLSE--AGCFVIAEGRYNT 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 695830318  195 PSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:pfam04131 156 PELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 159-215 3.75e-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: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 695830318  159 YTD-SRAKT-EGPDYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAI 215
Cdd:TIGR00007 164 YTDiSRDGTlSGPNFELTKELVK-AVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
 
Name Accession Description Interval E-value
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
11-231 5.39e-126

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


Pssm-ID: 442247  Cd Length: 226  Bit Score: 355.56  E-value: 5.39e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  11 LIDSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTL 88
Cdd:COG3010    3 LLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDypDSDVYITPTL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  89 RHARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSE-GAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTE 167
Cdd:COG3010   83 EEVDALAEAGADIIALDATRRPRPDGETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695830318 168 GPDYELLAQMLERHPhVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:COG3010  163 GPDLELLKELVAALG-VPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKK 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
13-231 4.23e-118

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 335.58  E-value: 4.23e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  13 DSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTLRH 90
Cdd:PRK01130   1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDypDSEVYITPTLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  91 ARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSE-GAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTEGP 169
Cdd:PRK01130  81 VDALAAAGADIIALDATLRPRPDGETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKKPEEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695830318 170 DYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:PRK01130 161 DFALLKELLK-AVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 11-225 3.43e-102

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: 295.25  E-value: 3.43e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  11 LIDSLHGKLIVSCQAYPGEPMRHPETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTL 88
Cdd:cd04729    3 LLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDypDSEVYITPTI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  89 RHARACIMAGADIVALDATDRPRPDGLTLQQTARQLKSEG-AILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTE 167
Cdd:cd04729   83 EEVDALAAAGADIIALDATDRPRPDGETLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAKTE 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695830318 168 GPDYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITHPMTITSWF 225
Cdd:cd04729  163 DPDFELLKELRK-ALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
 37-231 3.22e-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: 190.34  E-value: 3.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318   37 MAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIGIWKEG--DNGVYITPTLRHARACIMAGADIVALDATDRPRPdg 114
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDlpDSPVRITPFMKDIDELANAGADIIALDGTSRPRP-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  115 LTLQQTARQLKSEGAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTEgPDYELLAQMLErhPHVPVICEGRIHT 194
Cdd:pfam04131  79 VTIEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAE-PDFQLVKTLSE--AGCFVIAEGRYNT 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 695830318  195 PSDAAKAIEMGAWAAVVGTAITHPMTITSWFADAVRS 231
Cdd:pfam04131 156 PELAKKAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 34-213 1.72e-07

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


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 49.89  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  34 PETMAQVAQSVEIGGAAAIRCQGLADISAIKGQVKVPVIG---------IWKEGDNGVYITPTLRHARACIMAGADIVAL 104
Cdd:cd04722   11 SGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKevaaetdlpLGVQLAINDAAAAVDIAAAAARAAGADGVEI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318 105 DATDRPRPDGL--TLQQTARQLKSEGAILMADCGCIEDSDAAVDAGFDIISTTLAGYTDSRAKTEGPDYELLAQMLERHP 182
Cdd:cd04722   91 HGAVGYLAREDleLIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 695830318 183 hVPVICEGRIHTPSDAAKAIEMGAWAAVVGT 213
Cdd:cd04722  171 -VPVIAGGGINDPEDAAEALALGADGVIVGS 200
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 34-214 7.39e-06

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


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 45.55  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318  34 PETMAQVAQSVEIG--GAAAIRCQGLAD-ISAIKGQVKVPV-IGIWKEGDNgvyiTPTLRHARACIMAGADIVALDAtdr 109
Cdd:cd04730   16 PELAAAVSNAGGLGfiGAGYLTPEALRAeIRKIRALTDKPFgVNLLVPSSN----PDFEALLEVALEEGVPVVSFSF--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318 110 prpdGLTLQQTARqLKSEGAILMADCGCIEDSDAAVDAGFDIIS--TTLAGYTdsRAKTEGPDYELLAQMLERHPhVPVI 187
Cdd:cd04730   89 ----GPPAEVVER-LKAAGIKVIPTVTSVEEARKAEAAGADALVaqGAEAGGH--RGTFDIGTFALVPEVRDAVD-IPVI 160

                        170       180
                 ....*....|....*....|....*..
gi 695830318 188 CEGRIHTPSDAAKAIEMGAWAAVVGTA 214
Cdd:cd04730  161 AAGGIADGRGIAAALALGADGVQMGTR 187
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 176-231 2.98e-05

Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).


Pssm-ID: 240079  Cd Length: 248  Bit Score: 43.63  E-value: 2.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695830318 176 QMLERHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITH---PMTITSWFADAVRS 231
Cdd:cd04728  168 RIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAKakdPVAMARAFKLAVEA 226
thiG CHL00162
thiamin biosynthesis protein G; Validated
 184-215 5.01e-05

thiamin biosynthesis protein G; Validated


Pssm-ID: 214380  Cd Length: 267  Bit Score: 43.16  E-value: 5.01e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 695830318 184 VPVICEGRIHTPSDAAKAIEMGAWAAVVGTAI 215
Cdd:CHL00162 190 IPVIIDAGIGTPSEASQAMELGASGVLLNTAV 221
ThiG COG2022
Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and ...
 184-231 8.36e-05

Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) [Coenzyme transport and metabolism]; Thiazole synthase ThiGH, ThiG subunit (thiamin biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441625  Cd Length: 259  Bit Score: 42.33  E-value: 8.36e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695830318 184 VPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITH---PMTITSWFADAVRS 231
Cdd:COG2022  181 VPVIVDAGIGTPSDAAEAMELGADAVLLNTAIARagdPVAMARAFKLAVEA 231
thiG PRK00208
thiazole synthase; Reviewed
 184-230 1.23e-04

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 41.97  E-value: 1.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 695830318 184 VPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITH---PMTITSWFADAVR 230
Cdd:PRK00208 176 VPVIVDAGIGTPSDAAQAMELGADAVLLNTAIAVagdPVAMARAFKLAVE 225
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 176-229 2.47e-04

Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.


Pssm-ID: 428589  Cd Length: 247  Bit Score: 41.08  E-value: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 695830318  176 QMLERHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAITH---PMTITSWFADAV 229
Cdd:pfam05690 168 KIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTAIARakdPVAMARAFKLAV 224
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 143-212 4.50e-04

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. 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. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 40.63  E-value: 4.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695830318 143 AAVDAGFDIISTTLAGYTDSRAKTEGPDYEL-----LAQMLERHPHVPVICEGRIHTPSDAAKAIEMGaWAAVVG 212
Cdd:cd02803  236 ALEEAGVDALHVSGGSYESPPPIIPPPYVPEgyfleLAEKIKKAVKIPVIAVGGIRDPEVAEEILAEG-KADLVA 309
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 159-215 6.22e-04

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: 39.77  E-value: 6.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695830318 159 YTD-SRAKT-EGPDYELLAQMLERHpHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAI 215
Cdd:cd04732  165 YTDiSRDGTlSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKAL 222
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 167-230 8.79e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The 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. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 39.18  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695830318 167 EGPDYELLAQMLERHPHvPVICEGRIHTPSDAAKAIEMGAWAAVVGTAItHPMTITswFADAVR 230
Cdd:cd04723  174 QGPDLELLERLAARADI-PVIAAGGVRSVEDLELLKKLGASGALVASAL-HDGGLT--LEDVVR 233
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 121-214 3.17e-03

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


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 37.78  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318 121 ARQLKSEGAILMADCGCIEDSDAAVDAGFDIISttlagYTDSRA------KTEGPdYELLAQMLErHPHVPVICEGRIHT 194
Cdd:COG2070   97 IERLKEAGIKVIPIVTSVREARKAEKAGADAVV-----AEGAEAgghrgaDEVST-FALVPEVRD-AVDIPVIAAGGIAD 169

                         90       100
                 ....*....|....*....|
gi 695830318 195 PSDAAKAIEMGAWAAVVGTA 214
Cdd:COG2070  170 GRGIAAALALGADGVQMGTR 189
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 159-215 3.75e-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: 3.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 695830318  159 YTD-SRAKT-EGPDYELLAQMLErHPHVPVICEGRIHTPSDAAKAIEMGAWAAVVGTAI 215
Cdd:TIGR00007 164 YTDiSRDGTlSGPNFELTKELVK-AVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 138-215 4.02e-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: 37.58  E-value: 4.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318 138 IEDS----DAAVDAGFDIISTTLAGYTDSRAKtEGPDYELLAQMLERHPH--VPVICEGRIHTPSDAAKAIEMGAWAAVV 211
Cdd:cd04735  234 MEDTlalvDKLADKGLDYLHISLWDFDRKSRR-GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAI 312


                 ....
gi 695830318 212 GTAI 215
Cdd:cd04735  313 GRGL 316
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 138-212 4.90e-03

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: 37.46  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695830318 138 IEDSDAAV----DAGFDIISTTLAGY-TDSRAKTEGPD--YELLAQMLERHPHVPVICEGRIHTPSDAAKAIEMGaWAAV 210
Cdd:COG1902  235 LEESVELAkaleEAGVDYLHVSSGGYePDAMIPTIVPEgyQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASG-DADL 313


                 ..
gi 695830318 211 VG 212
Cdd:COG1902  314 VA 315
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH