|
Name |
Accession |
Description |
Interval |
E-value |
| NanE |
COG3010 |
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]; |
1-215 |
2.26e-92 |
|
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 442247 Cd Length: 226 Bit Score: 270.05 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 1 MRKLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKDR--NYQAFITPTFE 78
Cdd:COG3010 4 LEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDypDSDVYITPTLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 79 HARDVIKAGADFVAIDCTRSERP--VQLKTLFEEIRSSfPDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGCS 156
Cdd:COG3010 84 EVDALAEAGADIIALDATRRPRPdgETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 157 LPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRPWITIKKFVD 215
Cdd:COG3010 163 GPDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVD 221
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
1-213 |
8.64e-70 |
|
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: 212.44 E-value: 8.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 1 MRKLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQA---FITPTF 77
Cdd:cd04729 4 LEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIK-RDYPDsevYITPTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 78 EHARDVIKAGADFVAIDCTRSERPVQ--LKTLFEEIRSSFpDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGC 155
Cdd:cd04729 83 EEVDALAAAGADIIALDATDRPRPDGetLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAKT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 156 SLPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRP-WITiKKF 213
Cdd:cd04729 162 EDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPeHIT-GWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
3-215 |
7.03e-68 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 207.69 E-value: 7.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 3 KLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQA---FITPTFEH 79
Cdd:PRK01130 2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIK-RDYPDsevYITPTLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 80 ARDVIKAGADFVAIDCTRSERP--VQLKTLFEEIRSSfPDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGCSL 157
Cdd:PRK01130 81 VDALAAAGADIIALDATLRPRPdgETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKKPEE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 158 PNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRP-WITiKKFVD 215
Cdd:PRK01130 160 PDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPeEIT-KWFVD 217
|
|
| NanE |
pfam04131 |
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ... |
26-215 |
2.82e-38 |
|
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: 131.40 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 26 IVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQ---AFITPTFEHARDVIKAGADFVAIDCTRSERPV 102
Cdd:pfam04131 1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVK-RDLPdspVRITPFMKDIDELANAGADIIALDGTSRPRPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 103 QLKTLFEEIRSSFpdVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGcSLPNIELVRGLSRKmSIPIIAEGGYTT 182
Cdd:pfam04131 80 TIEDFIKRIKEKG--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP-AEPDFQLVKTLSEA-GCFVIAEGRYNT 155
|
170 180 190
....*....|....*....|....*....|...
gi 500833183 183 LEEVQNAFQNGAYAVVIGTAITRPWITIKKFVD 215
Cdd:pfam04131 156 PELAKKAIEIGADAVTVGSAITRLEHITQWFNN 188
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
34-203 |
6.12e-07 |
|
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: 48.35 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 34 DYAGAVAVRTNNADHVRAVKDSVSIPVI--GLVKDRNYqafitptfehARDVIKAGADFVAIdctrSERPVQLKTLFEEI 111
Cdd:TIGR00007 49 DLDGAKEGGPVNLPVIKKIVRETGVPVQvgGGIRSLED----------VEKLLDLGVDRVII----GTAAVENPDLVKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 RSSFPDVGIIADI------------ADEADAELVSALR-------PDFIAT------TLCGytpytlgcslPNIELVRGL 166
Cdd:TIGR00007 115 LKEYGPERIVVSLdarggevavkgwLEKSEVSLEELAKrleelglEGIIYTdisrdgTLSG----------PNFELTKEL 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 500833183 167 SRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAI 203
Cdd:TIGR00007 185 VKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NanE |
COG3010 |
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism]; |
1-215 |
2.26e-92 |
|
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 442247 Cd Length: 226 Bit Score: 270.05 E-value: 2.26e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 1 MRKLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKDR--NYQAFITPTFE 78
Cdd:COG3010 4 LEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDypDSDVYITPTLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 79 HARDVIKAGADFVAIDCTRSERP--VQLKTLFEEIRSSfPDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGCS 156
Cdd:COG3010 84 EVDALAEAGADIIALDATRRPRPdgETLAELIARIHEE-PGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKGTD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 157 LPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRPWITIKKFVD 215
Cdd:COG3010 163 GPDLELLKELVAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVD 221
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
1-213 |
8.64e-70 |
|
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: 212.44 E-value: 8.64e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 1 MRKLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQA---FITPTF 77
Cdd:cd04729 4 LEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIK-RDYPDsevYITPTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 78 EHARDVIKAGADFVAIDCTRSERPVQ--LKTLFEEIRSSFpDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGC 155
Cdd:cd04729 83 EEVDALAAAGADIIALDATDRPRPDGetLAELIKRIHEEY-NCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEETAKT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 156 SLPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRP-WITiKKF 213
Cdd:cd04729 162 EDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPeHIT-GWF 219
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
3-215 |
7.03e-68 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 207.69 E-value: 7.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 3 KLPRGIIISCQLEPGDPVQDVSFIVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQA---FITPTFEH 79
Cdd:PRK01130 2 QLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIK-RDYPDsevYITPTLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 80 ARDVIKAGADFVAIDCTRSERP--VQLKTLFEEIRSSfPDVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGCSL 157
Cdd:PRK01130 81 VDALAAAGADIIALDATLRPRPdgETLAELVKRIKEY-PGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEETKKPEE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 158 PNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRP-WITiKKFVD 215
Cdd:PRK01130 160 PDFALLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPeEIT-KWFVD 217
|
|
| NanE |
pfam04131 |
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ... |
26-215 |
2.82e-38 |
|
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: 131.40 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 26 IVNMARSADYAGAVAVRTNNADHVRAVKDSVSIPVIGLVKdRNYQ---AFITPTFEHARDVIKAGADFVAIDCTRSERPV 102
Cdd:pfam04131 1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVK-RDLPdspVRITPFMKDIDELANAGADIIALDGTSRPRPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 103 QLKTLFEEIRSSFpdVGIIADIADEADAELVSALRPDFIATTLCGYTPYTLGcSLPNIELVRGLSRKmSIPIIAEGGYTT 182
Cdd:pfam04131 80 TIEDFIKRIKEKG--CLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENP-AEPDFQLVKTLSEA-GCFVIAEGRYNT 155
|
170 180 190
....*....|....*....|....*....|...
gi 500833183 183 LEEVQNAFQNGAYAVVIGTAITRPWITIKKFVD 215
Cdd:pfam04131 156 PELAKKAIEIGADAVTVGSAITRLEHITQWFNN 188
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
33-203 |
7.32e-11 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 59.80 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 33 ADYAGAVAVRTNNADHVRAVKDSVSIPVI--GLVKDRnyqafitptfEHARDVIKAGADFVAIdctrSERPVQLKTLFEE 110
Cdd:pfam00977 49 VDLDAAKEGRPVNLDVVEEIAEEVFIPVQvgGGIRSL----------EDVERLLSAGADRVII----GTAAVKNPELIKE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 111 IRSSFPDVGIIADI------------ADEADAELVSALR-------PDFIAT------TLCGytpytlgcslPNIELVRG 165
Cdd:pfam00977 115 AAEKFGSQCIVVAIdarrgkvaingwREDTGIDAVEWAKeleelgaGEILLTdidrdgTLSG----------PDLELTRE 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 500833183 166 LSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAI 203
Cdd:pfam00977 185 LAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
|
|
| HisA |
COG0106 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ... |
37-203 |
2.12e-09 |
|
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: 55.43 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 37 GAVAVRTNNADHVRAVKDSVSIPV-----IglvkdRnyqafitpTFEHARDVIKAGADFVAIdctrSERPVQLKTLFEEI 111
Cdd:COG0106 53 GAFAGKPVNLELIEEIAKATGLPVqvgggI-----R--------SLEDIERLLDAGASRVIL----GTAAVKDPELVKEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 RSSFPD---VGI------IA-----DIADEADAELVSALRPDFIATTLC------GytpyTL-GcslPNIELVRGLSRKM 170
Cdd:COG0106 116 LEEFPErivVGLdardgkVAtdgwqETSGVDLEELAKRFEDAGVAAILYtdisrdG----TLqG---PNLELYRELAAAT 188
|
170 180 190
....*....|....*....|....*....|...
gi 500833183 171 SIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAI 203
Cdd:COG0106 189 GIPVIASGGVSSLDDLRALKELGVEGAIVGKAL 221
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
37-203 |
3.23e-09 |
|
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: 55.18 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 37 GAVAVRTNNADHVRAVKDSVSIPV-----IglvkdRNYQAfitptfehARDVIKAGADFVAIdctrSERPVQLKTLFEEI 111
Cdd:cd04732 53 GAKGGEPVNLELIEEIVKAVGIPVqvgggI-----RSLED--------IERLLDLGVSRVII----GTAAVKNPELVKEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 RSSFPDVGIIADIadeaDA-------------------ELVSALRPDFIATTLC------GytpyTLgcSLPNIELVRGL 166
Cdd:cd04732 116 LKEYGGERIVVGL----DAkdgkvatkgwletsevsleELAKRFEELGVKAIIYtdisrdG----TL--SGPNFELYKEL 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 500833183 167 SRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAI 203
Cdd:cd04732 186 AAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKAL 222
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
49-201 |
3.93e-08 |
|
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: 51.82 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 49 VRAVKDSVSIPVIGLVKDRNYQAfitPTFEHARDVIKAGADFVAIDCTRSERPVQLKTLFEEIRSSFPDVGIIADIA--D 126
Cdd:cd04722 49 LKEVAAETDLPLGVQLAINDAAA---AVDIAAAAARAAGADGVEIHGAVGYLAREDLELIRELREAVPDVKVVVKLSptG 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500833183 127 EADAELVSALRPDFIATTLCGYTPYTLGCSLPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGT 201
Cdd:cd04722 126 ELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
34-212 |
9.85e-08 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 51.06 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 34 DYAGAVAVRTNNADHVRAVKDSVSIPVI--GLVKdrnyqafitpTFEHARDVIKAGADFVAIDCTRSERPVQLKTLFEEI 111
Cdd:PRK13585 53 DLDGAFEGERKNAEAIEKIIEAVGVPVQlgGGIR----------SAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 RSSFPDVGIiadiaDEADAELVsalrpdfIA--TTLCGYTPYTLG--------CSL-------------PNIELVRGLSR 168
Cdd:PRK13585 123 GSERVMVSL-----DAKDGEVV-------IKgwTEKTGYTPVEAAkrfeelgaGSIlftnvdvegllegVNTEPVKELVD 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500833183 169 KMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAITRPWITIKK 212
Cdd:PRK13585 191 SVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEE 234
|
|
| TIGR00007 |
TIGR00007 |
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ... |
34-203 |
6.12e-07 |
|
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: 48.35 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 34 DYAGAVAVRTNNADHVRAVKDSVSIPVI--GLVKDRNYqafitptfehARDVIKAGADFVAIdctrSERPVQLKTLFEEI 111
Cdd:TIGR00007 49 DLDGAKEGGPVNLPVIKKIVRETGVPVQvgGGIRSLED----------VEKLLDLGVDRVII----GTAAVENPDLVKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 RSSFPDVGIIADI------------ADEADAELVSALR-------PDFIAT------TLCGytpytlgcslPNIELVRGL 166
Cdd:TIGR00007 115 LKEYGPERIVVSLdarggevavkgwLEKSEVSLEELAKrleelglEGIIYTdisrdgTLSG----------PNFELTKEL 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 500833183 167 SRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTAI 203
Cdd:TIGR00007 185 VKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
76-201 |
1.09e-06 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 48.28 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 76 TFEHARDVIKAGADFVAIDCTR--SERPVQLKtlfEEIRSSFPDVGIIA-DIAD-EADAELVSA----LR----PDFIAT 143
Cdd:cd00381 95 DKERAEALVEAGVDVIVIDSAHghSVYVIEMI---KFIKKKYPNVDVIAgNVVTaEAARDLIDAgadgVKvgigPGSICT 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500833183 144 TLcgytpYTLGCSLPNIELVRGLS---RKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGT 201
Cdd:cd00381 172 TR-----IVTGVGVPQATAVADVAaaaRDYGVPVIADGGIRTSGDIVKALAAGADAVMLGS 227
|
|
| PRK00748 |
PRK00748 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ... |
37-203 |
3.06e-06 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated
Pssm-ID: 179108 Cd Length: 233 Bit Score: 46.60 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 37 GAVAVRTNNADHVRAVKDSVSIPV-----IglvkdRnyqafitpTFEHARDVIKAGADFVAIDCTRSERPVQLKTLFEEi 111
Cdd:PRK00748 54 GAKAGKPVNLELIEAIVKAVDIPVqvgggI-----R--------SLETVEALLDAGVSRVIIGTAAVKNPELVKEACKK- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 112 rssFPD---VGIIA-------------------DIADE-ADAELVSALRPDfIAT--TLCGytpytlgcslPNIELVRGL 166
Cdd:PRK00748 120 ---FPGkivVGLDArdgkvatdgwletsgvtaeDLAKRfEDAGVKAIIYTD-ISRdgTLSG----------PNVEATREL 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 500833183 167 SRKMSIPIIAEGGYTTLEEVQNAFQNGA-YAVVIGTAI 203
Cdd:PRK00748 186 AAAVPIPVIASGGVSSLDDIKALKGLGAvEGVIVGRAL 223
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
18-200 |
6.99e-05 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 42.32 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 18 DPVQDVSFIVNMARSADYAG--AVAVRTNNADHVRAVKDSVSIPVIGLVKDRNYQAFITPTFEHARDVIKAGADFVAIDC 95
Cdd:cd00945 7 HPDATLEDIAKLCDEAIEYGfaAVCVNPGYVRLAADALAGSDVPVIVVVGFPTGLTTTEVKVAEVEEAIDLGADEIDVVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 96 TR-SERPVQLKTLFEEIRSSF-------PDVGIIADIADEADAELVSALR------PDFIATtlcGYTPYTLGCSLPNIE 161
Cdd:cd00945 87 NIgSLKEGDWEEVLEEIAAVVeaadgglPLKVILETRGLKTADEIAKAARiaaeagADFIKT---STGFGGGGATVEDVK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 500833183 162 LVRGLSRKmSIPIIAEGGYTTLEEVQNAFQNGAYAVVIG 200
Cdd:cd00945 164 LMKEAVGG-RVGVKAAGGIKTLEDALAAIEAGADGIGTS 201
|
|
| HisF |
cd04731 |
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ... |
158-217 |
1.09e-04 |
|
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). 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: 240082 Cd Length: 243 Bit Score: 42.07 E-value: 1.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500833183 158 PNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGT-AITRPWItIKKFVDLF 217
Cdd:cd04731 58 TMLDVVERVAEEVFIPLTVGGGIRSLEDARRLLRAGADKVSINSaAVENPEL-IREIAKRF 117
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
76-200 |
1.25e-04 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 42.33 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 76 TFEHARDVIKAGADFVAIDCTR--SERPVQLktlFEEIRSSFPDVGIIAD--IADEADAELVSA----LRPDFIATTLCG 147
Cdd:PRK06843 154 TIERVEELVKAHVDILVIDSAHghSTRIIEL---VKKIKTKYPNLDLIAGniVTKEAALDLISVgadcLKVGIGPGSICT 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 500833183 148 yTPYTLGCSLPNIEL---VRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIG 200
Cdd:PRK06843 231 -TRIVAGVGVPQITAicdVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIG 285
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
78-208 |
5.28e-04 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 40.08 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 78 EHARDVIKAGADFVAIdctrserPVQLKT--LFEEIRSSFPDvgiIADIADEADAelvsalrpDFIA----TTLCGYTPy 151
Cdd:COG0042 116 ELVAEIVKAVVEAVDV-------PVTVKIrlGWDDDDENALE---FARIAEDAGA--------AALTvhgrTREQRYKG- 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 500833183 152 tlgcsLPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQN-GAYAVVIG-TAITRPWI 208
Cdd:COG0042 177 -----PADWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEEtGCDGVMIGrGALGNPWL 230
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
44-203 |
1.58e-03 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 38.56 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 44 NNADHVRAVKDSVSIPVIglvkdrnyqAFITPTF----EHARDVIKAGAD-FVAIDCTRserpvqlktlfeeirssfpdv 118
Cdd:TIGR01037 144 LSADVVKAVKDKTDVPVF---------AKLSPNVtditEIAKAAEEAGADgLTLINTLR--------------------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 119 GIIADIadeadaelvSALRPdfIATTLCGytpytlGCSLPNIE-----LVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNG 193
Cdd:TIGR01037 194 GMKIDI---------KTGKP--ILANKTG------GLSGPAIKpialrMVYDVYKMVDIPIIGVGGITSFEDALEFLMAG 256
|
170
....*....|
gi 500833183 194 AYAVVIGTAI 203
Cdd:TIGR01037 257 ASAVQVGTAV 266
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
121-208 |
1.86e-03 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 38.46 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500833183 121 IADIADEADAELVsalrpdfiatTLCGYTPYTLGCSLPNIELVRGLSRKMSIPIIAEGGYTTLEEVQNAF-QNGAYAVVI 199
Cdd:pfam01207 143 IAKIVEDAGAQAL----------TVHGRTRAQNYEGTADWDAIKQVKQAVSIPVIANGDITDPEDAQRCLaYTGADGVMI 212
|
90
....*....|
gi 500833183 200 G-TAITRPWI 208
Cdd:pfam01207 213 GrGALGNPWL 222
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
76-135 |
2.68e-03 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 38.14 E-value: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500833183 76 TFEHARDVIKAGADFVAIDCTR--SERpvQLKTLfEEIRSSFPDVGIIA-DIAD-EADAELVSA 135
Cdd:pfam00478 221 TLERAEALVEAGVDVLVVDTAHghSKG--VIDTV-KWIKKKYPDVQVIAgNVATaEGAKALIEA 281
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
159-206 |
3.10e-03 |
|
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.
Pssm-ID: 425971 Cd Length: 228 Bit Score: 37.46 E-value: 3.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500833183 159 NIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGT-AITRP 206
Cdd:pfam00977 61 NLDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTaAVKNP 109
|
|
| HisA |
cd04732 |
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ... |
159-206 |
3.12e-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: 37.46 E-value: 3.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500833183 159 NIELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGT-AITRP 206
Cdd:cd04732 61 NLELIEEIVKAVGIPVQVGGGIRSLEDIERLLDLGVSRVIIGTaAVKNP 109
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
161-202 |
5.82e-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: 5.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 500833183 161 ELVRGLSRKMSIPIIAEGGYTTLEEVQNAFQNGAYAVVIGTA 202
Cdd:cd04730 146 ALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTR 187
|
|
| |
