|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07226 |
PRK07226 |
fructose-bisphosphate aldolase; Provisional |
1-250 |
2.84e-118 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 235973 [Multi-domain] Cd Length: 267 Bit Score: 339.09 E-value: 2.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 1 MSLGKNYRLARILKGLD-NYFIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHL 79
Cdd:PRK07226 2 MNIGKRIRLERIFNRRTgRTVIVPMDHGVSHGPIDGLVDIRDTVNKVAEGGADAVLMHKGLARHGHRGY-GRDVGLIVHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 80 SGSTNLSPDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDAD 159
Cdd:PRK07226 81 SASTSLSPDPNDKVLVGTVEEAIKLGADAVSVHVNVGSETEAEMLEDLGEVAEECEEWGMPLLAMMYPRGPGIKNEYDPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 160 AIAHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:PRK07226 161 VVAHAARVAAELGADIVKTNYTGDPESFREVVEGCPVPVVIAGGPKTDTDREFLEMVRDAMEAGAAGVAVGRNVFQHEDP 240
|
250
....*....|.
gi 495460700 240 SFISQEIAKVI 250
Cdd:PRK07226 241 EAITRAISAVV 251
|
|
| FbaB |
COG1830 |
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ... |
2-250 |
1.12e-112 |
|
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 441435 [Multi-domain] Cd Length: 259 Bit Score: 324.39 E-value: 1.12e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 2 SLGKNYRLARILKGLDNY-FIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLS 80
Cdd:COG1830 1 DMGKKIRLSRIFNAGTGRlVIVAVDHGVEHGPNPGLEDPEEIVRLAAEGGADAVALTKGILERLARKY-ARDIPLILKLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 81 GSTNLS-PDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDAD 159
Cdd:COG1830 80 GSTSLGyPDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPYPRGPAVKDETDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 160 AIAHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:COG1830 160 LVAHAARIAAELGADIVKTKYPGDPESFREVVAACPVPVVIAGGPKTPDDEDFLEMVRDAIDAGAAGVAVGRNIFQRPNP 239
|
250
....*....|.
gi 495460700 240 SFISQEIAKVI 250
Cdd:COG1830 240 EAMLRAISAIV 250
|
|
| AroFGH_arch |
TIGR01949 |
predicted phospho-2-dehydro-3-deoxyheptonate aldolase; This model represents a clade of ... |
3-250 |
1.65e-95 |
|
predicted phospho-2-dehydro-3-deoxyheptonate aldolase; This model represents a clade of sequences related to fructose-bisphosphate aldolase (class I, included within pfam01791). The members of this clade appear to be phospho-2-dehydro-3-deoxyheptonate aldolases. This enzyme is the first step of the chorismate biosynthesis pathway. Evidence for this assignment is based on gene clustering and phylogenetic profiling. A group of species lack members of the three other types of phospho-2-dehydro-3-deoxyheptonate aldolase (represented by TIGR00034, TIGR01358 and TIGR01361), and also aparrently lack the well-known forms of step 2 (3-dehydroquinate synthase), but contain all other steps of the pathway: Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium, Methanopyrus, Methanococcus and Methanobacterium. The clade of sequences represented here is limited strictly to this group of organisms. In Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium and Methanosarcina the genes found by this model are clustered with other genes from the chorismate, phenylalanine, tyrosine and tryptophan biosynthesis pathways. In addition, these genes in Desulfovibrio, Archaeoglobus, Halobacterium, Methanosarcina and Methanopyrus are adjacent to a gene which hits pfam01959 which also has the property of having members only in those species which lack steps 1 and 2. Together these two genes appear to perform the synthesis of 3-dehydroquinate. It is presumed that the substrates and the chemical transformations involved are identical, but this has not yet been proven experimentally.
Pssm-ID: 273890 [Multi-domain] Cd Length: 258 Bit Score: 280.98 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 3 LGKNYRLARILKGLDN-YFIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLSG 81
Cdd:TIGR01949 1 LGKLVRLERIFNRESGrTVIVPMDHGVSNGPIKGLVDIRKTVNEVAEGGADAVLLHKGIVRRGHRGY-GKDVGLIIHLSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 82 STNLSPDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKnEYDADAI 161
Cdd:TIGR01949 80 STSLSPDPNDKRIVTTVEDAIRMGADAVSIHVNVGSDTEWEQIRDLGMIAEICDDWGVPLLAMMYPRGPHID-DRDPELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 162 AHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNPSF 241
Cdd:TIGR01949 159 AHAARLGAELGADIVKTPYTGDIDSFRDVVKGCPAPVVVAGGPKTNSDREFLQMIKDAMEAGAAGVAVGRNIFQHDDPVG 238
|
....*....
gi 495460700 242 ISQEIAKVI 250
Cdd:TIGR01949 239 ITKAVCKIV 247
|
|
| DhnA |
cd00958 |
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ... |
20-250 |
5.94e-93 |
|
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.
Pssm-ID: 188645 [Multi-domain] Cd Length: 235 Bit Score: 273.70 E-value: 5.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 20 FIVPIDHGFTL--GPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGlIQKDISLILHLSGSTNLSP-DPSSKHLVS 96
Cdd:cd00958 2 VILAVDHGIEHgfGPNPGLEDPEETVKLAAEGGADAVALTKGIARAYGRE-YAGDIPLIVKLNGSTSLSPkDDNDKVLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 97 SVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDADAIAHSTRLAWELGADIV 176
Cdd:cd00958 81 SVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVKNEKDPDLIAYAARIGAELGADIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495460700 177 KVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNPSFISQEIAKVI 250
Cdd:cd00958 161 KTKYTGDAESFKEVVEGCPVPVVIAGGPKKDSEEEFLKMVYDAMEAGAAGVAVGRNIFQRPDPVAMLRAISAVV 234
|
|
| DeoC |
pfam01791 |
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ... |
21-236 |
7.96e-56 |
|
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.
Pssm-ID: 460332 Cd Length: 230 Bit Score: 178.74 E-value: 7.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 21 IVPIDHGFTLGPV--SGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLSGSTNLSPDPSSKHL-VSS 97
Cdd:pfam01791 3 ILAMDQGVANGPDfaFALEDPKVLVAEAATPGANAVLLDPGFIARAHRGY-GKDIGLIVALNHGTDLIPINGRDVDcVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 98 VEQAIKLGADGVSIHVN---LGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDADAIAHSTRLAWELGAD 174
Cdd:pfam01791 82 VEEAKAMGADAVKVVVYyrvDGSEEEQQMLDEIGRVKEDCHEWGMPLILEGYLRGEAIKDEKDPDLVADAARLGAELGAD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495460700 175 IVKVNYT--------GDVQSFKQVVNAVDIP-VIVAGGAKSNAdssILSMIKDA-IKAGGKGVAVGRNIFQH 236
Cdd:pfam01791 162 IVKVSYPknmknageEDADVFKRVIKAAPVPyVVLAGGVSEED---FLRTVRDAmIEAGAMGVSSGRNIFQK 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07226 |
PRK07226 |
fructose-bisphosphate aldolase; Provisional |
1-250 |
2.84e-118 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 235973 [Multi-domain] Cd Length: 267 Bit Score: 339.09 E-value: 2.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 1 MSLGKNYRLARILKGLD-NYFIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHL 79
Cdd:PRK07226 2 MNIGKRIRLERIFNRRTgRTVIVPMDHGVSHGPIDGLVDIRDTVNKVAEGGADAVLMHKGLARHGHRGY-GRDVGLIVHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 80 SGSTNLSPDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDAD 159
Cdd:PRK07226 81 SASTSLSPDPNDKVLVGTVEEAIKLGADAVSVHVNVGSETEAEMLEDLGEVAEECEEWGMPLLAMMYPRGPGIKNEYDPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 160 AIAHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:PRK07226 161 VVAHAARVAAELGADIVKTNYTGDPESFREVVEGCPVPVVIAGGPKTDTDREFLEMVRDAMEAGAAGVAVGRNVFQHEDP 240
|
250
....*....|.
gi 495460700 240 SFISQEIAKVI 250
Cdd:PRK07226 241 EAITRAISAVV 251
|
|
| FbaB |
COG1830 |
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ... |
2-250 |
1.12e-112 |
|
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 441435 [Multi-domain] Cd Length: 259 Bit Score: 324.39 E-value: 1.12e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 2 SLGKNYRLARILKGLDNY-FIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLS 80
Cdd:COG1830 1 DMGKKIRLSRIFNAGTGRlVIVAVDHGVEHGPNPGLEDPEEIVRLAAEGGADAVALTKGILERLARKY-ARDIPLILKLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 81 GSTNLS-PDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDAD 159
Cdd:COG1830 80 GSTSLGyPDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPYPRGPAVKDETDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 160 AIAHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:COG1830 160 LVAHAARIAAELGADIVKTKYPGDPESFREVVAACPVPVVIAGGPKTPDDEDFLEMVRDAIDAGAAGVAVGRNIFQRPNP 239
|
250
....*....|.
gi 495460700 240 SFISQEIAKVI 250
Cdd:COG1830 240 EAMLRAISAIV 250
|
|
| AroFGH_arch |
TIGR01949 |
predicted phospho-2-dehydro-3-deoxyheptonate aldolase; This model represents a clade of ... |
3-250 |
1.65e-95 |
|
predicted phospho-2-dehydro-3-deoxyheptonate aldolase; This model represents a clade of sequences related to fructose-bisphosphate aldolase (class I, included within pfam01791). The members of this clade appear to be phospho-2-dehydro-3-deoxyheptonate aldolases. This enzyme is the first step of the chorismate biosynthesis pathway. Evidence for this assignment is based on gene clustering and phylogenetic profiling. A group of species lack members of the three other types of phospho-2-dehydro-3-deoxyheptonate aldolase (represented by TIGR00034, TIGR01358 and TIGR01361), and also aparrently lack the well-known forms of step 2 (3-dehydroquinate synthase), but contain all other steps of the pathway: Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium, Methanopyrus, Methanococcus and Methanobacterium. The clade of sequences represented here is limited strictly to this group of organisms. In Desulfovibrio, Aquifex, Archaeoglobus, Halobacterium and Methanosarcina the genes found by this model are clustered with other genes from the chorismate, phenylalanine, tyrosine and tryptophan biosynthesis pathways. In addition, these genes in Desulfovibrio, Archaeoglobus, Halobacterium, Methanosarcina and Methanopyrus are adjacent to a gene which hits pfam01959 which also has the property of having members only in those species which lack steps 1 and 2. Together these two genes appear to perform the synthesis of 3-dehydroquinate. It is presumed that the substrates and the chemical transformations involved are identical, but this has not yet been proven experimentally.
Pssm-ID: 273890 [Multi-domain] Cd Length: 258 Bit Score: 280.98 E-value: 1.65e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 3 LGKNYRLARILKGLDN-YFIVPIDHGFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLSG 81
Cdd:TIGR01949 1 LGKLVRLERIFNRESGrTVIVPMDHGVSNGPIKGLVDIRKTVNEVAEGGADAVLLHKGIVRRGHRGY-GKDVGLIIHLSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 82 STNLSPDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKnEYDADAI 161
Cdd:TIGR01949 80 STSLSPDPNDKRIVTTVEDAIRMGADAVSIHVNVGSDTEWEQIRDLGMIAEICDDWGVPLLAMMYPRGPHID-DRDPELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 162 AHSTRLAWELGADIVKVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNPSF 241
Cdd:TIGR01949 159 AHAARLGAELGADIVKTPYTGDIDSFRDVVKGCPAPVVVAGGPKTNSDREFLQMIKDAMEAGAAGVAVGRNIFQHDDPVG 238
|
....*....
gi 495460700 242 ISQEIAKVI 250
Cdd:TIGR01949 239 ITKAVCKIV 247
|
|
| DhnA |
cd00958 |
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ... |
20-250 |
5.94e-93 |
|
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.
Pssm-ID: 188645 [Multi-domain] Cd Length: 235 Bit Score: 273.70 E-value: 5.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 20 FIVPIDHGFTL--GPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGlIQKDISLILHLSGSTNLSP-DPSSKHLVS 96
Cdd:cd00958 2 VILAVDHGIEHgfGPNPGLEDPEETVKLAAEGGADAVALTKGIARAYGRE-YAGDIPLIVKLNGSTSLSPkDDNDKVLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 97 SVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDADAIAHSTRLAWELGADIV 176
Cdd:cd00958 81 SVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVKNEKDPDLIAYAARIGAELGADIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495460700 177 KVNYTGDVQSFKQVVNAVDIPVIVAGGAKSNADSSILSMIKDAIKAGGKGVAVGRNIFQHSNPSFISQEIAKVI 250
Cdd:cd00958 161 KTKYTGDAESFKEVVEGCPVPVVIAGGPKKDSEEEFLKMVYDAMEAGAAGVAVGRNIFQRPDPVAMLRAISAVV 234
|
|
| DeoC |
pfam01791 |
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ... |
21-236 |
7.96e-56 |
|
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.
Pssm-ID: 460332 Cd Length: 230 Bit Score: 178.74 E-value: 7.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 21 IVPIDHGFTLGPV--SGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLiQKDISLILHLSGSTNLSPDPSSKHL-VSS 97
Cdd:pfam01791 3 ILAMDQGVANGPDfaFALEDPKVLVAEAATPGANAVLLDPGFIARAHRGY-GKDIGLIVALNHGTDLIPINGRDVDcVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 98 VEQAIKLGADGVSIHVN---LGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGEKIKNEYDADAIAHSTRLAWELGAD 174
Cdd:pfam01791 82 VEEAKAMGADAVKVVVYyrvDGSEEEQQMLDEIGRVKEDCHEWGMPLILEGYLRGEAIKDEKDPDLVADAARLGAELGAD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495460700 175 IVKVNYT--------GDVQSFKQVVNAVDIP-VIVAGGAKSNAdssILSMIKDA-IKAGGKGVAVGRNIFQH 236
Cdd:pfam01791 162 IVKVSYPknmknageEDADVFKRVIKAAPVPyVVLAGGVSEED---FLRTVRDAmIEAGAMGVSSGRNIFQK 230
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
24-230 |
3.76e-36 |
|
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: 127.44 E-value: 3.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 24 IDHgFTLGPVSGLAKVHQFIRSLPEKTISAIVAHQGIARAIHPGLIQKDISLILHLSGSTNLSPDpssKHLVSSVEQAIK 103
Cdd:cd00945 1 IDL-TLLHPDATLEDIAKLCDEAIEYGFAAVCVNPGYVRLAADALAGSDVPVIVVVGFPTGLTTT---EVKVAEVEEAID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 104 LGADGVSIHVNLGA---NDEYRMLKDFSQISAAChQWGMPLLAMVYARGEKikneyDADAIAHSTRLAWELGADIVKVNY 180
Cdd:cd00945 77 LGADEIDVVINIGSlkeGDWEEVLEEIAAVVEAA-DGGLPLKVILETRGLK-----TADEIAKAARIAAEAGADFIKTST 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495460700 181 T-----GDVQSFKQVVNAV--DIPVIVAGGAKSNADssilsmIKDAIKAGGKGVAVG 230
Cdd:cd00945 151 GfggggATVEDVKLMKEAVggRVGVKAAGGIKTLED------ALAAIEAGADGIGTS 201
|
|
| PRK08227 |
PRK08227 |
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase; |
1-250 |
7.48e-36 |
|
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;
Pssm-ID: 181306 [Multi-domain] Cd Length: 264 Bit Score: 128.23 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 1 MSLGKNYRLARILKGLDNYFIV-PIDHGFTLGPVSGLAKVHQFIRSLPEKTiSAIVAHQGIARAIHPGLIQKdiSLILHL 79
Cdd:PRK08227 5 LDWGMKNRLSRIFNPKTGRTVMlAFDHGYFQGPTTGLERIDINIAPLFPYA-DVLMCTRGILRSVVPPATNK--PVVLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 80 SGSTNLSPDPSSKHLVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAmVYARGEKIKNeyDAD 159
Cdd:PRK08227 82 SGGNSILKELSNEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYGMPVMA-VTAVGKDMVR--DAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 160 AIAHSTRLAWELGADIVKVNYTGDvqSFKQVVNAVDIPVIVAGGAK-SNADSsiLSMIKDAIKAGGKGVAVGRNIFQHSN 238
Cdd:PRK08227 159 YFSLATRIAAEMGAQIIKTYYVEE--GFERITAGCPVPIVIAGGKKlPERDA--LEMCYQAIDEGASGVDMGRNIFQSEH 234
|
250
....*....|..
gi 495460700 239 PSFISQEIAKVI 250
Cdd:PRK08227 235 PVAMIKAVHAVV 246
|
|
| PRK06852 |
PRK06852 |
aldolase; Validated |
71-237 |
9.59e-20 |
|
aldolase; Validated
Pssm-ID: 180731 Cd Length: 304 Bit Score: 86.20 E-value: 9.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 71 KDISLILHLSGSTNLSP----DPSSKHLVSsVEQAIKL----GAD--GVSIHVNLGANDEYRMLKDFSQISAACHQWGMP 140
Cdd:PRK06852 91 PDVPYLVKLNSKTNLVKtsqrDPLSRQLLD-VEQVVEFkensGLNilGVGYTIYLGSEYESEMLSEAAQIIYEAHKHGLI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 141 LLAMVYARGEKIKNEYDADAIAHSTRLAWELGADIVKVNY-----TGDVQSFKQVVNAV-DIPVIVAGGAKSNADsSILS 214
Cdd:PRK06852 170 AVLWIYPRGKAVKDEKDPHLIAGAAGVAACLGADFVKVNYpkkegANPAELFKEAVLAAgRTKVVCAGGSSTDPE-EFLK 248
|
170 180
....*....|....*....|....
gi 495460700 215 MIKDAIKAGG-KGVAVGRNIFQHS 237
Cdd:PRK06852 249 QLYEQIHISGaSGNATGRNIHQKP 272
|
|
| PRK09250 |
PRK09250 |
class I fructose-bisphosphate aldolase; |
73-235 |
6.76e-13 |
|
class I fructose-bisphosphate aldolase;
Pssm-ID: 236431 Cd Length: 348 Bit Score: 67.24 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 73 ISLILHLSGSTNLSPdPSSKH--LVSSVEQAIKLGADGVSIHVNLGANDEYRMLKDFSQISAACHQWGMPLLAMVYARGE 150
Cdd:PRK09250 126 IPFILKLNHNELLSY-PNTYDqaLTASVEDALRLGAVAVGATIYFGSEESRRQIEEISEAFEEAHELGLATVLWSYLRNS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 151 KIKNEYD----ADAIAHSTRLAWELGADIVKVNYTGDVQSFK--------------------------QVVNAVD--IPV 198
Cdd:PRK09250 205 AFKKDGDyhtaADLTGQANHLAATIGADIIKQKLPTNNGGYKainfgktddrvyskltsdhpidlvryQVANCYMgrRGL 284
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495460700 199 IVAGGAkSNADSSILSMIKDAI---KAGGKGVAVGRNIFQ 235
Cdd:PRK09250 285 INSGGA-SKGEDDLLDAVRTAVinkRAGGMGLIIGRKAFQ 323
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
98-253 |
4.51e-07 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 50.40 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 98 VEQAIKLGADGVSIhvnLGANDEyRMLKDfsQISAAcHQWGMPLLAmvyargEKIKNEydaDAIAHSTRLAwELGADIVK 177
Cdd:PRK07028 74 VEMAAKAGADIVCI---LGLADD-STIED--AVRAA-RKYGVRLMA------DLINVP---DPVKRAVELE-ELGVDYIN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 178 VNYTGDVQS--------FKQVVNAVDIPVIVAGGAksNADSSilsmiKDAIKAGGKGVAVGRNIFQHSNPSFISQEIAKV 249
Cdd:PRK07028 137 VHVGIDQQMlgkdplelLKEVSEEVSIPIAVAGGL--DAETA-----AKAVAAGADIVIVGGNIIKSADVTEAARKIREA 209
|
....
gi 495460700 250 ISNP 253
Cdd:PRK07028 210 IDSG 213
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
184-250 |
1.16e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 45.01 E-value: 1.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495460700 184 VQSFKQVVNAVDIPVIVAGGAKSNAdssilsmIKDAIKAGGKGVAVGRNIFQHSNPSFISQEIAKVI 250
Cdd:PRK07695 138 LEELSDIARALSIPVIAIGGITPEN-------TRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESI 197
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
86-239 |
1.01e-04 |
|
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: 42.12 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 86 SPDPSSKHLVSSVEQAIKLGADGVSI-HVNLGANDEYRMLKdfsQISAACHQWGMPL-------LAMVY-ARG------- 149
Cdd:cd00564 6 DRRLDGEDLLEVVEAALKGGVTLVQLrEKDLSARELLELAR---ALRELCRKYGVPLiindrvdLALAVgADGvhlgqdd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 150 ---EKIKNEYDADAI----AHST---RLAWELGADIV----------KVNYTG--DVQSFKQVVNAVDIPVIVAGGakSN 207
Cdd:cd00564 83 lpvAEARALLGPDLIigvsTHSLeeaLRAEELGADYVgfgpvfptptKPGAGPplGLELLREIAELVEIPVVAIGG--IT 160
|
170 180 190
....*....|....*....|....*....|..
gi 495460700 208 ADSsilsmIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:cd00564 161 PEN-----AAEVLAAGADGVAVISAITGADDP 187
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
98-231 |
1.52e-04 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 41.80 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 98 VEQAIKLGADGVSIHVNLGandeYRMLKDFSQISAACHQW-GMPLLAMVYARGEkikneyDADAIAHstrlawELGADIV 176
Cdd:cd04722 77 AAAARAAGADGVEIHGAVG----YLAREDLELIRELREAVpDVKVVVKLSPTGE------LAAAAAE------EAGVDEV 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495460700 177 KVNYTGDVQSF-----------KQVVNAVDIPVIVAGGAKSNADssilsmIKDAIKAGGKGVAVGR 231
Cdd:cd04722 141 GLGNGGGGGGGrdavpiadlllILAKRGSKVPVIAGGGINDPED------AAEALALGADGVIVGS 200
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
138-233 |
2.53e-04 |
|
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: 41.02 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 138 GMPLLAMVyargEKIKNEYDADAIAH-ST----RLAWELGADIVK---VNYTG--------DVQSFKQVVNAVDIPVIVA 201
Cdd:cd04729 108 GETLAELI----KRIHEEYNCLLMADiSTleeaLNAAKLGFDIIGttlSGYTEetaktedpDFELLKELRKALGIPVIAE 183
|
90 100 110
....*....|....*....|....*....|..
gi 495460700 202 GGAKSNAdssilsMIKDAIKAGGKGVAVGRNI 233
Cdd:cd04729 184 GRINSPE------QAAKALELGADAVVVGSAI 209
|
|
| His_biosynth |
pfam00977 |
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ... |
95-231 |
1.85e-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: 38.61 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 95 VSSVEQAIKLGADGVSIhvNLGAndeyrmLKDFSQISAACHQWGMPLLA--------MVYARGEKIKNEYDADAIAHstR 166
Cdd:pfam00977 85 LEDVERLLSAGADRVII--GTAA------VKNPELIKEAAEKFGSQCIVvaidarrgKVAINGWREDTGIDAVEWAK--E 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495460700 167 LAwELGA------DIVKVnytG-----DVQSFKQVVNAVDIPVIVAGGAKSNADssilsmIKDAIKAGGKGVAVGR 231
Cdd:pfam00977 155 LE-ELGAgeilltDIDRD---GtlsgpDLELTRELAEAVNIPVIASGGVGSLED------LKELFTEGVDGVIAGS 220
|
|
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
84-230 |
4.31e-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: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 84 NLSPDPSSKHLVSSVEQAIKLGADGVSIHvnLGANDEYrmlkdfsqiSAACHQWGMPLLAMVYARgekikneydADAiah 163
Cdd:COG2070 61 NLIVHPANPRFEELLEVVLEEGVPVVSTS--AGLPADL---------IERLKEAGIKVIPIVTSV---------REA--- 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495460700 164 stRLAWELGAD-IVKVNY-------TGDVQSF---KQVVNAVDIPVIVAGGAKSNADssilsmIKDAIKAGGKGVAVG 230
Cdd:COG2070 118 --RKAEKAGADaVVAEGAeagghrgADEVSTFalvPEVRDAVDIPVIAAGGIADGRG------IAAALALGADGVQMG 187
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
98-239 |
5.08e-03 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 37.24 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495460700 98 VEQAIKLGADGVSIHVNLGandeYRMLKDFSQisaACHQWGMPLLAMV-------YARGEKIKNEYDADAIAHSTRLAWE 170
Cdd:pfam00215 71 AKYKAKLGADIVTVHAYAG----EGTLKAAKE---AAEEYGRGLLLVAelsskgsLDLQEEGDLGYTQEIVHRAADLAAG 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495460700 171 LGADIVKVNY--TGDVQSFKQVVNAVDIPVIVAGGAKSNAdssilsMIKDAIKAGGKGVAVGRNIFQHSNP 239
Cdd:pfam00215 144 VDGVVASATEalREILPDFLILTPGIGLQGGDAGGQQRVT------TPAVAKEAGADIIIVGRGITGAGDP 208
|
|
| PRK13585 |
PRK13585 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ... |
188-230 |
5.35e-03 |
|
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;
Pssm-ID: 184165 Cd Length: 241 Bit Score: 37.19 E-value: 5.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 495460700 188 KQVVNAVDIPVIVAGGAKSNADSSILSmikdaiKAGGKGVAVG 230
Cdd:PRK13585 186 KELVDSVDIPVIASGGVTTLDDLRALK------EAGAAGVVVG 222
|
|
| |
