|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-275 |
4.52e-125 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 357.19 E-value: 4.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 1 MTQQVDRYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLT 80
Cdd:PRK00258 1 ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGGRGANVTVPFKEAAFALADELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 81 ERAELAGAVNTLkKLDDGEIIGDNTDGEGLVQDLLQHQ-VMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSK 159
Cdd:PRK00258 81 ERARLIGAVNTL-VLEDGRLIGDNTDGIGFVRALEERLgVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 160 AELLAEMFSSHGNIKGM-GLSDVNEGFDVIINSTSSGLSGQLP--EISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVH 236
Cdd:PRK00258 160 AEELAKLFGALGKAELDlELQEELADFDLIINATSAGMSGELPlpPLPLSLLRPGTIVYDMIYGPLPTPFLAWAKAQGAR 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1330499022 237 AAyDGLGMLVGQAAESFMLWRGLRPGTKQILRELRKNLE 275
Cdd:PRK00258 240 TI-DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRAALA 277
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
6-272 |
2.42e-105 |
|
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 306.68 E-value: 2.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 6 DRYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAEL 85
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPRARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 86 AGAVNTLKKlDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAE 165
Cdd:COG0169 85 IGAVNTVVF-EDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 166 MFsshgNIKGMGLSDVNE---GFDVIINSTSSGLSGQL-PEISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDG 241
Cdd:COG0169 164 RL----GVRAVPLDDLAAalaGADLVINATPLGMAGGDaLPLPASLLAPGAVVYDLVYNPLETPLLRAARARGARVI-DG 238
|
250 260 270
....*....|....*....|....*....|.
gi 1330499022 242 LGMLVGQAAESFMLWRGLRPGTKQILRELRK 272
Cdd:COG0169 239 LGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
8-261 |
4.21e-90 |
|
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 161904 [Multi-domain] Cd Length: 270 Bit Score: 268.13 E-value: 4.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 8 YAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAG 87
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 88 AVNTLkKLDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNpQQLVVANRTSSKAELLAEMF 167
Cdd:TIGR00507 83 AVNTL-VLEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKAD-CNVIIANRTVSKAEELAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 168 SSHGNIKGMGLSDVN-EGFDVIINSTSSGLSGQLPE--ISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDGLGM 244
Cdd:TIGR00507 161 QRYGEIQAFSMDELPlHRVDLIINATSAGMSGNIDEppVPAEYLKEGKLVYDLVYNPLETPFLAEAKSLGTKTI-DGLGM 239
|
250
....*....|....*..
gi 1330499022 245 LVGQAAESFMLWRGLRP 261
Cdd:TIGR00507 240 LVYQAALSFELWTGVEP 256
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
105-258 |
3.55e-43 |
|
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 144.34 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 105 TDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSSHG-NIKGMGLSDVNE 183
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGiAIAYLDLEELLA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330499022 184 GFDVIINSTSSGL--SGQLPeISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDGLGMLVGQAAESFMLWRG 258
Cdd:cd01065 81 EADLIINTTPVGMkpGDELP-LPPSLLKPGGVVYDVVYNPLETPLLKEARALGAKTI-DGLEMLVYQAAEAFELWTG 155
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
10-92 |
1.04e-26 |
|
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.
Pssm-ID: 400688 [Multi-domain] Cd Length: 83 Bit Score: 99.60 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 10 VFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAGAV 89
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 1330499022 90 NTL 92
Cdd:pfam08501 81 NTI 83
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-275 |
4.52e-125 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 357.19 E-value: 4.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 1 MTQQVDRYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLT 80
Cdd:PRK00258 1 ITGKTRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGGRGANVTVPFKEAAFALADELS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 81 ERAELAGAVNTLkKLDDGEIIGDNTDGEGLVQDLLQHQ-VMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSK 159
Cdd:PRK00258 81 ERARLIGAVNTL-VLEDGRLIGDNTDGIGFVRALEERLgVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 160 AELLAEMFSSHGNIKGM-GLSDVNEGFDVIINSTSSGLSGQLP--EISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVH 236
Cdd:PRK00258 160 AEELAKLFGALGKAELDlELQEELADFDLIINATSAGMSGELPlpPLPLSLLRPGTIVYDMIYGPLPTPFLAWAKAQGAR 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1330499022 237 AAyDGLGMLVGQAAESFMLWRGLRPGTKQILRELRKNLE 275
Cdd:PRK00258 240 TI-DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRAALA 277
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
6-272 |
2.42e-105 |
|
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 306.68 E-value: 2.42e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 6 DRYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAEL 85
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPRARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 86 AGAVNTLKKlDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAE 165
Cdd:COG0169 85 IGAVNTVVF-EDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 166 MFsshgNIKGMGLSDVNE---GFDVIINSTSSGLSGQL-PEISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDG 241
Cdd:COG0169 164 RL----GVRAVPLDDLAAalaGADLVINATPLGMAGGDaLPLPASLLAPGAVVYDLVYNPLETPLLRAARARGARVI-DG 238
|
250 260 270
....*....|....*....|....*....|.
gi 1330499022 242 LGMLVGQAAESFMLWRGLRPGTKQILRELRK 272
Cdd:COG0169 239 LGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
8-261 |
4.21e-90 |
|
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 161904 [Multi-domain] Cd Length: 270 Bit Score: 268.13 E-value: 4.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 8 YAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAG 87
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 88 AVNTLkKLDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNpQQLVVANRTSSKAELLAEMF 167
Cdd:TIGR00507 83 AVNTL-VLEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKAD-CNVIIANRTVSKAEELAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 168 SSHGNIKGMGLSDVN-EGFDVIINSTSSGLSGQLPE--ISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDGLGM 244
Cdd:TIGR00507 161 QRYGEIQAFSMDELPlHRVDLIINATSAGMSGNIDEppVPAEYLKEGKLVYDLVYNPLETPFLAEAKSLGTKTI-DGLGM 239
|
250
....*....|....*..
gi 1330499022 245 LVGQAAESFMLWRGLRP 261
Cdd:TIGR00507 240 LVYQAALSFELWTGVEP 256
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
105-258 |
3.55e-43 |
|
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 144.34 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 105 TDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSSHG-NIKGMGLSDVNE 183
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGiAIAYLDLEELLA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330499022 184 GFDVIINSTSSGL--SGQLPeISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAyDGLGMLVGQAAESFMLWRG 258
Cdd:cd01065 81 EADLIINTTPVGMkpGDELP-LPPSLLKPGGVVYDVVYNPLETPLLKEARALGAKTI-DGLEMLVYQAAEAFELWTG 155
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
7-266 |
3.45e-33 |
|
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of shikimate-5-dehydrogenases found in Corynebacterium, Mycobacteria and fungi. The fungal sequences are pentafunctional proteins known as AroM which contain the central five seven steps in the chorismate biosynthesis pathway. The Corynebacterium and Mycobacterial sequences represent the sole shikimate-5-dehydrogenases in species which otherwise have every enzyme of the chorismate biosynthesis pathway. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273813 [Multi-domain] Cd Length: 282 Bit Score: 122.33 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 7 RYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELA 86
Cdd:TIGR01809 7 KAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGFGPQFGGASVTIPLKFAILRFADEHTDRASLI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 87 GAVNTLKKLDDGEIIGDNTDGEGLVQDLLQHQVM--LEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLA 164
Cdd:TIGR01809 87 GSVNTLLRTQNGIWKGDNTDWDGIAGALANIGKFepLAGFRGLVIGAGGTSRAAVYALASLGVTDITVINRNPDKLSRLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 165 EMFSSHGNIKGM----GLSDVNEGFDVIINS--TSSGLSGQLPEISEIIFN-----SNSSVYDMVYGSGTTVFNQWALDN 233
Cdd:TIGR01809 167 DLGVQVGVITRLegdsGGLAIEKAAEVLVSTvpADVPADYVDLFATVPFLLlkrksSEGIFLDAAYDPWPTPLVAIVSAA 246
|
250 260 270
....*....|....*....|....*....|...
gi 1330499022 234 GVHAAYdGLGMLVGQAAESFMLWRGLRPGTKQI 266
Cdd:TIGR01809 247 GWRVIS-GLQMLLHQGFAQFEQWTGMPAPREAM 278
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
9-259 |
3.52e-27 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 106.75 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 9 AVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAGA 88
Cdd:PRK12548 13 GLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIPVDKVPDAIKAIKTFNMRGANVTMPCKSEAAKYMDELSPAARIIGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 89 VNTLKKlDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGV-IQPLLDqNPQQLVVANRTSS---KAELLA 164
Cdd:PRK12548 93 VNTIVN-DDGKLTGHITDGLGFVRNLREHGVDVKGKKLTVIGAGGAATAIqVQCALD-GAKEITIFNIKDDfyeRAEQTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 165 EMFSSHGNIKGMGLSDVN---------EGFDVIINSTSSGL---SGQLPEISEIIFNSNSSVYDMVYGSGTTVFNQWALD 232
Cdd:PRK12548 171 EKIKQEVPECIVNVYDLNdteklkaeiASSDILVNATLVGMkpnDGETNIKDTSVFRKDLVVADTVYNPKKTKLLEDAEA 250
|
250 260
....*....|....*....|....*..
gi 1330499022 233 NGVHAAyDGLGMLVGQAAESFMLWRGL 259
Cdd:PRK12548 251 AGCKTV-GGLGMLLWQGAEAYKLYTGK 276
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
10-92 |
1.04e-26 |
|
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.
Pssm-ID: 400688 [Multi-domain] Cd Length: 83 Bit Score: 99.60 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 10 VFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAGAV 89
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 1330499022 90 NTL 92
Cdd:pfam08501 81 NTI 83
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
8-256 |
4.60e-23 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 97.95 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 8 YAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFiiaaQAFFSEGG----RGCNVTAPFKEDAYQFANRLTERA 83
Cdd:PRK09310 218 YGLIGDPVDRSISHLSHNPLFSQLSLNCPYIKLPLTPQEL----PKFFSTIRdlpfLGLSVTMPLKTAVLDFLDKLDPSV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 84 ELAGAVNTLKkLDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNpQQLVVANRTSSKAELL 163
Cdd:PRK09310 294 KLCGSCNTLV-FRNGKIEGYNTDGEGLFSLLKQKNIPLNNQHVAIVGAGGAAKAIATTLARAG-AELLIFNRTKAHAEAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 164 AEMFsshgNIKGMGLSDVNE--GFDVIINStssglsgqLPEISEIIFNSNSSVYDMVYGSGTTVFNQWALDNGVHAAYdG 241
Cdd:PRK09310 372 ASRC----QGKAFPLESLPElhRIDIIINC--------LPPSVTIPKAFPPCVVDINTLPKHSPYTQYARSQGSSIIY-G 438
|
250
....*....|....*
gi 1330499022 242 LGMLVGQAAESFMLW 256
Cdd:PRK09310 439 YEMFAEQALLQFRLW 453
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
1-258 |
1.36e-20 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 88.91 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 1 MTQQVDRYAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQGEFIIAAQAFFSEGGRGCNVTAPFKEDAYQFANRLT 80
Cdd:PRK12749 3 VTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 81 ERAELAGAVNTLKKlDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTS--- 157
Cdd:PRK12749 83 PAAKLVGAINTIVN-DDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDeff 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 158 SKAELLAEMFSSHGN----IKGMG----LSDVNEGFDVIINSTSSGLSgqlPEISEIIFNSNSS------VYDMVYGSGT 223
Cdd:PRK12749 162 DKALAFAQRVNENTDcvvtVTDLAdqqaFAEALASADILTNGTKVGMK---PLENESLVNDISLlhpgllVTECVYNPHM 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1330499022 224 TVFNQWALDNGVHAAyDGLGMLVGQAAESFMLWRG 258
Cdd:PRK12749 239 TKLLQQAQQAGCKTI-DGYGMLLWQGAEQFTLWTG 272
|
|
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
8-270 |
1.43e-20 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 90.98 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 8 YAVFGNPIGQSKSPFIHTLFARQTSQQLTYTALQPEQ-GEFIiaaQAFFSEGGRGCNVTAPFKEDAYQFANRLTERAELA 86
Cdd:PLN02520 255 YGIIGKPVGHSKSPILHNEAFKSVGFNGVYVHLLVDDlAKFL---QTYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKSI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 87 GAVNT-LKKLDDGEIIGDNTDGEG---LVQDLLQHQVM-------LEGARVLLLGAGGAARGVIQPlLDQNPQQLVVANR 155
Cdd:PLN02520 332 GAINTiIRRPSDGKLVGYNTDYIGaisAIEDGLRASGSspasgspLAGKLFVVIGAGGAGKALAYG-AKEKGARVVIANR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 156 TSSKAELLAEMFSSHgnikGMGLSDVN-----EGFdVIINSTSSGLSGQLPE--ISEIIFNSNSSVYDMVYGSGTTVFNQ 228
Cdd:PLN02520 411 TYERAKELADAVGGQ----ALTLADLEnfhpeEGM-ILANTTSVGMQPNVDEtpISKHALKHYSLVFDAVYTPKITRLLR 485
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1330499022 229 WALDNGVHAAYdGLGMLVGQAAESFMLWRGLrPGTKQILREL 270
Cdd:PLN02520 486 EAEESGAIIVS-GTEMFIRQAYEQFERFTGL-PAPKELFREI 525
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
12-268 |
4.81e-16 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 76.09 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 12 GNPIGQSKSPFIHTLFARQ------------TSQQLTYTALqpeqGEFIIAAQAffsEGGRGCNVTAPFKEDAYQFANRL 79
Cdd:PRK12549 12 GAGIQASLSPAMHEAEGDAqglryvyrlidlDALGLTADAL----PELLDAAER---MGFAGLNITHPCKQAVIPHLDEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 80 TERAELAGAVNTLKkLDDGEIIGDNTDGEGLVQDLlqhQVMLEGA---RVLLLGAGGAARGVIQPLLDQNPQQLVVANRT 156
Cdd:PRK12549 85 SDDARALGAVNTVV-FRDGRRIGHNTDWSGFAESF---RRGLPDAsleRVVQLGAGGAGAAVAHALLTLGVERLTIFDVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 157 SSKAELLAEMFSSH---GNIK-GMGLSDVNEGFDVIINSTSSGLSGQ--LPEISEIIfNSNSSVYDMVYGSGTTVFNQWA 230
Cdd:PRK12549 161 PARAAALADELNARfpaARATaGSDLAAALAAADGLVHATPTGMAKHpgLPLPAELL-RPGLWVADIVYFPLETELLRAA 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1330499022 231 LDNGVhAAYDGLGMLVGQAAESFMLWRGLRPGTKQILR 268
Cdd:PRK12549 240 RALGC-RTLDGGGMAVFQAVDAFELFTGREPDAERMLA 276
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
53-266 |
6.36e-15 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 72.76 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 53 AFFSEGGRGCNVTAPFKEDAYQFANRLTERAELAGAVNTLKKLDDGEIIGDNTDGEGLVQDLLQHQVMLEGARVLLLGAG 132
Cdd:PRK14027 57 AALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDATGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 133 GAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSS-------HGnIKGMGLSDVNEGFDVIINSTSSGL---SGQLPE 202
Cdd:PRK14027 137 GVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNavgreavVG-VDARGIEDVIAAADGVVNATPMGMpahPGTAFD 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330499022 203 ISeiIFNSNSSVYDMVYGSGTTVFNQWALDNGVHaAYDGLGMLVGQAAESFMLWRGLRPGTKQI 266
Cdd:PRK14027 216 VS--CLTKDHWVGDVVYMPIETELLKAARALGCE-TLDGTRMAIHQAVDAFRLFTGLEPDVSRM 276
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
58-266 |
1.19e-14 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 71.91 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 58 GGRGCNVTAPFKEDAYQFANRLTERAELAGAVNTLKKlDDGEIIGDNTDGEGLVQDLLQHQVMlEGARVLLLGAGGAARG 137
Cdd:PRK12550 59 GIRGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVN-TDGHLKAYNTDYIAIAKLLASYQVP-PDLVVALRGSGGMAKA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 138 VIQPLLDQN-PQQLVVA-NRTSSKAelLAEMF-----SSHGNIKGmglsdvnegfDVIINSTSSGLSGQlPEISEIIFNS 210
Cdd:PRK12550 137 VAAALRDAGfTDGTIVArNEKTGKA--LAELYgyewrPDLGGIEA----------DILVNVTPIGMAGG-PEADKLAFPE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330499022 211 N-----SSVYDMVYGSGTTVFNQWALDNGVhAAYDGLGMLVGQAAESFMLWRGLRPGTKQI 266
Cdd:PRK12550 204 AeidaaSVVFDVVALPAETPLIRYARARGK-TVITGAEVIALQAVEQFVLYTGVRPSDELI 263
|
|
| Shikimate_DH |
pfam01488 |
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
110-194 |
3.30e-13 |
|
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.
Pssm-ID: 460229 [Multi-domain] Cd Length: 136 Bit Score: 65.29 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330499022 110 LVQDLLQHqvmLEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSSHGNIKgmgLSDVNEG---FD 186
Cdd:pfam01488 2 LAKKIFGD---LKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGGVEALP---LDDLKEYlaeAD 75
|
....*...
gi 1330499022 187 VIINSTSS 194
Cdd:pfam01488 76 IVISATSS 83
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
121-194 |
9.23e-13 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 67.52 E-value: 9.23e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330499022 121 LEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFsshgNIKGMGLSDVNE---GFDVIINSTSS 194
Cdd:PRK00045 180 LSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEF----GGEAIPLDELPEalaEADIVISSTGA 252
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
121-194 |
6.20e-12 |
|
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 65.13 E-value: 6.20e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330499022 121 LEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFsshgNIKGMGLSDVNEG---FDVIINSTSS 194
Cdd:COG0373 180 LSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEF----GGEAVPLEELPEAlaeADIVISSTGA 252
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
121-194 |
2.60e-09 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 56.89 E-value: 2.60e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330499022 121 LEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSshGNIKGM-GLSDVNEGFDVIINSTSS 194
Cdd:cd05213 176 LKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELG--GNAVPLdELLELLNEADVVISATGA 248
|
|
| hemA |
TIGR01035 |
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
121-194 |
1.23e-07 |
|
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273407 [Multi-domain] Cd Length: 417 Bit Score: 52.00 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330499022 121 LEGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSKAELLAEMFSShgniKGMGLSDVNEGF---DVIINSTSS 194
Cdd:TIGR01035 178 LKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGG----EAVKFEDLEEYLaeaDIVISSTGA 250
|
|
| SDH_C |
pfam18317 |
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ... |
241-271 |
4.85e-07 |
|
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of Shikimate 5'-dehydrogenase (SDH) present in Methanocaldococcus jannaschii. SDH catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate in the shikimate pathway. The domain is found just after the C-terminal domain (pfam01488) which is responsible for NADP binding.
Pssm-ID: 436404 [Multi-domain] Cd Length: 31 Bit Score: 45.10 E-value: 4.85e-07
10 20 30
....*....|....*....|....*....|.
gi 1330499022 241 GLGMLVGQAAESFMLWRGLRPGTKQILRELR 271
Cdd:pfam18317 1 GLGMLVEQGAEQFELWTGREPPVEVMREALL 31
|
|
| PLN00203 |
PLN00203 |
glutamyl-tRNA reductase |
122-195 |
6.41e-03 |
|
glutamyl-tRNA reductase
Pssm-ID: 215101 [Multi-domain] Cd Length: 519 Bit Score: 37.81 E-value: 6.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330499022 122 EGARVLLLGAGGAARGVIQPLLDQNPQQLVVANRTSSK-AELLAEMFSSHGNIKGMG-LSDVNEGFDVIINSTSSG 195
Cdd:PLN00203 265 ASARVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERvAALREEFPDVEIIYKPLDeMLACAAEADVVFTSTSSE 340
|
|
| PRK08618 |
PRK08618 |
ornithine cyclodeaminase family protein; |
122-194 |
8.91e-03 |
|
ornithine cyclodeaminase family protein;
Pssm-ID: 236313 [Multi-domain] Cd Length: 325 Bit Score: 36.96 E-value: 8.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330499022 122 EGARVL-LLGAGGAARGVIQPLLD-QNPQQLVVANRTSSKAELLAEMFSSHGNIKGMGLSDVNEGF---DVIINSTSS 194
Cdd:PRK08618 125 EDAKTLcLIGTGGQAKGQLEAVLAvRDIERVRVYSRTFEKAYAFAQEIQSKFNTEIYVVNSADEAIeeaDIIVTVTNA 202
|
|
| |
