|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-270 |
1.21e-110 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 320.60 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 1 MDKYAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAK 80
Cdd:PRK00258 5 TRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGGRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 81 IAGAVNTIKqLEDGSLLGDNTDGVGLVKDLLAN-NVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKAL 159
Cdd:PRK00258 85 LIGAVNTLV-LEDGRLIGDNTDGIGFVRALEERlGVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 160 ASHFNGEINVQGFALNDIPANNYDVVINSTSSSVTGDLPG--IAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTL 237
Cdd:PRK00258 164 AKLFGALGKAELDLELQEELADFDLIINATSAGMSGELPLppLPLSLLRPGTIVYDMIYGPLPTPFLAWAKAQG--ARTI 241
|
250 260 270
....*....|....*....|....*....|...
gi 966689749 238 DGCGMLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:PRK00258 242 DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRA 274
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1-270 |
1.82e-101 |
|
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: 297.05 E-value: 1.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 1 MDKYAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAK 80
Cdd:COG0169 4 TRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 81 IAGAVNTIKqLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALA 160
Cdd:COG0169 84 LIGAVNTVV-FEDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 161 SHFngeiNVQGFALNDIPA--NNYDVVINSTSSSVTG-DLPGIAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTL 237
Cdd:COG0169 163 ARL----GVRAVPLDDLAAalAGADLVINATPLGMAGgDALPLPASLLAPGAVVYDLVYNPLETPLLRAARARG--ARVI 236
|
250 260 270
....*....|....*....|....*....|...
gi 966689749 238 DGCGMLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:COG0169 237 DGLGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
4-270 |
1.32e-88 |
|
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: 264.28 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 4 YAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAG 83
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 84 AVNTIKqLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIEsLTIANRTAEKAKALASHF 163
Cdd:TIGR00507 83 AVNTLV-LEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADCN-VIIANRTVSKAEELAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 164 NGEINVQGFALNDIPANNYDVVINSTSSSVTGDLPGIAED--HVAKCQCAYDMFYANDDTAFISWVKSNNptCLTLDGCG 241
Cdd:TIGR00507 161 QRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPPVPaeYLKEGKLVYDLVYNPLETPFLAEAKSLG--TKTIDGLG 238
|
250 260
....*....|....*....|....*....
gi 966689749 242 MLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:TIGR00507 239 MLVYQAALSFELWTGVEPDIEKMFEQLIS 267
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
101-256 |
4.55e-36 |
|
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: 125.85 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 101 TDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEINVQGFALNDIPAN 180
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEELLA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966689749 181 NYDVVINSTSS--SVTGDLPgIAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTLDGCGMLVGQAAQAYFVWRN 256
Cdd:cd01065 81 EADLIINTTPVgmKPGDELP-LPPSLLKPGGVVYDVVYNPLETPLLKEARALG--AKTIDGLEMLVYQAAEAFELWTG 155
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
6-88 |
2.08e-28 |
|
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: 103.83 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 6 VFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAGAV 85
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 966689749 86 NTI 88
Cdd:pfam08501 81 NTI 83
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-270 |
1.21e-110 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 320.60 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 1 MDKYAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAK 80
Cdd:PRK00258 5 TRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGGRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 81 IAGAVNTIKqLEDGSLLGDNTDGVGLVKDLLAN-NVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKAL 159
Cdd:PRK00258 85 LIGAVNTLV-LEDGRLIGDNTDGIGFVRALEERlGVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 160 ASHFNGEINVQGFALNDIPANNYDVVINSTSSSVTGDLPG--IAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTL 237
Cdd:PRK00258 164 AKLFGALGKAELDLELQEELADFDLIINATSAGMSGELPLppLPLSLLRPGTIVYDMIYGPLPTPFLAWAKAQG--ARTI 241
|
250 260 270
....*....|....*....|....*....|...
gi 966689749 238 DGCGMLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:PRK00258 242 DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRA 274
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1-270 |
1.82e-101 |
|
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: 297.05 E-value: 1.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 1 MDKYAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAK 80
Cdd:COG0169 4 TRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 81 IAGAVNTIKqLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALA 160
Cdd:COG0169 84 LIGAVNTVV-FEDGRLIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 161 SHFngeiNVQGFALNDIPA--NNYDVVINSTSSSVTG-DLPGIAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTL 237
Cdd:COG0169 163 ARL----GVRAVPLDDLAAalAGADLVINATPLGMAGgDALPLPASLLAPGAVVYDLVYNPLETPLLRAARARG--ARVI 236
|
250 260 270
....*....|....*....|....*....|...
gi 966689749 238 DGCGMLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:COG0169 237 DGLGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
4-270 |
1.32e-88 |
|
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: 264.28 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 4 YAVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAG 83
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 84 AVNTIKqLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIEsLTIANRTAEKAKALASHF 163
Cdd:TIGR00507 83 AVNTLV-LEDGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADCN-VIIANRTVSKAEELAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 164 NGEINVQGFALNDIPANNYDVVINSTSSSVTGDLPGIAED--HVAKCQCAYDMFYANDDTAFISWVKSNNptCLTLDGCG 241
Cdd:TIGR00507 161 QRYGEIQAFSMDELPLHRVDLIINATSAGMSGNIDEPPVPaeYLKEGKLVYDLVYNPLETPFLAEAKSLG--TKTIDGLG 238
|
250 260
....*....|....*....|....*....
gi 966689749 242 MLVGQAAQAYFVWRNKMPEIIPVVTALKA 270
Cdd:TIGR00507 239 MLVYQAALSFELWTGVEPDIEKMFEQLIS 267
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
101-256 |
4.55e-36 |
|
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: 125.85 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 101 TDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEINVQGFALNDIPAN 180
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEELLA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966689749 181 NYDVVINSTSS--SVTGDLPgIAEDHVAKCQCAYDMFYANDDTAFISWVKSNNptCLTLDGCGMLVGQAAQAYFVWRN 256
Cdd:cd01065 81 EADLIINTTPVgmKPGDELP-LPPSLLKPGGVVYDVVYNPLETPLLKEARALG--AKTIDGLEMLVYQAAEAFELWTG 155
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
6-88 |
2.08e-28 |
|
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: 103.83 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 6 VFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAGAV 85
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 966689749 86 NTI 88
Cdd:pfam08501 81 NTI 83
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
3-254 |
2.95e-28 |
|
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: 109.23 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 3 KYAVFGNPIKHSKSPAIHaqfaaslneQIQYSAILAP--TDAFE----KTVAEFFAAGGK---GANVTLPFKEQAFAMVD 73
Cdd:TIGR01809 7 KAFIIGKPIAHSRSPHLH---------NAGYEILGLPdkTYEFEtcsaEELKEVLSGFGPqfgGASVTIPLKFAILRFAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 74 ELTEQAKIAGAVNTIKQLEDGSLLGDNTDGVGLVKDLLANNVTLK--GQRVLLIGAGGAARGVIQPLLNEHIESLTIANR 151
Cdd:TIGR01809 78 EHTDRASLIGSVNTLLRTQNGIWKGDNTDWDGIAGALANIGKFEPlaGFRGLVIGAGGTSRAAVYALASLGVTDITVINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 152 TAEKAKALASHFNGEINVQGF-ALNDIPANNYDVVInsTSSSVTGDLPGIAEDhVAKCQCAYDMFYANDDTAFISWVKSN 230
Cdd:TIGR01809 158 NPDKLSRLVDLGVQVGVITRLeGDSGGLAIEKAAEV--LVSTVPADVPADYVD-LFATVPFLLLKRKSSEGIFLDAAYDP 234
|
250 260 270
....*....|....*....|....*....|....
gi 966689749 231 NPTCLT----------LDGCGMLVGQAAQAYFVW 254
Cdd:TIGR01809 235 WPTPLVaivsaagwrvISGLQMLLHQGFAQFEQW 268
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
5-259 |
2.64e-26 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 104.05 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 5 AVFGNPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAGA 84
Cdd:PRK12548 13 GLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIPVDKVPDAIKAIKTFNMRGANVTMPCKSEAAKYMDELSPAARIIGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 85 VNTIKQlEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGV-IQPLLnEHIESLTIANR----------TA 153
Cdd:PRK12548 93 VNTIVN-DDGKLTGHITDGLGFVRNLREHGVDVKGKKLTVIGAGGAATAIqVQCAL-DGAKEITIFNIkddfyeraeqTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 154 EKAKALAShfngEINVQGFALNDIPANN-----YDVVINST--------SSSVTGDLPGIAEDHVAKcqcayDMFYANDD 220
Cdd:PRK12548 171 EKIKQEVP----ECIVNVYDLNDTEKLKaeiasSDILVNATlvgmkpndGETNIKDTSVFRKDLVVA-----DTVYNPKK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 966689749 221 TAFISWVKSNNptCLTLDGCGMLVGQAAQAYFVWRNK-MP 259
Cdd:PRK12548 242 TKLLEDAEAAG--CKTVGGLGMLLWQGAEAYKLYTGKdMP 279
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
8-251 |
3.69e-25 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 101.13 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 8 GNPIKHSKSPAIHAQFAASLNEQIQYSAI-LA----PTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIA 82
Cdd:PRK12549 12 GAGIQASLSPAMHEAEGDAQGLRYVYRLIdLDalglTADALPELLDAAERMGFAGLNITHPCKQAVIPHLDELSDDARAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 83 GAVNTIKqLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASH 162
Cdd:PRK12549 92 GAVNTVV-FRDGRRIGHNTDWSGFAESFRRGLPDASLERVVQLGAGGAGAAVAHALLTLGVERLTIFDVDPARAAALADE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 163 FNGEINVQGF-ALNDIPAN--NYDVVINSTSSSVTGdLPG-------IAEDH-VAkcqcayDMFYANDDTAFISWVKSNN 231
Cdd:PRK12549 171 LNARFPAARAtAGSDLAAAlaAADGLVHATPTGMAK-HPGlplpaelLRPGLwVA------DIVYFPLETELLRAARALG 243
|
250 260
....*....|....*....|
gi 966689749 232 ptCLTLDGCGMLVGQAAQAY 251
Cdd:PRK12549 244 --CRTLDGGGMAVFQAVDAF 261
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
3-257 |
4.05e-25 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 100.85 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 3 KYAVFG---NPIKHSKSPAIHAQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQA 79
Cdd:PRK12749 6 KYELIGlmaYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 80 KIAGAVNTIKQlEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTA---EKA 156
Cdd:PRK12749 86 KLVGAINTIVN-DDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDeffDKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 157 KALASHFNGEIN--VQGFALNDIPA-----NNYDVVINST--------SSSVTGDL----PGIAedhVAKCqcaydmFYA 217
Cdd:PRK12749 165 LAFAQRVNENTDcvVTVTDLADQQAfaealASADILTNGTkvgmkpleNESLVNDIsllhPGLL---VTEC------VYN 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 966689749 218 NDDTAFISwvKSNNPTCLTLDGCGMLVGQAAQAYFVWRNK 257
Cdd:PRK12749 236 PHMTKLLQ--QAQQAGCKTIDGYGMLLWQGAEQFTLWTGK 273
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
4-194 |
7.48e-24 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 99.87 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 4 YAVFGNPIKHSKSPAIHAQFAASLneQIQYSAILAPTDAFEktVAEFFAAGGK----GANVTLPFKEQAFAMVDELTEQA 79
Cdd:PRK09310 218 YGLIGDPVDRSISHLSHNPLFSQL--SLNCPYIKLPLTPQE--LPKFFSTIRDlpflGLSVTMPLKTAVLDFLDKLDPSV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 80 KIAGAVNTIkQLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIEsLTIANRTAEKAKAL 159
Cdd:PRK09310 294 KLCGSCNTL-VFRNGKIEGYNTDGEGLFSLLKQKNIPLNNQHVAIVGAGGAAKAIATTLARAGAE-LLIFNRTKAHAEAL 371
|
170 180 190
....*....|....*....|....*....|....*.
gi 966689749 160 ASHFNGeinvQGFALNDIPAN-NYDVVINSTSSSVT 194
Cdd:PRK09310 372 ASRCQG----KAFPLESLPELhRIDIIINCLPPSVT 403
|
|
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
4-251 |
1.32e-20 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 90.98 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 4 YAVFGNPIKHSKSPAIHAQFAASlneqIQYSAILAP--TDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKI 81
Cdd:PLN02520 255 YGIIGKPVGHSKSPILHNEAFKS----VGFNGVYVHllVDDLAKFLQTYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 82 AGAVNTI-KQLEDGSLLGDNTDGVGLV----KDLLANNVT------LKGQRVLLIGAGGAARGVIQPlLNEHIESLTIAN 150
Cdd:PLN02520 331 IGAINTIiRRPSDGKLVGYNTDYIGAIsaieDGLRASGSSpasgspLAGKLFVVIGAGGAGKALAYG-AKEKGARVVIAN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 151 RTAEKAKALASHFNGeinvQGFALNDIpaNNYD-----VVINSTSssvTGDLPGIAEDHVAK-----CQCAYDMFYANDD 220
Cdd:PLN02520 410 RTYERAKELADAVGG----QALTLADL--ENFHpeegmILANTTS---VGMQPNVDETPISKhalkhYSLVFDAVYTPKI 480
|
250 260 270
....*....|....*....|....*....|.
gi 966689749 221 TAFISWVKSNNPTCLTldGCGMLVGQAAQAY 251
Cdd:PLN02520 481 TRLLREAEESGAIIVS--GTEMFIRQAYEQF 509
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
5-261 |
4.62e-20 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 87.40 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 5 AVFGNPIKHSKSPAIH-----AQFAASLNEQIQYSAILAPTDAFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQA 79
Cdd:PRK14027 8 GLIGQGLDLSRTPAMHeaeglAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 80 KIAGAVNTIKQLEDGSLLGDNTDGVGLVKDLLANNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKAL 159
Cdd:PRK14027 88 TQLGAVNTVVIDATGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 160 ASHFNGEI------NVQGFALNDIPANNyDVVINSTSSSVTGDlPGIAEDH--VAKCQCAYDMFYANDDTAFISWVKSNN 231
Cdd:PRK14027 168 ADVINNAVgreavvGVDARGIEDVIAAA-DGVVNATPMGMPAH-PGTAFDVscLTKDHWVGDVVYMPIETELLKAARALG 245
|
250 260 270
....*....|....*....|....*....|
gi 966689749 232 ptCLTLDGCGMLVGQAAQAYFVWRNKMPEI 261
Cdd:PRK14027 246 --CETLDGTRMAIHQAVDAFRLFTGLEPDV 273
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
104-192 |
2.18e-17 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 81.00 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 104 VGLVKDLLANnvtLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEInvqgFALNDIPA--NN 181
Cdd:PRK00045 170 VELAKQIFGD---LSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGGEA----IPLDELPEalAE 242
|
90
....*....|.
gi 966689749 182 YDVVINSTSSS 192
Cdd:PRK00045 243 ADIVISSTGAP 253
|
|
| Shikimate_DH |
pfam01488 |
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
106-192 |
4.34e-17 |
|
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: 75.69 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 106 LVKDLLANnvtLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEINVqgfALNDIPA--NNYD 183
Cdd:pfam01488 2 LAKKIFGD---LKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGGVEAL---PLDDLKEylAEAD 75
|
....*....
gi 966689749 184 VVINSTSSS 192
Cdd:pfam01488 76 IVISATSSP 84
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
104-192 |
6.49e-16 |
|
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: 76.15 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 104 VGLVKDLLANnvtLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGeiNVQGFA-LNDIPaNNY 182
Cdd:cd05213 166 VELAEKIFGN---LKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGG--NAVPLDeLLELL-NEA 239
|
90
....*....|
gi 966689749 183 DVVINSTSSS 192
Cdd:cd05213 240 DVVISATGAP 249
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
103-192 |
1.15e-15 |
|
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: 75.92 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 103 GVGLVKDLLANnvtLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEInvqgFALNDIPA--N 180
Cdd:COG0373 169 AVELAKKIFGD---LSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGGEA----VPLEELPEalA 241
|
90
....*....|..
gi 966689749 181 NYDVVINSTSSS 192
Cdd:COG0373 242 EADIVISSTGAP 253
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
33-189 |
1.25e-15 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 74.61 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 33 YSAIlAPTDaFEKTVAEFFAAGGKGANVTLPFKEQAFAMVDELTEQAKIAGAVNTIKQlEDGSLLGDNTDGVGlVKDLLA 112
Cdd:PRK12550 40 YKAF-TTTD-LTAAIGGVRALGIRGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVN-TDGHLKAYNTDYIA-IAKLLA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966689749 113 NNVTLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFngeinvqGFA-LNDIPANNYDVVINST 189
Cdd:PRK12550 116 SYQVPPDLVVALRGSGGMAKAVAAALRDAGFTDGTIVARNEKTGKALAELY-------GYEwRPDLGGIEADILVNVT 186
|
|
| hemA |
TIGR01035 |
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
104-192 |
4.38e-11 |
|
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: 62.40 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 104 VGLVKDLLANnvtLKGQRVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNGEinvqGFALNDIPA--NN 181
Cdd:TIGR01035 168 VELAERIFGS---LKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGE----AVKFEDLEEylAE 240
|
90
....*....|.
gi 966689749 182 YDVVINSTSSS 192
Cdd:TIGR01035 241 ADIVISSTGAP 251
|
|
| PLN00203 |
PLN00203 |
glutamyl-tRNA reductase |
121-207 |
4.33e-06 |
|
glutamyl-tRNA reductase
Pssm-ID: 215101 [Multi-domain] Cd Length: 519 Bit Score: 47.44 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 121 RVLLIGAGGAARGVIQPLLNEHIESLTIANRTAEKAKALASHFNG-EINVQgfALNDI--PANNYDVVINSTSSSVtgdl 197
Cdd:PLN00203 268 RVLVIGAGKMGKLLVKHLVSKGCTKMVVVNRSEERVAALREEFPDvEIIYK--PLDEMlaCAAEADVVFTSTSSET---- 341
|
90
....*....|
gi 966689749 198 PGIAEDHVAK 207
Cdd:PLN00203 342 PLFLKEHVEA 351
|
|
| Sacchrp_dh_NADP |
pfam03435 |
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
122-187 |
7.57e-04 |
|
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 38.34 E-value: 7.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966689749 122 VLLIGAGGAARGVIqPLL--NEHIESLTIANRTAEKAKALASHFNG-EINVQGFALNDIPA------NNYDVVIN 187
Cdd:pfam03435 1 VLIIGAGSVGQGVA-PLLarHFDVDRITVADRTLEKAQALAAKLGGvRFIAVAVDADNYEAvlaallKEGDLVVN 74
|
|
| PRK08618 |
PRK08618 |
ornithine cyclodeaminase family protein; |
105-192 |
1.54e-03 |
|
ornithine cyclodeaminase family protein;
Pssm-ID: 236313 [Multi-domain] Cd Length: 325 Bit Score: 39.27 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966689749 105 GLVKDLLANnvtlKGQRVL-LIGAGGAARGVIQPLLN-EHIESLTIANRTAEKAKALA----SHFNGEINVqgFALNDIP 178
Cdd:PRK08618 116 GVATKYLAR----EDAKTLcLIGTGGQAKGQLEAVLAvRDIERVRVYSRTFEKAYAFAqeiqSKFNTEIYV--VNSADEA 189
|
90
....*....|....
gi 966689749 179 ANNYDVVINSTSSS 192
Cdd:PRK08618 190 IEEADIIVTVTNAK 203
|
|
|