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Conserved domains on  [gi|966689749|gb|KTG22581|]
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shikimate dehydrogenase [Pseudoalteromonas sp. XI10]

Protein Classification

shikimate dehydrogenase( domain architecture ID 11478370)

(NADP(+)) dependent shikimate dehydrogenase catalyzes the reversible reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA), part of the chorismate biosynthesis pathway

CATH:  3.40.50.720
Gene Ontology:  GO:0004764|GO:0050661|GO:0009423
PubMed:  17825835

Graphical summary

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List of domain hits

 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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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