|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-272 |
2.30e-132 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 375.68 E-value: 2.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 1 MDQYVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQ 79
Cdd:PRK00258 5 TRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGgRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLsKLDDGTLLGDNTDGAGLVRDLTVNCGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERL 159
Cdd:PRK00258 85 LIGAVNTL-VLEDGRLIGDNTDGIGFVRALEERLGVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 160 AEEFADLGPV-FASSFDWLEEPVDLIINATSASLAGELP--PVSPNLVQPGaTFCYDMMYGKEPTAFCRWASEHGaAQSV 236
Cdd:PRK00258 164 AKLFGALGKAeLDLELQEELADFDLIINATSAGMSGELPlpPLPLSLLRPG-TIVYDMIYGPLPTPFLAWAKAQG-ARTI 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 492583493 237 DGLGMLVEQAAEAFLLWRGVRPDSAPVLAELRRLLA 272
Cdd:PRK00258 242 DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRAALA 277
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1-270 |
9.25e-108 |
|
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: 312.84 E-value: 9.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 1 MDQYVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQ 79
Cdd:COG0169 4 TRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGiRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLsKLDDGTLLGDNTDGAGLVRDLTvNCGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERL 159
Cdd:COG0169 84 LIGAVNTV-VFEDGRLIGDNTDGIGFVRALR-EAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 160 AEEFadlgPVFASSFDWLEE---PVDLIINATSASLAG-ELPPVSPNLVQPGAtFCYDMMYGKEPTAFCRWASEHGaAQS 235
Cdd:COG0169 162 AARL----GVRAVPLDDLAAalaGADLVINATPLGMAGgDALPLPASLLAPGA-VVYDLVYNPLETPLLRAARARG-ARV 235
|
250 260 270
....*....|....*....|....*....|....*
gi 492583493 236 VDGLGMLVEQAAEAFLLWRGVRPDSAPVLAELRRL 270
Cdd:COG0169 236 IDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRAL 270
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
4-272 |
7.65e-89 |
|
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: 265.05 E-value: 7.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 4 YVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQRAG 82
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGfKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 83 AVNTLsKLDDGTLLGDNTDGAGLVRDLTVNcgVELR-GRRVLLLGAGGAVRGALEPLLaEQPAVLVIANRTVEKAERLAE 161
Cdd:TIGR00507 83 AVNTL-VLEDGKLVGYNTDGIGLVSDLEQL--IPLRpNQNVLIIGAGGAAKAVALELL-KADCNVIIANRTVSKAEELAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 162 EFADLGPVFASSFDWLE-EPVDLIINATSASLAGEL--PPVSPNLVQPGAtFCYDMMYGKEPTAFCRWASEHGaAQSVDG 238
Cdd:TIGR00507 159 RFQRYGEIQAFSMDELPlHRVDLIINATSAGMSGNIdePPVPAEYLKEGK-LVYDLVYNPLETPFLAEAKSLG-TKTIDG 236
|
250 260 270
....*....|....*....|....*....|....
gi 492583493 239 LGMLVEQAAEAFLLWRGVRPDSAPVLAELRRLLA 272
Cdd:TIGR00507 237 LGMLVYQAALSFELWTGVEPDIEKMFEQLISVLA 270
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
100-255 |
1.42e-44 |
|
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: 147.80 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 100 TDGAGLVRDLTVNcGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVfASSFDWLEE 179
Cdd:cd01065 1 TDGLGFVRALEEA-GIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIA-IAYLDLEEL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492583493 180 P--VDLIINATSASLAGELP-PVSPNLVQPGATfCYDMMYGKEPTAFCRWASEHGaAQSVDGLGMLVEQAAEAFLLWRG 255
Cdd:cd01065 79 LaeADLIINTTPVGMKPGDElPLPPSLLKPGGV-VYDVVYNPLETPLLKEARALG-AKTIDGLEMLVYQAAEAFELWTG 155
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
6-87 |
1.62e-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: 98.82 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 6 VFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQRAGAV 84
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGfRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 492583493 85 NTL 87
Cdd:pfam08501 81 NTI 83
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1-272 |
2.30e-132 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 375.68 E-value: 2.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 1 MDQYVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQ 79
Cdd:PRK00258 5 TRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVKGFFALGgRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLsKLDDGTLLGDNTDGAGLVRDLTVNCGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERL 159
Cdd:PRK00258 85 LIGAVNTL-VLEDGRLIGDNTDGIGFVRALEERLGVDLKGKRILILGAGGAARAVILPLLDLGVAEITIVNRTVERAEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 160 AEEFADLGPV-FASSFDWLEEPVDLIINATSASLAGELP--PVSPNLVQPGaTFCYDMMYGKEPTAFCRWASEHGaAQSV 236
Cdd:PRK00258 164 AKLFGALGKAeLDLELQEELADFDLIINATSAGMSGELPlpPLPLSLLRPG-TIVYDMIYGPLPTPFLAWAKAQG-ARTI 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 492583493 237 DGLGMLVEQAAEAFLLWRGVRPDSAPVLAELRRLLA 272
Cdd:PRK00258 242 DGLGMLVHQAAEAFELWTGVRPPVEPMLAALRAALA 277
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1-270 |
9.25e-108 |
|
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: 312.84 E-value: 9.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 1 MDQYVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQ 79
Cdd:COG0169 4 TRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPPEDLAAAVAGLRALGiRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLsKLDDGTLLGDNTDGAGLVRDLTvNCGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERL 159
Cdd:COG0169 84 LIGAVNTV-VFEDGRLIGDNTDGIGFVRALR-EAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 160 AEEFadlgPVFASSFDWLEE---PVDLIINATSASLAG-ELPPVSPNLVQPGAtFCYDMMYGKEPTAFCRWASEHGaAQS 235
Cdd:COG0169 162 AARL----GVRAVPLDDLAAalaGADLVINATPLGMAGgDALPLPASLLAPGA-VVYDLVYNPLETPLLRAARARG-ARV 235
|
250 260 270
....*....|....*....|....*....|....*
gi 492583493 236 VDGLGMLVEQAAEAFLLWRGVRPDSAPVLAELRRL 270
Cdd:COG0169 236 IDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRAL 270
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
4-272 |
7.65e-89 |
|
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: 265.05 E-value: 7.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 4 YVVFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQRAG 82
Cdd:TIGR00507 3 YGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEDALSGFFALGfKGANVTSPFKERAFQFLDEIDGRAKLAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 83 AVNTLsKLDDGTLLGDNTDGAGLVRDLTVNcgVELR-GRRVLLLGAGGAVRGALEPLLaEQPAVLVIANRTVEKAERLAE 161
Cdd:TIGR00507 83 AVNTL-VLEDGKLVGYNTDGIGLVSDLEQL--IPLRpNQNVLIIGAGGAAKAVALELL-KADCNVIIANRTVSKAEELAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 162 EFADLGPVFASSFDWLE-EPVDLIINATSASLAGEL--PPVSPNLVQPGAtFCYDMMYGKEPTAFCRWASEHGaAQSVDG 238
Cdd:TIGR00507 159 RFQRYGEIQAFSMDELPlHRVDLIINATSAGMSGNIdePPVPAEYLKEGK-LVYDLVYNPLETPFLAEAKSLG-TKTIDG 236
|
250 260 270
....*....|....*....|....*....|....
gi 492583493 239 LGMLVEQAAEAFLLWRGVRPDSAPVLAELRRLLA 272
Cdd:TIGR00507 237 LGMLVYQAALSFELWTGVEPDIEKMFEQLISVLA 270
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
100-255 |
1.42e-44 |
|
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: 147.80 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 100 TDGAGLVRDLTVNcGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVfASSFDWLEE 179
Cdd:cd01065 1 TDGLGFVRALEEA-GIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIA-IAYLDLEEL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492583493 180 P--VDLIINATSASLAGELP-PVSPNLVQPGATfCYDMMYGKEPTAFCRWASEHGaAQSVDGLGMLVEQAAEAFLLWRG 255
Cdd:cd01065 79 LaeADLIINTTPVGMKPGDElPLPPSLLKPGGV-VYDVVYNPLETPLLKEARALG-AKTIDGLEMLVYQAAEAFELWTG 155
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
7-255 |
2.30e-33 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 122.93 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 7 FGHPIGHSKSPLIHRLFAEQTGqsLDYrASLA---PLDDF--TVFAKAFFQIgRGANVTVPFKEEAYRLADSLTERGQRA 81
Cdd:PRK12548 15 IGSPVGHSGSPAMYNYSFQKAG--LDY-AYLAfdiPVDKVpdAIKAIKTFNM-RGANVTMPCKSEAAKYMDELSPAARII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 82 GAVNTLSKlDDGTLLGDNTDGAGLVRDLTVNcGVELRGRRVLLLGAGGA-----VRGALEPllAEQPAVLVIANRTVEKA 156
Cdd:PRK12548 91 GAVNTIVN-DDGKLTGHITDGLGFVRNLREH-GVDVKGKKLTVIGAGGAataiqVQCALDG--AKEITIFNIKDDFYERA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 157 ERLAEEFADLGPVFASSFDWLE---------EPVDLIINATsasLAGELPPVSPNLVQPGATF-----CYDMMYGKEPTA 222
Cdd:PRK12548 167 EQTAEKIKQEVPECIVNVYDLNdteklkaeiASSDILVNAT---LVGMKPNDGETNIKDTSVFrkdlvVADTVYNPKKTK 243
|
250 260 270
....*....|....*....|....*....|...
gi 492583493 223 FCRWASEHGaAQSVDGLGMLVEQAAEAFLLWRG 255
Cdd:PRK12548 244 LLEDAEAAG-CKTVGGLGMLLWQGAEAYKLYTG 275
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
3-255 |
5.90e-29 |
|
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: 111.16 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 3 QYVVFGHPIGHSKSPLIHRLFAEQTGqsLDYRASLAPLDDFTVFAKAFFQIGR---GANVTVPFKEEAYRLADSLTERGQ 79
Cdd:TIGR01809 7 KAFIIGKPIAHSRSPHLHNAGYEILG--LPDKTYEFETCSAEELKEVLSGFGPqfgGASVTIPLKFAILRFADEHTDRAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLSKLDDGTLLGDNTDGAGLVRDLTVNCGVE-LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAER 158
Cdd:TIGR01809 85 LIGSVNTLLRTQNGIWKGDNTDWDGIAGALANIGKFEpLAGFRGLVIGAGGTSRAAVYALASLGVTDITVINRNPDKLSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 159 LAEEFADLGPV----FASSFDWLEEPVDLII------NATSASLAGELPPVSPNLVQPGATFCYDMMYGKEPTAFCRWAS 228
Cdd:TIGR01809 165 LVDLGVQVGVItrleGDSGGLAIEKAAEVLVstvpadVPADYVDLFATVPFLLLKRKSSEGIFLDAAYDPWPTPLVAIVS 244
|
250 260
....*....|....*....|....*..
gi 492583493 229 EHGaAQSVDGLGMLVEQAAEAFLLWRG 255
Cdd:TIGR01809 245 AAG-WRVISGLQMLLHQGFAQFEQWTG 270
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
6-87 |
1.62e-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: 98.82 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 6 VFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQRAGAV 84
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNLPDFVEGLRALGfRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 492583493 85 NTL 87
Cdd:pfam08501 81 NTI 83
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
6-255 |
1.34e-22 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 94.30 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 6 VFGHPIGHSKSPLIHRLFAEQTGQSLDYRASLApldDFTVFAKAFFQIG----RGANVTVPFKEEAYRLADSLTERGQRA 81
Cdd:PRK12749 12 LMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEV---DNDSFPGAIEGLKalkmRGTGVSMPNKQLACEYVDELTPAAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 82 GAVNTLSKlDDGTLLGDNTDGAGLVRDLTvNCGVELRGRRVLLLGAGGA-----VRGALEPLLAeqpavLVIANRT---V 153
Cdd:PRK12749 89 GAINTIVN-DDGYLRGYNTDGTGHIRAIK-ESGFDIKGKTMVLLGAGGAstaigAQGAIEGLKE-----IKLFNRRdefF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 154 EKAERLAEEFADLGPVFASSFDWLEE--------PVDLIINATSAS---LAGELPPVSPNLVQPG--ATFCydmMYGKEP 220
Cdd:PRK12749 162 DKALAFAQRVNENTDCVVTVTDLADQqafaealaSADILTNGTKVGmkpLENESLVNDISLLHPGllVTEC---VYNPHM 238
|
250 260 270
....*....|....*....|....*....|....*
gi 492583493 221 TAFCRWASEHGAaQSVDGLGMLVEQAAEAFLLWRG 255
Cdd:PRK12749 239 TKLLQQAQQAGC-KTIDGYGMLLWQGAEQFTLWTG 272
|
|
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
4-250 |
2.41e-22 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 95.99 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 4 YVVFGHPIGHSKSPLIHrlfaEQTGQSLDYRASLAPL--DDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQR 80
Cdd:PLN02520 255 YGIIGKPVGHSKSPILH----NEAFKSVGFNGVYVHLlvDDLAKFLQTYSSPDfAGFSCTIPHKEDALKCCDEVDPIAKS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 81 AGAVNT-LSKLDDGTLLGDNTDGAGLVR---------DLTVNCGVELRGRRVLLLGAGGAVRgALEPLLAEQPAVLVIAN 150
Cdd:PLN02520 331 IGAINTiIRRPSDGKLVGYNTDYIGAISaiedglrasGSSPASGSPLAGKLFVVIGAGGAGK-ALAYGAKEKGARVVIAN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 151 RTVEKAERLAEEFAdlGPvfASSFDWLE--EPVDLIINATSASLaGELPPVSPNLVQPGA----TFCYDMMYGKEPTAFC 224
Cdd:PLN02520 410 RTYERAKELADAVG--GQ--ALTLADLEnfHPEEGMILANTTSV-GMQPNVDETPISKHAlkhySLVFDAVYTPKITRLL 484
|
250 260
....*....|....*....|....*.
gi 492583493 225 RWASEHGAAqSVDGLGMLVEQAAEAF 250
Cdd:PLN02520 485 REAEESGAI-IVSGTEMFIRQAYEQF 509
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
11-272 |
3.01e-20 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 87.64 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 11 IGHSKSPLIHRlfAEQTGQSLDYRASLAPLDDFTVFAKAFFQIGRGA--------NVTVPFKEEAYRLADSLTERGQRAG 82
Cdd:PRK12549 15 IQASLSPAMHE--AEGDAQGLRYVYRLIDLDALGLTADALPELLDAAermgfaglNITHPCKQAVIPHLDELSDDARALG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 83 AVNTLSkLDDGTLLGDNTD----GAGLVRDLTvncGVELRgrRVLLLGAGGA---VRGALEPLLAEQpavLVIANRTVEK 155
Cdd:PRK12549 93 AVNTVV-FRDGRRIGHNTDwsgfAESFRRGLP---DASLE--RVVQLGAGGAgaaVAHALLTLGVER---LTIFDVDPAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 156 AERLAEEFA------------DLGPVFASSfdwleepvDLIINATSASLAGeLP--PVSPNLVQPGaTFCYDMMYGKEPT 221
Cdd:PRK12549 164 AAALADELNarfpaaratagsDLAAALAAA--------DGLVHATPTGMAK-HPglPLPAELLRPG-LWVADIVYFPLET 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 492583493 222 AFCRWASEHGAAqSVDGLGMLVEQAAEAFLLWRGVRPDSAPVLAELRRLLA 272
Cdd:PRK12549 234 ELLRAARALGCR-TLDGGGMAVFQAVDAFELFTGREPDAERMLAHFASLVA 283
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
4-253 |
5.65e-18 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 82.92 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 4 YVVFGHPIGHSKSPLIHRLFAEQTGQSLDY-RASLAPLDdftvfAKAFFQIGR-----GANVTVPFKEEAYRLADSLTER 77
Cdd:PRK09310 218 YGLIGDPVDRSISHLSHNPLFSQLSLNCPYiKLPLTPQE-----LPKFFSTIRdlpflGLSVTMPLKTAVLDFLDKLDPS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 78 GQRAGAVNTLSkLDDGTLLGDNTDGAGLVRDLTVNcGVELRGRRVLLLGAGGAVRgALEPLLAEQPAVLVIANRTVEKAE 157
Cdd:PRK09310 293 VKLCGSCNTLV-FRNGKIEGYNTDGEGLFSLLKQK-NIPLNNQHVAIVGAGGAAK-AIATTLARAGAELLIFNRTKAHAE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 158 RLAEEFAdlgpvfASSFDWLEEP----VDLIINAtsaslageLPPVS--PNLVQPgatFCYDMMYGKEPTAFCRWASEHG 231
Cdd:PRK09310 370 ALASRCQ------GKAFPLESLPelhrIDIIINC--------LPPSVtiPKAFPP---CVVDINTLPKHSPYTQYARSQG 432
|
250 260
....*....|....*....|..
gi 492583493 232 aAQSVDGLGMLVEQAAEAFLLW 253
Cdd:PRK09310 433 -SSIIYGYEMFAEQALLQFRLW 453
|
|
| Shikimate_DH |
pfam01488 |
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
117-192 |
2.03e-11 |
|
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: 60.28 E-value: 2.03e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFadlGPVFASSFDWLEEPV---DLIINATSASL 192
Cdd:pfam01488 10 LKDKKVLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKF---GGVEALPLDDLKEYLaeaDIVISATSSPT 85
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
117-191 |
3.57e-11 |
|
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: 62.28 E-value: 3.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSFDWLEEpVDLIINATSAS 191
Cdd:cd05213 176 LKGKKVLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGGNAVPLDELLELLNE-ADVVISATGAP 249
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
117-192 |
7.20e-11 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 61.74 E-value: 7.20e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSFDWLEEpVDLIINATSASL 192
Cdd:PRK00045 180 LSGKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFGGEAIPLDELPEALAE-ADIVISSTGAPH 254
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
6-259 |
9.38e-11 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 60.82 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 6 VFGHPIGHSKSPLIHRLFAEQTGQSLDYR-----ASLAPLDDFTVFAKAFFQIG-RGANVTVPFKEEAYRLADSLTERGQ 79
Cdd:PRK14027 9 LIGQGLDLSRTPAMHEAEGLAQGRATVYRridtlGSRASGQDLKTLLDAALYLGfNGLNITHPYKQAVLPLLDEVSEQAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 80 RAGAVNTLSKLDDGTLLGDNTDGAGLVRDLTVNCGvELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERL 159
Cdd:PRK14027 89 QLGAVNTVVIDATGHTTGHNTDVSGFGRGMEEGLP-NAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 160 AEEFAD-LGPVFASSFD--WLEEPV---DLIINATSASLagelppvspnLVQPGATF---CY-------DMMYGKEPTAF 223
Cdd:PRK14027 168 ADVINNaVGREAVVGVDarGIEDVIaaaDGVVNATPMGM----------PAHPGTAFdvsCLtkdhwvgDVVYMPIETEL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 492583493 224 CRWASEHGaAQSVDGLGMLVEQAAEAFLLWRGVRPD 259
Cdd:PRK14027 238 LKAARALG-CETLDGTRMAIHQAVDAFRLFTGLEPD 272
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
55-263 |
1.05e-10 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 60.74 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 55 RGANVTVPFKEEAYRLADSLTERGQRAGAVNTLSKlDDGTLLGDNTDG---AGLVRDLTVNcgvelRGRRVLLLGAGG-- 129
Cdd:PRK12550 61 RGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVN-TDGHLKAYNTDYiaiAKLLASYQVP-----PDLVVALRGSGGma 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 130 -AVRGALEPllAEQPAVLVIAnRTVEKAERLAEefadlgpvfASSFDWLEEP----VDLIINATSASLAG-----ELpPV 199
Cdd:PRK12550 135 kAVAAALRD--AGFTDGTIVA-RNEKTGKALAE---------LYGYEWRPDLggieADILVNVTPIGMAGgpeadKL-AF 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492583493 200 SPNLVQpGATFCYDMMYGKEPTAFCRWASEHGaAQSVDGLGMLVEQAAEAFLLWRGVRPDSAPV 263
Cdd:PRK12550 202 PEAEID-AASVVFDVVALPAETPLIRYARARG-KTVITGAEVIALQAVEQFVLYTGVRPSDELI 263
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
116-192 |
1.73e-10 |
|
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: 60.90 E-value: 1.73e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492583493 116 ELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEF-ADLGPvFASSFDWLEEpVDLIINATSASL 192
Cdd:COG0373 179 DLSGKTVLVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFgGEAVP-LEELPEALAE-ADIVISSTGAPH 254
|
|
| SDH_C |
pfam18317 |
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ... |
238-268 |
1.55e-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: 46.64 E-value: 1.55e-07
10 20 30
....*....|....*....|....*....|.
gi 492583493 238 GLGMLVEQAAEAFLLWRGVRPDSAPVLAELR 268
Cdd:pfam18317 1 GLGMLVEQGAEQFELWTGREPPVEVMREALL 31
|
|
| hemA |
TIGR01035 |
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
117-193 |
3.17e-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: 50.85 E-value: 3.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSFDWLEEpVDLIINATSASLA 193
Cdd:TIGR01035 178 LKGKKALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVKFEDLEEYLAE-ADIVISSTGAPHP 253
|
|
| fabG |
PRK05653 |
3-oxoacyl-ACP reductase FabG; |
117-167 |
1.51e-04 |
|
3-oxoacyl-ACP reductase FabG;
Pssm-ID: 235546 [Multi-domain] Cd Length: 246 Bit Score: 42.07 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLG 167
Cdd:PRK05653 3 LQGKTALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAG 53
|
|
| PRK08618 |
PRK08618 |
ornithine cyclodeaminase family protein; |
124-208 |
4.17e-04 |
|
ornithine cyclodeaminase family protein;
Pssm-ID: 236313 [Multi-domain] Cd Length: 325 Bit Score: 41.20 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 124 LLGAGGAVRGALEPLLA-EQPAVLVIANRTVEKAERLAEEFADLGPVFASSFDWLEEPV---DLIINATSASlagelPPV 199
Cdd:PRK08618 132 LIGTGGQAKGQLEAVLAvRDIERVRVYSRTFEKAYAFAQEIQSKFNTEIYVVNSADEAIeeaDIIVTVTNAK-----TPV 206
|
....*....
gi 492583493 200 SPNLVQPGA 208
Cdd:PRK08618 207 FSEKLKKGV 215
|
|
| PRK13940 |
PRK13940 |
glutamyl-tRNA reductase; Provisional |
120-191 |
6.01e-04 |
|
glutamyl-tRNA reductase; Provisional
Pssm-ID: 172450 [Multi-domain] Cd Length: 414 Bit Score: 40.77 E-value: 6.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492583493 120 RRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSFDWLEEPVDLIINATSAS 191
Cdd:PRK13940 182 KNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSAFRNASAHYLSELPQLIKKADIIIAAVNVL 253
|
|
| PRK12936 |
PRK12936 |
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed |
116-174 |
1.07e-03 |
|
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
Pssm-ID: 171820 [Multi-domain] Cd Length: 245 Bit Score: 39.51 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 492583493 116 ELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSF 174
Cdd:PRK12936 3 DLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANL 61
|
|
| PRK09072 |
PRK09072 |
SDR family oxidoreductase; |
117-169 |
5.24e-03 |
|
SDR family oxidoreductase;
Pssm-ID: 236372 [Multi-domain] Cd Length: 263 Bit Score: 37.61 E-value: 5.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPV 169
Cdd:PRK09072 3 LKDKRVLLTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARLPYPGRH 55
|
|
| PRK06125 |
PRK06125 |
short chain dehydrogenase; Provisional |
117-199 |
6.04e-03 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 235703 [Multi-domain] Cd Length: 259 Bit Score: 37.33 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLGPVFASSFdwleePVDLIINATSASLAGEL 196
Cdd:PRK06125 5 LAGKRVLITGASKGIGAAAAEAFAAEGCHLHLVARDADALEALAADLRAAHGVDVAVH-----ALDLSSPEAREQLAAEA 79
|
...
gi 492583493 197 PPV 199
Cdd:PRK06125 80 GDI 82
|
|
| PRK08085 |
PRK08085 |
gluconate 5-dehydrogenase; Provisional |
117-175 |
9.68e-03 |
|
gluconate 5-dehydrogenase; Provisional
Pssm-ID: 181225 [Multi-domain] Cd Length: 254 Bit Score: 36.66 E-value: 9.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 117 LRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLG-PVFASSFD 175
Cdd:PRK08085 7 LAGKNILITGSAQGIGFLLATGLAEYGAEIIINDITAERAELAVAKLRQEGiKAHAAPFN 66
|
|
| NAD_bind_H4MPT_DH |
cd01078 |
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ... |
97-211 |
9.79e-03 |
|
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. 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 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: 133446 [Multi-domain] Cd Length: 194 Bit Score: 36.22 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583493 97 GDNTDGAGLVRDLT---VNCGVELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEF-----ADLGP 168
Cdd:cd01078 3 GSNTTAAAAVAAAGkalELMGKDLKGKTAVVLGGTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLrarfgEGVGA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 492583493 169 VFASSFDWLEEPV---DLIINATSASLagELPPVSPNLVQPGATFC 211
Cdd:cd01078 83 VETSDDAARAAAIkgaDVVFAAGAAGV--ELLEKLAWAPKPLAVAA 126
|
|
| PRK08277 |
PRK08277 |
D-mannonate oxidoreductase; Provisional |
115-167 |
9.95e-03 |
|
D-mannonate oxidoreductase; Provisional
Pssm-ID: 236216 [Multi-domain] Cd Length: 278 Bit Score: 36.80 E-value: 9.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 492583493 115 VELRGRRVLLLGAGGAVRGALEPLLAEQPAVLVIANRTVEKAERLAEEFADLG 167
Cdd:PRK08277 6 FSLKGKVAVITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAG 58
|
|
| |
