|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
19-538 |
0e+00 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 1030.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 19 VGMGSGGVRRNPTLICTPIMADSVDKMAILMAEAKSVGADLVEIRLDSLKDFNPNSDIKTLILHSPLPTLFTYRPMWEGG 98
Cdd:PLN02520 11 DLQGSGGVRRNPTLICVPIMADSVDKMLIEMAKAKELGADLVEIRLDFLKNFNPREDLKTLIKQSPLPTLVTYRPKWEGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 99 QYNGDEKPRLDALRLAMELGADYIDVELKVAHEFNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVK 178
Cdd:PLN02520 91 QYEGDENKRQDALRLAMELGADYVDVELKVAHEFINSISGKKPEKCKVIVSSHNYENTPSVEELGNLVARIQATGADIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 179 IATTALDISDVARIFQITVHSQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESGVVSAPGQPTIKDLLDLYNFRLIGP 258
Cdd:PLN02520 171 IATTALDITDVARMFQITVHSQVPTIGLVMGERGLISRILCPKFGGYLTFGTLEAGKVSAPGQPTIKDLLDLYNFRQIGP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 259 DTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLVDDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKS 338
Cdd:PLN02520 251 DTKVYGIIGKPVGHSKSPILHNEAFKSVGFNGVYVHLLVDDLAKFLQTYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 339 IGAVNCIIRRQNDGKLFGYNTDYVGAISAIEEGLRASqNVSNTVGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIAN 418
Cdd:PLN02520 331 IGAINTIIRRPSDGKLVGYNTDYIGAISAIEDGLRAS-GSSPASGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIAN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 419 RTYERAKVLADIIGGDAITLADLENFHPEDGMILANTTSIGMQPKVDETPVSKNALRSYSLVFDAVYTPKITRLLREAEE 498
Cdd:PLN02520 410 RTYERAKELADAVGGQALTLADLENFHPEEGMILANTTSVGMQPNVDETPISKHALKHYSLVFDAVYTPKITRLLREAEE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 224107417 499 SGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQKIMSKY 538
Cdd:PLN02520 490 SGAIIVSGTEMFIRQAYEQFERFTGLPAPKELFREIMSKY 529
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
258-537 |
6.03e-85 |
|
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: 264.31 E-value: 6.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 258 PDTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV--DDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPV 335
Cdd:COG0169 2 GKTRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVppEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 336 AKSIGAVNCIIRRqnDGKLFGYNTDYVGAISAIEEGlrasqnvsntvGSPLAGKLFVVIgaggagkalaygakekGA--- 412
Cdd:COG0169 82 ARLIGAVNTVVFE--DGRLIGDNTDGIGFVRALREA-----------GVDLAGKRVLVL----------------GAgga 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 413 --------------RVVIANRTYERAKVLADIIGGDAITLADLENFhPEDGMILANTTSIGMQPKvDETPVSKNALRSYS 478
Cdd:COG0169 133 aravaaalaeagaaEITIVNRTPERAEALAARLGVRAVPLDDLAAA-LAGADLVINATPLGMAGG-DALPLPASLLAPGA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224107417 479 LVFDAVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQKIMSK 537
Cdd:COG0169 211 VVYDLVYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
34-251 |
7.18e-83 |
|
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.
Pssm-ID: 426287 Cd Length: 227 Bit Score: 257.10 E-value: 7.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 34 CTPIMADSVDKMAILMAEAKSvGADLVEIRLDSLKDFNPNSD-----IKTLILHSPLPTLFTYRPMWEGGQYNGDEKPRL 108
Cdd:pfam01487 1 CVPLTGKTLEEILEELESGKE-GADLVELRVDLLEEPVEDAEdvseqLALLRRVGDLPLIFTFRTKSEGGEPDGSEEEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 109 DALRLAMELGADYIDVELKVAHEFNELLRGNKP-GKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTALDIS 187
Cdd:pfam01487 80 ELLRLALRLGVDYVDVELFLPEEILKELIEAKHeGGTKVIGSYHDFEGTPSWEELISRYEKMQALGADIVKIAVMAKSIE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224107417 188 DVARIFQITVH----SQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESGVVSAPGQPTIKDLLDLY 251
Cdd:pfam01487 160 DVLALLRFTSEmkslADKPLIAMSMGELGRISRVLGPIFGSPVTFAALGLAEKSAPGQLTAKELREAL 227
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
32-251 |
4.15e-77 |
|
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273439 Cd Length: 229 Bit Score: 242.67 E-value: 4.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 32 LICTPIMADSVDKMAILMAEAKSVGADLVEIRLDSLKDFNPNSDIKTLI-----LHSPLPTLFTYRPMWEGGQYNGDEKP 106
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEKGADIVELRVDLLKDVSSNNDVDALSeqlseLRVDKPLIFTIRTQSEGGKFPGNEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 107 RLDALRLAME-LGADYIDVELKVAHEF-NELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTAL 184
Cdd:TIGR01093 81 YFEELKRAAEsLGPDFVDIELFLPDDAvKELINIAKKGGTKIIMSNHDFQKTPSWEEIVERLRKALSYGADIVKIAVMAN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224107417 185 DISDVARIFQITVHSQ----VPIIGLVMGERGLISRILCAKFGGYLTFGTLesGVVSAPGQPTIKDLLDLY 251
Cdd:TIGR01093 161 SKEDVLTLLSATNKVDthydVPLITMSMGDRGKISRVLGAVFGSVLTFGSL--GKASAPGQISVDDLRELL 229
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
32-253 |
8.54e-67 |
|
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.
Pssm-ID: 188633 Cd Length: 225 Bit Score: 215.67 E-value: 8.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 32 LICTPIMADSVDKMAILMAEaKSVGADLVEIRLDSLKD---FNPNSDIKTLILHSPLPTLFTYRPMWEGGQYNGDEKPRL 108
Cdd:cd00502 1 KICVPLTGPDLLEEALSLLE-LLLGADAVELRVDLLEDpsiDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFEGSEEEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 109 DALRLAMELGADYIDVELKVAhEFNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTALDISD 188
Cdd:cd00502 80 ELLEEALKLGPDYVDIELDSA-LLEELINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAALGADIVKIAVMANSIED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224107417 189 VARIFQITV----HSQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESgvVSAPGQPTIKDLLDLYNF 253
Cdd:cd00502 159 NLRLLKFTRqvknLYDIPLIAINMGELGKLSRILSPVFGSPLTYASLPE--PSAPGQLSVEELKQALSL 225
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
19-538 |
0e+00 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 1030.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 19 VGMGSGGVRRNPTLICTPIMADSVDKMAILMAEAKSVGADLVEIRLDSLKDFNPNSDIKTLILHSPLPTLFTYRPMWEGG 98
Cdd:PLN02520 11 DLQGSGGVRRNPTLICVPIMADSVDKMLIEMAKAKELGADLVEIRLDFLKNFNPREDLKTLIKQSPLPTLVTYRPKWEGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 99 QYNGDEKPRLDALRLAMELGADYIDVELKVAHEFNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVK 178
Cdd:PLN02520 91 QYEGDENKRQDALRLAMELGADYVDVELKVAHEFINSISGKKPEKCKVIVSSHNYENTPSVEELGNLVARIQATGADIVK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 179 IATTALDISDVARIFQITVHSQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESGVVSAPGQPTIKDLLDLYNFRLIGP 258
Cdd:PLN02520 171 IATTALDITDVARMFQITVHSQVPTIGLVMGERGLISRILCPKFGGYLTFGTLEAGKVSAPGQPTIKDLLDLYNFRQIGP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 259 DTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLVDDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKS 338
Cdd:PLN02520 251 DTKVYGIIGKPVGHSKSPILHNEAFKSVGFNGVYVHLLVDDLAKFLQTYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 339 IGAVNCIIRRQNDGKLFGYNTDYVGAISAIEEGLRASqNVSNTVGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIAN 418
Cdd:PLN02520 331 IGAINTIIRRPSDGKLVGYNTDYIGAISAIEDGLRAS-GSSPASGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIAN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 419 RTYERAKVLADIIGGDAITLADLENFHPEDGMILANTTSIGMQPKVDETPVSKNALRSYSLVFDAVYTPKITRLLREAEE 498
Cdd:PLN02520 410 RTYERAKELADAVGGQALTLADLENFHPEEGMILANTTSVGMQPNVDETPISKHALKHYSLVFDAVYTPKITRLLREAEE 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 224107417 499 SGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQKIMSKY 538
Cdd:PLN02520 490 SGAIIVSGTEMFIRQAYEQFERFTGLPAPKELFREIMSKY 529
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
258-537 |
6.03e-85 |
|
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: 264.31 E-value: 6.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 258 PDTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV--DDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPV 335
Cdd:COG0169 2 GKTRLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVppEDLAAAVAGLRALGIRGLNVTIPHKEAAIPLLDELDPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 336 AKSIGAVNCIIRRqnDGKLFGYNTDYVGAISAIEEGlrasqnvsntvGSPLAGKLFVVIgaggagkalaygakekGA--- 412
Cdd:COG0169 82 ARLIGAVNTVVFE--DGRLIGDNTDGIGFVRALREA-----------GVDLAGKRVLVL----------------GAgga 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 413 --------------RVVIANRTYERAKVLADIIGGDAITLADLENFhPEDGMILANTTSIGMQPKvDETPVSKNALRSYS 478
Cdd:COG0169 133 aravaaalaeagaaEITIVNRTPERAEALAARLGVRAVPLDDLAAA-LAGADLVINATPLGMAGG-DALPLPASLLAPGA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224107417 479 LVFDAVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQKIMSK 537
Cdd:COG0169 211 VVYDLVYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRA 269
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
34-251 |
7.18e-83 |
|
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.
Pssm-ID: 426287 Cd Length: 227 Bit Score: 257.10 E-value: 7.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 34 CTPIMADSVDKMAILMAEAKSvGADLVEIRLDSLKDFNPNSD-----IKTLILHSPLPTLFTYRPMWEGGQYNGDEKPRL 108
Cdd:pfam01487 1 CVPLTGKTLEEILEELESGKE-GADLVELRVDLLEEPVEDAEdvseqLALLRRVGDLPLIFTFRTKSEGGEPDGSEEEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 109 DALRLAMELGADYIDVELKVAHEFNELLRGNKP-GKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTALDIS 187
Cdd:pfam01487 80 ELLRLALRLGVDYVDVELFLPEEILKELIEAKHeGGTKVIGSYHDFEGTPSWEELISRYEKMQALGADIVKIAVMAKSIE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224107417 188 DVARIFQITVH----SQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESGVVSAPGQPTIKDLLDLY 251
Cdd:pfam01487 160 DVLALLRFTSEmkslADKPLIAMSMGELGRISRVLGPIFGSPVTFAALGLAEKSAPGQLTAKELREAL 227
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
32-251 |
4.15e-77 |
|
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273439 Cd Length: 229 Bit Score: 242.67 E-value: 4.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 32 LICTPIMADSVDKMAILMAEAKSVGADLVEIRLDSLKDFNPNSDIKTLI-----LHSPLPTLFTYRPMWEGGQYNGDEKP 106
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEKGADIVELRVDLLKDVSSNNDVDALSeqlseLRVDKPLIFTIRTQSEGGKFPGNEEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 107 RLDALRLAME-LGADYIDVELKVAHEF-NELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTAL 184
Cdd:TIGR01093 81 YFEELKRAAEsLGPDFVDIELFLPDDAvKELINIAKKGGTKIIMSNHDFQKTPSWEEIVERLRKALSYGADIVKIAVMAN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224107417 185 DISDVARIFQITVHSQ----VPIIGLVMGERGLISRILCAKFGGYLTFGTLesGVVSAPGQPTIKDLLDLY 251
Cdd:TIGR01093 161 SKEDVLTLLSATNKVDthydVPLITMSMGDRGKISRVLGAVFGSVLTFGSL--GKASAPGQISVDDLRELL 229
|
|
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
260-529 |
9.52e-72 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 230.46 E-value: 9.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 260 TKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV--DDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAK 337
Cdd:PRK00258 5 TRLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVppEDLEDAVKGFFALGGRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 338 SIGAVNCIIRRqnDGKLFGYNTDYVGAISAIEEGLrasqnvsntvGSPLAGKLFVVIgaggagkalaygakekGA----- 412
Cdd:PRK00258 85 LIGAVNTLVLE--DGRLIGDNTDGIGFVRALEERL----------GVDLKGKRILIL----------------GAggaar 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 413 ------------RVVIANRTYERAKVLADIIGGDAITLADLENFHPEDGM-ILANTTSIGMQPKVDETPVSKNALRSYSL 479
Cdd:PRK00258 137 avilplldlgvaEITIVNRTVERAEELAKLFGALGKAELDLELQEELADFdLIINATSAGMSGELPLPPLPLSLLRPGTI 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224107417 480 VFDAVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKE 529
Cdd:PRK00258 217 VYDMIYGPLPTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVRPPVE 266
|
|
| AroD |
COG0710 |
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ... |
29-253 |
2.90e-70 |
|
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440474 Cd Length: 236 Bit Score: 224.79 E-value: 2.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 29 NPTLICTPIMADSVDKMAILMAEAKSVGADLVEIRLDSLKDFNPNS---DIKTLILHSPLPTLFTYRPMWEGGQYNGDEK 105
Cdd:COG0710 2 GRPKICVPLVGATPEDLLAEAEAAARAGADLVELRLDYLEDPDLEElkeLLEALREYGGLPLIFTFRTAEEGGEFEGSEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 106 PRLDALRLAMEL-GADYIDVELKVAHE-FNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTA 183
Cdd:COG0710 82 ERLELLRAAADSaGVDLVDVELDTLEDdVDDLIEAAREAGVKVIVSYHDFEKTPSAEELVEILEKMQELGADIVKIAVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224107417 184 LDISDVARIFQIT----VHSQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESgvVSAPGQPTIKDLLDLYNF 253
Cdd:COG0710 162 KSPEDVLRLLEATleakEELDRPVITMAMGELGKISRILGPLFGSALTYASVGE--ASAPGQIDVEELRELLEL 233
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
32-253 |
8.54e-67 |
|
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.
Pssm-ID: 188633 Cd Length: 225 Bit Score: 215.67 E-value: 8.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 32 LICTPIMADSVDKMAILMAEaKSVGADLVEIRLDSLKD---FNPNSDIKTLILHSPLPTLFTYRPMWEGGQYNGDEKPRL 108
Cdd:cd00502 1 KICVPLTGPDLLEEALSLLE-LLLGADAVELRVDLLEDpsiDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFEGSEEEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 109 DALRLAMELGADYIDVELKVAhEFNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADIVKIATTALDISD 188
Cdd:cd00502 80 ELLEEALKLGPDYVDIELDSA-LLEELINSRKKGNTKIIGSYHDFSGTPSDEELVSRLEKMAALGADIVKIAVMANSIED 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224107417 189 VARIFQITV----HSQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESgvVSAPGQPTIKDLLDLYNF 253
Cdd:cd00502 159 NLRLLKFTRqvknLYDIPLIAINMGELGKLSRILSPVFGSPLTYASLPE--PSAPGQLSVEELKQALSL 225
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
261-522 |
6.48e-53 |
|
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: 180.69 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 261 KVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV--DDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKS 338
Cdd:TIGR00507 1 KLYGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVppDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 339 IGAVNCIIRRqnDGKLFGYNTDYVGAISAIEEglrasqnvsntVGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIAN 418
Cdd:TIGR00507 81 AGAVNTLVLE--DGKLVGYNTDGIGLVSDLEQ-----------LIPLRPNQNVLIIGAGGAAKAVALELLKADCNVIIAN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 419 RTYERAKVLADII---GGD-AITLADLEnFHPEDGMIlaNTTSIGMQPKVDETPVSKNALRSYSLVFDAVYTPKITRLLR 494
Cdd:TIGR00507 148 RTVSKAEELAERFqryGEIqAFSMDELP-LHRVDLII--NATSAGMSGNIDEPPVPAEYLKEGKLVYDLVYNPLETPFLA 224
|
250 260
....*....|....*....|....*...
gi 224107417 495 EAEESGAKIVTGLEMFIGQAYEQFERFT 522
Cdd:TIGR00507 225 EAKSLGTKTIDGLGMLVYQAALSFELWT 252
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
256-533 |
1.76e-42 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 153.36 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 256 IGPDTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYV--HLLVDDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVH 333
Cdd:PRK12548 5 ISGTTGLLGLIGSPVGHSGSPAMYNYSFQKAGLDYAYLafDIPVDKVPDAIKAIKTFNMRGANVTMPCKSEAAKYMDELS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 334 PVAKSIGAVNCIIrrQNDGKLFGYNTDYVGAISAIEEGlrasqnvsntvGSPLAGKLFVVIGAGGAGKALAYGAKEKGAR 413
Cdd:PRK12548 85 PAARIIGAVNTIV--NDDGKLTGHITDGLGFVRNLREH-----------GVDVKGKKLTVIGAGGAATAIQVQCALDGAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 414 -VVIANRT---YERAKVLADIIGGDA----ITLADLENFHP-----EDGMILANTTSIGMQPKVDETPVSK-NALRSYSL 479
Cdd:PRK12548 152 eITIFNIKddfYERAEQTAEKIKQEVpeciVNVYDLNDTEKlkaeiASSDILVNATLVGMKPNDGETNIKDtSVFRKDLV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 224107417 480 VFDAVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQK 533
Cdd:PRK12548 232 VADTVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAEAYKLYTGKDMPVEEVKE 285
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
58-532 |
9.40e-42 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 156.11 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 58 DLVEIRLDSLKDFNPNsDIKTLILHSPLPTLfTYRPMWEGGQYNGDEKprldALRLAmELGADYIDVELKVAHEFNELLR 137
Cdd:PRK09310 26 DCIELRVDLLLSLSDL-ELKKLIELAPIPIL-TWKKHESCSQAAWIDK----MQSLA-KLNPNYLDIDKDFPKEALIRIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 138 GNKPgKCKLIVSSHNYENtpsvEELGNLVARIQAAGADIVKIATTALDISDVARIFQITVHSQVPIIGLVMGERGLISRI 217
Cdd:PRK09310 99 KLHP-KIKIILSYHTSEH----EDIIQLYNEMLASAADYYKIAVSSSSSTDLLNIIHQKRSLPENTTVLCMGGMGRPSRI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 218 LCAKFGGYLTFGTLESGVVSAPGQPTIKDLLdLYNFRLIGPDTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV 297
Cdd:PRK09310 174 LSPLLQNAFNYAAGIGAPPVAPGQLSLEHLL-FYNYANLSAQSPIYGLIGDPVDRSISHLSHNPLFSQLSLNCPYIKLPL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 298 D--DIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKSIGAVNCIIRRQNdgKLFGYNTDYVGAISAIEEglras 375
Cdd:PRK09310 253 TpqELPKFFSTIRDLPFLGLSVTMPLKTAVLDFLDKLDPSVKLCGSCNTLVFRNG--KIEGYNTDGEGLFSLLKQ----- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 376 QNVsntvgsPLAGKLFVVIGAGGAGKALAYGAKEKGARVVIANRTYERAKVLADIIGGDAITLADLENFHPEDGMILANT 455
Cdd:PRK09310 326 KNI------PLNNQHVAIVGAGGAAKAIATTLARAGAELLIFNRTKAHAEALASRCQGKAFPLESLPELHRIDIIINCLP 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224107417 456 TSIGMQPKVDETPVSKNALrsyslvfdavytPKITRLLREAEESGAKIVTGLEMFIGQAYEQFerftELPAPKELFQ 532
Cdd:PRK09310 400 PSVTIPKAFPPCVVDINTL------------PKHSPYTQYARSQGSSIIYGYEMFAEQALLQF----RLWFPTLLFK 460
|
|
| aroD |
PRK02412 |
type I 3-dehydroquinate dehydratase; |
31-247 |
4.71e-41 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 235036 Cd Length: 253 Bit Score: 148.51 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 31 TLICTPIMADSVDKmaiLMAEAKSV---GADLVEIRLDSLKDFnpnSDIKTLILHSP--------LPTLFTYRPMWEGGQ 99
Cdd:PRK02412 16 PKIIVPIMGKTLEE---VLAEALAIskyDADIIEWRADFLEKI---SDVESVLAAAPairekfagKPLLFTFRTAKEGGE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 100 YNGDEKPRLDALRLAMELGA-DYIDVELkVAHE--FNELLRGNKPGKCKLIVSSHNYENTPSVEELGNLVARIQAAGADI 176
Cdd:PRK02412 90 IALSDEEYLALIKAVIKSGLpDYIDVEL-FSGKdvVKEMVAFAHEHGVKVVLSYHDFEKTPPKEEIVERLRKMESLGADI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224107417 177 VKIATTALDISDVARIFQITVH-----SQVPIIGLVMGERGLISRILCAKFGGYLTFGTLESgvVSAPGQPTIKDL 247
Cdd:PRK02412 169 VKIAVMPQSEQDVLTLLNATREmkelyADQPLITMSMGKLGRISRLAGEVFGSSWTFASLDK--ASAPGQISVEDL 242
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
359-522 |
4.73e-34 |
|
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: 126.23 E-value: 4.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 359 TDYVGAISAIEEGLrasQNVSNT----VGSPLAGK--LFVVIgaggagkalaygaKEKGARVVIANRTYERAKVLADIIG 432
Cdd:cd01065 1 TDGLGFVRALEEAG---IELKGKkvliLGAGGAARavAYALA-------------ELGAAKIVIVNRTLEKAKALAERFG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 433 --GDAITLADLENFHpEDGMILANTTSIGMQPkVDETPVSKNALRSYSLVFDAVYTPKITRLLREAEESGAKIVTGLEMF 510
Cdd:cd01065 65 elGIAIAYLDLEELL-AEADLIINTTPVGMKP-GDELPLPPSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEML 142
|
170
....*....|..
gi 224107417 511 IGQAYEQFERFT 522
Cdd:cd01065 143 VYQAAEAFELWT 154
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
261-535 |
3.44e-33 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 127.81 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 261 KVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLVDD--IARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKS 338
Cdd:PRK12749 8 ELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNdsFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 339 IGAVNCIIrrQNDGKLFGYNTDYVGAISAIEEGlrasqnvsntvGSPLAGKLFVVIGAGGAGKALAYGAKEKGARVV-IA 417
Cdd:PRK12749 88 VGAINTIV--NDDGYLRGYNTDGTGHIRAIKES-----------GFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIkLF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 418 NRT---YERAKVLADIIGGDA---ITLADLENFHP-----EDGMILANTTSIGMQPKVDETPVS-KNALRSYSLVFDAVY 485
Cdd:PRK12749 155 NRRdefFDKALAFAQRVNENTdcvVTVTDLADQQAfaealASADILTNGTKVGMKPLENESLVNdISLLHPGLLVTECVY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 224107417 486 TPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKELFQKIM 535
Cdd:PRK12749 235 NPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVM 284
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
265-345 |
2.67e-29 |
|
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: 110.38 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 265 IIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLV--DDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKSIGAV 342
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVppDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 224107417 343 NCI 345
Cdd:pfam08501 81 NTI 83
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
255-529 |
3.97e-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: 116.55 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 255 LIGPdtKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVYVHLLVDDIARFLQTYSST--DFAGFSCTIPHKEDAAKCCDEV 332
Cdd:TIGR01809 2 NKGP--KKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGFgpQFGGASVTIPLKFAILRFADEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 333 HPVAKSIGAVNCIIRRQNdGKLFGYNTDYVGAISAIeeglrasqnVSNTVGSPLAGKLFVVIGAGGAGKALAYGAKEKG- 411
Cdd:TIGR01809 80 TDRASLIGSVNTLLRTQN-GIWKGDNTDWDGIAGAL---------ANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 412 ARVVIANRTYERAKVLAD---------IIGGDAITLADleNFHPEdgmILANT--TSIGMQPKVDETPV---SKNALRSY 477
Cdd:TIGR01809 150 TDITVINRNPDKLSRLVDlgvqvgvitRLEGDSGGLAI--EKAAE---VLVSTvpADVPADYVDLFATVpflLLKRKSSE 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 224107417 478 SLVFDAVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTELPAPKE 529
Cdd:TIGR01809 225 GIFLDAAYDPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPRE 276
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
280-533 |
1.05e-25 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 106.58 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 280 NEAFKSVGINGVYVHLLVDDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVAKSIGAVNCIIrrQNDGKLFGYNT 359
Cdd:PRK12550 28 NYLYEALGLNFLYKAFTTTDLTAAIGGVRALGIRGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIV--NTDGHLKAYNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 360 DYVGAISAIEE---------GLRASQNVSNTVGSPLAGKLFvvigaggagkalaygakekgARVVIANRTYERAKVLADI 430
Cdd:PRK12550 106 DYIAIAKLLASyqvppdlvvALRGSGGMAKAVAAALRDAGF--------------------TDGTIVARNEKTGKALAEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 431 IGGDAItlADLENFHPEdgmILANTTSIGMQ--PKVDETPVSKNALRSYSLVFDAVYTPKITRLLREAEESGAKIVTGLE 508
Cdd:PRK12550 166 YGYEWR--PDLGGIEAD---ILVNVTPIGMAggPEADKLAFPEAEIDAASVVFDVVALPAETPLIRYARARGKTVITGAE 240
|
250 260
....*....|....*....|....*
gi 224107417 509 MFIGQAYEQFERFTELPAPKELFQK 533
Cdd:PRK12550 241 VIALQAVEQFVLYTGVRPSDELIAE 265
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
264-522 |
5.43e-21 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 93.04 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 264 GIIGKPVGHSKSPVLFNEAFKSVGINGVY-------VHLLVDDIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDEVHPVA 336
Cdd:PRK12549 9 GLIGAGIQASLSPAMHEAEGDAQGLRYVYrlidldaLGLTADALPELLDAAERMGFAGLNITHPCKQAVIPHLDELSDDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 337 KSIGAVNCIIRRqnDGKLFGYNTDYVGAISAIEEGL------RASQNVSNTVGSPLAGKLfvvigaggagkalaygAKEK 410
Cdd:PRK12549 89 RALGAVNTVVFR--DGRRIGHNTDWSGFAESFRRGLpdasleRVVQLGAGGAGAAVAHAL----------------LTLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 411 GARVVIANRTYERAKVLADII-----GGDAITLADLENFHPE-DGMIlaNTTSIGMqPKVDETPVSKNALRSYSLVFDAV 484
Cdd:PRK12549 151 VERLTIFDVDPARAAALADELnarfpAARATAGSDLAAALAAaDGLV--HATPTGM-AKHPGLPLPAELLRPGLWVADIV 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 224107417 485 YTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFT 522
Cdd:PRK12549 228 YFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFT 265
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
259-524 |
2.03e-16 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 79.70 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 259 DTKVFGIIGKPVGHSKSPVLFNEAFKSVGINGVY--VHLLVD-----DIARFLQTYSSTDFAGFSCTIPHKEDAAKCCDE 331
Cdd:PRK14027 3 DSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYrrIDTLGSrasgqDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 332 VHPVAKSIGAVNCIIRRQnDGKLFGYNTDYVGAISAIEEGL-RASQNVSNTVGSPLAGKlfvvigaggagKALAYGAKEK 410
Cdd:PRK14027 83 VSEQATQLGAVNTVVIDA-TGHTTGHNTDVSGFGRGMEEGLpNAKLDSVVQVGAGGVGN-----------AVAYALVTHG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 411 GARVVIANRTYERAKVLADII----GGDAITLADL----ENFHPEDGMIlaNTTSIGMqPKVDETPVSKNALRSYSLVFD 482
Cdd:PRK14027 151 VQKLQVADLDTSRAQALADVInnavGREAVVGVDArgieDVIAAADGVV--NATPMGM-PAHPGTAFDVSCLTKDHWVGD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 224107417 483 AVYTPKITRLLREAEESGAKIVTGLEMFIGQAYEQFERFTEL 524
Cdd:PRK14027 228 VVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGL 269
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
408-442 |
1.74e-06 |
|
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: 50.50 E-value: 1.74e-06
10 20 30
....*....|....*....|....*....|....*.
gi 224107417 408 KEKGA-RVVIANRTYERAKVLADIIGGDAITLADLE 442
Cdd:COG0373 202 AAKGVkRITVANRTLERAEELAEEFGGEAVPLEELP 237
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
408-442 |
1.93e-06 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 50.18 E-value: 1.93e-06
10 20 30
....*....|....*....|....*....|....*.
gi 224107417 408 KEKGAR-VVIANRTYERAKVLADIIGGDAITLADLE 442
Cdd:PRK00045 202 AEKGVRkITVANRTLERAEELAEEFGGEAIPLDELP 237
|
|
| PRK13576 |
PRK13576 |
type I 3-dehydroquinate dehydratase; |
57-185 |
2.45e-06 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 237433 Cd Length: 216 Bit Score: 48.60 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224107417 57 ADLVEIRLDSLKDFnpNSDIKTLILHSPLPTLFTYRPMWEGGQYNGDEKPRLDALRLAMELGADYiDVELKVahefneLL 136
Cdd:PRK13576 26 ADLIELRLDYLKDR--EVSVIEFLDKYKDKLIVTLRDKAEGGINELDDELKISLLKELYDKQFLY-DVEASF------LQ 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 224107417 137 RGNKPGKCKlIVSSHNYENTPSVEELGNLVARIQAAgADIVKIATTALD 185
Cdd:PRK13576 97 KYNVPYDNK-IVSIHYFDYLPTSEEVKEIVSKFYEK-AFSVKIAVLGLK 143
|
|
| SDH_C |
pfam18317 |
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ... |
506-535 |
4.13e-06 |
|
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: 43.56 E-value: 4.13e-06
10 20 30
....*....|....*....|....*....|
gi 224107417 506 GLEMFIGQAYEQFERFTELPAPKELFQKIM 535
Cdd:pfam18317 1 GLGMLVEQGAEQFELWTGREPPVEVMREAL 30
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
408-442 |
6.06e-05 |
|
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: 45.33 E-value: 6.06e-05
10 20 30
....*....|....*....|....*....|....*
gi 224107417 408 KEKGARVVIANRTYERAKVLADIIGGDAITLADLE 442
Cdd:cd05213 199 AKGVAEITIANRTYERAEELAKELGGNAVPLDELL 233
|
|
| hemA |
TIGR01035 |
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
386-457 |
1.61e-04 |
|
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: 44.30 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224107417 386 LAGKLFVVIGAGGAGKALAYGAKEKGA-RVVIANRTYERAKVLADIIGGDAITLADLENFHPEDGMILANTTS 457
Cdd:TIGR01035 178 LKGKKALLIGAGEMGELVAKHLLRKGVgKILIANRTYERAEDLAKELGGEAVKFEDLEEYLAEADIVISSTGA 250
|
|
| Shikimate_DH |
pfam01488 |
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
409-442 |
8.06e-04 |
|
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: 39.86 E-value: 8.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 224107417 409 EKGAR-VVIANRTYERAKVLADIIGGD-AITLADLE 442
Cdd:pfam01488 33 AKGAKeVTIANRTIERAQELAEKFGGVeALPLDDLK 68
|
|
| |
