|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
17-415 |
0e+00 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 721.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVrDARPDQRSFVCASAGNHAQGVAYACRHFGVKG 96
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQL-SDEELAAGVVCASAGNHAQGVAYACRHLGIPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 97 TIFMPVTTPQQKIAKTRTFGGEAVEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRA-- 174
Cdd:PRK08639 100 VIFMPVTTPQQKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKEgs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 175 PDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMLDWVr 254
Cdd:PRK08639 180 PDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 255 PDQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEVKERAQRYSGLKKY 334
Cdd:PRK08639 259 VDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMPEIKERSLIYEGLKHY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 335 FILRMPQRPGALREFLM-MLGPDDDIARFEYLKKSARNFGSVLIGIETREAGNFARLTAVMEEAGLNYRDITGDGALAEF 413
Cdd:PRK08639 339 FIVNFPQRPGALREFLDdVLGPNDDITRFEYLKKNNRETGPVLVGIELKDAEDYDGLIERMEAFGPSYIDINPNEPLYNL 418
|
..
gi 506401820 414 LV 415
Cdd:PRK08639 419 LI 420
|
|
| THD1 |
TIGR02079 |
threonine dehydratase; This model represents threonine dehydratase, the first step in the ... |
17-415 |
0e+00 |
|
threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273957 [Multi-domain] Cd Length: 409 Bit Score: 547.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDqRSFVCASAGNHAQGVAYACRHFGVKG 96
Cdd:TIGR02079 12 EVVPHTPLQLNERLSEKYGANIYLKREDLQPVRSYKIRGAYNFLKQLSDAQLA-KGVVCASAGNHAQGFAYACRHLGVHG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 97 TIFMPVTTPQQKIAKTRTFGGEAVEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPD 176
Cdd:TIGR02079 91 TVFMPATTPKQKIDRVKIFGGEFIEIILVGDTFDQCAAAAREHVEDHGGTFIPPFDDPRIIEGQGTVAAEILDQLPEKPD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 177 LVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMLDWVrPD 256
Cdd:TIGR02079 171 YVVVPVGGGGLISGLTTYLAGTSPKTKIIGVEPEGAPSMKASLEAGEVVTLDKIDNFVDGAAVKRVGDLNFKALKDV-PD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 257 QVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEVKERAQRYSGLKKYFI 336
Cdd:TIGR02079 250 EVTLVPEGAVCTTILDLYNLEGIVAEPAGALSIAALERLGEEIKGKTVVCVVSGGNNDIERTEEIRERSLLYEGLKHYFI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 337 LRMPQRPGALREFL-MMLGPDDDIARFEYLKKSARNFGSVLIGIETREAGNFARLTAVMEEAGLNYRDITGDGALAEFLV 415
Cdd:TIGR02079 330 VRFPQRPGALREFLnDVLGPNDDITRFEYTKKSNRETGPALIGIELNDKEDFAGLLERMAAADIHYEDINENDILYNLLI 409
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
17-330 |
3.67e-134 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 387.86 E-value: 3.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPdQRSFVCASAGNHAQGVAYACRHFGVKG 96
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEER-ARGVVAASAGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 97 TIFMPVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGrAPD 176
Cdd:COG1171 99 TIVMPETAPAVKVAATRAYGA---EVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLP-DLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 177 LVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSML-DWVrp 255
Cdd:COG1171 175 AVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILrDLV-- 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506401820 256 DQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEVKERAQRYSG 330
Cdd:COG1171 253 DDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILERGLVGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
20-314 |
8.78e-111 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 327.52 E-value: 8.78e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 20 PETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKvrdARPDQRS--FVCASAGNHAQGVAYACRHFGVKGT 97
Cdd:cd01562 16 RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLS---LSEEERAkgVVAASAGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 98 IFMPVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGrAPDL 177
Cdd:cd01562 93 IVMPETAPAAKVDATRAYGA---EVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQVP-DLDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 178 VVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMLDwVRPDQ 257
Cdd:cd01562 169 VFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIR-KLVDD 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 506401820 258 VHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFD 314
Cdd:cd01562 248 VVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
21-407 |
2.51e-96 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 297.44 E-value: 2.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:PRK09224 20 ETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQ-LARGVITASAGNHAQGVALSAARLGIKAVIVM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPDLVVL 180
Cdd:PRK09224 99 PVTTPDIKVDAVRAFGGE---VVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 181 PVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSML-DWVrpDQVH 259
Cdd:PRK09224 176 PVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCqEYV--DDVI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 260 LAPEDRICITMLEML-NVEGIvLEPAGALSVDVLPELADR--IRGRTVVCVTSGGNFDFERLPEVKERAQrySGLKKYFI 336
Cdd:PRK09224 254 TVDTDEICAAIKDVFeDTRSI-AEPAGALALAGLKKYVAQhgIEGETLVAILSGANMNFDRLRYVAERAE--LGEQREAL 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506401820 337 L--RMPQRPGALREFLMMLGpDDDIARFEYlKKSARNFGSVLIGIETREAGNF-ARLTAVMEEAGLNYRDITGD 407
Cdd:PRK09224 331 LavTIPEEPGSFLKFCELLG-GRNVTEFNY-RYADAKEAHIFVGVQLSRGQEErAEIIAQLRAHGYPVVDLSDD 402
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
17-407 |
1.32e-88 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 277.83 E-value: 1.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVrDARPDQRSFVCASAGNHAQGVAYACRHFGVKG 96
Cdd:PRK12483 33 DVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARL-PAEQLARGVITASAGNHAQGVALAAARLGVKA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 97 TIFMPVTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPD 176
Cdd:PRK12483 112 VIVMPRTTPQLKVDGVRAHGGE---VVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 177 LVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSML-DWVrp 255
Cdd:PRK12483 189 AIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCrHYV-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 256 DQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADR--IRGRTVVCVTSGGNFDFERLPEVKERAQRYSGLKK 333
Cdd:PRK12483 267 DEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAERegIEGQTLVAIDSGANVNFDRLRHVAERAELGEQREA 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506401820 334 YFILRMPQRPGALREFLMMLGPdDDIARFEYLKKSARNfGSVLIGIETREAGN-FARLTAVMEEAGLNYRDITGD 407
Cdd:PRK12483 347 IIAVTIPEQPGSFKAFCAALGK-RQITEFNYRYADARE-AHLFVGVQTHPRHDpRAQLLASLRAQGFPVLDLTDD 419
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
17-405 |
7.86e-75 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 244.06 E-value: 7.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVrDARPDQRSFVCASAGNHAQGVAYACRHFGVKG 96
Cdd:PLN02550 105 DVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKL-PKEQLDKGVICSSAGNHAQGVALSAQRLGCDA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 97 TIFMPVTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPD 176
Cdd:PLN02550 184 VIAMPVTTPEIKWQSVERLGAT---VVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLH 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 177 LVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMLDWVRpD 256
Cdd:PLN02550 261 AIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELV-D 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 257 QVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADR--IRGRTVVCVTSGGNFDFERLPEVKERAQrySGLKKY 334
Cdd:PLN02550 340 GVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYygLKDENVVAITSGANMNFDRLRIVTELAD--VGRQQE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506401820 335 FILR--MPQRPGALREFLMMLGPdDDIARFEYLKKSARNfGSVLIGIETREAGNFARLTAVMEEAGLNYRDIT 405
Cdd:PLN02550 418 AVLAtfMPEEPGSFKRFCELVGP-MNITEFKYRYSSEKE-ALVLYSVGVHTEQELQALKKRMESAQLRTVNLT 488
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
22-310 |
2.15e-72 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 228.73 E-value: 2.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPdQRSFVCASAGNHAQGVAYACRHFGVKGTIFMP 101
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEG-GKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 102 VTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQAWCAE-QKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPDLVVL 180
Cdd:pfam00291 87 EDAPPGKLLLMRALGAE---VVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 181 PVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVAR-LGQLPFSMLDWVRpDQVH 259
Cdd:pfam00291 164 PVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYV-GEVV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 506401820 260 LAPEDRICITMLEMLNVEGIVLEPAGALSVDVLP-ELADRIR-GRTVVCVTSG 310
Cdd:pfam00291 243 TVSDEEALEAMRLLARREGIVVEPSSAAALAALKlALAGELKgGDRVVVVLTG 295
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
22-402 |
1.98e-70 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 226.55 E-value: 1.98e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVrDARPDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMP 101
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL-SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 102 VTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRApDLVVLP 181
Cdd:TIGR01127 80 ESAPPSKVKATKSYGA---EVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDV-DTVIVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 182 VGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSM-LDWVrpDQVHL 260
Cdd:TIGR01127 156 VGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIiKEYV--DDVVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 261 APEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEVKERAQRYSGLKKYFILRMP 340
Cdd:TIGR01127 234 VDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506401820 341 QRPGALREFLMMLGPDD----DIARFEYLKKSARNFGSVLIGIETREAGNFARLTAVMEEAGLNYR 402
Cdd:TIGR01127 314 DRPGALYHLLESIAEARanivKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKILRDMGYNFY 379
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
22-311 |
5.87e-63 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 202.75 E-value: 5.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKV-RDARPDQRSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAeEEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGgeaVEIVLTGDYFDQTLAAAQAWCAEQ-KAHFLAPFDDPDVIEGQASVGVELLEQL-GRAPDLV 178
Cdd:cd00640 81 PEGASPEKVAQMRALG---AEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VLPVGGGGLASGVTAFLRSEAPETDFRFVEPaggasllaaleaggptalprvnsfvdgaavarlgqlpfsmldwvrpdQV 258
Cdd:cd00640 158 VVPVGGGGNIAGIARALKELLPNVKVIGVEP-----------------------------------------------EV 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 506401820 259 HLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRI-RGRTVVCVTSGG 311
Cdd:cd00640 191 VTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
21-323 |
3.64e-62 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 203.81 E-value: 3.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAE-KRKGVVACSAGNHAQGVALSCALLGIDGKVVM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRApDLVVL 180
Cdd:PRK08638 106 PKGAPKSKVAATCGYGA---EVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDV-DTVIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 181 PVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMldwVRP--DQV 258
Cdd:PRK08638 182 PIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEI---VRElvDDI 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506401820 259 HLAPEDRICITMLEMLNVEGIVLEPAGALSVDVL--PELADRIRGRTVVCVTSGGNFDFERLPEVKE 323
Cdd:PRK08638 259 VLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALlsGKLDQYIQNKKVVAIISGGNVDLSRVSQITG 325
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
21-346 |
5.69e-60 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 200.12 E-value: 5.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:PRK07334 23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEE-RARGVIAMSAGNHAQGVAYHAQRLGIPATIVM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQlgrAPDL--V 178
Cdd:PRK07334 102 PRFTPTVKVERTRGFGA---EVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLED---APDLdtL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALeaGGPTALPRVNSFVDGAAVARLGQLPfsmLDWVRP--D 256
Cdd:PRK07334 176 VVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAI--KGVALPCGGSTIAEGIAVKQPGQLT---LEIVRRlvD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 257 QVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEVKERAQRYSGLKKYFI 336
Cdd:PRK07334 251 DILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLR 330
|
330
....*....|
gi 506401820 337 LRMPQRPGAL 346
Cdd:PRK07334 331 VDIRDRPGAL 340
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
20-321 |
2.43e-56 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 187.98 E-value: 2.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 20 PETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVrDARPDQRSFVCASAGNHAQGVAYACRHFGVKGTIF 99
Cdd:PRK06815 19 RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLL-NEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRaPDLVV 179
Cdd:PRK06815 98 APEQASAIKLDAIRALGA---EVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPD-LDAVF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 180 LPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVA-RLGQLPFSMLDWVRPDQV 258
Cdd:PRK06815 174 VAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFPLCQQLIDQKV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506401820 259 hLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEV 321
Cdd:PRK06815 254 -LVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEA 315
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
20-316 |
9.39e-52 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 176.31 E-value: 9.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 20 PETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIF 99
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQE-RARGVVTASTGNHGRALAYAARALGIRATIC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLgraPDL-- 177
Cdd:PRK07476 97 MSRLVPANKVDAIRALGAE---VRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEAL---PDVat 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 178 VVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVD--GAAVARLGQLPFSMldwVRP 255
Cdd:PRK07476 171 VLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslGGGIGLDNRYTFAM---CRA 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506401820 256 --DQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLpeLADRIRGRT--VVCVTSGGNFDFE 316
Cdd:PRK07476 248 llDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAAL--LAGKIAARDgpIVVVVSGANIDME 310
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
19-327 |
1.13e-47 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 166.34 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 19 FPETPLqrndHLSARYGadIWLKREDLTPVRSYKLRGAFTAMRKVRDaRPDQRSFVCASAGNHAQGVAYACRHFGVKGTI 98
Cdd:PRK08813 37 LSPTPL----HYAERFG--VWLKLENLQRTGSYKVRGALNALLAGLE-RGDERPVICASAGNHAQGVAWSAYRLGVQAIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 99 FMPVTTPQQKIAKTRTFGGEAVEivlTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELleqLGRAPDLV 178
Cdd:PRK08813 110 VMPHGAPQTKIAGVAHWGATVRQ---HGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIEL---AAHAPDVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VLPVGGGGLASGVTAFLRSEAPETDFRFVEpagGASLLAALEAGGPTALPRVNSFVDGAAVARLG----QLPFSMLdwvr 254
Cdd:PRK08813 184 IVPIGGGGLASGVALALKSQGVRVVGAQVE---GVDSMARAIRGDLREIAPVATLADGVKVKIPGfltrRLCSSLL---- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506401820 255 pDQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVlpelADRIRGRTVVCVTSGGNFD----FERLPEVKERAQR 327
Cdd:PRK08813 257 -DDVVIVREAELRETLVRLALEEHVIAEGAGALALAA----GRRVSGKRKCAVVSGGNIDatvlATLLSEVRPRPPR 328
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
21-314 |
3.97e-43 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 153.77 E-value: 3.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRD--ARPDQrsFVCASAGNHAQGVAYACRHFGVKGTI 98
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEqgKLPDK--IVAYSTGNHGQAVAYASKLFGIKTRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 99 FMPVTTPQQKIAKTRTFGGEaVEIVLTGDYFDQTLAAAQawcaEQKAHFLAPFDDPDVIEGQASVGVELLEQLGRAPDLV 178
Cdd:PRK06608 101 YLPLNTSKVKQQAALYYGGE-VILTNTRQEAEEKAKEDE----EQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRV-NSFVDGAAVARLGQLPFSMLDwvRPDQ 257
Cdd:PRK06608 176 FASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLK--KLDD 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 506401820 258 VHLAPEDRICITMLEMLNVEGIVLEPAGALSVD-VLPELADRIRGRTVVCVTSGGNFD 314
Cdd:PRK06608 254 FYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVaVVNWLKTQSKPQKLLVILSGGNID 311
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
38-314 |
1.45e-42 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 151.65 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 38 IWLKREDLTPVRSYKLRGAFTAMRKvrdARPDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQKIAKTRTFGG 117
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRLLA---APVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 118 EaveIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGrAPDLVVLPVGGGGLASGVTAFLrs 197
Cdd:PRK08246 116 E---VVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAP-GVDTVLVAVGGGGLIAGIAAWF-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 198 eAPETDFRFVEPAGGASLLAALEAGGPTALPrVNSFV-DGAAVARLGQLPFSMLDwVRPDQVHLAPEDRICITMLEMLNV 276
Cdd:PRK08246 190 -EGRARVVAVEPEGAPTLHAALAAGEPVDVP-VSGIAaDSLGARRVGEIAFALAR-AHVVTSVLVSDEAIIAARRALWEE 266
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 506401820 277 EGIVLEPAGALSVDVLpeLADRIR---GRTVVCVTSGGNFD 314
Cdd:PRK08246 267 LRLAVEPGAATALAAL--LSGAYVpapGERVAVVLCGANTD 305
|
|
| PLN02970 |
PLN02970 |
serine racemase |
22-321 |
1.11e-41 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 149.83 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDarpDQRSF--VCASAGNHAQGVAYACRHFGVKGTIF 99
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSD---DQAEKgvVTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLgraPDL-- 177
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGG---IITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV---PELdv 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 178 VVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAvARLGQLPFSML-DWVrpD 256
Cdd:PLN02970 179 IIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLR-ASLGDLTWPVVrDLV--D 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506401820 257 QVHLAPEDRICITM---LEMLNVegiVLEPAGALSVDVLpeLADRIR-------GRTVVCVTSGGNFDFERLPEV 321
Cdd:PLN02970 256 DVITVDDKEIIEAMklcYERLKV---VVEPSGAIGLAAA--LSDSFRsnpawkgCKNVGIVLSGGNVDLGVLWES 325
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
22-318 |
1.81e-41 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 149.01 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMP 101
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQ-RRAGVVTFSSGNHAQAIALSARLLGIPATIVMP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 102 VTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGrAPDLVVLP 181
Cdd:PRK07048 104 QDAPAAKVAATRGYGG---EVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVG-PLDALFVC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 182 VGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSMldwVRP--DQVH 259
Cdd:PRK07048 180 LGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPI---IRRlvDDIV 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 506401820 260 LAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERL 318
Cdd:PRK07048 257 TVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARF 315
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
21-325 |
1.38e-40 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 146.68 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRK-VRDARPDQRSFVCASAGNHAQGVAYACRHFGVKGTIF 99
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKsAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGgeaVEIVLTGD-------YFDQTLAAAQ-AWCaeqkahFLAPFDDPDVIEGQASVGVELLEQL 171
Cdd:cd06448 81 VPESTKPRVVEKLRDEG---ATVVVHGKvwweadnYLREELAENDpGPV------YVHPFDDPLIWEGHSSMVDEIAQQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 172 G--RAPDLVVLPVGGGGLASGVTAFLRsEAPETDFRF--VEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPF 247
Cdd:cd06448 152 QsqEKVDAIVCSVGGGGLLNGIVQGLE-RNGWGDIPVvaVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 248 SmlDWVRPDQVHLAPEDRICI-TMLEMLNVEGIVLEPA--GALSV-------DVLPELADRIRGRTVVCVTSGGNFDFER 317
Cdd:cd06448 231 E--YAQEHNIKSEVVSDRDAVqACLRFADDERILVEPAcgAALAVvysgkilDLQLEVLLTPLDNVVVVVCGGSNITLEQ 308
|
....*...
gi 506401820 318 LPEVKERA 325
Cdd:cd06448 309 LKEYKKQL 316
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
21-314 |
1.73e-36 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 135.75 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQ-RAAGVVAASTGNHGRALAYAAAEEGVRATICM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGEaVEIVltGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQlgrAPDL--V 178
Cdd:TIGR02991 98 SELVPQNKVDEIRRLGAE-VRIV--GRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQ---MPDLatV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVD--GAAVARLGQLPFSMLDWVRpD 256
Cdd:TIGR02991 172 LVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTFAMCKALL-D 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 506401820 257 QVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRIRGRTVVCVtSGGNFD 314
Cdd:TIGR02991 251 EIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGPCAVIV-SGRNID 307
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
22-310 |
1.03e-33 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 128.09 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGA-DIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDQrsFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKA--VACASTGNTSASLAAYAARAGIKCVVFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGEAVEIVltGDyFDQTLAAAQAWCAEQKAhFLAPFDDPDVIEGQASVGVELLEQLG-RAPDLVV 179
Cdd:cd01563 101 PAGKALGKLAQALAYGATVLAVE--GN-FDDALRLVRELAEENWI-YLSNSLNPYRLEGQKTIAFEIAEQLGwEVPDYVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 180 LPVGGGGLASGV----TAFLRSEAPETDFRF--VEPAGGASLLAALEAGGPTALP--RVNSFVDGAAVarlGQLP--FSM 249
Cdd:cd01563 177 VPVGNGGNITAIwkgfKELKELGLIDRLPRMvgVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRI---GNPAsgPKA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506401820 250 LDWVRPD--QVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADR---IRGRTVVCVTSG 310
Cdd:cd01563 254 LRAVRESggTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiiDKGERVVVVLTG 319
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-321 |
1.36e-30 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 119.71 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 19 FPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDQRSFVCASAGNHAQGVAYACRHFGVKGTI 98
Cdd:PRK06110 19 MPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRGVISATRGNHGQSVAFAARRHGLAATI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 99 FMPVTTPQQKIAKTRTFGGEAVEivlTGDYFDQTLAAAQAWCAEQKAHFLAPFdDPDVIEGQASVGVELLEQlgrAPDLV 178
Cdd:PRK06110 99 VVPHGNSVEKNAAMRALGAELIE---HGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRA---VPDLD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 179 VL--PVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLLAALEAGGPTALPRVNSFVDGAAVARLGQLPFSML-----D 251
Cdd:PRK06110 172 VVyvPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIragadR 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 252 WVRPDQVHLAPEDRICITMLEMlnvegiVLEPAGALSVDVLPELADRIRGRTVVCVTSGGNFDFERLPEV 321
Cdd:PRK06110 252 IVRVTDDEVAAAMRAYFTDTHN------VAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARV 315
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
22-325 |
3.76e-30 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 119.92 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDArpDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMP 101
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALER--GAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 102 VT-TPQQKIAKTRTFGGEAVEIvlTGDyFDQTLAAAQAWCAEQKAHFLAPFDdPDVIEGQASVGVELLEQLGRAPDLVVL 180
Cdd:COG0498 145 EGkVSPGQLAQMLTYGAHVIAV--DGN-FDDAQRLVKELAADEGLYAVNSIN-PARLEGQKTYAFEIAEQLGRVPDWVVV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 181 PVGGGGLASGV-TAFLRSEAPETDFR-----FVEPAGGASLLAALEAGGPTALPRV-NSFVDGAAVARlgqlPFS---ML 250
Cdd:COG0498 221 PTGNGGNILAGyKAFKELKELGLIDRlprliAVQATGCNPILTAFETGRDEYEPERpETIAPSMDIGN----PSNgerAL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 251 DWVRP--DQVHLAPEDRICITMLEMLNVEGIVLEPAGALSVDVLPELADRI---RGRTVVCVTSGGNFDFerlPEVKERA 325
Cdd:COG0498 297 FALREsgGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGeidPDEPVVVLSTGHGLKF---PDAVREA 373
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
22-307 |
4.67e-23 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 97.97 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFtAMrkVRDA------RPDQRsFVCASAGNHAQGVAYACRHFGVK 95
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIAL-YM--IEDAekrgllKPGTT-IIEPTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 96 GTIFMPVTTPQQKIAKTRTFGGeavEIVLT----GDYFDQTLAAAQAWCAEQ-KAHFLAPFDDPDVIEG-QASVGVELLE 169
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGA---EVILTpeaeADGMKGAIAKARELAAETpNAFWLNQFENPANPEAhYETTAPEIWE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 170 QLGRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGgaSLLAALEAGGPTALP-----RVNSFVDGAAVarlgq 244
Cdd:cd01561 156 QLDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVG--SVLFSGGPPGPHKIEgigagFIPENLDRSLI----- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506401820 245 lpfsmldwvrpDQVHLAPeDRICITMLEMLNV-EGIVLEPAGALSVDVLPELADRI-RGRTVVCV 307
Cdd:cd01561 229 -----------DEVVRVS-DEEAFAMARRLAReEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTI 281
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
332-414 |
9.24e-23 |
|
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes the second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153179 [Multi-domain] Cd Length: 81 Bit Score: 91.07 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 332 KKYFILRMPQRPGALREFLMMLGPDDDIARFEYLKKSArNFGSVLIGIETREAgNFARLTAVMEEAGLNYRDITGDGALA 411
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGS-DYGRVLVGIQVPDA-DLDELKERLDALGYPYQEETDNPAYK 78
|
...
gi 506401820 412 EFL 414
Cdd:cd04907 79 LFL 81
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
22-307 |
6.90e-19 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 86.26 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFtAMrkVRDA------RPDQRsFVCASAGNHAQGVAYACRHFGVK 95
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIAL-SM--IEDAekrgllKPGGT-IVEATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 96 GTIFMPVTTPQQKIAKTRTFGGeavEIVLT--GDYFDQTLAAAQAWCAEQK-AHFLAPFDDPDVIEG-QASVGVELLEQL 171
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGA---EVVLTpgAEGMKGAIDKAEELAAETPgAFWPNQFENPANPEAhYETTGPEIWEQT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 172 GRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASLlaALEAGGPTALPRV-NSFVDGAavarlgqlpfsmL 250
Cdd:COG0031 167 DGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLL--SGGEPGPHKIEGIgAGFVPKI------------L 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506401820 251 DWVRPDQVHLAPEDRICITMLEMLNVEGIVLEP------AGALsvdvlpELADRI-RGRTVVCV 307
Cdd:COG0031 233 DPSLIDEVITVSDEEAFAMARRLAREEGILVGIssgaavAAAL------RLAKRLgPGKTIVTI 290
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
22-316 |
2.75e-18 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 85.13 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGAD-IWLKREDLTPVRSYKLRGAFTAMRKVRDARPDqrSFVCASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:TIGR00260 23 TPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGND--TVLCASTGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PV-TTPQQKIAKTRTFGGEAVEIvlTGDyFDQTLAAAQAWCAEQKAHFLAPFDD-PDVIEGQASVGVELLEQLG-RAPDL 177
Cdd:TIGR00260 101 PAgKISLGKLAQALGYNAEVVAI--DGN-FDDAQRLVKQLFEDKPALGLNSANSiPYRLEGQKTYAFEAVEQLGwEAPDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 178 VVLPVGGGGLASGVTA-FL------RSEAPetDFRFVEPAGGASLLAA-LEAGGPTALPRVNSFVDGAAVARLGQLPFSM 249
Cdd:TIGR00260 178 VVVPVPNSGNFGAIWKgFKekkmlgLDSLP--VKRGIQAEGAADIVRAfLEGGQWEPIETPETLSTAMDIGNPANWPRAL 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506401820 250 LDWVRPDQVHLAPEDRICI-TMLEMLNVEGIVLEPAGALSVDVLPEL--ADRI-RGRTVVCVTSG-GNFDFE 316
Cdd:TIGR00260 256 EAFRRSNGYAEDLSDEEILeAIKLLAREEGYFVEPHSAVAVAALLKLveKGTAdPAERVVCALTGnGLKDPE 327
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
323-414 |
1.02e-17 |
|
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the pfam01842 domain.
Pssm-ID: 395467 [Multi-domain] Cd Length: 91 Bit Score: 77.71 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 323 ERAQRYSGLKKYFILRMPQRPGALREFLMMLGPDDDIARFEYLKKSARNfGSVLIGIETREAGNFARLTAVMEEAGLNYR 402
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKN-GCVLVGIELSQAEDLDEFIERLNKLGYDYE 79
|
90
....*....|..
gi 506401820 403 DITGDGALAEFL 414
Cdd:pfam00585 80 DLSDNEAAYEHL 91
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
335-403 |
3.44e-16 |
|
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153157 [Multi-domain] Cd Length: 68 Bit Score: 72.54 E-value: 3.44e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506401820 335 FILRMPQRPGALREFLMMLGPDDDIARFEYLKKSaRNFGSVLIGIETREAGNFARLTAVMEEAGLNYRD 403
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQG-GDEARVLVGIQVPDREDLAELKERLEALGYPYVD 68
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
22-314 |
1.59e-15 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 77.58 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARY-GADIWLKREDLTPVRSYKLRgafTAMRKVRDARPDQRSFVCAS--AGNHAQGVAYACRHFGVKGTI 98
Cdd:cd06446 35 TPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKIN---NALGQALLAKRMGKKRVIAEtgAGQHGVATATACALFGLECEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 99 FM-PVTTPQQKIAKTR--TFGGEaVEIVLTGdyfDQTL-----AAAQAWCA-EQKAHF-----LAPFDDPD-VIEGQASV 163
Cdd:cd06446 112 YMgAVDVERQPLNVFRmeLLGAE-VVPVPSG---SGTLkdaisEAIRDWVTnVEDTHYllgsvVGPHPYPNmVRDFQSVI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 164 GVE----LLEQLGRAPDLVVLPVGGGGLASGVT-AFLRSEapETDFRFVEPAGGASLL----AALEAGGPTALPRVNSFV 234
Cdd:cd06446 188 GEEakkqILEKEGELPDVVIACVGGGSNAAGLFyPFINDK--DVKLIGVEAGGCGLETgghaAYLFGGTAGVLHGLKMYT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 235 DGAAvarLGQL--PFSM---LDW--VRPDQVHLAPEDRI---CITMLEMLN-------VEGIV--LEPAGALSVDVlpEL 295
Cdd:cd06446 266 LQDE---DGQIvpPHSIsagLDYpgVGPEHAYLKDSGRVeyvAVTDEEALEafkllarTEGIIpaLESSHAIAYAI--KL 340
|
330 340
....*....|....*....|.
gi 506401820 296 ADRIRGRTVVCVT-SG-GNFD 314
Cdd:cd06446 341 AKKLGKEKVIVVNlSGrGDKD 361
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
22-310 |
5.54e-15 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 76.19 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGAD-IWLKREDLTPVRSYKLRGAFTAMRKVRDARpdQRSFVCASAGNHAQGVA-YACRHfGVKGTIF 99
Cdd:PRK08197 80 TPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLAVGVSRAKELG--VKHLAMPTNGNAGAAWAaYAARA-GIRATIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGGEAVEIV-LTGDYFDQTLAAAQAWcaeqkahflAPFD-----DPDVIEGQASVGVELLEQLG- 172
Cdd:PRK08197 157 MPADAPEITRLECALAGAELYLVDgLISDAGKIVAEAVAEY---------GWFDvstlkEPYRIEGKKTMGLELAEQLGw 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 173 RAPDLVVLPVGGG-GLASGVTAFLRSEA----PETDFRF--VEPAGGASLLAALEAGGPTALPrvnsFVDGAAVARLGQL 245
Cdd:PRK08197 228 RLPDVILYPTGGGvGLIGIWKAFDELEAlgwiGGKRPRLvaVQAEGCAPIVKAWEEGKEESEF----WEDAHTVAFGIRV 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506401820 246 P-----FSMLDWVR-PDQVHLAPEDRICITMLEMLNV-EGIVLEPAGALSVDVLPELadRIRGR-----TVVCVTSG 310
Cdd:PRK08197 304 PkalgdFLVLDAVReTGGCAIAVSDDAILAAQRELAReEGLFACPEGAATFAAARQL--RESGWlkgdeRVVLFNTG 378
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
21-226 |
1.69e-14 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 74.53 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARYG-ADIWLKREDltpVR----SYK-LRGAFTAMR--------KVRDARPD------------QRSFV 74
Cdd:PRK08206 44 PTPLVALPDLAAELGvGSILVKDES---YRfglnAFKaLGGAYAVARllaeklglDISELSFEeltsgevreklgDITFA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 75 CASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQKIAKTRTFGGEAveIVLTGDYfDQT--LAAAQA----WCAEQKAHFL 148
Cdd:PRK08206 121 TATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAEC--IITDGNY-DDSvrLAAQEAqengWVVVQDTAWE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 149 APFDDP-DVIEGQASVGVELLEQL---GRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRF--VEPAGGASLLAALEAG 222
Cdd:PRK08206 198 GYEEIPtWIMQGYGTMADEAVEQLkemGVPPTHVFLQAGVGSLAGAVLGYFAEVYGEQRPHFvvVEPDQADCLYQSAVDG 277
|
....
gi 506401820 223 GPTA 226
Cdd:PRK08206 278 KPVA 281
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
22-283 |
6.30e-12 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 65.97 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTP-------VRsyKLRGAftamrkVRDARpDQRSFVCASAG----NHAQGVAYACR 90
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLTGpaiggnkTR--KLEYL------LADAL-AQGADTLVTFGgaqsNHARATAAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 91 HFGVKGTIFM---PVTTPQQKIAKTRTFGgeaVEIVLTGDYFDQTL-AAAQAWCAEQKAHFLAPF------DDPDVIEGQ 160
Cdd:COG2515 83 KLGLKCVLVLrgeEPTPLNGNLLLDRLLG---AELHFVSRGEYRDRdEAMEAVAAELRARGGKPYvipeggSNPLGALGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 161 ASVGVELLEQL---GRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRfvepagGASLLaaleAGGPTALPRVNSFVDGA 237
Cdd:COG2515 160 VEAAAELAAQLaelGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVI------GISVL----KGADFLRERVAELARAT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 506401820 238 AvARLGQLPFS----MLDWVRPDQVHLAPEDRICITMLEMLnvEGIVLEP 283
Cdd:COG2515 230 A-ALLGLVSRAdielDDDYHGGGYGKPTPELIEAIRLFART--EGILLDP 276
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
22-185 |
8.88e-12 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 66.37 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDhLSARYGADIWLKREDLTPVRSYKLRGAFTAmrkVRDARPD-QRSFVCASAGNHAQGV-AYACRHfGVKGTIF 99
Cdd:PRK05638 67 TPLIRAR-ISEKLGENVYIKDETRNPTGSFRDRLATVA---VSYGLPYaANGFIVASDGNAAASVaAYSARA-GKEAFVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 100 MPVTTPQQKIAKTRTFGGeavEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGraPDLVV 179
Cdd:PRK05638 142 VPRKVDKGKLIQMIAFGA---KIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVI 216
|
....*.
gi 506401820 180 LPVGGG 185
Cdd:PRK05638 217 VPTGSG 222
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
21-224 |
2.57e-11 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 64.89 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARY-GADIWLKREDLTPVRSYKLRG----AFTA--MRKVRdarpdqrsfVCAS--AGNHAQGVAYACRH 91
Cdd:PRK13028 62 PTPLYHAKRLSEELgGAQIYLKREDLNHTGAHKINNclgqALLAkrMGKKR---------LIAEtgAGQHGVATATAAAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 92 FGVKGTIFM-PVTTPQQK--IAKTRTFGGEAVEiVLTGdyfDQTL-----AAAQAWCAE-QKAHFL-------APFddPD 155
Cdd:PRK13028 133 FGLECEIYMgEVDIERQHpnVFRMKLLGAEVVP-VTRG---GRTLkeavdSAFEDYLKDpDNTHYAigsvvgpHPF--PM 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506401820 156 -VIEGQASVGVE----LLEQLGRAPDLVVLPVGGGGLASGV-TAFLrsEAPETDFRFVEPAGGASLL----AALEAGGP 224
Cdd:PRK13028 207 mVRDFQSVIGEEareqFLEMTGRLPDAVVACVGGGSNAIGLfSAFL--DDESVRLVGVEPAGRGLDLgehaATLTLGKP 283
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
20-191 |
1.82e-10 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 61.65 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 20 PETPLQRNDHLSARYGAD-IWLKREDLTPVRSYKLRGAFTamrKVRDARPDQRSFVC-ASAGNHAQGVAYACRHFGVKGT 97
Cdd:PRK06381 14 GGTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEA---HVRRAMRLGYSGITvGTCGNYGASIAYFARLYGLKAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 98 IFMPVTTPQQKIAKTRTFGGEAVEIvlTGDYFDQTLAAAQAwcAEQKAHFLA-PFDDPDVI--EGQASVGVELLEQLGRA 174
Cdd:PRK06381 91 IFIPRSYSNSRVKEMEKYGAEIIYV--DGKYEEAVERSRKF--AKENGIYDAnPGSVNSVVdiEAYSAIAYEIYEALGDV 166
|
170
....*....|....*..
gi 506401820 175 PDLVVLPVGGGGLASGV 191
Cdd:PRK06381 167 PDAVAVPVGNGTTLAGI 183
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
22-195 |
1.43e-09 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 59.82 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAF------TAMRKVRdarpdqrsfVCAS--AGNHAQGVAYACRHFG 93
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALgqallaKRMGKTR---------IIAEtgAGQHGVATATACALFG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 94 VKGTIFMPVTTPQ---QKIAKTRTFGGEAVEiVLTGdyfDQTLA-----AAQAWCAE-QKAHFL-----APFDDPD-VIE 158
Cdd:PRK13803 343 LKCTIFMGEEDIKrqaLNVERMKLLGANVIP-VLSG---SKTLKdavneAIRDWVASvPDTHYLigsavGPHPYPEmVAY 418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506401820 159 GQASVGVE----LLEQLGRAPDLVVLPVGGGGLASGV-TAFL 195
Cdd:PRK13803 419 FQSVIGEEakeqLKEQTGKLPDAIIACVGGGSNAIGIfYHFL 460
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
21-191 |
3.00e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 58.21 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRndhlsaryGADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDQRSFvcASAGNHAQGVAYACRHFGVKGTIFM 100
Cdd:PRK06450 58 RTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISE--DSSGNAGASIAAYGAAAGIEVKIFV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 101 PVTTPQQKIAKTRTFGGEAVEIVLTGDyfDQTlAAAQAWCAEQKAHFLAP-FDDpdvieGQASVGVELLEQLG-RAPDLV 178
Cdd:PRK06450 128 PETASGGKLKQIESYGAEVVRVRGSRE--DVA-KAAENSGYYYASHVLQPqFRD-----GIRTLAYEIAKDLDwKIPNYV 199
|
170
....*....|...
gi 506401820 179 VLPVGGGGLASGV 191
Cdd:PRK06450 200 FIPVSAGTLLLGV 212
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
36-198 |
3.21e-09 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 58.89 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 36 ADIWLKREDLTPVRSYKLRGAFTAMRKVRDArPDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQK---IAKT 112
Cdd:PRK13802 347 ARVFLKREDLNHTGAHKINNALGQALLVKRM-GKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQalnVARM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 113 RTFGGEAVEIVLtGDYF--DQTLAAAQAWCAEQK-AHFL-----APFDDPDVIEG-QASVGVELLEQLGR-----APDLV 178
Cdd:PRK13802 426 RMLGAEVVEVTL-GDRIlkDAINEALRDWVTNVKdTHYLlgtvaGPHPFPAMVRDfQKIIGEEAKQQLQDwygidHPDAI 504
|
170 180
....*....|....*....|.
gi 506401820 179 VLPVGGGGLASGV-TAFLRSE 198
Cdd:PRK13802 505 CACVGGGSNAIGVmNAFLDDE 525
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
21-191 |
6.85e-09 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 57.46 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARY------GADIWLKREDLTPVRSYKLRGAFT-AMRKVRDARpdQRSFVCASAGNHAQGVAYACRHFG 93
Cdd:PLN02618 66 ETPLYFAERLTEHYkradgeGPEIYLKREDLNHTGAHKINNAVAqALLAKRLGK--KRIIAETGAGQHGVATATVCARFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 94 VKGTIFMPVTTPQQK---IAKTRTFGGEAVEI-VLTGDYFDQTLAAAQAWCAE-QKAHFLA-----PFDDPDVI-EGQAS 162
Cdd:PLN02618 144 LECIVYMGAQDMERQalnVFRMRLLGAEVRPVhSGTATLKDATSEAIRDWVTNvETTHYILgsvagPHPYPMMVrDFHSV 223
|
170 180 190
....*....|....*....|....*....|...
gi 506401820 163 VGVEL----LEQLGRAPDLVVLPVGGGGLASGV 191
Cdd:PLN02618 224 IGKETrrqaMEKWGGKPDVLVACVGGGSNAMGL 256
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
33-194 |
1.67e-08 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 56.36 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 33 RYGA------DIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDQRSFV---CASAGNHAQGVAYACRHFGVKGTIFMPVT 103
Cdd:PLN02569 141 RLGKeflgmnDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAKPVVgvgCASTGDTSAALSAYCAAAGIPSIVFLPAD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 104 TPQ-----QKIAKTRTfggeaveiVLTGD-YFDQTLAAAQAWCAEQKAhFLAPFDDPDVIEGQASVGVELLEQLG-RAPD 176
Cdd:PLN02569 221 KISiaqlvQPIANGAL--------VLSIDtDFDGCMRLIREVTAELPI-YLANSLNSLRLEGQKTAAIEILQQFDwEVPD 291
|
170
....*....|....*...
gi 506401820 177 LVVLPVGGGGlasGVTAF 194
Cdd:PLN02569 292 WVIVPGGNLG---NIYAF 306
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
18-210 |
5.29e-08 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 54.58 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 18 LFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDAR---PDQRSFVCASAGNHAQGVAYACRHFGV 94
Cdd:PLN02556 56 LIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNlitPGKTTLIEPTSGNMGISLAFMAAMKGY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 95 KGTIFMPVTTPQQKIAKTRTFGGEAVEIVLTGDYFDQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQ-ASVGVELLEQLGR 173
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHfETTGPEIWEDTLG 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 506401820 174 APDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPA 210
Cdd:PLN02556 216 QVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPA 252
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
35-195 |
5.36e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 54.45 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 35 GADIWLKREDLTPVRSYKLRGAFTAMRKVRDARPDQrsFVCASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQKIAKTRT 114
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE--VVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 115 FGGEAVEIvlTGDYFdQTLAAAQAWCAEQKAHFLAPFDDPDVIEGQASVGVELLEQLGrAPDLVVLPVGGGglasgvTAF 194
Cdd:PRK08329 149 LGAELHFV--EGDRM-EVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIG-VPDYAFVPVGSG------TLF 218
|
.
gi 506401820 195 L 195
Cdd:PRK08329 219 L 219
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
36-311 |
1.09e-07 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 53.08 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 36 ADIWLKREDLTPVRSYKLRGAFTAMRKVRDA---RPDQRSFVCASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQKIAKT 112
Cdd:PLN00011 32 ARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKgliTPGKSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIIL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 113 RTFGGEaVEIVLTGDYFDQTLAAAQAWCAEQK-AHFLAPFDDPDVIEGQ-ASVGVELLEQLGRAPDLVVLPVGGGGLASG 190
Cdd:PLN00011 112 RALGAE-VHLTDQSIGLKGMLEKAEEILSKTPgGYIPQQFENPANPEIHyRTTGPEIWRDSAGKVDILVAGVGTGGTATG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 191 VTAFLRSEAPETDFRFVEPAGGASLLAAleAGGPTALPRVNSfvdgaavarlGQLPFSmLDWVRPDQV-HLAPEDRICIT 269
Cdd:PLN00011 191 VGKFLKEKNKDIKVCVVEPVESAVLSGG--QPGPHLIQGIGS----------GIIPFN-LDLTIVDEIiQVTGEEAIETA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 506401820 270 MLEMLNvEGIVL------EPAGALSVDVLPELADRIrgrTVVCVTSGG 311
Cdd:PLN00011 258 KLLALK-EGLLVgissgaAAAAALKVAKRPENAGKL---IVVIFPSGG 301
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
21-211 |
1.62e-07 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 53.15 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 21 ETPLQRNDHLSARY-GADIWLKREDLTPVRSYKLR---G-AFTA--MRKVRdarpdqrsfVCAS--AGNHaqGVAYA--C 89
Cdd:PRK04346 58 PTPLYFAERLSEHLgGAKIYLKREDLNHTGAHKINnvlGqALLAkrMGKKR---------IIAEtgAGQH--GVATAtaA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 90 RHFGVKGTIFMPVT-TPQQK--IAKTRTFGGEaVEIVLTGdyfDQTL-----AAAQAWCAE-QKAHFL-------APFdd 153
Cdd:PRK04346 127 ALLGLECVIYMGAEdVERQAlnVFRMKLLGAE-VVPVTSG---SRTLkdavnEALRDWVTNvEDTHYLigsvagpHPY-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506401820 154 PD-VIEGQASVGVE----LLEQLGRAPDLVVLPVGGGGLASGV-TAFLrseaPETDFRF--VEPAG 211
Cdd:PRK04346 201 PTmVRDFQSVIGEEakaqILEKEGRLPDAVVACVGGGSNAIGIfHPFI----DDESVRLigVEAAG 262
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
22-311 |
6.49e-07 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 50.99 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 22 TPLQRNDHLSARYGADIWLKREDLTPVrsyklrgaftAM--RKVR-------DARpDQRSFVCASAG----NHAQGVAYA 88
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGL----------ALggNKTRklefllaDAL-AQGADTLITAGaiqsNHARQTAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 89 CRHFGVKGTIFMPVTTPQQKIAKT--------RTFGGEaVEIVLTGDYFDqtlAAAQAWCAEQKAHFLAPFddpdVIEGQ 160
Cdd:PRK03910 85 AAKLGLKCVLLLENPVPTEAENYLangnvlldDLFGAE-IHVVPAGTDMD---AQLEELAEELRAQGRRPY----VIPVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 161 ASVGV----------ELLEQL---GRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVepaggasllaALEAGGPTAL 227
Cdd:PRK03910 157 GSNALgalgyvacalEIAQQLaegGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGV----------TVSRSAAEQE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 228 PRVNSFVDgaAVARLGQLP-------FSMLD-WVRPDQVHLAPEDRICITMLEMLnvEGIVLEP-------AGalsvdvl 292
Cdd:PRK03910 227 PKVAKLAQ--ATAELLGLPteipradIRLWDdYVGPGYGVPTDEMLEAVKLLART--EGILLDPvytgkamAG------- 295
|
330 340
....*....|....*....|....*
gi 506401820 293 peLADRIR------GRTVVCVTSGG 311
Cdd:PRK03910 296 --LIDLIRqgrfkkGGNVLFIHTGG 318
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
18-209 |
1.78e-06 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 49.78 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 18 LFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAmrkVRDAR------PDQRSFVCASAGNHAQGVAYACRH 91
Cdd:PLN03013 120 LIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSM---VTDAEqkgfisPGKSVLVEPTSGNTGIGLAFIAAS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 92 FGVKGTIFMPVTTPQQKIAKTRTFGGEaveIVLTGDYFDQTLAAAQA---WCAEQKAHFLAPFDDPDVIEGQ-ASVGVEL 167
Cdd:PLN03013 197 RGYRLILTMPASMSMERRVLLKAFGAE---LVLTDPAKGMTGAVQKAeeiLKNTPDAYMLQQFDNPANPKIHyETTGPEI 273
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506401820 168 LEQLGRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEP 209
Cdd:PLN03013 274 WDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP 315
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
18-286 |
3.83e-06 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 48.88 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 18 LFPET---------PLQRNDH----LSARYGADI----WLKREDLTPVR-SYKLRGAF---------TAM---------- 60
Cdd:cd06447 40 VFPETaashgiiesPLLPIPRmkqaLEKLYHQPIkgrlLLKADSHLPISgSIKARGGIyevlkhaekLALehglltledd 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 61 -RKVRDARP----DQRSFVCASAGNHAQGVAYACRHFGVKGTIFMPVTTPQQKIAKTRTFGGEAVEivLTGDYFDQTLAA 135
Cdd:cd06447 120 ySKLASEKFrklfSQYSIAVGSTGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVE--YETDYSKAVEEG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 136 AQAWCAEQKAHFLapfDD---PDVIEGQASVGVEL---LEQLGRAPDL-----VVLPVGGGGLASGVTAFLRseapeTDF 204
Cdd:cd06447 198 RKQAAADPMCYFV---DDensRDLFLGYAVAASRLkaqLAELGIKVDAehplfVYLPCGVGGAPGGVAFGLK-----LIF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 205 R------FVEPAGGASLLAALeAGGPTALPRVNSF-------VDGAAVAR----LGQLPFSMLDWVrpdqvhLAPEDRIC 267
Cdd:cd06447 270 GdnvhcfFAEPTHSPCMLLGM-ATGLHDKISVQDIgidnrtaADGLAVGRpsglVGKLMEPLLSGI------YTVEDDEL 342
|
330 340
....*....|....*....|
gi 506401820 268 ITMLEMLNV-EGIVLEPAGA 286
Cdd:cd06447 343 YRLLAMLKDsENIEVEPSAA 362
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
17-215 |
7.77e-05 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 44.53 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 17 DLFPETPLQRNDHLSARYGADIWLKREDLTPVRSYKLRGAFTAMRKVRDA---RPDQRSFVCASAGNHAQGVAYACRHFG 93
Cdd:PLN02565 11 ELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKgliKPGESVLIEPTSGNTGIGLAFMAAAKG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 94 VKGTIFMPVTTPQQKIAKTRTFGgeaVEIVLTGDYFDQTLAAAQAWCAEQK---AHFLAPFDDPDVIEGQ-ASVGVELLE 169
Cdd:PLN02565 91 YKLIITMPASMSLERRIILLAFG---AELVLTDPAKGMKGAVQKAEEILAKtpnSYILQQFENPANPKIHyETTGPEIWK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506401820 170 QLGRAPDLVVLPVGGGGLASGVTAFLRSEAPETDFRFVEPAGGASL 215
Cdd:PLN02565 168 GTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVL 213
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
339-407 |
5.50e-03 |
|
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes the first of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153178 [Multi-domain] Cd Length: 85 Bit Score: 35.60 E-value: 5.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506401820 339 MPQRPGALREFLMMLGPdDDIARFEYLKKSARNfGSVLIGIET-REAGNFARLTAVMEEAGLNYRDITGD 407
Cdd:cd04906 8 IPERPGSFKKFCELIGP-RNITEFNYRYADEKD-AHIFVGVSVaNGAEELAELLEDLKSAGYEVVDLSDD 75
|
|
| |
