|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
16-515 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 983.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 16 YVESILAAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLA 95
Cdd:PRK09224 5 YLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 96 LAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILR 175
Cdd:PRK09224 85 LSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 176 QHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEV 255
Cdd:PRK09224 165 QHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 256 CKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDSGANINFDRLRHVAERAELG 335
Cdd:PRK09224 245 CQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAERAELG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 336 EQREAIIAVTVAERPGSFKAFCAALGRRQITEFNYRYHSDRQAHLFVGVQTHPLTDSRADLLAGLREQGFPVLDLTDNEM 415
Cdd:PRK09224 325 EQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDLSDDEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 416 AKLHIRHMVGGHGTEVRRERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPDEERGELEAALQ 495
Cdd:PRK09224 405 AKLHVRYMVGGRPPKPLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADEPEFEAFLD 484
|
490 500
....*....|....*....|
gi 15596523 496 AIGYPYWEETHNPAYRLFAG 515
Cdd:PRK09224 485 ELGYPYWDETDNPAYRLFLA 504
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
1-515 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 966.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 1 MSASTLSASKPLLAGYVESILAAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKAR 80
Cdd:PRK12483 7 VSPTTIAPRAALLADYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 81 GVITASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDP 160
Cdd:PRK12483 87 GVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 161 DVIAGQGTVAMEILRQHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFA 240
Cdd:PRK12483 167 DVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 241 DGVAVAQIGACNFEVCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDSGANI 320
Cdd:PRK12483 247 DGVAVAQIGEHTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 321 NFDRLRHVAERAELGEQREAIIAVTVAERPGSFKAFCAALGRRQITEFNYRYHSDRQAHLFVGVQTHPLTDSRADLLAGL 400
Cdd:PRK12483 327 NFDRLRHVAERAELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 401 REQGFPVLDLTDNEMAKLHIRHMVGGHGTEVRRERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGL 480
Cdd:PRK12483 407 RAQGFPVLDLTDDELAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGL 486
|
490 500 510
....*....|....*....|....*....|....*
gi 15596523 481 QVPDEERGELEAALQAIGYPYWEETHNPAYRLFAG 515
Cdd:PRK12483 487 QVPEDERAALDAALAALGYPYWEETGNPAYRLFLG 521
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
16-513 |
0e+00 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 780.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 16 YVESILAAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLA 95
Cdd:TIGR01124 2 YLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 96 LAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILR 175
Cdd:TIGR01124 82 FSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 176 QHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEV 255
Cdd:TIGR01124 162 QVANPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 256 CKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDSGANINFDRLRHVAERAELG 335
Cdd:TIGR01124 242 CQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCELG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 336 EQREAIIAVTVAERPGSFKAFCAALGRRQITEFNYRYHSDRQAHLFVGVQTHPLTDsRADLLAGLREQGFPVLDLTDNEM 415
Cdd:TIGR01124 322 EQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNPQE-RQEILARLNDGGYSVVDLTDDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 416 AKLHIRHMVGGHGTEVRRERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPDEERGELEAALQ 495
Cdd:TIGR01124 401 AKLHVRYMVGGRPPHVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDQFEQFLA 480
|
490
....*....|....*...
gi 15596523 496 AIGYPYWEETHNPAYRLF 513
Cdd:TIGR01124 481 ELGYRYHDETNNPAYRLF 498
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
15-512 |
0e+00 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 591.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 15 GYVESILAAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGL 94
Cdd:PLN02550 93 EYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 95 ALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEIL 174
Cdd:PLN02550 173 ALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 175 RQHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFE 254
Cdd:PLN02550 253 RQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 255 VCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDSGANINFDRLRHVAERAEL 334
Cdd:PLN02550 333 LCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVTELADV 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 335 GEQREAIIAVTVAERPGSFKAFCAALGRRQITEFNYRYHSDRQAHLFVGVQTHPLTDSRAdLLAGLREQGFPVLDLTDNE 414
Cdd:PLN02550 413 GRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHTEQELQA-LKKRMESAQLRTVNLTSND 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 415 MAKLHIRHMVGGHgTEVRRERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPDEERGELEAAL 494
Cdd:PLN02550 492 LVKDHLRYLMGGR-AIVKDELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQVPPEEMQEFKSRA 570
|
490
....*....|....*...
gi 15596523 495 QAIGYPYWEETHNPAYRL 512
Cdd:PLN02550 571 NALGYEYQDECDNEAFQL 588
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
16-337 |
5.29e-164 |
|
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: 467.59 E-value: 5.29e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 16 YVESILAA--PVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQG 93
Cdd:COG1171 7 TLADIEAAaaRIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 94 LALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEI 173
Cdd:COG1171 87 VAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 174 LRQHsGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNF 253
Cdd:COG1171 167 LEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 254 EVCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYvaRERTEGQTLVAIDSGANINFDRLRHVAERAE 333
Cdd:COG1171 246 EILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG--KERLKGKRVVVVLSGGNIDPDRLAEILERGL 323
|
....
gi 15596523 334 LGEQ 337
Cdd:COG1171 324 VGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
17-321 |
3.06e-156 |
|
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: 446.93 E-value: 3.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 17 VESILAAPVY--DVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGL 94
Cdd:cd01562 1 LEDILAAAARikPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 95 ALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEIL 174
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 175 RQHsGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFE 254
Cdd:cd01562 161 EQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFE 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596523 255 VCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYvaRERTEGQTLVAIDSGANIN 321
Cdd:cd01562 240 IIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG--KLDLKGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
27-416 |
6.71e-131 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 386.85 E-value: 6.71e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 27 DVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAV 106
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 107 IVMPRTTPELKVKGVLARGGEAL---LHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHS--GRL 181
Cdd:PRK08639 101 IFMPVTTPQQKIDQVRFFGGEFVeivLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEkeGSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 182 DAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVD 261
Cdd:PRK08639 181 DYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVVD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 262 EVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYvaRERTEGQTLVAIDSGANINFDRLRHVAERAELGEQREAI 341
Cdd:PRK08639 261 DVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELY--KDEIKGKTVVCVISGGNNDIERMPEIKERSLIYEGLKHY 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596523 342 IAVTVAERPGSFKAFCAA-LG-RRQITEFNYRYHSDRQ-AHLFVGVQTHPLTDSrADLLAGLREQGFPVLDLTDNEMA 416
Cdd:PRK08639 339 FIVNFPQRPGALREFLDDvLGpNDDITRFEYLKKNNREtGPVLVGIELKDAEDY-DGLIERMEAFGPSYIDINPNEPL 415
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
32-360 |
8.56e-96 |
|
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: 295.50 E-value: 8.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPR 111
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 112 TTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQhSGRLDAIFVPVGGG 191
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMED-IPDVDTVIVPVGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 192 SLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVDEVITVGSDEI 271
Cdd:TIGR01127 160 GLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 272 CAAIKDIYDDTRSITEPAGALAVAGIKKYVARERteGQTLVAIDSGANINFDRLRHVAERAELGEQREAIIAVTVAERPG 351
Cdd:TIGR01127 240 ANAIYLLLERHKILAEGAGAAGVAALLEQKVDVK--GKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPG 317
|
....*....
gi 15596523 352 SFKAFCAAL 360
Cdd:TIGR01127 318 ALYHLLESI 326
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
31-330 |
1.09e-92 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 285.86 E-value: 1.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALLGIDGKVVMP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGrLDAIFVPVGG 190
Cdd:PRK08638 107 KGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWD-VDTVIVPIGG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 191 GSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVDEVITVGSDE 270
Cdd:PRK08638 186 GGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDE 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596523 271 ICAAIKDIYDDTRSITEPAGALAVAG-----IKKYVarertEGQTLVAIDSGANINFDRLRHVAE 330
Cdd:PRK08638 266 IRNAMKDLIQRNKVVTEGAGALATAAllsgkLDQYI-----QNKKVVAIISGGNVDLSRVSQITG 325
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
30-407 |
6.54e-89 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 278.32 E-value: 6.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 30 VETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVM 109
Cdd:PRK07334 22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 110 PRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILrQHSGRLDAIFVPVG 189
Cdd:PRK07334 102 PRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEML-EDAPDLDTLVVPIG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 190 GGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVglFADGVAVAQIGACNFEVCKDHVDEVITVGSD 269
Cdd:PRK07334 181 GGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALPCGGST--IAEGIAVKQPGQLTLEIVRRLVDDILLVSEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 270 EICAAIKDIYDDTRSITEPAGALAVAGIKKYvaRERTEGQTLVAIDSGANINFDRLRHVAERAELGEQREAIIAVTVAER 349
Cdd:PRK07334 259 DIEQAVSLLLEIEKTVVEGAGAAGLAALLAY--PERFRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLRVDIRDR 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596523 350 PGSFKAFCAALGRRQ--ITEFNY-RYHSD---RQAHLFVGVQTHPlTDSRADLLAGLREQGFPV 407
Cdd:PRK07334 337 PGALARVTALIGEAGanIIEVSHqRLFTDlpaKGAELELVIETRD-AAHLQEVIAALRAAGFEA 399
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
31-328 |
3.66e-88 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 273.49 E-value: 3.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHsGRLDAIFVPVGG 190
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVAVGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 191 GSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVA-QIGACNFEVCKDHVDEVITVGSD 269
Cdd:PRK06815 179 GGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFPLCQQLIDQKVLVSEE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596523 270 EICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERteGQTLVAIDSGANINFDRLRHV 328
Cdd:PRK06815 259 EIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ--GKKVAVVLCGKNIVLEKYLEA 315
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
32-317 |
4.03e-85 |
|
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: 264.94 E-value: 4.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPR 111
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 112 TTPELKVKGVLARGGEALLHGDAFPDALAHALQLA-EREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGRLDAIFVPVGG 190
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 191 GSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQI-GACNFEVCKDHVDEVITVGSD 269
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 15596523 270 EICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDSG 317
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
32-317 |
3.72e-76 |
|
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: 239.72 E-value: 3.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARG--VITASAGNHAQGLALAAQRLGVRAVIVM 109
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 110 PRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAER-EGMTFVPPYDDPDVIAGQGTVAMEILRQHSG-RLDAIFVP 187
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 188 VGGGSLIAGIAAYVKHLRPDIRVIGVEPedsnclqaalaagervvlgqvglfadgvavaqigacnfevckdhvdEVITVG 267
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15596523 268 SDEICAAIKDIYDDTRSITEPAGALAVAGIKKYvARERTEGQTLVAIDSG 317
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKL-AKKLGKGKTVVVILTG 243
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
29-328 |
1.29e-75 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 241.41 E-value: 1.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 29 AVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIV 108
Cdd:PRK07476 17 VRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATIC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 109 MPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSgRLDAIFVPV 188
Cdd:PRK07476 97 MSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALP-DVATVLVPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 189 GGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAvAQIGACN---FEVCKDHVDEVIT 265
Cdd:PRK07476 176 SGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADSLG-GGIGLDNrytFAMCRALLDDVVL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596523 266 VGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERteGQTLVAIDSGANINFDRLRHV 328
Cdd:PRK07476 255 LDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAAR--DGPIVVVVSGANIDMELHRRI 315
|
|
| PLN02970 |
PLN02970 |
serine racemase |
17-325 |
4.85e-75 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 239.97 E-value: 4.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 17 VESILAAP--VYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGL 94
Cdd:PLN02970 11 LSSIREARkrIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 95 ALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEIL 174
Cdd:PLN02970 91 ALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 175 RQHSGrLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAvAQIGACNFE 254
Cdd:PLN02970 171 EQVPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLR-ASLGDLTWP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596523 255 VCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGI--KKYVARERTEGQTLVAID-SGANINFDRL 325
Cdd:PLN02970 249 VVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsDSFRSNPAWKGCKNVGIVlSGGNVDLGVL 322
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
22-325 |
1.24e-72 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 233.37 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 22 AAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRL 101
Cdd:PRK07048 15 AARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 102 GVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEiLRQHSGRL 181
Cdd:PRK07048 95 GIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE-LFEEVGPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 182 DAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVD 261
Cdd:PRK07048 174 DALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPIIRRLVD 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596523 262 EVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKyvARERTEGQTLVAIDSGANINFDRL 325
Cdd:PRK07048 254 DIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR--GKVPLKGKRVGVIISGGNVDLARF 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
48-325 |
9.94e-61 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 202.11 E-value: 9.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 48 VLLKREDLQPVFSFKIRGAYTRVarLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKGVLARGGE 127
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 128 ALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQhSGRLDAIFVPVGGGSLIAGIAAYVkhlRPD 207
Cdd:PRK08246 117 VVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQ-APGVDTVLVAVGGGGLIAGIAAWF---EGR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 208 IRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVDEVITVGSDEICAAIKDIYDDTRSITE 287
Cdd:PRK08246 193 ARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVE 272
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15596523 288 PAGALAVAGI--KKYVARertEGQTLVAIDSGANINFDRL 325
Cdd:PRK08246 273 PGAATALAALlsGAYVPA---PGERVAVVLCGANTDPATL 309
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
22-328 |
1.50e-59 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 199.45 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 22 AAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQ-KARGVITASAGNHAQGLALAAQR 100
Cdd:PRK06110 12 AAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 101 LGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDdPDVIAGQGTVAMEILRQHSGr 180
Cdd:PRK06110 92 HGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFH-PDLVRGVATYALELFRAVPD- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 181 LDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHV 260
Cdd:PRK06110 170 LDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596523 261 DEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKyvARERTEGQTLVAIDSGANINFDRLRHV 328
Cdd:PRK06110 250 DRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ--ERERLAGKRVGLVLSGGNIDRAVFARV 315
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
32-321 |
5.64e-49 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 172.12 E-value: 5.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVApqlsQRLGnrVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPR 111
Cdd:PRK08813 40 TPLHYA----ERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 112 TTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEiLRQHSGrlDAIFVPVGGG 191
Cdd:PRK08813 114 GAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIE-LAAHAP--DVVIVPIGGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 192 SLIAGIAAYVKhlRPDIRVIGVEPEDSNCLQAALaAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVDEVITVGSDEI 271
Cdd:PRK08813 191 GLASGVALALK--SQGVRVVGAQVEGVDSMARAI-RGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAEL 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15596523 272 CAAIKDIYDDTRSITEPAGALAVAgikkyvARERTEGQTLVAIDSGANIN 321
Cdd:PRK08813 268 RETLVRLALEEHVIAEGAGALALA------AGRRVSGKRKCAVVSGGNID 311
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
31-321 |
1.22e-48 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 171.11 E-value: 1.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQK-ARGVITASAGNHAQGLALAAQRLGVRAVIVM 109
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlPDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 110 PRTTPELKVKGVLARGGEALLHgDAFPDALAHALQlAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGRLDAIFVPVG 189
Cdd:PRK06608 103 PLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASCG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 190 GGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQV-GLFADGVAVAQIGACNFEVCK--DHVDEVitv 266
Cdd:PRK06608 181 GGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKklDDFYLV--- 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596523 267 gsDEicaaiKDIYDDTRSIT-------EPAGALAVAGIKKYVAReRTEGQTLVAIDSGANIN 321
Cdd:PRK06608 258 --EE-----YEIYYWTAWLThllkvicEPSSAINMVAVVNWLKT-QSKPQKLLVILSGGNID 311
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
434-513 |
1.01e-43 |
|
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: 149.24 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 434 ERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPDEERGELEAALQAIGYPYWEETHNPAYRLF 513
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADLDELKERLDALGYPYQEETDNPAYKLF 80
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
31-327 |
1.80e-42 |
|
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: 153.61 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRG--AYTRVARLSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIV 108
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGigHLCQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 109 MPRTTPELKVKGVLARGGEALLHGDAFPDA-LAHALQLAERE-GMTFVPPYDDPDVIAGQGTVAMEILRQ--HSGRLDAI 184
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWWEAdNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQlqSQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 185 FVPVGGGSLIAGIAA-YVKHLRPDIRVIGVEPEDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGACNFEVCKDHVDEV 263
Cdd:cd06448 161 VCSVGGGGLLNGIVQgLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596523 264 ITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARERTEGQTLVAIDS-------GANINFDRLRH 327
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLTPLDNvvvvvcgGSNITLEQLKE 311
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
339-423 |
7.36e-40 |
|
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: 138.83 E-value: 7.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 339 EAIIAVTVAERPGSFKAFCAALGRRQITEFNYRYHSDRQAHLFVGVQTHPLTDSRADLLAGLREQGFPVLDLTDNEMAKL 418
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 15596523 419 HIRHM 423
Cdd:cd04906 81 HLRYM 85
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
32-303 |
1.03e-33 |
|
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: 131.48 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSdEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPR 111
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLAL-ERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 112 T-TPELKVKGVLARGGEALL-HGDaFPDALAHALQLAEREGMTFVPPYDdPDVIAGQGTVAMEILRQHSGRLDAIFVPVG 189
Cdd:COG0498 146 GkVSPGQLAQMLTYGAHVIAvDGN-FDDAQRLVKELAADEGLYAVNSIN-PARLEGQKTYAFEIAEQLGRVPDWVVVPTG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 190 GGSLIAGI--------AAYVKHLRPdiRVIGVEPEDSNCLQAALAAGERVVLGQVGLF-ADGVAVAQigACNFEVCKDHV 260
Cdd:COG0498 224 NGGNILAGykafkelkELGLIDRLP--RLIAVQATGCNPILTAFETGRDEYEPERPETiAPSMDIGN--PSNGERALFAL 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15596523 261 DE----VITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVAR 303
Cdd:COG0498 300 REsggtAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREE 346
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
32-303 |
7.09e-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: 127.71 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLG-NRVLLKREDLQPVFSFKIRGAYTRVARLSdEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:cd01563 23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAK-ELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTTPELKVKGVLARGGEAL-LHGDaFPDALAHALQLAEREGMTFVPpYDDPDVIAGQGTVAMEILRQHSGRL-DAIFVPV 188
Cdd:cd01563 102 AGKALGKLAQALAYGATVLaVEGN-FDDALRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQLGWEVpDYVVVPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 189 GGGSLIAGIAAYVKHL--------RPdiRVIGVEPEDSNCLQAALAAG----ERVVlgQVGLFADGVAVAQigACNFEVC 256
Cdd:cd01563 180 GNGGNITAIWKGFKELkelglidrLP--RMVGVQAEGAAPIVRAFKEGkddiEPVE--NPETIATAIRIGN--PASGPKA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15596523 257 KDHVDE----VITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVAR 303
Cdd:cd01563 254 LRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE 304
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
437-503 |
1.10e-28 |
|
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: 107.98 E-value: 1.10e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596523 437 FRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPD-EERGELEAALQAIGYPYWE 503
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDrEDLAELKERLEALGYPYVD 68
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
32-317 |
1.36e-28 |
|
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: 114.92 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLsdeqKARGVIT-------ASAGNHAQGLALAAQRLGVR 104
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDA----EKRGLLKpgttiiePTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAER---EGMTFVPP--YDDPD-VIAGQGTVAMEILRQHS 178
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARElaaETPNAFWLnqFENPAnPEAHYETTAPEIWEQLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 179 GRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQaALAAGERVVLGqvglfadgvavaqIGAcNFE---V 255
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFS-GGPPGPHKIEG-------------IGA-GFIpenL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596523 256 CKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKyVARERTEGQTLVAI--DSG 317
Cdd:cd01561 224 DRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALK-LAKRLGPGKTIVTIlpDSG 286
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
433-513 |
4.68e-28 |
|
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: 106.98 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 433 RERLFRFEFPERPGALLNFLDKLGSRWNISLFHYRNHGAADGRVLAGLQVPD-EERGELEAALQAIGYPYWEETHNPAYR 511
Cdd:pfam00585 9 LEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQaEDLDEFIERLNKLGYDYEDLSDNEAAY 88
|
..
gi 15596523 512 LF 513
Cdd:pfam00585 89 EH 90
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
32-317 |
1.13e-24 |
|
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: 103.97 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYtrvaRLSDEQKARGVIT-------ASAGNHAQGLALAAQRLGVR 104
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIAL----SMIEDAEKRGLLKpggtiveATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMPRTTPELKVKGVLARGGEALL--HGDAFPDALAHALQLAEREGMTFVP-PYDDPD-VIAGQGTVAMEILRQHSGR 180
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAFWPnQFENPAnPEAHYETTGPEIWEQTDGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 181 LDAIFVPVG-GGSlIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAAlAAGERVVLGqvglfadgvavaqIGA------CNF 253
Cdd:COG0031 170 VDAFVAGVGtGGT-ITGVGRYLKERNPDIKIVAVEPEGSPLLSGG-EPGPHKIEG-------------IGAgfvpkiLDP 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596523 254 EVckdhVDEVITVGSDEicaAIkdiyDDTRSITEPAGAL-------AVAGIKKyVARERTEGQTLVAI--DSG 317
Cdd:COG0031 235 SL----IDEVITVSDEE---AF----AMARRLAREEGILvgissgaAVAAALR-LAKRLGPGKTIVTIlpDSG 295
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
330-420 |
6.75e-23 |
|
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: 92.73 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 330 ERAELGEQREAIIAVTVAERPGSFKAFCAALG-RRQITEFNYRYHSDRQAHLFVGVQTHPLTDsRADLLAGLREQGFPVL 408
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGgRNNITLFEYRKHGDKNGCVLVGIELSQAED-LDEFIERLNKLGYDYE 79
|
90
....*....|..
gi 15596523 409 DLTDNEMAKLHI 420
Cdd:pfam00585 80 DLSDNEAAYEHL 91
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
43-314 |
1.05e-20 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 93.35 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 43 RLGNRVLLKREDLQPVFSFKIRGAYTRVARLSdEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKgvL 122
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKIS--L 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 123 ARGGEALLH---GDAFpDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQhSGRLDAIFVPVGGGSLIAGIAA 199
Cdd:PRK08329 146 LSRLGAELHfveGDRM-EVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQ-IGVPDYAFVPVGSGTLFLGIWK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 200 YVKHLR--------PDIRVIGVEPEDSNClqaalaagERVVlgQVGLFADGVAVAQIGACN--FEVCKDHVDEVITVGSD 269
Cdd:PRK08329 224 GFKELHemgeiskmPKLVAVQAEGYESLC--------KRSK--SENKLADGIAIPEPPRKEemLRALEESNGFCISVGEE 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 15596523 270 EICAAIKDIYdDTRSITEPAGALAVAGIKKYVARERTEGQTLVAI 314
Cdd:PRK08329 294 ETRAALHWLR-RMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLL 337
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
31-234 |
1.48e-20 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 93.79 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLG-NRVLLKREDLQ-PVFSFKIRGAYTRVARL------------------SDEQKARG----VITAS 86
Cdd:PRK08206 44 PTPLVALPDLAAELGvGSILVKDESYRfGLNAFKALGGAYAVARLlaeklgldiselsfeeltSGEVREKLgditFATAT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 87 AGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFV-----PPYDDP- 160
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVqdtawEGYEEIp 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 161 -DVIAGQGTVAMEILRQHSGRLDA---IFVPVGGGSLIAGIAAY-VKHLRPDI-RVIGVEPEDSNCLQAALAAGERVVLG 234
Cdd:PRK08206 204 tWIMQGYGTMADEAVEQLKEMGVPpthVFLQAGVGSLAGAVLGYfAEVYGEQRpHFVVVEPDQADCLYQSAVDGKPVAVT 283
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
32-320 |
5.05e-20 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 91.99 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLG-NRVLLKREDLQPVFSFKIRGAYTRVARlSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSR-AKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGRL-DAIFVPVG 189
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGWRLpDVILYPTG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 190 GGSLIAGIAAYVKHL---------RPdiRVIGVEPEDSNCLQAALAAGERvvlgQVGLFADGVAVA-------QIGacNF 253
Cdd:PRK08197 239 GGVGLIGIWKAFDELealgwiggkRP--RLVAVQAEGCAPIVKAWEEGKE----ESEFWEDAHTVAfgirvpkALG--DF 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596523 254 EVCkDHVDE----VITVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVARER-TEGQTLVAIDSGANI 320
Cdd:PRK08197 311 LVL-DAVREtggcAIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWlKGDERVVLFNTGSGL 381
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
342-409 |
5.39e-19 |
|
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: 81.01 E-value: 5.39e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596523 342 IAVTVAERPGSFKAFCAALG-RRQITEFNYRYHSDRQAHLFVGVQTHPLTDsRADLLAGLREQGFPVLD 409
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGpPRNITEFHYRNQGGDEARVLVGIQVPDRED-LAELKERLEALGYPYVD 68
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
32-318 |
5.06e-17 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 82.22 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAytrvARLSDEQKARGVITA-------SAGNHAQGLALAAQRLGVR 104
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAA----LNIIWDAEKRGLLKPggtivegTAGNTGIGLALVAAARGYK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMPRTTPELKVKGVLARGGEaLLHGDAFPDA-----------LAHALQLAEREGMTFVPPYDDPD-VIAGQGTVAME 172
Cdd:PRK10717 90 TVIVMPETQSQEKKDLLRALGAE-LVLVPAAPYAnpnnyvkgagrLAEELVASEPNGAIWANQFDNPAnREAHYETTGPE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 173 ILRQHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNcLQAALAAGERVVLGqvGLFADGVAVAQIGAcN 252
Cdd:PRK10717 169 IWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSA-LYSYYKTGELKAEG--SSITEGIGQGRITA-N 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596523 253 FEvcKDHVDEVITVGSDEicaAIKDIYDdtrsITEPAG-------ALAVAGIKKyVARERTEGQTLVAI--DSGA 318
Cdd:PRK10717 245 LE--GAPIDDAIRIPDEE---ALSTAYR----LLEEEGlclggssGINVAAALR-LARELGPGHTIVTIlcDSGE 309
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
32-302 |
1.52e-15 |
|
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: 77.81 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLG-NRVLLKREDLQPVFSFKIRG---AYTRVArlsdEQKARGVITASAGNHAQGLALAAQRLGVRAVI 107
Cdd:TIGR00260 23 TPLFRAPALAANVGiKNLYVKELGHNPTLSFKDRGmavALTKAL----ELGNDTVLCASTGNTGAAAAAYAGKAGLKVVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 108 VMPR-TTPELKVKGVLARGGEAL-LHGDaFPDALAHALQLAE-REGMTFVPPYDDPDVIAGQGTVAMEILRQHSGRL-DA 183
Cdd:TIGR00260 99 LYPAgKISLGKLAQALGYNAEVVaIDGN-FDDAQRLVKQLFEdKPALGLNSANSIPYRLEGQKTYAFEAVEQLGWEApDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 184 IFVPVGGGSLI----AGIAAYvKHLRPDI--RVIGVEPEDSN-CLQAALAAGERVVLGQVGLFADGVAVAQigACNFEVC 256
Cdd:TIGR00260 178 VVVPVPNSGNFgaiwKGFKEK-KMLGLDSlpVKRGIQAEGAAdIVRAFLEGGQWEPIETPETLSTAMDIGN--PANWPRA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15596523 257 KDHVDEVI----TVGSDEICAAIKDIYDDTRSITEPAGALAVAGIKKYVA 302
Cdd:TIGR00260 255 LEAFRRSNgyaeDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVE 304
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
32-363 |
8.56e-15 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 76.39 E-value: 8.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLqVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARLSDeQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPR 111
Cdd:PRK05638 67 TPL-IRARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLP-YAANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 112 TTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGrlDAIFVPVGGG 191
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINP--THVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 192 SLIAGIAAYVKHLR--------PdiRVIGVEPEDSNCLQAAlaagervVLGQVglfadgvavaqiGACNFE--------- 254
Cdd:PRK05638 223 SYLYSIYKGFKELLeigvieeiP--KLIAVQTERCNPIASE-------ILGNK------------TKCNETkalglyvkn 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 255 -VCKDHVDEVITVGSDEICAAIKDIYDDTRSI-------TEPAGALAVAGIKKYVAR---ERTEGQTLVAIDSGANINFD 323
Cdd:PRK05638 282 pVMKEYVSEAIKESGGTAVVVNEEEIMAGEKLlakegifAELSSAVVMPALLKLGEEgyiEKGDKVVLVVTGSGLKGYGE 361
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15596523 324 RLRhvaERAELGEQREAIIAVtVAERPGSFKAFCAALGRR 363
Cdd:PRK05638 362 GGR---EKFTIGGTKLEILKI-LSEREMYGYEIWKALGKP 397
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
21-314 |
2.39e-13 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 71.11 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 21 LAAPVYDVAVETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVArlsdEQKARGVITA--------SAGNHAQ 92
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMIT----DAEEKGLIKPgesvliepTSGNTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 93 GLALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDA--FPDALAHALQLAEREGMTFV-PPYDDP-DVIAGQGT 168
Cdd:PLN02565 81 GLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAkgMKGAVQKAEEILAKTPNSYIlQQFENPaNPKIHYET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 169 VAMEILRQHSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAAlAAGERVVLGQVGLFADGVavaqi 248
Cdd:PLN02565 161 TGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGG-KPGPHKIQGIGAGFIPGV----- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596523 249 gacnFEVckDHVDEVITVGSDEICAAIKDI-YDDTRSITEPAGALAVAGIkKYVARERTEGQTLVAI 314
Cdd:PLN02565 235 ----LDV--DLLDEVVQVSSDEAIETAKLLaLKEGLLVGISSGAAAAAAI-KIAKRPENAGKLIVVI 294
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
32-197 |
3.13e-13 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 70.51 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLG-NRVLLKREDLQPVFSFKIRGAYTRVARlSDEQKARGVITASAGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRR-AMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMTFVPPYDDPDVIA--GQGTVAMEILRQHSGRLDAIFVPV 188
Cdd:PRK06381 95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVPDAVAVPV 174
|
....*....
gi 15596523 189 GGGSLIAGI 197
Cdd:PRK06381 175 GNGTTLAGI 183
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
32-213 |
6.65e-13 |
|
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: 69.44 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDL-QPVFSfkirGAYTRVAR--LSD--EQKARGVITASAG--NHAQGLALAAQRLGVR 104
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLtGPAIG----GNKTRKLEylLADalAQGADTLVTFGGAqsNHARATAAAAAKLGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMpRTTPELKVKGVLA-------------RGGEALLHgDAFPDALAhalQLAEREGMTFVPPYDDPDVIAGQGTV-- 169
Cdd:COG2515 88 CVLVL-RGEEPTPLNGNLLldrllgaelhfvsRGEYRDRD-EAMEAVAA---ELRARGGKPYVIPEGGSNPLGALGYVea 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596523 170 AMEILRQ---HSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGV 213
Cdd:COG2515 163 AAELAAQlaeLGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGI 209
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
32-213 |
9.20e-13 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 69.48 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFS--FKIRG-AYTRVARLsdEQKARGVITASA--GNHAQGLALAAQRLGVRAV 106
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGLALggNKTRKlEFLLADAL--AQGADTLITAGAiqSNHARQTAAAAAKLGLKCV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 107 IVMPRTTPElKVKGVLARGGEALLH----------GDAFPDALAHAL--QLAEREGMTFVPPYDDPDVIAGQGTV--AME 172
Cdd:PRK03910 94 LLLENPVPT-EAENYLANGNVLLDDlfgaeihvvpAGTDMDAQLEELaeELRAQGRRPYVIPVGGSNALGALGYVacALE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15596523 173 ILRQ---HSGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGV 213
Cdd:PRK03910 173 IAQQlaeGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGV 216
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
45-204 |
1.30e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 65.91 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 45 GNRVLLKREDLQPVFSFKIRGAYTRVARLSDeQKARGVITASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKGVLAR 124
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 125 GGEaLLHGDAFPDALAHAlqlAEREGMTFVPPYDDPDVIAGQGTVAMEILRQHSGRL-DAIFVPVGGGSLIAGIAAYVKH 203
Cdd:PRK06450 143 GAE-VVRVRGSREDVAKA---AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKIpNYVFIPVSAGTLLLGVYSGFKH 218
|
.
gi 15596523 204 L 204
Cdd:PRK06450 219 L 219
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
31-221 |
2.27e-11 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 65.37 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAytrVARLSDEQKaRGVITA--------SAGNHAQGLALAAQRLG 102
Cdd:PLN02556 59 KTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPA---LAMIEDAEK-KNLITPgkttliepTSGNMGISLAFMAAMKG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 103 VRAVIVMPRTTPELKVKGVLARGGEALL--HGDAFPDALAHALQLAEREGMTFV-PPYDDP-DVIAGQGTVAMEILRQHS 178
Cdd:PLN02556 135 YKMILTMPSYTSLERRVTMRAFGAELVLtdPTKGMGGTVKKAYELLESTPDAFMlQQFSNPaNTQVHFETTGPEIWEDTL 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596523 179 GRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCL 221
Cdd:PLN02556 215 GQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVL 257
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
31-314 |
3.57e-11 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 65.18 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVArlSDEQKA------RGVITASAGNHAQGLALAAQRLGVR 104
Cdd:PLN03013 123 KTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVT--DAEQKGfispgkSVLVEPTSGNTGIGLAFIAASRGYR 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMPRTTPELKVKGVLARGGEALLHGDAfpDALAHALQLAErEGMTFVP------PYDDP-DVIAGQGTVAMEILRQH 177
Cdd:PLN03013 201 LILTMPASMSMERRVLLKAFGAELVLTDPA--KGMTGAVQKAE-EILKNTPdaymlqQFDNPaNPKIHYETTGPEIWDDT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 178 SGRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAALAAGERVvlgqvglfaDGVAVAQIGAcNFEvcK 257
Cdd:PLN03013 278 KGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKI---------QGIGAGFIPK-NLD--Q 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596523 258 DHVDEVITVGSDEICAAIKDI-YDDTRSITEPAGALAVAGIKkyVARERTEGQTLVAI 314
Cdd:PLN03013 346 KIMDEVIAISSEEAIETAKQLaLKEGLMVGISSGAAAAAAIK--VAKRPENAGKLIAV 401
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
47-330 |
8.19e-11 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 63.48 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 47 RVLLKREDLQPVFSFKIRGAYTRVARLSDeqkaRGVIT--------ASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKV 118
Cdd:PLN00011 33 RIAAKLEMMEPCSSVKDRIAYSMIKDAED----KGLITpgkstlieATAGNTGIGLACIGAARGYKVILVMPSTMSLERR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 119 KGVLARGGEALL--HGDAFPDALAHALQLAEREGMTFVPPY----DDPDViaGQGTVAMEILRQHSGRLDAIFVPVGGGS 192
Cdd:PLN00011 109 IILRALGAEVHLtdQSIGLKGMLEKAEEILSKTPGGYIPQQfenpANPEI--HYRTTGPEIWRDSAGKVDILVAGVGTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 193 LIAGIAAYVKHLRPDIRVIGVEPEDSNCLQAAlAAGERVVLG-QVGLFADGVavaqigacNFEVckdhVDEVITVGSDEI 271
Cdd:PLN00011 187 TATGVGKFLKEKNKDIKVCVVEPVESAVLSGG-QPGPHLIQGiGSGIIPFNL--------DLTI----VDEIIQVTGEEA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596523 272 CAAIKDI-YDDTRSITEPAGALAVAGIkKYVARERTEGQTLVAI-DSG-----ANINFDRLRHVAE 330
Cdd:PLN00011 254 IETAKLLaLKEGLLVGISSGAAAAAAL-KVAKRPENAGKLIVVIfPSGgerylSTKLFESVRYEAE 318
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
32-227 |
6.26e-10 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 60.51 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLL--KREDLQPVFSF---KIRgaytRVARLSDEQKARG---VITASA--GNHAQGLALAAQRL 101
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIyaKRDDCNSGLAFggnKIR----KLEYLLPDALAKGadtLVTVGGiqSNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 102 GVRAVIVM----PRTTPELKVKG--VLAR--GGEALLHGDAFP----DALAHALQLAEREGMT--FVPPYDDPDVIAGQG 167
Cdd:cd06449 77 GLKCVLVQenwvPYSDAVYDRVGniLLSRimGADVRLVSAGFDigirKSFEEAAEEVEAKGGKpyVIPAGGSEHPLGGLG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596523 168 TV--AMEILRQHSG---RLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGVE----PEDS-----NCLQAALAA 227
Cdd:cd06449 157 YVgfVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDasakPEKTkaqvlRIAQAKLAE 230
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
31-213 |
3.28e-09 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 58.36 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 31 ETPLQVAPQLSQRLGNRVLLKREDLQ--PVFSFKIRgaytRVARLSDEQKARG---VITASA--GNHAQGLALAAQRLGV 103
Cdd:PRK14045 21 ETPIQYLPNISRELGADVYVKRDDLTglGIGGNKIR----KLEYLLGDALSRGadvVITVGAvhSNHAFVTGLAAKKLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 104 RAVIVMpRTTPEL-------KVKGVLARGGEAllhGDAFpDALAHALQLAE---REGMT--FVPPYDDPDV-----IAGQ 166
Cdd:PRK14045 97 DAVLVL-RGKEELkgnylldKIMGIETRVYEA---KDSF-ELMKYAEEVAEelkGEGRKpyIIPPGGASPVgtlgyVRAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15596523 167 GTVAMEILRQHSgRLDAIFVPVGGGSLIAGIAAYVKHLRPDIRVIGV 213
Cdd:PRK14045 172 GEIATQVKKLGV-RFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGI 217
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
32-216 |
5.37e-09 |
|
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: 57.93 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGN-RVLLKREDLQPVFSFKIRGAYTRvARLSDEQKARGVITAS-AGNHAQGLALAAQRLGVRAVIVM 109
Cdd:cd06446 35 TPLYRAKRLSEYLGGaKIYLKREDLNHTGAHKINNALGQ-ALLAKRMGKKRVIAETgAGQHGVATATACALFGLECEIYM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 110 PRTTPE-----------LKVKGVLARGGEALLhGDAFPDALAHALqlaEREGMTF------VPPYDDPD-VIAGQGTVAM 171
Cdd:cd06446 114 GAVDVErqplnvfrmelLGAEVVPVPSGSGTL-KDAISEAIRDWV---TNVEDTHyllgsvVGPHPYPNmVRDFQSVIGE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15596523 172 EILRQ---HSGRL-DAIFVPVGGGSLIAGIA-AYVKHlrPDIRVIGVEPE 216
Cdd:cd06446 190 EAKKQileKEGELpDVVIACVGGGSNAAGLFyPFIND--KDVKLIGVEAG 237
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
32-217 |
1.65e-08 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 56.03 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRVARlsdeQKARG-------VITASAGNHAQGLALAAQRLGVR 104
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ----AEKRGeikpgdtLIEATSGNTGIALAMIAAIKGYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 105 AVIVMPRTTPELKVKGVLARGGEALL--HGDAFPDALAHALQLAEREGMTFVPPYDDPD-VIAGQGTVAMEILRQHSGRL 181
Cdd:PRK11761 89 MKLIMPENMSQERRAAMRAYGAELILvpKEQGMEGARDLALQMQAEGEGKVLDQFANPDnPLAHYETTGPEIWRQTEGRI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 15596523 182 DAiFVPVGG--GSlIAGIAAYVKHLRPDIRVIGVEPED 217
Cdd:PRK11761 169 TH-FVSSMGttGT-IMGVSRYLKEQNPAVQIVGLQPEE 204
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
30-297 |
9.45e-08 |
|
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: 54.27 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 30 VETPLQVAPQLSQRLGN--------RVLLKREDLQPVF-SFKIRGAYTRV--------------------ARLsDEQKAR 80
Cdd:cd06447 51 IESPLLPIPRMKQALEKlyhqpikgRLLLKADSHLPISgSIKARGGIYEVlkhaeklalehglltleddySKL-ASEKFR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 81 ------GVITASAGNHAQGLALAAQRLGVRAVIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALQLAEREGMT-F 153
Cdd:cd06447 130 klfsqySIAVGSTGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCyF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 154 VPPYDDPDVIAGQGTVAMEILRQHSG---RLDA-----IFVPVGGGSLIAGIAAYVKHLRPD-IRVIGVEPEDSNCLQAA 224
Cdd:cd06447 210 VDDENSRDLFLGYAVAASRLKAQLAElgiKVDAehplfVYLPCGVGGAPGGVAFGLKLIFGDnVHCFFAEPTHSPCMLLG 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596523 225 LAAG--ERVVLGQVGL----FADGVAVAQIGACNFEVCKDHVDEVITVGSDEICAAIKDIYDDTRSITEPAGALAVAGI 297
Cdd:cd06447 290 MATGlhDKISVQDIGIdnrtAADGLAVGRPSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGP 368
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
434-507 |
1.25e-07 |
|
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: 49.08 E-value: 1.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596523 434 ERLFRFEFPERPGALLNFLDKLGSRwNISLFHYRNHGAADGRVLAGLQVPD--EERGELEAALQAIGYPYWEETHN 507
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPR-NITEFNYRYADEKDAHIFVGVSVANgaEELAELLEDLKSAGYEVVDLSDD 75
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
32-214 |
9.74e-07 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 51.35 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLGNRVLLKREDLQPVFSFKIRGAYTRvARLSDEQKARGVITAS-AGNHAQGLALAAQRLGVRAVIVMP 110
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQ-ALLAKRMGKTRIIAETgAGQHGVATATACALFGLKCTIFMG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 111 RTT---PELKVKGVLARGGE--ALLHGD-AFPDALAHALQ--LAEREGM-----TFVPPYDDPDVIAG-QGTVAMEI--- 173
Cdd:PRK13803 351 EEDikrQALNVERMKLLGANviPVLSGSkTLKDAVNEAIRdwVASVPDThyligSAVGPHPYPEMVAYfQSVIGEEAkeq 430
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15596523 174 LRQHSGRL-DAIFVPVGGGSLIAGI-AAYVKHlrPDIRVIGVE 214
Cdd:PRK13803 431 LKEQTGKLpDAIIACVGGGSNAIGIfYHFLDD--PSVKLIGVE 471
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
32-202 |
8.17e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 45.19 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 32 TPLQVAPQLSQRLG--NRVLLKREDLQPVFSFKIRG---AYTRVARLSDEQK-ARGVITASAGNHAQGLALAAQRLGVRA 105
Cdd:PLN02569 134 SNLFWAERLGKEFLgmNDLWVKHCGISHTGSFKDLGmtvLVSQVNRLRKMAKpVVGVGCASTGDTSAALSAYCAAAGIPS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 106 VIVMPRTTPELKVKGVLARGGEALLHGDAFPDALAHALqlaeREGMTFVPPYD----DPDVIAGQGTVAMEILRQHSGRL 181
Cdd:PLN02569 214 IVFLPADKISIAQLVQPIANGALVLSIDTDFDGCMRLI----REVTAELPIYLanslNSLRLEGQKTAAIEILQQFDWEV 289
|
170 180
....*....|....*....|..
gi 15596523 182 -DAIFVPVGGGSliaGIAAYVK 202
Cdd:PLN02569 290 pDWVIVPGGNLG---NIYAFYK 308
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
28-197 |
1.75e-04 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 44.25 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 28 VAVETPLQVAPQLSQR------LGNRVLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRL 101
Cdd:PRK13802 323 VGRPSPLTEAPRFAERvkektgLDARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAML 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 102 GVRAVIVMPRTTPE---LKVKGVLARGGEAL---LHGDAFPDALAHALqlaeREGMTFVP-----------PYDDPDVIA 164
Cdd:PRK13802 403 GLKCRIYMGQIDARrqaLNVARMRMLGAEVVevtLGDRILKDAINEAL----RDWVTNVKdthyllgtvagPHPFPAMVR 478
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596523 165 G----QGTVAMEILRQHSG--RLDAIFVPVGGGSLIAGI 197
Cdd:PRK13802 479 DfqkiIGEEAKQQLQDWYGidHPDAICACVGGGSNAIGV 517
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
28-233 |
1.11e-03 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 41.28 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 28 VAVETPLQVAPQLSQRLGNR------VLLKREDLQPVFSFKIRGAYTRVARLSDEQKARGVITASAGNHAQGLALAAQRL 101
Cdd:PLN02618 63 VGRETPLYFAERLTEHYKRAdgegpeIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596523 102 GVRAVIVMPRTTPELKVKGVLAR---GGE--ALLHGDA-FPDALAHALqlaeREGMTFVP-----------PYDDPDVIA 164
Cdd:PLN02618 143 GLECIVYMGAQDMERQALNVFRMrllGAEvrPVHSGTAtLKDATSEAI----RDWVTNVEtthyilgsvagPHPYPMMVR 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596523 165 G-QGTVAMEILRQH----SGRLDAIFVPVGGGSLIAGI-AAYVKHlrPDIRVIGVEPE----DSNCLQAALAAGERVVL 233
Cdd:PLN02618 219 DfHSVIGKETRRQAmekwGGKPDVLVACVGGGSNAMGLfHEFIDD--EDVRLIGVEAAgfglDSGKHAATLTKGEVGVL 295
|
|
| |
