|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
14-516 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 992.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 14 SGADYLRNILRAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHA 93
Cdd:PRK09224 1 MGADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 94 QGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGI 173
Cdd:PRK09224 81 QGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 174 ELVQQNGH-LDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSE 252
Cdd:PRK09224 161 EILQQHPHpLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 253 TFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKDQQLAAILSGANLNFHGLRYVSER 332
Cdd:PRK09224 241 TFRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAER 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 333 CELGEKREGLLAVTIPERPGAFLDFCHLIGGRAVTEFNYRYNDDSLANVFVGVRLMQGQEELDGIIQDLRKGGYPVVDLS 412
Cdd:PRK09224 321 AELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDLS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 413 DDEMAKVHVRYMIGGRPSKPLKERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELEDKDLLSFT 492
Cdd:PRK09224 401 DDELAKLHVRYMVGGRPPKPLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADEPEFE 480
|
490 500
....*....|....*....|....
gi 496276300 493 SHLRELGYHWQDETENPAYKFFLA 516
Cdd:PRK09224 481 AFLDELGYPYWDETDNPAYRLFLA 504
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
17-515 |
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: 817.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 17 DYLRNILRAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGL 96
Cdd:TIGR01124 1 DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 97 ALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELV 176
Cdd:TIGR01124 81 AFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 177 QQNG-HLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFR 255
Cdd:TIGR01124 161 RQVAnPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 256 LCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKDQQLAAILSGANLNFHGLRYVSERCEL 335
Cdd:TIGR01124 241 LCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 336 GEKREGLLAVTIPERPGAFLDFCHLIGGRAVTEFNYRYNDDSLANVFVGVRLMQGQEELDgIIQDLRKGGYPVVDLSDDE 415
Cdd:TIGR01124 321 GEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNPQERQE-ILARLNDGGYSVVDLTDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 416 MAKVHVRYMIGGRPSKPLKERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELEDKDLLSFTSHL 495
Cdd:TIGR01124 400 LAKLHVRYMVGGRPPHVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDQFEQFL 479
|
490 500
....*....|....*....|
gi 496276300 496 RELGYHWQDETENPAYKFFL 515
Cdd:TIGR01124 480 AELGYRYHDETNNPAYRLFL 499
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
7-516 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 687.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 7 ATDEVLLSgaDYLRNILRAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIA 86
Cdd:PRK12483 13 APRAALLA--DYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 87 ASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIA 166
Cdd:PRK12483 91 ASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 167 GQGTIGIE-LVQQNGHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVA 245
Cdd:PRK12483 171 GQGTVAMEiLRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 246 VKRIGSETFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKDQQLAAILSGANLNFHG 325
Cdd:PRK12483 251 VAQIGEHTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNFDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 326 LRYVSERCELGEKREGLLAVTIPERPGAFLDFCHLIGGRAVTEFNYRYNDDSLANVFVGVRLMQGQEELDGIIQDLRKGG 405
Cdd:PRK12483 331 LRHVAERAELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASLRAQG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 406 YPVVDLSDDEMAKVHVRYMIGGRPSKPLKERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELED 485
Cdd:PRK12483 411 FPVLDLTDDELAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGLQVPE 490
|
490 500 510
....*....|....*....|....*....|.
gi 496276300 486 KDLLSFTSHLRELGYHWQDETENPAYKFFLA 516
Cdd:PRK12483 491 DERAALDAALAALGYPYWEETGNPAYRLFLG 521
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
7-515 |
0e+00 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 523.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 7 ATDEVLLSGADYLRNILRAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIA 86
Cdd:PLN02550 83 AENGSIPEAMEYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVIC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 87 ASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIA 166
Cdd:PLN02550 163 SSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 167 GQGTIGIELVQQ-NGHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVA 245
Cdd:PLN02550 243 GQGTVGMEIVRQhQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 246 VKRIGSETFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKDQQLAAILSGANLNFHG 325
Cdd:PLN02550 323 VKEVGEETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 326 LRYVSERCELGEKREGLLAVTIPERPGAFLDFCHLIGGRAVTEFNYRYNDDSLANVFVGVRLMQgQEELDGIIQDLRKGG 405
Cdd:PLN02550 403 LRIVTELADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHT-EQELQALKKRMESAQ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 406 YPVVDLSDDEMAKVHVRYMIGGRPSKPlKERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELED 485
Cdd:PLN02550 482 LRTVNLTSNDLVKDHLRYLMGGRAIVK-DELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQVPP 560
|
490 500 510
....*....|....*....|....*....|
gi 496276300 486 KDLLSFTSHLRELGYHWQDETENPAYKFFL 515
Cdd:PLN02550 561 EEMQEFKSRANALGYEYQDECDNEAFQLLM 590
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
17-338 |
4.87e-151 |
|
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: 434.46 E-value: 4.87e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 17 DYLRNIL--RAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQ 94
Cdd:COG1171 6 PTLADIEaaAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 95 GLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIE 174
Cdd:COG1171 86 GVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 175 LVQQNGHLDCVFVPvgggglaagvavllKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETF 254
Cdd:COG1171 166 ILEQLPDLDAVFVPvggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 255 RLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVElhQLKDQQLAAILSGANLNFHGLRYVSERCE 334
Cdd:COG1171 246 EILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKE--RLKGKRVVVVLSGGNIDPDRLAEILERGL 323
|
....
gi 496276300 335 LGEK 338
Cdd:COG1171 324 VGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
19-322 |
2.12e-143 |
|
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: 414.19 E-value: 2.12e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 19 LRNILRAPVY--EVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGL 96
Cdd:cd01562 1 LEDILAAAARikPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 97 ALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELV 176
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 177 QQNGHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRL 256
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496276300 257 CQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVElhQLKDQQLAAILSGANLN 322
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKL--DLKGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
29-417 |
1.07e-111 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 337.55 E-value: 1.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 29 EVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKAT 108
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 109 IVMPRTTPDIKVDAVRSFGG---HVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHL--- 182
Cdd:PRK08639 101 IFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKEgsp 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 183 DCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYLD 262
Cdd:PRK08639 181 DYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVVD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 263 DVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVElhQLKDQQLAAILSGANLNFHGLRYVSERCELGEKREGL 342
Cdd:PRK08639 261 DVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKD--EIKGKTVVCVISGGNNDIERMPEIKERSLIYEGLKHY 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496276300 343 LAVTIPERPGAFLDFCHLIGGRA--VTEFNY-RYNDDSLANVFVGVRLmQGQEELDGIIQDLRKGGYPVVDLSDDEMA 417
Cdd:PRK08639 339 FIVNFPQRPGALREFLDDVLGPNddITRFEYlKKNNRETGPVLVGIEL-KDAEDYDGLIERMEAFGPSYIDINPNEPL 415
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
34-409 |
5.72e-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: 295.89 E-value: 5.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPR 113
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 114 TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGGG 193
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 194 LAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYLDDVVTVSSDEIC 273
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 274 SAVKDIFEDTRAIAEPSGALSLAGLkkyveLHQ---LKDQQLAAILSGANLNFHGLRYVSERCELGEKREGLLAVTIPER 350
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAAL-----LEQkvdVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496276300 351 PGAFLDFCHLI---GGRAVTEFNYRYNDDsLANVFVGVRL---MQGQEELDGIIQDLRKGGYPVV 409
Cdd:TIGR01127 316 PGALYHLLESIaeaRANIVKIDHDRLSKE-IPPGFAMVEItleTRGKEHLDEILKILRDMGYNFY 379
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
24-340 |
4.52e-88 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 273.92 E-value: 4.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 24 RAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQL 103
Cdd:PRK08638 18 KQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 104 GVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLD 183
Cdd:PRK08638 98 GIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 184 CVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYLDD 263
Cdd:PRK08638 178 TVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDD 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496276300 264 VVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKDQQLAAILSGANLNfhgLRYVSERCELGEKRE 340
Cdd:PRK08638 258 IVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVD---LSRVSQITGHVVAAD 331
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
34-408 |
2.25e-83 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 264.06 E-value: 2.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPR 113
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 114 TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGGG 193
Cdd:PRK07334 104 FTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 194 LAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALdagQPVTLDQVG-MFADGVAVKRIGSETFRLCQQYLDDVVTVSSDEI 272
Cdd:PRK07334 184 LISGMATAAKALKPDIEIIGVQTELYPSMYAAI---KGVALPCGGsTIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 273 CSAVKDIFEDTRAIAEPSGALSLAGLKKYVELhqLKDQQLAAILSGANLNFHGLRYVSERcelGEKREGLLA---VTIPE 349
Cdd:PRK07334 261 EQAVSLLLEIEKTVVEGAGAAGLAALLAYPER--FRGRKVGLVLSGGNIDTRLLANVLLR---GLVRAGRLArlrVDIRD 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496276300 350 RPGAFLDFCHLIG--GRAVTEFNYRYNDDSLANVFVGVRLM---QGQEELDGIIQDLRKGGYPV 408
Cdd:PRK07334 336 RPGALARVTALIGeaGANIIEVSHQRLFTDLPAKGAELELVietRDAAHLQEVIAALRAAGFEA 399
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
34-320 |
2.27e-77 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 246.03 E-value: 2.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPR 113
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMSR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 114 TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGGG 193
Cdd:PRK07476 100 LVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALPDVATVLVPLSGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 194 LAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAvKRIGSE---TFRLCQQYLDDVVTVSSD 270
Cdd:PRK07476 180 LASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADSLG-GGIGLDnryTFAMCRALLDDVVLLDEA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 496276300 271 EICSAVKDIFEDTRAIAEPSGALSLAGLKKyvelHQLKDQQ--LAAILSGAN 320
Cdd:PRK07476 259 EIAAGIRHAYREERLVVEGAGAVGIAALLA----GKIAARDgpIVVVVSGAN 306
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
30-322 |
7.03e-77 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 244.54 E-value: 7.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 30 VAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATI 109
Cdd:PRK07048 21 VAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 110 VMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPV 189
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALFVCL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 190 GGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYLDDVVTVSS 269
Cdd:PRK07048 181 GGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPIIRRLVDDIVTVSD 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 496276300 270 DEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVelHQLKDQQLAAILSGANLN 322
Cdd:PRK07048 261 AELVDAMRFFAERMKIVVEPTGCLGAAAALRGK--VPLKGKRVGVIISGGNVD 311
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
34-318 |
4.50e-75 |
|
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: 239.13 E-value: 4.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPR 113
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 114 TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQ-HGYTFIPPFDHPSVIAGQGTIGIELV-QQNGHLDCVFVPVGG 191
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILeQLGGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 192 GGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRI-GSETFRLCQQYLDDVVTVSSD 270
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496276300 271 EICSAVKDIFEDTRAIAEPSGALSLAGLkKYVELHQLK-DQQLAAILSG 318
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAAL-KLALAGELKgGDRVVVVLTG 295
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
33-327 |
2.97e-74 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 237.67 E-value: 2.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 33 VTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMP 112
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 113 RTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGG 192
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 193 GLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVA--VKRiGSETFRLCQQYLDDVVTVSSD 270
Cdd:PRK06815 180 GLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVEP-GAITFPLCQQLIDQKVLVSEE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 496276300 271 EICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQLKdqQLAAILSGANLNFHGLR 327
Cdd:PRK06815 259 EIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGK--KVAVVLCGKNIVLEKYL 313
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
34-318 |
3.51e-65 |
|
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: 211.60 E-value: 3.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAG--VIAASAGNHAQGLALSSQQLGVKATIVM 111
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 112 PRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQ-HGYTFIPPFDHPSVIAGQGTIGIELVQQ--NGHLDCVFVP 188
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQlgGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 189 VGGGGLAAGVAVLLKQLLPEIKVVGVEAEdsaclkaaldagqpvtldqvgmfadgvavkrigsetfrlcqqylddVVTVS 268
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 496276300 269 SDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHqLKDQQLAAILSG 318
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILTG 243
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
19-298 |
9.97e-63 |
|
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: 207.78 E-value: 9.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 19 LRNILRAPVYEVAQV--TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGL 96
Cdd:TIGR02991 3 LQDIERAAARISGRVeeTPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 97 ALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELV 176
Cdd:TIGR02991 83 AYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 177 QQNGHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFAD--GVAVKRIGSETF 254
Cdd:TIGR02991 163 EQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTF 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 496276300 255 RLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGL 298
Cdd:TIGR02991 243 AMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL 286
|
|
| PLN02970 |
PLN02970 |
serine racemase |
30-326 |
4.17e-62 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 206.45 E-value: 4.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 30 VAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATI 109
Cdd:PLN02970 24 FIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 110 VMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPV 189
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 190 GGGGLAAGVAVLLKQLLPEIKVVGVE---AEDSACLKAaldAGQPVTLDQVGMFADGVAVkRIGSETFRLCQQYLDDVVT 266
Cdd:PLN02970 184 SGGGLISGIALAAKAIKPSIKIIAAEpkgADDAAQSKA---AGEIITLPVTNTIADGLRA-SLGDLTWPVVRDLVDDVIT 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496276300 267 VSSDEICSAVKDIFEDTRAIAEPSGALSLAGL--KKYVELHQLKD-QQLAAILSGANLNFHGL 326
Cdd:PLN02970 260 VDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsDSFRSNPAWKGcKNVGIVLSGGNVDLGVL 322
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
49-322 |
2.09e-57 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 193.25 E-value: 2.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 49 QIQLKREDRQPVHSFKLRGAYNMMsqLTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGG 128
Cdd:PRK08246 38 PVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 129 HVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGGGLAAGVAVLLKqllPE 208
Cdd:PRK08246 116 EVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFE---GR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 209 IKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAE 288
Cdd:PRK08246 193 ARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVE 272
|
250 260 270
....*....|....*....|....*....|....*.
gi 496276300 289 PSGALSLAGL--KKYVElhqLKDQQLAAILSGANLN 322
Cdd:PRK08246 273 PGAATALAALlsGAYVP---APGERVAVVLCGANTD 305
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
24-323 |
3.47e-52 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 179.80 E-value: 3.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 24 RAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQL--TEPQkAAGVIAASAGNHAQGLALSSQ 101
Cdd:PRK06110 12 AAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLarRGPR-VRGVISATRGNHGQSVAFAAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 102 QLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFdHPSVIAGQGTIGIELVQQNGH 181
Cdd:PRK06110 91 RHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 182 LDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSETFRLCQQYL 261
Cdd:PRK06110 170 LDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496276300 262 DDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKyvELHQLKDQQLAAILSGANLNF 323
Cdd:PRK06110 250 DRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ--ERERLAGKRVGLVLSGGNIDR 309
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
9-322 |
3.84e-51 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 177.90 E-value: 3.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 9 DEVLLSGADYLRNILRAPVYevAQVTPLQNMSRLSarianqIQLKREDRQPVHSFKLRGAYNMMSQLTEPQKAAGVIAAS 88
Cdd:PRK08813 17 GDVAVSVADVLAAQARLRRY--LSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 89 AGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQ 168
Cdd:PRK08813 89 AGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 169 GTIGIELVQQNGhlDCVFVPVGGGGLAAGVAVLLKQllPEIKVVGVEAEDSACLKAALdAGQPVTLDQVGMFADGVAVKR 248
Cdd:PRK08813 169 GTVGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAI-RGDLREIAPVATLADGVKVKI 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496276300 249 IGSETFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKyvelhqLKDQQLAAILSGANLN 322
Cdd:PRK08813 244 PGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGRR------VSGKRKCAVVSGGNID 311
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
340-424 |
1.90e-44 |
|
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: 151.16 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 340 EGLLAVTIPERPGAFLDFCHLIGGRAVTEFNYRYNDDSLANVFVGVRLMQGQEELDGIIQDLRKGGYPVVDLSDDEMAKV 419
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 496276300 420 HVRYM 424
Cdd:cd04906 81 HLRYM 85
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
34-322 |
1.96e-41 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 151.46 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTE----PQKaagVIAASAGNHAQGLALSSQQLGVKATI 109
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEqgklPDK---IVAYSTGNHGQAVAYASKLFGIKTRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 110 VMPRTTPDIKVDAVRSFGGHVVLHGSNfDEAKGYAEQlAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGH-LDCVFVP 188
Cdd:PRK06608 101 YLPLNTSKVKQQAALYYGGEVILTNTR-QEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFsPDAIFAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 189 VGGGGLAAGVAVLLKQLLPEIKVVGVE---AEDSAclkAALDAGQPVTLDQV-GMFADGVAVKRIGSETFRLCQQyLDDV 264
Cdd:PRK06608 179 CGGGGLISGTYLAKELISPTSLLIGSEplnANDAY---LSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKK-LDDF 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 496276300 265 VTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVeLHQLKDQQLAAILSGANLN 322
Cdd:PRK06608 255 YLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWL-KTQSKPQKLLVILSGGNID 311
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
435-515 |
3.39e-39 |
|
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: 137.30 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 435 ERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELEDKDLLSFTSHLRELGYHWQDETENPAYKFF 514
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADLDELKERLDALGYPYQEETDNPAYKLF 80
|
.
gi 496276300 515 L 515
Cdd:cd04907 81 L 81
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
33-296 |
1.05e-37 |
|
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: 140.90 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 33 VTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTE--PQKAAGVIAASAGNHAQGLALSSQQLGVKATIV 110
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKqgLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 111 MPRTTPDIKVDAVRSFGGHVVLHGSN-FDEAKGYAEQLAEQHGYT-FIPPFDHPSVIAGQGTIGIELVQQ---------- 178
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELAENDPGPvYVHPFDDPLIWEGHSSMVDEIAQQlqsqekvdai 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 179 -----NGHLDCVFVpvgggglaagvAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKRIGSET 253
Cdd:cd06448 161 vcsvgGGGLLNGIV-----------QGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 496276300 254 FRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLA 296
Cdd:cd06448 230 LEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALA 272
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
426-515 |
8.52e-31 |
|
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: 114.68 E-value: 8.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 426 GGRPSKPLKERLYSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELEDK-DLLSFTSHLRELGYHWQD 504
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQAeDLDEFIERLNKLGYDYED 80
|
90
....*....|.
gi 496276300 505 ETENPAYKFFL 515
Cdd:pfam00585 81 LSDNEAAYEHL 91
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
34-328 |
1.84e-29 |
|
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: 118.08 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARI-ANQIQLKREDRQPVHSFKLRGAYNMMSQLtepqKAAG---VIAASAGNHAQGLALSSQQLGVKATI 109
Cdd:cd01563 23 TPLVRAPRLGERLgGKNLYVKDEGLNPTGSFKDRGMTVAVSKA----KELGvkaVACASTGNTSASLAAYAARAGIKCVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 110 VMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPpFDHPSVIAGQGTIGIELVQQNGHL--DCVFV 187
Cdd:cd01563 99 FLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQLGWEvpDYVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 188 PVGGGGLAAGVAVLLKQL--------LPeiKVVGVEAEDSACLKAALDAGQ--PVTLDQVGMFADGVavkRIGS-----E 252
Cdd:cd01563 178 PVGNGGNITAIWKGFKELkelglidrLP--RMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAI---RIGNpasgpK 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496276300 253 TFRLCQQYLDDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQL-KDQQLAAILSGanlnfHGLRY 328
Cdd:cd01563 253 ALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVVVVLTG-----HGLKD 324
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
331-421 |
3.07e-29 |
|
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: 110.45 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 331 ERCELGEKREGLLAVTIPERPGAFLDFCHLIGGRA-VTEFNYRYNDDSLANVFVGVRLMQGqEELDGIIQDLRKGGYPVV 409
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNnITLFEYRKHGDKNGCVLVGIELSQA-EDLDEFIERLNKLGYDYE 79
|
90
....*....|..
gi 496276300 410 DLSDDEMAKVHV 421
Cdd:pfam00585 80 DLSDNEAAYEHL 91
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
438-504 |
2.16e-25 |
|
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: 99.12 E-value: 2.16e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496276300 438 YSFEFPEYPGALIRFLKTLGSHWNISLFNYRNHGADYGRVLCGFELED-KDLLSFTSHLRELGYHWQD 504
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDrEDLAELKERLEALGYPYVD 68
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
343-410 |
2.11e-23 |
|
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: 93.34 E-value: 2.11e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496276300 343 LAVTIPERPGAFLDFCHLIGG-RAVTEFNYRYNDDSLANVFVGVRLmQGQEELDGIIQDLRKGGYPVVD 410
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPpRNITEFHYRNQGGDEARVLVGIQV-PDREDLAELKERLEALGYPYVD 68
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
33-303 |
2.26e-23 |
|
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: 101.82 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 33 VTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEpQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMP 112
Cdd:COG0498 66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALE-RGAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 113 RT-TPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFdHPSVIAGQGTIGIELVQQNGHL-DCVFVP-- 188
Cdd:COG0498 145 EGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVpDWVVVPtg 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 189 --------------VGGGGLAAGvavllkqlLPeiKVVGVEAEDSACLKAALDAGQP-VTLDQVGMFADGVAVKRigSET 253
Cdd:COG0498 224 nggnilagykafkeLKELGLIDR--------LP--RLIAVQATGCNPILTAFETGRDeYEPERPETIAPSMDIGN--PSN 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 496276300 254 FRLCQQYLD----DVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVE 303
Cdd:COG0498 292 GERALFALResggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLRE 345
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
34-301 |
1.30e-17 |
|
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: 83.33 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLTE-----PQKAagVIAASAGNHAQGLALSSQQLGVKAT 108
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKrgllkPGTT--IIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 109 IVMPRTTPDIKVDAVRSFGGHVVL-HGSNFDEAKGY---AEQLAEQHGYTFIP-PFDHPS-VIAGQGTIGIELVQQ-NGH 181
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILtPEAEADGMKGAiakARELAAETPNAFWLnQFENPAnPEAHYETTAPEIWEQlDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 182 LDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSaclkAALDAGQPVTLDQVGMFADGVavkrigSETFRlcQQYL 261
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGS----VLFSGGPPGPHKIEGIGAGFI------PENLD--RSLI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496276300 262 DDVVTVSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKY 301
Cdd:cd01561 229 DEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKL 268
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
34-351 |
1.53e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 84.86 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNmSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQlTEPQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPR 113
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSY-GLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 114 TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHlDCVFVPVGGGG 193
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINP-THVIVPTGSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 194 LAAGVAVLLKQLLP-----EI-KVVGVEAEDSACLKAALdAGQPVTLDQ---VGMFADGVAVKRIGSETFRlcqQYLDDV 264
Cdd:PRK05638 224 YLYSIYKGFKELLEigvieEIpKLIAVQTERCNPIASEI-LGNKTKCNEtkaLGLYVKNPVMKEYVSEAIK---ESGGTA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 265 VTVSSDEICSAVKDIFEDTrAIAEPSGALSLAGLKKYVELHQL-KDQQLAAILSGANLNFHGlRYVSERCELGEKREGLL 343
Cdd:PRK05638 300 VVVNEEEIMAGEKLLAKEG-IFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTGSGLKGYG-EGGREKFTIGGTKLEIL 377
|
....*...
gi 496276300 344 AVtIPERP 351
Cdd:PRK05638 378 KI-LSERE 384
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
28-178 |
1.09e-16 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 81.85 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 28 YEVAQVTPLQNMSRLSARIA-NQIQLKRED-RQPVHSFK-LRGAYNM----------------MSQLTEPQKAA-----G 83
Cdd:PRK08206 39 FPGYAPTPLVALPDLAAELGvGSILVKDESyRFGLNAFKaLGGAYAVarllaeklgldiselsFEELTSGEVREklgdiT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 84 VIAASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAEQH-----------G 152
Cdd:PRK08206 119 FATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENgwvvvqdtaweG 198
|
170 180
....*....|....*....|....*.
gi 496276300 153 YTFIPPFdhpsVIAGQGTIGIELVQQ 178
Cdd:PRK08206 199 YEEIPTW----IMQGYGTMADEAVEQ 220
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
45-324 |
2.28e-15 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 77.56 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 45 RIANQIQLKREDRQPVHSFKLRGAYNMMSQLTEpQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVR 124
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKE-EGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 125 SFGGhvVLHGSNFDEAKGYAE--QLAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHLDCVFVPVGGGGLAAGVAVLL 202
Cdd:PRK08329 148 RLGA--ELHFVEGDRMEVHEEavKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 203 KQL--LPEI----KVVGVEAE--DSACLKAaldagqpvtlDQVGMFADGVAV---------KRIGSETFRLCqqylddvV 265
Cdd:PRK08329 226 KELheMGEIskmpKLVAVQAEgyESLCKRS----------KSENKLADGIAIpepprkeemLRALEESNGFC-------I 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496276300 266 TVSSDEICSAVKDIfedTRA--IAEPSGALSLAGLKKYVELHQLKDQQLAAI-LSGANLNFH 324
Cdd:PRK08329 289 SVGEEETRAALHWL---RRMgfLVEPTSAVALAAYWKLLEEGLIEGGSKVLLpLSGSGLKNL 347
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
26-180 |
9.49e-15 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 75.81 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 26 PVYEVAQV-------TPLQNMSRLSARI-ANQIQLKREDRQPVHSFKLRGAYNMMSQltepQKAAGV--IA-ASAGNHAQ 94
Cdd:PRK08197 65 PVRDPEHIvslgegmTPLLPLPRLGKALgIGRLWVKDEGLNPTGSFKARGLAVGVSR----AKELGVkhLAmPTNGNAGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 95 GLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVL-HGSNFDEAKGYAEQLAEqHGYTFIPPFDHPSVIAGQGTIGI 173
Cdd:PRK08197 141 AWAAYAARAGIRATIFMPADAPEITRLECALAGAELYLvDGLISDAGKIVAEAVAE-YGWFDVSTLKEPYRIEGKKTMGL 219
|
....*..
gi 496276300 174 ELVQQNG 180
Cdd:PRK08197 220 ELAEQLG 226
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
34-303 |
3.65e-14 |
|
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: 73.16 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLtepqKAAG-------VIAASAGNHAQGLALSSQQLGVK 106
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDA----EKRGllkpggtIVEATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 107 ATIVMPRTTPDIKVDAVRSFGGHVVL--HGSNFDEAKGYAEQLAEQHGYTFIP--------PFDHpsviagQGTIGIELV 176
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAFWPnqfenpanPEAH------YETTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 177 QQ-NGHLDCVFVPvgggglaagvavllKQLLPEIKVVGVEAEDSaclkAALDAGQPVTLDQVGMFADGVavkrigSETFR 255
Cdd:COG0031 164 EQtDGKVDAFVAGvgtggtitgvgrylKERNPDIKIVAVEPEGS----PLLSGGEPGPHKIEGIGAGFV------PKILD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496276300 256 LcqQYLDDVVTVSSDEicsAvkdiFEDTRAIAE-------PSGALSLAGLKKYVE 303
Cdd:COG0031 234 P--SLIDEVITVSDEE---A----FAMARRLAReegilvgISSGAAVAAALRLAK 279
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
33-322 |
1.36e-08 |
|
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: 56.62 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 33 VTPLQNMSRLSARI-ANQIQLKREDRQPVHSFKLRGAYNMMSQLTEpQKAAGVIAASAGNHAQGLALSSQQLGVKATIVM 111
Cdd:TIGR00260 22 VTPLFRAPALAANVgIKNLYVKELGHNPTLSFKDRGMAVALTKALE-LGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 112 PR-TTPDIKVDAVRSFGGHVVLHGSNFDEAKGYAEQLAE---QHGYTFIPPFdhPSVIAGQGTIGIELVQQNGHLD---- 183
Cdd:TIGR00260 101 PAgKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEdkpALGLNSANSI--PYRLEGQKTYAFEAVEQLGWEApdkv 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 184 CVFVPV-----GGGGLAAGVAVLLKQLLPeiKVVGVEAEDSA-CLKAALDAGQ------PVTLD---QVGMFADGVAVKR 248
Cdd:TIGR00260 179 VVPVPNsgnfgAIWKGFKEKKMLGLDSLP--VKRGIQAEGAAdIVRAFLEGGQwepietPETLStamDIGNPANWPRALE 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496276300 249 IgsetFRLCQQYLDDVvtvSSDEICSAVKDIFEDTRAIAEPSGALSLAGLKKYVELHQL-KDQQLAAILSGANLN 322
Cdd:TIGR00260 257 A----FRRSNGYAEDL---SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTAdPAERVVCALTGNGLK 324
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
58-321 |
4.69e-08 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 54.74 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 58 QPVHSFKLRGAYNMMSQLTEpQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVV-LHGSN 136
Cdd:PRK06450 75 NPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVrVRGSR 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 137 FDEAKGyaeqlAEQHGYTFIPPFDHPSVIAGQGTIGIELVQQNGHL--DCVFVPVGGGGLAAGVAVLLKQLLP--EI--- 209
Cdd:PRK06450 154 EDVAKA-----AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKipNYVFIPVSAGTLLLGVYSGFKHLLDsgVIsem 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 210 -KVVGVEAEDSACLKAALDAGQPVTLDQVGMFADGVAVKR--IGSETFRLCQQYlDDVVTVSSDEICSAVKDIfEDTRAI 286
Cdd:PRK06450 229 pKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRpfLLDYMVKALSEY-GECIVVSDNEIVEAWKEL-AKKGLL 306
|
250 260 270
....*....|....*....|....*....|....*
gi 496276300 287 AEPSGALSLAGLKKYvelhqlKDQQLAAILSGANL 321
Cdd:PRK06450 307 VEYSSATVYAAYKKY------SVNDSVLVLTGSGL 335
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
27-299 |
1.82e-07 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 53.00 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 27 VYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQ-----LTEPQKAAgVIAASAGNHAQGLALSSQ 101
Cdd:PLN02565 9 VTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDaeekgLIKPGESV-LIEPTSGNTGIGLAFMAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 102 QLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHgsnfDEAKGY------AEQLAEQHGYTFI-PPFDHPS--VIAGQgTIG 172
Cdd:PLN02565 88 AKGYKLIITMPASMSLERRIILLAFGAELVLT----DPAKGMkgavqkAEEILAKTPNSYIlQQFENPAnpKIHYE-TTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 173 IELVQ-QNGHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAgqPVTLDQVGM-FADGVavkrig 250
Cdd:PLN02565 163 PEIWKgTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPG--PHKIQGIGAgFIPGV------ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 496276300 251 setfrLCQQYLDDVVTVSSDEICSAVKDI-FEDTRAIAEPSGALSLAGLK 299
Cdd:PLN02565 235 -----LDVDLLDEVVQVSSDEAIETAKLLaLKEGLLVGISSGAAAAAAIK 279
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
48-188 |
2.46e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 52.40 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 48 NQIQLKREDRQPVHSFKLRGAYNMMSQLTEpQKAAGVIAASAGNHAQGLALSSQQLGVKATIVMPRTTPDIKVDAVRSFG 127
Cdd:PRK06381 31 RKIYLKFEGANPTGTQKDRIAEAHVRRAMR-LGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496276300 128 GHVVLHGSNFDEAKGYAEQLAEQHGYTFIPPFDHPSVIA--GQGTIGIELVQQNGHL-DCVFVP 188
Cdd:PRK06381 110 AEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVpDAVAVP 173
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
34-132 |
6.41e-07 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 51.40 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMsQLTEPQ---KAAGVIA-ASAGNHAQGLALSSQQLGVKATI 109
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII-WDAEKRgllKPGGTIVeGTAGNTGIGLALVAAARGYKTVI 92
|
90 100
....*....|....*....|...
gi 496276300 110 VMPRTTPDIKVDAVRSFGGHVVL 132
Cdd:PRK10717 93 VMPETQSQEKKDLLRALGAELVL 115
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
435-508 |
3.69e-06 |
|
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: 45.23 E-value: 3.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496276300 435 ERLYSFEFPEYPGALIRFLKTLGSHwNISLFNYRNHGADYGRVLCGFELED--KDLLSFTSHLRELGYHWQDETEN 508
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPR-NITEFNYRYADEKDAHIFVGVSVANgaEELAELLEDLKSAGYEVVDLSDD 75
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
20-299 |
4.30e-06 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 48.85 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 20 RNILRAPVYEVAQVTPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQ-----LTEPQKAAgVIAASAGNHAQ 94
Cdd:PLN00011 4 RCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDaedkgLITPGKST-LIEATAGNTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 95 GLALSSQQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHgsnfDEAKGY------AEQLAEQHGYTFIP-PFDHPSVIAG 167
Cdd:PLN00011 83 GLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLT----DQSIGLkgmlekAEEILSKTPGGYIPqQFENPANPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 168 Q-GTIGIELVQQN-GHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSaclkAALDAGQPVTLDQVGMFAdgva 245
Cdd:PLN00011 159 HyRTTGPEIWRDSaGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVES----AVLSGGQPGPHLIQGIGS---- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 496276300 246 vkriGSETFRLCQQYLDDVVTVSSDEICSAVKDI-FEDTRAIAEPSGALSLAGLK 299
Cdd:PLN00011 231 ----GIIPFNLDLTIVDEIIQVTGEEAIETAKLLaLKEGLLVGISSGAAAAAALK 281
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
34-153 |
7.47e-06 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 47.95 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQLT---EPQKAAGVIAASAGNHAQGLALSSQQLGVKATIV 110
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEkrgEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLI 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 496276300 111 MPRTTPDIKVDAVRSFGGHVVL--HGSNFDEAKGYAEQLAEQHGY 153
Cdd:PRK11761 93 MPENMSQERRAAMRAYGAELILvpKEQGMEGARDLALQMQAEGEG 137
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
29-299 |
7.52e-06 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 48.03 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 29 EVAQV---TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMS-----QLTEPQKAAgVIAASAGNHAQGLALSS 100
Cdd:PLN02556 52 DASQLigkTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEdaekkNLITPGKTT-LIEPTSGNMGISLAFMA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 101 QQLGVKATIVMPRTTPDIKVDAVRSFGGHVVLHgsnfDEAKGY------AEQLAEQHGYTF-IPPFDHPS-VIAGQGTIG 172
Cdd:PLN02556 131 AMKGYKMILTMPSYTSLERRVTMRAFGAELVLT----DPTKGMggtvkkAYELLESTPDAFmLQQFSNPAnTQVHFETTG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 173 IELVQQN-GHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKAALDAGQPVTLDQVGMFADgvavkrigs 251
Cdd:PLN02556 207 PEIWEDTlGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPD--------- 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 496276300 252 etfRLCQQYLDDVVTVSSDEICSAVKDI-FEDTRAIAEPSGALSLAGLK 299
Cdd:PLN02556 278 ---ILDMDVMEKVLEVSSEDAVNMARELaLKEGLMVGISSGANTVAALR 323
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
34-299 |
7.61e-06 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 48.23 E-value: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRQPVHSFKLRGAYNMMSQ-----LTEPQKAAgVIAASAGNHAQGLALSSQQLGVKAT 108
Cdd:PLN03013 124 TPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDaeqkgFISPGKSV-LVEPTSGNTGIGLAFIAASRGYRLI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 109 IVMPRTTPDIKVDAVRSFGGHVVLHgsnfDEAKGY--AEQLAEQ------HGYtFIPPFDHPSVIAGQ-GTIGIELVQQN 179
Cdd:PLN03013 203 LTMPASMSMERRVLLKAFGAELVLT----DPAKGMtgAVQKAEEilkntpDAY-MLQQFDNPANPKIHyETTGPEIWDDT 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 180 -GHLDCVFVPVGGGGLAAGVAVLLKQLLPEIKVVGVEAEDSACLKaaldAGQPVTLDQVGMFAdgvavkriGSETFRLCQ 258
Cdd:PLN03013 278 kGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILS----GGKPGPHKIQGIGA--------GFIPKNLDQ 345
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 496276300 259 QYLDDVVTVSSDEICSAVKDI-FEDTRAIAEPSGALSLAGLK 299
Cdd:PLN03013 346 KIMDEVIAISSEEAIETAKQLaLKEGLMVGISSGAAAAAAIK 387
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
34-188 |
8.19e-05 |
|
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: 44.79 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 34 TPLQNMSRLSARIANQIQLKREDRqpVHSF----KLRGA-YNmmsqLTEP--QKAAGVIaaSAG----NHAQGLALSSQQ 102
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDL--TGPAiggnKTRKLeYL----LADAlaQGADTLV--TFGgaqsNHARATAAAAAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496276300 103 LGVKATIVMPRTTPDIKVDAV---RSFGGHVVLHGSNF-----DEAKGYAEQLAEQ-HGYTFIPPFDHpSVIAGQGTIGI 173
Cdd:COG2515 84 LGLKCVLVLRGEEPTPLNGNLlldRLLGAELHFVSRGEyrdrdEAMEAVAAELRARgGKPYVIPEGGS-NPLGALGYVEA 162
|
170 180
....*....|....*....|.
gi 496276300 174 --ELVQQ----NGHLDCVFVP 188
Cdd:COG2515 163 aaELAAQlaelGVDFDYIVVA 183
|
|
| |
