|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
1-512 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 892.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 1 MLSRLVRQILQATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHA 80
Cdd:PRK09224 1 MGADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 81 QGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGN 160
Cdd:PRK09224 81 QGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 161 EILRQWRD-VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEK 239
Cdd:PRK09224 161 EILQQHPHpLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 240 PFDVIRLQKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCGANMNF 319
Cdd:PRK09224 241 TFRLCQEYVDD---------VITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 320 DRLRYIAERTELGERKEAIFAVTIPEEKGSFLNFCRALQGRNITEFNYRASHASAAQVFVGISLKSGEKERQDIYEALKV 399
Cdd:PRK09224 312 DRLRYVAERAELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 400 K-FDVDDLSDDEVAKLHIRYLIGGHADL-ENERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEA 477
Cdd:PRK09224 392 HgYPVVDLSDDELAKLHVRYMVGGRPPKpLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQV 471
|
490 500 510
....*....|....*....|....*....|....*
gi 1778564574 478 EDAqqNPDGLIETLESISYPYDEITNNLGYQRFLK 512
Cdd:PRK09224 472 PDA--DEPEFEAFLDELGYPYWDETDNPAYRLFLA 504
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
5-511 |
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: 702.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 5 LVRQILQATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVA 84
Cdd:TIGR01124 2 YLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 85 LSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILR 164
Cdd:TIGR01124 82 FSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 165 QW-RDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDV 243
Cdd:TIGR01124 162 QVaNPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 244 IRLQKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCGANMNFDRLR 323
Cdd:TIGR01124 242 CQQYLDD---------IVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 324 YIAERTELGERKEAIFAVTIPEEKGSFLNFCRALQGRNITEFNYRASHASAAQVFVGISLkSGEKERQDIYEAL-KVKFD 402
Cdd:TIGR01124 313 YVSERCELGEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQL-SNPQERQEILARLnDGGYS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 403 VDDLSDDEVAKLHIRYLIGGHAD-LENERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEAEDAQ 481
Cdd:TIGR01124 392 VVDLTDDELAKLHVRYMVGGRPPhVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHE 471
|
490 500 510
....*....|....*....|....*....|
gi 1778564574 482 qnPDGLIETLESISYPYDEITNNLGYQRFL 511
Cdd:TIGR01124 472 --PDQFEQFLAELGYRYHDETNNPAYRLFL 499
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
1-511 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 673.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 1 MLSRLVRQILQATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHA 80
Cdd:PRK12483 18 LLADYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 81 QGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGN 160
Cdd:PRK12483 98 QGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 161 EILRQWRD-VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEK 239
Cdd:PRK12483 178 EILRQHPGpLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 240 PFDVIRLQKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCGANMNF 319
Cdd:PRK12483 258 TFELCRHYVDE---------VVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 320 DRLRYIAERTELGERKEAIFAVTIPEEKGSFLNFCRALQGRNITEFNYRASHASAAQVFVGISLKSGEKERQDIYEALKV 399
Cdd:PRK12483 329 DRLRHVAERAELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASLRA 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 400 K-FDVDDLSDDEVAKLHIRYLIGGHADL-ENERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEA 477
Cdd:PRK12483 409 QgFPVLDLTDDELAKLHIRHMVGGRAPLaHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGLQV 488
|
490 500 510
....*....|....*....|....*....|....
gi 1778564574 478 EDAQQNpdGLIETLESISYPYDEITNNLGYQRFL 511
Cdd:PRK12483 489 PEDERA--ALDAALAALGYPYWEETGNPAYRLFL 520
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
8-512 |
0e+00 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 521.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 8 QILQATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSG 87
Cdd:PLN02550 97 NILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 88 QKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWR 167
Cdd:PLN02550 177 QRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQ 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 168 D-VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFdviRL 246
Cdd:PLN02550 257 GpLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETF---RL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 247 QKSDNSGpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCGANMNFDRLRYIA 326
Cdd:PLN02550 334 CRELVDG------VVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 327 ERTELGERKEAIFAVTIPEEKGSFLNFCRALQGRNITEFNYRASHASAAQVFVGISLKSgEKERQDIYEALK-VKFDVDD 405
Cdd:PLN02550 408 ELADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHT-EQELQALKKRMEsAQLRTVN 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 406 LSDDEVAKLHIRYLIGGHADLENERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEAedAQQNPD 485
Cdd:PLN02550 487 LTSNDLVKDHLRYLMGGRAIVKDELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQV--PPEEMQ 564
|
490 500
....*....|....*....|....*..
gi 1778564574 486 GLIETLESISYPYDEITNNLGYQRFLK 512
Cdd:PLN02550 565 EFKSRANALGYEYQDECDNEAFQLLMH 591
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
11-334 |
2.20e-150 |
|
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: 432.54 E-value: 2.20e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 11 QATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKL 90
Cdd:COG1171 15 AARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVD 170
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPDLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 171 YVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRLQKSD 250
Cdd:COG1171 175 AVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLVDD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 251 nsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANMNFDRLRYIAERTE 330
Cdd:COG1171 255 ---------IVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER--LKGKRVVVVLSGGNIDPDRLAEILERGL 323
|
....
gi 1778564574 331 LGER 334
Cdd:COG1171 324 VGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
9-318 |
4.88e-141 |
|
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: 408.03 E-value: 4.88e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 9 ILQATVY--DVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALS 86
Cdd:cd01562 4 ILAAAARikPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGVAYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 87 GQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQW 166
Cdd:cd01562 84 AKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 167 RDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRL 246
Cdd:cd01562 164 PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRK 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1778564574 247 QKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHgiENKNLVSIVCGANMN 318
Cdd:cd01562 244 LVDD---------VVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
6-504 |
6.17e-126 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 374.14 E-value: 6.17e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 6 VRQILQA--TVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGV 83
Cdd:PRK08639 9 AKDIDKAakRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 84 ALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGG---EVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGN 160
Cdd:PRK08639 89 AYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 161 EILRQWR---DVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIG 237
Cdd:PRK08639 169 EILEQLEkegSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 238 EKPFDVIRlqksdnsgpIVEPNVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANM 317
Cdd:PRK08639 249 DLTFEILK---------DVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDE--IKGKTVVCVISGGNN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 318 NFDRlryiaerteLGERKEaifavtipeekgsflnfcRALqgrnitefnyrashasaaqvfvgislksgekerqdIYEAL 397
Cdd:PRK08639 318 DIER---------MPEIKE------------------RSL-----------------------------------IYEGL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 398 KvkfdvddlsddevaklhiRYLIgghadlenerlfrVEFPERPGALLTFLER-LGPTHNITLFHY-----RNHGAaegrV 471
Cdd:PRK08639 336 K------------------HYFI-------------VNFPQRPGALREFLDDvLGPNDDITRFEYlkknnRETGP----V 380
|
490 500 510
....*....|....*....|....*....|...
gi 1778564574 472 LVGLEAEDAqQNPDGLIETLESISYPYDEITNN 504
Cdd:PRK08639 381 LVGIELKDA-EDYDGLIERMEAFGPSYIDINPN 412
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
7-327 |
4.81e-88 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 273.54 E-value: 4.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 7 RQILQATVYdvaiETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALS 86
Cdd:PRK08638 18 KQRLAGRIR----KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 87 GQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQW 166
Cdd:PRK08638 94 CALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 167 RDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRl 246
Cdd:PRK08638 174 WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVR- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 247 qksdnsgPIVEpNVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCGANMNFDRLRYIA 326
Cdd:PRK08638 253 -------ELVD-DIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRVSQIT 324
|
.
gi 1778564574 327 E 327
Cdd:PRK08638 325 G 325
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
20-323 |
2.24e-79 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 250.77 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGG 179
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 180 GLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVA-QIGEKPFDVIRlQKSDNSgpivep 258
Cdd:PRK06815 180 GLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGvEPGAITFPLCQ-QLIDQK------ 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778564574 259 nvVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHgiENKNLVSIVCGANMNFDRLR 323
Cdd:PRK06815 253 --VLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY--QGKKVAVVLCGKNIVLEKYL 313
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
21-399 |
9.54e-79 |
|
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: 251.20 E-value: 9.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMPK 100
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 101 TTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGGG 180
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 181 LIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRLQKSDnsgpivepnV 260
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDD---------V 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 261 VLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANMNFDRLRYIAERTELGERKEAIFA 340
Cdd:TIGR01127 232 VTVDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVD--VKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIE 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778564574 341 VTIPEEKGSFLNFCRAL--QGRNITEFNYRASHASAAQVFVGISLKSGEKERQDIYEALKV 399
Cdd:TIGR01127 310 TVLPDRPGALYHLLESIaeARANIVKIDHDRLSKEIPPGFAMVEITLETRGKEHLDEILKI 370
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
21-314 |
2.57e-77 |
|
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: 244.53 E-value: 2.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMPK 100
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 101 TTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAED-GMTFIPPYDDELVMAGQGTIGNEILRQW-RDVDYVFVAVGG 178
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 179 GGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQI-GEKPFDVIRlqksDNSGPive 257
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLD----EYVGE--- 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1778564574 258 pnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIVCG 314
Cdd:pfam00291 241 --VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
21-314 |
2.74e-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: 240.11 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERG--VITASAGNHAQGVALSGQKLGIRAIIVM 98
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 99 PKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAED-GMTFIPPYDDELVMAGQGTIGNEILRQ--WRDVDYVFVA 175
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQlgGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 176 VGGGGLIAGVAAYLGDVAPHVKVIpveydesaclkaaletnervilptvglfadgtavaqigekpfdvirlqksdnsgpI 255
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVI-------------------------------------------------------G 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1778564574 256 VEPNVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGiENKNLVSIVCG 314
Cdd:cd00640 186 VEPEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTG 243
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
19-376 |
4.79e-68 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 224.00 E-value: 4.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 19 IETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVM 98
Cdd:PRK07334 22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 99 PKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGG 178
Cdd:PRK07334 102 PRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 179 GGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETnerVILPTVG-LFADGTAVAQIGEKPFDVIRLQKSDnsgpive 257
Cdd:PRK07334 182 GGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKG---VALPCGGsTIAEGIAVKQPGQLTLEIVRRLVDD------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 258 pnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANMNFDRLRYIAERTELGERKEA 337
Cdd:PRK07334 252 --ILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPER--FRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLA 327
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1778564574 338 IFAVTIPEEKGSFLNFCR--ALQGRNITEFNY-RASHASAAQ 376
Cdd:PRK07334 328 RLRVDIRDRPGALARVTAliGEAGANIIEVSHqRLFTDLPAK 369
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
39-322 |
9.93e-64 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 209.81 E-value: 9.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 39 FKREDLQPVFSFKLRGAYNRIsqLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVV 118
Cdd:PRK08246 41 LKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 119 LHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGGGLIAGVAAYlgdVAPHVKV 198
Cdd:PRK08246 119 VVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAW---FEGRARV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 199 IPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRLQKSDnsgpivepnVVLVNTDEICAAIKDTYDE 278
Cdd:PRK08246 196 VAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVT---------SVLVSDEAIIAARRALWEE 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1778564574 279 CRSIVEPSGAMALAGI--KKYVAEHGienKNLVSIVCGANMNFDRL 322
Cdd:PRK08246 267 LRLAVEPGAATALAALlsGAYVPAPG---ERVAVVLCGANTDPATL 309
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
20-329 |
2.69e-63 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 209.05 E-value: 2.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:PRK07476 19 RTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGG 179
Cdd:PRK07476 99 RLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALPDVATVLVPLSGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 180 GLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFAD--GTAVAQIGEKPFDVIRLQKSDnsgpive 257
Cdd:PRK07476 179 GLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslGGGIGLDNRYTFAMCRALLDD------- 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778564574 258 pnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGI--KKYVAEHGienkNLVSIVCGANMNFD-RLRYIAERT 329
Cdd:PRK07476 252 --VVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALlaGKIAARDG----PIVVVVSGANIDMElHRRIINGEV 320
|
|
| PLN02970 |
PLN02970 |
serine racemase |
11-322 |
1.68e-62 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 207.22 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 11 QATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKL 90
Cdd:PLN02970 18 RKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDvANKYAIAR-AAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDV 169
Cdd:PLN02970 98 GIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVE-SREAVAARvQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 170 DYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVE---YDESACLKAAletNERVILPTVGLFADGtAVAQIGEKPFDVIRL 246
Cdd:PLN02970 177 DVIIVPISGGGLISGIALAAKAIKPSIKIIAAEpkgADDAAQSKAA---GEIITLPVTNTIADG-LRASLGDLTWPVVRD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 247 QKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGI------KKYVAEHGienKNLVSIVCGANMNFD 320
Cdd:PLN02970 253 LVDD---------VITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsdsfrSNPAWKGC---KNVGIVLSGGNVDLG 320
|
..
gi 1778564574 321 RL 322
Cdd:PLN02970 321 VL 322
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
11-322 |
1.71e-60 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 201.79 E-value: 1.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 11 QATVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKL 90
Cdd:PRK07048 15 AARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDvaNKYAIAR--AAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRD 168
Cdd:PRK07048 95 GIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTE--DREEIGRrlAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 169 VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRLQK 248
Cdd:PRK07048 173 LDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPIIRRLV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778564574 249 SDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANMNFDRL 322
Cdd:PRK07048 253 DD---------IVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP--LKGKRVGVIISGGNVDLARF 315
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
20-325 |
3.49e-48 |
|
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: 169.26 E-value: 3.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGG 179
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQMPDLATVLVPLSGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 180 GLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFAD--GTAVAQIGEKPFDVIRLQKSDnsgpive 257
Cdd:TIGR02991 179 GLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTFAMCKALLDE------- 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778564574 258 pnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIkkyVAEHGIENKNLVSIVCGANMNFDRLRYI 325
Cdd:TIGR02991 252 --IVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL---LAGKIKNPGPCAVIVSGRNIDMDLHKRI 314
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
7-323 |
2.02e-42 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 153.61 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 7 RQILQA--TVYDVAIETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQ-LERGVITASAGNHAQGV 83
Cdd:PRK06110 6 AELEAAaaVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 84 ALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVmAGQGTIGNEIL 163
Cdd:PRK06110 86 AFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFHPDLV-RGVATYALELF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 164 RQWRDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDV 243
Cdd:PRK06110 165 RAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 244 IRLQKSDnsgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEhgIENKNLVSIVCGANMNFDRLR 323
Cdd:PRK06110 245 IRAGADR---------IVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERER--LAGKRVGLVLSGGNIDRAVFA 313
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
11-318 |
2.05e-39 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 146.31 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 11 QATVYDVAIETPLEAAPRISeklknnIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKL 90
Cdd:PRK08813 30 QARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVd 170
Cdd:PRK08813 104 GVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPDV- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 171 yVFVAVGGGGLIAGVAAYLGdvAPHVKVIPVEYDESACLKAALETNERVILPtVGLFADGTAVAQIGekpFDVIRLQKSd 250
Cdd:PRK08813 183 -VIVPIGGGGLASGVALALK--SQGVRVVGAQVEGVDSMARAIRGDLREIAP-VATLADGVKVKIPG---FLTRRLCSS- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778564574 251 nsgpiVEPNVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKyvaehgIENKNLVSIVCGANMN 318
Cdd:PRK08813 255 -----LLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAGRR------VSGKRKCAVVSGGNID 311
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
20-318 |
5.51e-39 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 144.91 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQL-PKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVM 98
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELkEQGKLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 99 PKTTPDIKVQAVKRLGGEVVLHgDSFDVANKyAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQW-RDVDYVFVAVG 177
Cdd:PRK06608 103 PLNTSKVKQQAALYYGGEVILT-NTRQEAEE-KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLgFSPDAIFASCG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 178 GGGLIAGvaAYLGD--VAPHVKVI---PVEYDESAclkAALETNERVILPTV-GLFADGTAVAQIGEKPFDVirLQKSDn 251
Cdd:PRK06608 181 GGGLISG--TYLAKelISPTSLLIgsePLNANDAY---LSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEY--LKKLD- 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778564574 252 sgpivepNVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKNLVsIVCGANMN 318
Cdd:PRK06608 253 -------DFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKPQKLLV-ILSGGNID 311
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
336-419 |
6.44e-38 |
|
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: 133.83 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 336 EAIFAVTIPEEKGSFLNFCRALQGRNITEFNYRASHASAAQVFVGISLKSGEKERQDIYEALKVK-FDVDDLSDDEVAKL 414
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAgYEVVDLSDDELAKT 80
|
....*
gi 1778564574 415 HIRYL 419
Cdd:cd04906 81 HLRYM 85
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
20-323 |
8.27e-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: 138.20 E-value: 8.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPK--SQLERGVITASAGNHAQGVALSGQKLGIRAIIV 97
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKqgLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 98 MPKTTPDIKVQAVKRLGGEVVLHGD-SFDVANKYAIARAAED-GMTFIPPYDDELVMAGQGTIGNEILRQWRD---VDYV 172
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKvWWEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 173 FVAVGGGGLIAGVAAYLGDV-APHVKVIPVEYDESACLKAALETNERVILPTVGLFADGTAVAQIGEKPFDVIRlqksdn 251
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNgWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQ------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 252 sgpivEPNVV-LVNTD-EICAAIKDTYDECRSIVEPSGAMALAG-----IKKYVAE-HGIENKNLVSIVC-GANMNFDRL 322
Cdd:cd06448 235 -----EHNIKsEVVSDrDAVQACLRFADDERILVEPACGAALAVvysgkILDLQLEvLLTPLDNVVVVVCgGSNITLEQL 309
|
.
gi 1778564574 323 R 323
Cdd:cd06448 310 K 310
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
429-511 |
1.80e-34 |
|
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: 124.20 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 429 ERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEAEDAqqNPDGLIETLESISYPYDEITNNLGYQ 508
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDA--DLDELKERLDALGYPYQEETDNPAYK 78
|
...
gi 1778564574 509 RFL 511
Cdd:cd04907 79 LFL 81
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
21-314 |
8.13e-28 |
|
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: 113.46 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLK-NNIRFKREDLQPVFSFKLRGAYNRISQLpKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:cd01563 23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKA-KELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIP---PYDDElvmaGQGTIGNEILRQ--WRDVDYVFV 174
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNslnPYRLE----GQKTIAFEIAEQlgWEVPDYVVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 175 AVGGGGLIAGV--------AAYLGDVAPHVKVIPVEYDESACL--KAALETNERVILPTVglFADGtavAQIGEKP--FD 242
Cdd:cd01563 178 PVGNGGNITAIwkgfkelkELGLIDRLPRMVGVQAEGAAPIVRafKEGKDDIEPVENPET--IATA---IRIGNPAsgPK 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778564574 243 VIRLQKSdnSGPIVEPnvvlVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGI-ENKNLVSIVCG 314
Cdd:cd01563 253 ALRAVRE--SGGTAVA----VSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVVVVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
21-313 |
2.77e-25 |
|
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: 107.59 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLpksqLERG---VITASAGNHAQGVALSGQKLGIRAIIV 97
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLA----LERGaktIVCASSGNGSAALAAYAARAGIEVFVF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 98 MPKT-TPDIKVQAVKRLGGEVVL-HGDsFDVANKYAIARAAEDGMTF---IPPYddelVMAGQGTIGNEILRQWRDV-DY 171
Cdd:COG0498 143 VPEGkVSPGQLAQMLTYGAHVIAvDGN-FDDAQRLVKELAADEGLYAvnsINPA----RLEGQKTYAFEIAEQLGRVpDW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 172 VFVAVGGGGLIAGV--------AAYLGDVAPhvKVIPVEYDESACLKAALETNERVILPTVGLF-ADGTAVAqigeKPFD 242
Cdd:COG0498 218 VVVPTGNGGNILAGykafkelkELGLIDRLP--RLIAVQATGCNPILTAFETGRDEYEPERPETiAPSMDIG----NPSN 291
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778564574 243 VIR----LQKSDNSgpivepnVVLVNTDEICAAIKDTYDECRSIVEPSGAMALAGIKKYVAEHGIENKnlVSIVC 313
Cdd:COG0498 292 GERalfaLRESGGT-------AVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPD--EPVVV 357
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
432-500 |
2.92e-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: 98.35 E-value: 2.92e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778564574 432 FRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEAEDAQQNPDgLIETLESISYPYDE 500
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDREDLAE-LKERLEALGYPYVD 68
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
21-207 |
6.56e-25 |
|
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: 104.52 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLpksqLERGVIT-------ASAGNHAQGVALSGQKLGIR 93
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDA----EKRGLLKpgttiiePTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 94 AIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARA----AEDGMTFIP-PYDDEL-VMAGQGTIGNEILRQWR 167
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKArelaAETPNAFWLnQFENPAnPEAHYETTAPEIWEQLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1778564574 168 D-VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESA 207
Cdd:cd01561 159 GkVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSV 199
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
428-511 |
1.96e-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: 94.27 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 428 NERLFRVEFPERPGALLTFLERLGPTHNITLFHYRNHGAAEGRVLVGLEAEDAQQNPDgLIETLESISYPYDEITNNLGY 507
Cdd:pfam00585 9 LEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQAEDLDE-FIERLNKLGYDYEDLSDNEAA 87
|
....
gi 1778564574 508 QRFL 511
Cdd:pfam00585 88 YEHL 91
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
20-209 |
3.17e-22 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 98.41 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLK-NNIRFKREDLQ-PVFSFK-LRGAY-----------NRISQLPKSQLERG----------VITAS 75
Cdd:PRK08206 44 PTPLVALPDLAAELGvGSILVKDESYRfGLNAFKaLGGAYavarllaeklgLDISELSFEELTSGevreklgditFATAT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 76 AGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFI-----PPYDD-- 148
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVqdtawEGYEEip 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778564574 149 ELVMAGQGTIGNEILRQWRDVD----YVFVAVGGGGLIAGVAAYL----GDVAPHVKVipVEYDESACL 209
Cdd:PRK08206 204 TWIMQGYGTMADEAVEQLKEMGvpptHVFLQAGVGSLAGAVLGYFaevyGEQRPHFVV--VEPDQADCL 270
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
21-313 |
1.04e-21 |
|
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: 95.50 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLpksqLERGVIT-------ASAGNHAQGVALSGQKLGIR 93
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDA----EKRGLLKpggtiveATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 94 AIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVanKYAIARA---AEDgmtfIPPYddelVMAGQ-----------GTIG 159
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLTPGAEGM--KGAIDKAeelAAE----TPGA----FWPNQfenpanpeahyETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 160 NEILRQWR-DVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESAclkaaletnervilptvglFADGTAVAQ--- 235
Cdd:COG0031 160 PEIWEQTDgKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSP-------------------LLSGGEPGPhki 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 236 --IGEkpfdvirlqksdnsgPIVEPNVVLVNTDEIcaaIK----DTYDECRSIVE-------PSGAMALAGIKKYVAEHG 302
Cdd:COG0031 221 egIGA---------------GFVPKILDPSLIDEV---ITvsdeEAFAMARRLAReegilvgISSGAAVAAALRLAKRLG 282
|
330
....*....|.
gi 1778564574 303 iENKNLVSIVC 313
Cdd:COG0031 283 -PGKTIVTILP 292
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
339-398 |
1.56e-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: 82.55 E-value: 1.56e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1778564574 339 FAVTIPEEKGSFLNFCRALQG-RNITEFNYRASHASAAQVFVGISLKSGEkERQDIYEALK 398
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPpRNITEFHYRNQGGDEARVLVGIQVPDRE-DLAELKERLE 60
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
32-311 |
1.63e-19 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 89.89 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 32 KLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASaGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVK 111
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSS-GNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 112 RLGGEV-VLHGDSFDVaNKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEILRQWRDVDYVFVAVGGGGLIAGV----- 185
Cdd:PRK08329 148 RLGAELhFVEGDRMEV-HEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIwkgfk 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 186 -AAYLGDVAPHVKVIPVEYD--ESACLKAALETNervilptvglFADGTAvaqIGEKPfdvirlQKSDNSGPIVEPN--V 260
Cdd:PRK08329 227 eLHEMGEISKMPKLVAVQAEgyESLCKRSKSENK----------LADGIA---IPEPP------RKEEMLRALEESNgfC 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1778564574 261 VLVNTDEICAAIKDTYDEcRSIVEPSGAMALAGIKKYVAEHGIENKNLVSI 311
Cdd:PRK08329 288 ISVGEEETRAALHWLRRM-GFLVEPTSAVALAAYWKLLEEGLIEGGSKVLL 337
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
327-416 |
3.62e-19 |
|
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: 82.33 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 327 ERTELGERKEAIFAVTIPEEKGSFLNFCRALQGR-NITEFNYRASHASAAQVFVGISLKSGEkERQDIYEAL-KVKFDVD 404
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRnNITLFEYRKHGDKNGCVLVGIELSQAE-DLDEFIERLnKLGYDYE 79
|
90
....*....|..
gi 1778564574 405 DLSDDEVAKLHI 416
Cdd:pfam00585 80 DLSDNEAAYEHL 91
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
21-312 |
2.91e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 84.09 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAApRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQ-LPksQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:PRK05638 67 TPLIRA-RISEKLGENVYIKDETRNPTGSFRDRLATVAVSYgLP--YAANGFIVASDGNAAASVAAYSARAGKEAFVVVP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMTFIPPYDDELVMAGQGTIGNEIlrqWRDVD--YVFVAVG 177
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFEL---WEEINptHVIVPTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 178 GGGLIAGVaaYLG-------DVAPHV-KVIPVEYDESACLKAALETNERVILPTVGLfadGTAVAQIGEKPFDVIRLQKS 249
Cdd:PRK05638 221 SGSYLYSI--YKGfkelleiGVIEEIpKLIAVQTERCNPIASEILGNKTKCNETKAL---GLYVKNPVMKEYVSEAIKES 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778564574 250 DNSgpivepnVVLVNTDEICAAIKDTYDEcRSIVEPSGAMALAGIKKYVAEHGIENKNLVSIV 312
Cdd:PRK05638 296 GGT-------AVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIEKGDKVVLV 350
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
72-209 |
3.48e-15 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 77.24 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 72 ITASAGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVL----HGDSFDVANKYA-------IARAAEDGM 140
Cdd:TIGR01747 98 ATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTItdmnYDDTVRLAMQMAqqhgwvvVQDTAWEGY 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778564574 141 TFIPPYddelVMAGQGTIGNEILRQWRDVD-----YVFVAVGGGGLIAGVAAYLGDVAPH--VKVIPVEYDESACL 209
Cdd:TIGR01747 178 EKIPTW----IMQGYATLADEAVEQLREMGsvtptHVLLQAGVGSMAGGVLGYFVDVYSEnnPHSIVVEPDKADCL 249
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
72-209 |
4.37e-15 |
|
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.
Pssm-ID: 274631 Cd Length: 396 Bit Score: 77.07 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 72 ITASAGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAE-----------DGM 140
Cdd:TIGR03528 117 VTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGAECTITDLNYDDAVRLAWKMAQEngwvmvqdtawEGY 196
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778564574 141 TFIPPYddelVMAGQGTIGNEILRQWRD-----VDYVFVAVGGGGLIAGVAAYLGDV----APHVKVipVEYDESACL 209
Cdd:TIGR03528 197 EKIPTW----IMQGYGTLALEALEQLKEqgvekPTHVFLQAGVGSFAGAVQGYFASVygeeRPITVI--VEPDKADCI 268
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
21-207 |
7.17e-14 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 72.59 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRIsqlpKSQLERGVITA-------SAGNHAQGVALSGQKLGIR 93
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII----WDAEKRGLLKPggtivegTAGNTGIGLALVAAARGYK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 94 AIIVMPKTTPDIKVQAVKRLGGEVVL-HGDSFDVANKY---AIARAAEDGMTFIPPYddelVMAGQ-----------GTI 158
Cdd:PRK10717 90 TVIVMPETQSQEKKDLLRALGAELVLvPAAPYANPNNYvkgAGRLAEELVASEPNGA----IWANQfdnpanreahyETT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1778564574 159 GNEIlrqWRD----VDyVFV-AVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESA 207
Cdd:PRK10717 166 GPEI---WEQtdgkVD-GFVcAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSA 215
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
21-182 |
1.61e-12 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 69.26 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLK-NNIRFKREDLQPVFSFKLRGAYNRISQlPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSR-AKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGM----TFIPPYDDElvmaGQGTIGNEILRQ--WRDVDYVF 173
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWfdvsTLKEPYRIE----GKKTMGLELAEQlgWRLPDVIL 234
|
170
....*....|
gi 1778564574 174 VAVGGG-GLI 182
Cdd:PRK08197 235 YPTGGGvGLI 244
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
21-219 |
5.20e-12 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 66.74 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDL-QPVFS----FKLRgaYNrisqLPKSqLERG---VITASAG--NHAQGVALSGQKL 90
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLtGPAIGgnktRKLE--YL----LADA-LAQGadtLVTFGGAqsNHARATAAAAAKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIK---VQAVKRLGGEVVLHGDSF----DVANKYAIARAAEDGMT--FIPP-YDDELVMAGQGTIGN 160
Cdd:COG2515 85 GLKCVLVLRGEEPTPLngnLLLDRLLGAELHFVSRGEyrdrDEAMEAVAAELRARGGKpyVIPEgGSNPLGALGYVEAAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778564574 161 EILRQ----WRDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVeydesACLKAALETNERV 219
Cdd:COG2515 165 ELAAQlaelGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGI-----SVLKGADFLRERV 222
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
34-185 |
1.39e-11 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 65.91 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 34 KNNIRFKREDLQPVFSFKLRGAYNRISQLpkSQLERGVITA-SAGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKR 112
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYL--AEKGIKQISEdSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIES 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 113 LGGEVV-LHGDSFDVankyaiARAAED------GMTFIPPYDDelvmaGQGTIGNEILRQ--WRDVDYVFVAVGGGGLIA 183
Cdd:PRK06450 142 YGAEVVrVRGSREDV------AKAAENsgyyyaSHVLQPQFRD-----GIRTLAYEIAKDldWKIPNYVFIPVSAGTLLL 210
|
..
gi 1778564574 184 GV 185
Cdd:PRK06450 211 GV 212
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
429-504 |
4.22e-11 |
|
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: 59.10 E-value: 4.22e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778564574 429 ERLFRVEFPERPGALLTFLERLGPtHNITLFHYRNHGAAEGRVLVGLEAEDAQQNPDGLIETLESISYPYDEITNN 504
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGP-RNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDD 75
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
21-209 |
5.57e-10 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 60.79 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRIsqlpKSQLERGVIT--------ASAGNHAQGVALSGQKLGI 92
Cdd:PLN00011 18 TPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMI----KDAEDKGLITpgkstlieATAGNTGIGLACIGAARGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 93 RAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKY----AIARAAEDGM---TFIPPYDDELVMAgqgTIGNEIlrq 165
Cdd:PLN00011 94 KVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLekaeEILSKTPGGYipqQFENPANPEIHYR---TTGPEI--- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1778564574 166 WRD----VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACL 209
Cdd:PLN00011 168 WRDsagkVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVL 215
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
20-209 |
2.39e-09 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 59.20 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPKSQL----ERGVITASAGNHAQGVALSGQKLGIRAI 95
Cdd:PLN02556 59 KTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLitpgKTTLIEPTSGNMGISLAFMAAMKGYKMI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 96 IVMPKTTPDIKVQAVKRLGGEVVL----HGDSFDVANKYAIARAAEDGM---TFIPPYDDELVMAgqgTIGNEIlrqWRD 168
Cdd:PLN02556 139 LTMPSYTSLERRVTMRAFGAELVLtdptKGMGGTVKKAYELLESTPDAFmlqQFSNPANTQVHFE---TTGPEI---WED 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1778564574 169 ----VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACL 209
Cdd:PLN02556 213 tlgqVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVL 257
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
21-202 |
2.41e-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: 59.09 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKN-NIRFKREDLQPVFSFKLRgayNRISQ--LPKSQLERGVITAS-AGNHAQGVALSGQKLGIRAII 96
Cdd:cd06446 35 TPLYRAKRLSEYLGGaKIYLKREDLNHTGAHKIN---NALGQalLAKRMGKKRVIAETgAGQHGVATATACALFGLECEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 97 VMPKTtpDIKVQAVKR-----LGGEVV--------LhGDSFDVANKYAIARAAED----GMTFIPPYDDELVMAGQGTIG 159
Cdd:cd06446 112 YMGAV--DVERQPLNVfrmelLGAEVVpvpsgsgtL-KDAISEAIRDWVTNVEDThyllGSVVGPHPYPNMVRDFQSVIG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1778564574 160 NEILRQ-----WRDVDYVFVAVGGGGLIAGVA-AYLGDvaPHVKVIPVE 202
Cdd:cd06446 189 EEAKKQilekeGELPDVVIACVGGGSNAAGLFyPFIND--KDVKLIGVE 235
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
21-185 |
7.04e-09 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 57.41 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLK-NNIRFKREDLQPVFSFKLRGAYNRISQlPKSQLERGVITASAGNHAQGVALSGQKLGIRAIIVMP 99
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRR-AMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 100 KTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMtfippYD-------DELVMAGQGTIGNEILRQWRDV-DY 171
Cdd:PRK06381 95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI-----YDanpgsvnSVVDIEAYSAIAYEIYEALGDVpDA 169
|
170
....*....|....
gi 1778564574 172 VFVAVGGGGLIAGV 185
Cdd:PRK06381 170 VAVPVGNGTTLAGI 183
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
21-201 |
7.23e-09 |
|
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: 57.05 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKL--KNNIRFKREDLQPVFSF---KLRgaynRISQLPKSQLERG---VITASA--GNHAQGVALSGQKL 90
Cdd:cd06449 1 TPIQYLPRLSEHLggKVEIYAKRDDCNSGLAFggnKIR----KLEYLLPDALAKGadtLVTVGGiqSNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIKVQAV--------KRLGGEVVLHGDSFDVANKYAIARAAED-----GMTF-IPPYDDELVMAGQG 156
Cdd:cd06449 77 GLKCVLVQENWVPYSDAVYDrvgnillsRIMGADVRLVSAGFDIGIRKSFEEAAEEveakgGKPYvIPAGGSEHPLGGLG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1778564574 157 TIG--NEILRQ----WRDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPV 201
Cdd:cd06449 157 YVGfvLEIAQQeeelGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGI 207
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
336-414 |
1.01e-08 |
|
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: 52.17 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 336 EAIFAVTIPEEKGSFLNFCRALQGR-NITEFNYRASHASAAQVFVGISLKsgEKERQDIYEAL-KVKFDVDDLSDDEVAK 413
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKwNITLFHYRNQGSDYGRVLVGIQVP--DADLDELKERLdALGYPYQEETDNPAYK 78
|
.
gi 1778564574 414 L 414
Cdd:cd04907 79 L 79
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
21-202 |
3.67e-08 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 55.97 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRgayNRISQ-LPKSQLERGVITAS--AGNHAQGVALSGQKLGIRAIIV 97
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKIN---NALGQaLLAKRMGKTRIIAEtgAGQHGVATATACALFGLKCTIF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 98 MPKTtpDIKVQA-----VKRLGGEV--VLHG-----DSFDVANKYAIARAAED----GMTFIP-PYdDELVMAGQGTIGN 160
Cdd:PRK13803 349 MGEE--DIKRQAlnverMKLLGANVipVLSGsktlkDAVNEAIRDWVASVPDThyliGSAVGPhPY-PEMVAYFQSVIGE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1778564574 161 EILRQ-----WRDVDYVFVAVGGGGLIAGV-AAYLGDvaPHVKVIPVE 202
Cdd:PRK13803 426 EAKEQlkeqtGKLPDAIIACVGGGSNAIGIfYHFLDD--PSVKLIGVE 471
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
21-223 |
2.22e-07 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 52.91 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPvfsfkLRGAYNRISQLP---KSQLERG---VITASA--GNHAQGVALSGQKLGI 92
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTG-----LALGGNKTRKLEfllADALAQGadtLITAGAiqSNHARQTAAAAAKLGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 93 RAIIVMPKTTPDIKVQAVKR--------LGGEVVLHGDSFDvANKYAIARAAE---DGMT--FIPpyddelvMAGQGTIG 159
Cdd:PRK03910 91 KCVLLLENPVPTEAENYLANgnvllddlFGAEIHVVPAGTD-MDAQLEELAEElraQGRRpyVIP-------VGGSNALG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 160 --------NEILRQWR----DVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVI------PVEYDESACLKAALETNERVIL 221
Cdd:PRK03910 163 algyvacaLEIAQQLAeggvDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIgvtvsrSAAEQEPKVAKLAQATAELLGL 242
|
..
gi 1778564574 222 PT 223
Cdd:PRK03910 243 PT 244
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
21-207 |
2.27e-07 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 52.57 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQlpksQLERG-------VITASAGNHAQGVALSGQKLGIR 93
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ----AEKRGeikpgdtLIEATSGNTGIALAMIAAIKGYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 94 AIIVMPKTTPDIKVQAVKRLGGEVVLhgdsfdvankyaiaRAAEDGMTFIPPYDDELVMAGQG----------------- 156
Cdd:PRK11761 89 MKLIMPENMSQERRAAMRAYGAELIL--------------VPKEQGMEGARDLALQMQAEGEGkvldqfanpdnplahye 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1778564574 157 TIGNEIlrqWRDVDYV---FV-AVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESA 207
Cdd:PRK11761 155 TTGPEI---WRQTEGRithFVsSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGS 206
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
20-212 |
3.24e-07 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 52.47 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQPVFSFKLRGAYNRISQLPK----SQLERGVITASAGNHAQGVALSGQKLGIRAI 95
Cdd:PLN03013 123 KTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQkgfiSPGKSVLVEPTSGNTGIGLAFIAASRGYRLI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 96 IVMPKTTPDIKVQAVKRLGGEVVL----HGDSFDVANKYAIARAAEDG---MTFIPPYDDELVMAgqgTIGNEIlrqWRD 168
Cdd:PLN03013 203 LTMPASMSMERRVLLKAFGAELVLtdpaKGMTGAVQKAEEILKNTPDAymlQQFDNPANPKIHYE---TTGPEI---WDD 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1778564574 169 ----VDYVFVAVGGGGLIAGVAAYLGDVAPHVKVIPVEYDESACLKAA 212
Cdd:PLN03013 277 tkgkVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGG 324
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
21-191 |
2.37e-06 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 50.41 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKLKNN------IRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKLGIRA 94
Cdd:PRK13802 327 SPLTEAPRFAERVKEKtgldarVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKC 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 95 IIVMPKTtpDIKVQAV-----KRLGGEV--VLHGDSFdvaNKYAIARAAEDGMTFI------------PPYDDELVMAGQ 155
Cdd:PRK13802 407 RIYMGQI--DARRQALnvarmRMLGAEVveVTLGDRI---LKDAINEALRDWVTNVkdthyllgtvagPHPFPAMVRDFQ 481
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1778564574 156 GTIGNEI---LRQWRDVDY---VFVAVGGGGLIAGVA-AYLGD 191
Cdd:PRK13802 482 KIIGEEAkqqLQDWYGIDHpdaICACVGGGSNAIGVMnAFLDD 524
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
21-184 |
3.36e-06 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 49.43 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 21 TPLEAAPRISEKL--KNNIRFKREDLQPVFSFKLRG------AYNRISQLPKSQLerGVITASAGNhaQGVALSG--QKL 90
Cdd:PLN02569 134 SNLFWAERLGKEFlgMNDLWVKHCGISHTGSFKDLGmtvlvsQVNRLRKMAKPVV--GVGCASTGD--TSAALSAycAAA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMPKTTPDIK--VQAVkrLGGEVVLHGDS-FDVANKYAIARAAEdgmtfIPPYD----DELVMAGQGTIGNEIL 163
Cdd:PLN02569 210 GIPSIVFLPADKISIAqlVQPI--ANGALVLSIDTdFDGCMRLIREVTAE-----LPIYLanslNSLRLEGQKTAAIEIL 282
|
170 180
....*....|....*....|...
gi 1778564574 164 RQ--WRDVDYVFVAVGGGGLIAG 184
Cdd:PLN02569 283 QQfdWEVPDWVIVPGGNLGNIYA 305
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
20-199 |
3.42e-05 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 46.04 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKNNIRFKREDLQ--PVFSFKLRgaynRISQLPKSQLERG---VITASA--GNHAQGVALSGQKLGI 92
Cdd:PRK14045 21 ETPIQYLPNISRELGADVYVKRDDLTglGIGGNKIR----KLEYLLGDALSRGadvVITVGAvhSNHAFVTGLAAKKLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 93 RAIIVMpKTTPDIKVQAV--KRLGGEVVLH--GDSFDVAnKYAIARAAE---DGMT--FIPPYDDELV-----MAGQGTI 158
Cdd:PRK14045 97 DAVLVL-RGKEELKGNYLldKIMGIETRVYeaKDSFELM-KYAEEVAEElkgEGRKpyIIPPGGASPVgtlgyVRAVGEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1778564574 159 GNEILRQWRDVDYVFVAVGGGGLIAGVAAYLGDVAPHVKVI 199
Cdd:PRK14045 175 ATQVKKLGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVV 215
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
20-202 |
2.09e-04 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 43.70 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 20 ETPLEAAPRISEKLKN-NIRFKREDLQPVFSFKLRgayNRISQ--LPKSQLERGVITAS-AGNHaqGVALS--GQKLGIR 93
Cdd:PRK13028 62 PTPLYHAKRLSEELGGaQIYLKREDLNHTGAHKIN---NCLGQalLAKRMGKKRLIAETgAGQH--GVATAtaAALFGLE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 94 AIIVMPKTtpDIKVQA-----VKRLGGEV--VLHG-----DSFDVANKyAIARAAEDGMTFI-----P-PYDdELVMAGQ 155
Cdd:PRK13028 137 CEIYMGEV--DIERQHpnvfrMKLLGAEVvpVTRGgrtlkEAVDSAFE-DYLKDPDNTHYAIgsvvgPhPFP-MMVRDFQ 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1778564574 156 GTIGNEILRQWRDV-----DYVFVAVGGGGLIAGV-AAYLGDvaPHVKVIPVE 202
Cdd:PRK13028 213 SVIGEEAREQFLEMtgrlpDAVVACVGGGSNAIGLfSAFLDD--ESVRLVGVE 263
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
19-294 |
4.38e-04 |
|
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: 42.72 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 19 IETPLEAAPRISEKLKNNIR--------FKREDLQPVF-SFKLRGA-YNRISQLPKSQLERGVIT--------------- 73
Cdd:cd06447 51 IESPLLPIPRMKQALEKLYHqpikgrllLKADSHLPISgSIKARGGiYEVLKHAEKLALEHGLLTleddysklasekfrk 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 74 ---------ASAGNHAQGVALSGQKLGIRAIIVMPKTTPDIKVQAVKRLGGEVVLHGDSFDVANKYAIARAAEDGMT-FI 143
Cdd:cd06447 131 lfsqysiavGSTGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCyFV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 144 ppyDDE---LVMAGQGTIGNEILRQW----RDVD-------YVFVAVGG--GGLIAGVAAYLGDvapHVKVIPVEYDESA 207
Cdd:cd06447 211 ---DDEnsrDLFLGYAVAASRLKAQLaelgIKVDaehplfvYLPCGVGGapGGVAFGLKLIFGD---NVHCFFAEPTHSP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 208 CLKAALET--NERVILPTVGL----FADGTAVAqigekpfdvirlQKSDNSGPIVEP---NVVLVNTDEI---CAAIKDT 275
Cdd:cd06447 285 CMLLGMATglHDKISVQDIGIdnrtAADGLAVG------------RPSGLVGKLMEPllsGIYTVEDDELyrlLAMLKDS 352
|
330
....*....|....*....
gi 1778564574 276 YDecrSIVEPSGAMALAGI 294
Cdd:cd06447 353 EN---IEVEPSAAAGFTGP 368
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
17-180 |
1.69e-03 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 40.89 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 17 VAIETPLEAAPRISEKLKN------NIRFKREDLQPVFSFKLRGAYNRISQLPKSQLERGVITASAGNHAQGVALSGQKL 90
Cdd:PLN02618 63 VGRETPLYFAERLTEHYKRadgegpEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778564574 91 GIRAIIVMpkTTPDIKVQA-----VKRLGGEV--VLHGD-SFDVANKYAIARAAEDGMT--FI------P-PYdDELVMA 153
Cdd:PLN02618 143 GLECIVYM--GAQDMERQAlnvfrMRLLGAEVrpVHSGTaTLKDATSEAIRDWVTNVETthYIlgsvagPhPY-PMMVRD 219
|
170 180 190
....*....|....*....|....*....|.
gi 1778564574 154 GQGTIGNEILRQ----WRDVDYVFVAVGGGG 180
Cdd:PLN02618 220 FHSVIGKETRRQamekWGGKPDVLVACVGGG 250
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