|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
96-599 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 724.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 96 PDYLRLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQG 175
Cdd:PRK09224 3 ADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 176 VAYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEI 255
Cdd:PRK09224 83 VALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 256 LHQiDLRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEET 335
Cdd:PRK09224 163 LQQ-HPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 336 FRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAaqVCILSGANMDFDRLRFIAE 415
Cdd:PRK09224 242 FRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETL--VAILSGANMNFDRLRYVAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 416 RADLGLNKEVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKDRATELPLILQQISEQNMVAEDI 495
Cdd:PRK09224 320 RAELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 496 SDNELAKTHARYLIGGKSS-VSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKL 574
Cdd:PRK09224 400 SDDELAKLHVRYMVGGRPPkPLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADEPEF 479
|
490 500
....*....|....*....|....*
gi 19113433 575 HSVLEEIGYNWVDETNNPVYLRYLR 599
Cdd:PRK09224 480 EAFLDELGYPYWDETDNPAYRLFLA 504
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
97-598 |
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: 610.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 97 DYLRLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGV 176
Cdd:TIGR01124 1 DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 177 AYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEIL 256
Cdd:TIGR01124 81 AFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 257 HQiDLRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETF 336
Cdd:TIGR01124 161 RQ-VANPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 337 RLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAaqVCILSGANMDFDRLRFIAER 416
Cdd:TIGR01124 240 RLCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTL--VAILSGANMNFHRLRYVSER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 417 ADLGLNKEVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKDRAtELPLILQQISEQNMVAEDIS 496
Cdd:TIGR01124 318 CELGEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNPQ-ERQEILARLNDGGYSVVDLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 497 DNELAKTHARYLIGGKSS-VSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKLH 575
Cdd:TIGR01124 397 DDELAKLHVRYMVGGRPPhVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDQFE 476
|
490 500
....*....|....*....|...
gi 19113433 576 SVLEEIGYNWVDETNNPVYLRYL 598
Cdd:TIGR01124 477 QFLAELGYRYHDETNNPAYRLFL 499
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
97-599 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 588.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 97 DYLRLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGV 176
Cdd:PRK12483 21 DYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 177 AYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEIL 256
Cdd:PRK12483 101 ALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 257 HQIDLRkLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETF 336
Cdd:PRK12483 181 RQHPGP-LDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 337 RLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKnpNAAQVCILSGANMDFDRLRFIAER 416
Cdd:PRK12483 260 ELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIE--GQTLVAIDSGANVNFDRLRHVAER 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 417 ADLGLNKEVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKDRATELPLILQQISEQNMVAEDIS 496
Cdd:PRK12483 338 AELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASLRAQGFPVLDLT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 497 DNELAKTHARYLIGGKS-SVSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKLH 575
Cdd:PRK12483 418 DDELAKLHIRHMVGGRApLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGLQVPEDERAALD 497
|
490 500
....*....|....*....|....
gi 19113433 576 SVLEEIGYNWVDETNNPVYLRYLR 599
Cdd:PRK12483 498 AALAALGYPYWEETGNPAYRLFLG 521
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
97-594 |
1.89e-173 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 504.84 E-value: 1.89e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 97 DYLRLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGV 176
Cdd:PLN02550 93 EYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 177 AYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEIL 256
Cdd:PLN02550 173 ALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 257 HQIDlRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETF 336
Cdd:PLN02550 253 RQHQ-GPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 337 RLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAaqVCILSGANMDFDRLRFIAER 416
Cdd:PLN02550 332 RLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENV--VAITSGANMNFDRLRIVTEL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 417 ADLGLNKEVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKdRATELPLILQQISEQNMVAEDIS 496
Cdd:PLN02550 410 ADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVH-TEQELQALKKRMESAQLRTVNLT 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 497 DNELAKTHARYLIGGKSSVSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKLHS 576
Cdd:PLN02550 489 SNDLVKDHLRYLMGGRAIVKDELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQVPPEEMQEFKS 568
|
490
....*....|....*...
gi 19113433 577 VLEEIGYNWVDETNNPVY 594
Cdd:PLN02550 569 RANALGYEYQDECDNEAF 586
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
110-406 |
4.80e-144 |
|
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: 418.81 E-value: 4.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 110 VIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATI 189
Cdd:cd01562 14 VVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGVAYAAKLLGIPATI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 190 VMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDlrKLDAIYC 269
Cdd:cd01562 94 VMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQVP--DLDAVFV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 270 AVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVLV 349
Cdd:cd01562 172 PVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRKLVDDVVTV 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19113433 350 DKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPnaaqVCILSGANMD 406
Cdd:cd01562 252 SEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKV----VVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
107-420 |
1.20e-137 |
|
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: 403.65 E-value: 1.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 107 VYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVK 186
Cdd:COG1171 18 IAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 187 ATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQidLRKLDA 266
Cdd:COG1171 98 ATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQ--LPDLDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 267 IYCAVggggliagiaTYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDV 346
Cdd:COG1171 176 VFVPVggggliagvaAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLVDDI 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113433 347 VLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPnaaqVCILSGANMDFDRLRFIAERADLG 420
Cdd:COG1171 256 VTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRV----VVVLSGGNIDPDRLAEILERGLVG 325
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
109-509 |
1.48e-106 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 327.15 E-value: 1.48e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 109 EVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKAT 188
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 189 IVMPQNTPEIKWRNVKRLGAN---VLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQID-LRKL 264
Cdd:PRK08639 101 IFMPVTTPQQKIDQVRFFGGEfveIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEkEGSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 265 DAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNID 344
Cdd:PRK08639 181 DYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVVD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 345 DVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNpnaaQVCILSGANMDFDRLRFIAERA--DLGLn 422
Cdd:PRK08639 261 DVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKT----VVCVISGGNNDIERMPEIKERSliYEGL- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 423 KEVFLsVTIPERPGSF-EALHNIITPR-SITEFSYrydnddyaniytsfvVK---------------DRATELPLILQQI 485
Cdd:PRK08639 336 KHYFI-VNFPQRPGALrEFLDDVLGPNdDITRFEY---------------LKknnretgpvlvgielKDAEDYDGLIERM 399
|
410 420
....*....|....*....|....
gi 19113433 486 SEQNMVAEDISDNELAkthARYLI 509
Cdd:PRK08639 400 EAFGPSYIDINPNEPL---YNLLI 420
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
114-486 |
1.28e-86 |
|
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: 274.32 E-value: 1.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIVMPQ 193
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 194 NTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHqiDLRKLDAIYCAVGG 273
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIME--DIPDVDTVIVPVGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 274 GGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVLVDKDE 353
Cdd:TIGR01127 159 GGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 354 ICAAIKDVFLDTRSVVEPSGAMAVAGMkryvaKHKPKNPNAAQVCI-LSGANMDFDRLRFIAERADLGLNKEVFLSVTIP 432
Cdd:TIGR01127 239 IANAIYLLLERHKILAEGAGAAGVAAL-----LEQKVDVKGKKIAVvLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLP 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 19113433 433 ERPGSFEALHNIITPRSitefsyrydnddyANIYTSFVvkDR-ATELPLILQQIS 486
Cdd:TIGR01127 314 DRPGALYHLLESIAEAR-------------ANIVKIDH--DRlSKEIPPGFAMVE 353
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
109-415 |
1.22e-79 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 254.66 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 109 EVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKAT 188
Cdd:PRK08638 23 GRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALLGIDGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 189 IVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHqiDLRKLDAIY 268
Cdd:PRK08638 103 VVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILE--DLWDVDTVI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 269 CAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVL 348
Cdd:PRK08638 181 VPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVL 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113433 349 VDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAaqVCILSGANMDFDRLRFIAE 415
Cdd:PRK08638 261 VSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKV--VAIISGGNVDLSRVSQITG 325
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
111-418 |
5.50e-71 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 231.39 E-value: 5.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:PRK07476 17 VRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATIC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHqiDLRKLDAIYCA 270
Cdd:PRK07476 97 MSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILE--ALPDVATVLVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFAD--GTAVKLVGEETFRLVSKNIDDVVL 348
Cdd:PRK07476 175 LSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslGGGIGLDNRYTFAMCRALLDDVVL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113433 349 VDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMkryvAKHKPKNPNAAQVCILSGANMDFD-RLRFIAERAD 418
Cdd:PRK07476 255 LDEAEIAAGIRHAYREERLVVEGAGAVGIAAL----LAGKIAARDGPIVVVVSGANIDMElHRRIINGEVA 321
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
111-445 |
9.64e-71 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 233.63 E-value: 9.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:PRK07334 21 VLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHqiDLRKLDAIYCA 270
Cdd:PRK07334 101 MPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLE--DAPDLDTLVVP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVKRIAPHVKVIGVETfdadALKKSLKDKKRVTLKEVG--LFADGTAVKLVGEETFRLVSKNIDDVVL 348
Cdd:PRK07334 179 IGGGGLISGMATAAKALKPDIEIIGVQT----ELYPSMYAAIKGVALPCGgsTIAEGIAVKQPGQLTLEIVRRLVDDILL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 349 VDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNaaqvCILSGANMDFDRLRFIAERADLGLNKEVFLS 428
Cdd:PRK07334 255 VSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVG----LVLSGGNIDTRLLANVLLRGLVRAGRLARLR 330
|
330 340
....*....|....*....|....*
gi 19113433 429 VTIPERPGSF--------EALHNII 445
Cdd:PRK07334 331 VDIRDRPGALarvtaligEAGANII 355
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
107-402 |
1.02e-70 |
|
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: 229.89 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 107 VYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVK 186
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 187 ATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKE-QNLEVIHPFDDPYVIAGQGTIGLEILHQIDlRKLD 265
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLG-GDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 266 AIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLV-GEETFRLVSKNID 344
Cdd:pfam00291 160 AVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113433 345 DVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPknPNAAQVCILSG 402
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELK--GGDRVVVVLTG 295
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
111-411 |
2.28e-69 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 227.27 E-value: 2.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:PRK06815 18 VRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDlrKLDAIYCA 270
Cdd:PRK06815 98 APEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQP--DLDAVFVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKL-VGEETFRLVSKNIDDVVLV 349
Cdd:PRK06815 176 VGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGVePGAITFPLCQQLIDQKVLV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113433 350 DKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNpnaaQVCILSGANMDFDRLR 411
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKK----VAVVLCGKNIVLEKYL 313
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
114-402 |
1.62e-67 |
|
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: 219.69 E-value: 1.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDK-QSLKNGVIACSA-GNHAQGVAYSARTLGVKATIVM 191
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEeGKLPKGVIIESTgGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 192 PQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQ-NLEVIHPFDDPYVIAGQGTIGLEILHQIDLRKLDAIYCA 270
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLGGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVKRIAPHVKVIGVETfdadalkkslkdkkrvtlkevglfadgtavklvgeetfrlvsknidDVVLVD 350
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19113433 351 KDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHkpkNPNAAQVCILSG 402
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL---GKGKTVVVILTG 243
|
|
| PLN02970 |
PLN02970 |
serine racemase |
110-410 |
1.16e-57 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 196.44 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 110 VIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATI 189
Cdd:PLN02970 24 FIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 190 VMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIdlRKLDAIYC 269
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV--PELDVIIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 270 AVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLvGEETFRLVSKNIDDVVLV 349
Cdd:PLN02970 182 PISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASL-GDLTWPVVRDLVDDVITV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113433 350 DKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKNPNAAQV-CILSGANMDFDRL 410
Cdd:PLN02970 261 DDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAWKGCKNVgIVLSGGNVDLGVL 322
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
111-408 |
4.87e-54 |
|
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: 186.60 E-value: 4.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:TIGR02991 17 VEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATIC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDlrKLDAIYCA 270
Cdd:TIGR02991 97 MSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQMP--DLATVLVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFAD--GTAVKLVGEETFRLVSKNIDDVVL 348
Cdd:TIGR02991 175 LSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTFAMCKALLDEIVL 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 349 VDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMkryvAKHKPKNPNAAqVCILSGANMDFD 408
Cdd:TIGR02991 255 VSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL----LAGKIKNPGPC-AVIVSGRNIDMD 309
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
110-410 |
2.55e-53 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 184.84 E-value: 2.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 110 VIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATI 189
Cdd:PRK07048 21 VAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 190 VMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDlrKLDAIY- 268
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVG--PLDALFv 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 269 ----------CAVGgggliagiatyVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRL 338
Cdd:PRK07048 179 clggggllsgCALA-----------ARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPI 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113433 339 VSKNIDDVVLVDKDEICAAIKdvFLDTRS--VVEPSGAMAVAGMKRYVAKHKPKnpnaaQV-CILSGANMDFDRL 410
Cdd:PRK07048 248 IRRLVDDIVTVSDAELVDAMR--FFAERMkiVVEPTGCLGAAAALRGKVPLKGK-----RVgVIISGGNVDLARF 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
111-410 |
1.61e-46 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 165.90 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKgVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMasLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:PRK08246 21 IRRTPVLE-ADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIdlRKLDAIYCA 270
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA--PGVDTVLVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 271 VGGGGLIAGIATYVkriAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVLVD 350
Cdd:PRK08246 176 VGGGGLIAGIAAWF---EGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVS 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113433 351 KDEICAAIKDVFLDTRSVVEPSGAMAVAGM--KRYVakhkpknPNAA-QVC-ILSGANMDFDRL 410
Cdd:PRK08246 253 DEAIIAARRALWEELRLAVEPGAATALAALlsGAYV-------PAPGeRVAvVLCGANTDPATL 309
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
111-406 |
4.00e-44 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 160.32 E-value: 4.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 111 IKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQS-LKNGVIACSAGNHAQGVAYSARTLGVKATI 189
Cdd:PRK06608 21 LHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGkLPDKIVAYSTGNHGQAVAYASKLFGIKTRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 190 VMPQNTPEIKWRNVKRLGANVLLhgANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDLrKLDAIYC 269
Cdd:PRK06608 101 YLPLNTSKVKQQAALYYGGEVIL--TNTRQEAEEKAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGF-SPDAIFA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 270 AVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEV-GLFADGTAVKLVGEETFRLVsKNIDDVVL 348
Cdd:PRK06608 178 SCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYL-KKLDDFYL 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 349 VDKDEIcaAIKDVFLDT--RSVVEPSGAMAVAGMKRYVAKHKPknPNAAQVcILSGANMD 406
Cdd:PRK06608 257 VEEYEI--YYWTAWLTHllKVICEPSSAINMVAVVNWLKTQSK--PQKLLV-ILSGGNID 311
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
107-411 |
1.80e-43 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 158.23 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 107 VYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQ-SLKNGVIACSAGNHAQGVAYSARTLGV 185
Cdd:PRK06110 15 VYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRgPRVRGVISATRGNHGQSVAFAARRHGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 186 KATIVMPQ-NTPEiKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFdDPYVIAGQGTIGLEILHQidLRKL 264
Cdd:PRK06110 95 AATIVVPHgNSVE-KNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRA--VPDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 265 DAIY---------CAVGGGGLIAGIATyvkriaphvKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEET 335
Cdd:PRK06110 171 DVVYvpigmgsgiCGAIAARDALGLKT---------RIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113433 336 FRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAgmkryvAKHKPKNPNAAQVC--ILSGANMDFDRLR 411
Cdd:PRK06110 242 LEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALA------AALQERERLAGKRVglVLSGGNIDRAVFA 313
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
113-378 |
1.14e-41 |
|
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: 152.84 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 113 ETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHN--KMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHlcQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARL--AKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDLR-KLDAI 267
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElaENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 268 YCAVGGGGLIAGIATYVKRI-APHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGTAVKLVGEETFRLVSK-NIDD 345
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNgWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEhNIKS 240
|
250 260 270
....*....|....*....|....*....|...
gi 19113433 346 VVLVDKDEIcAAIKDVFLDTRSVVEPSGAMAVA 378
Cdd:cd06448 241 EVVSDRDAV-QACLRFADDERILVEPACGAALA 272
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
130-406 |
1.98e-41 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 153.24 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 130 VYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIACSAGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKRLGAN 209
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 210 VLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDlrklDAIYCAVGGGGLIAGIATYVKriAP 289
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAP----DVVIVPIGGGGLASGVALALK--SQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 290 HVKVIGVETFDADALKKSLKDKKRvTLKEVGLFADGTAVKLVGEETFRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVV 369
Cdd:PRK08813 204 GVRVVGAQVEGVDSMARAIRGDLR-EIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIA 282
|
250 260 270
....*....|....*....|....*....|....*..
gi 19113433 370 EPSGAMAVAGMKRYVAKHKpknpnaaqVCILSGANMD 406
Cdd:PRK08813 283 EGAGALALAAGRRVSGKRK--------CAVVSGGNID 311
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
424-508 |
2.97e-39 |
|
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes the first of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153178 [Multi-domain] Cd Length: 85 Bit Score: 138.45 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 424 EVFLSVTIPERPGSFEALHNIITPRSITEFSYRYDNDDYANIYTSFVVKDRATELPLILQQISEQNMVAEDISDNELAKT 503
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 19113433 504 HARYL 508
Cdd:cd04906 81 HLRYM 85
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
518-598 |
1.08e-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: 125.74 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 518 ERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQVEKLHSVLEEIGYNWVDETNNPVYLRY 597
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADLDELKERLDALGYPYQEETDNPAYKLF 80
|
.
gi 19113433 598 L 598
Cdd:cd04907 81 L 81
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
521-587 |
4.25e-21 |
|
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: 87.18 E-value: 4.25e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113433 521 YRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQ-VEKLHSVLEEIGYNWVD 587
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDREdLAELKERLEALGYPYVD 68
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
114-402 |
7.48e-20 |
|
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: 90.73 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVP-VYLKREDLTPVFSFKIRGAhnKMA-SLDKQSLKNGVIACSAGNHAQGVA-YSARTlGVKATIV 190
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGM--TVAvSKAKELGVKAVACASTGNTSASLAaYAARA-GIKCVVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHpFDDPYVIAGQGTIGLEILHQIDLRKLDAI--- 267
Cdd:cd01563 100 LPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQLGWEVPDYVvvp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 268 ------YCAVGGGGLIAGIATYVKRIaphVKVIGVETFDAD----ALKKSLKDKKRVTLKEVglFADGTAVK--LVGEET 335
Cdd:cd01563 179 vgnggnITAIWKGFKELKELGLIDRL---PRMVGVQAEGAApivrAFKEGKDDIEPVENPET--IATAIRIGnpASGPKA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113433 336 FRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKnPNAAQVCILSG 402
Cdd:cd01563 254 LRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIID-KGERVVVVLTG 319
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
427-494 |
4.62e-19 |
|
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153157 [Multi-domain] Cd Length: 68 Bit Score: 81.40 E-value: 4.62e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113433 427 LSVTIPERPGSFEALHNII-TPRSITEFSYRYDNDDYANIYTSFVVKDRAtELPLILQQISEQNMVAED 494
Cdd:cd04885 1 FAVTFPERPGALKKFLELLgPPRNITEFHYRNQGGDEARVLVGIQVPDRE-DLAELKERLEALGYPYVD 68
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
114-402 |
6.43e-19 |
|
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: 89.10 E-value: 6.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGahnkMASLDKQSLKNG--VIAC-SAGNHAQGVA-YSARTlGVKATI 189
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRA----MQVAVSLALERGakTIVCaSSGNGSAALAaYAARA-GIEVFV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 190 VMPQN-TPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFdDPYVIAGQGTIGLEILHQIDlRKLDAIY 268
Cdd:COG0498 142 FVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLG-RVPDWVV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 269 ---------CAVGGGGLIAGIATYVKRIaPhvKVIGVETFDADALKKSLKDKKRVTLKEVGLF-ADGTAVK--LVGEETF 336
Cdd:COG0498 220 vptgnggniLAGYKAFKELKELGLIDRL-P--RLIAVQATGCNPILTAFETGRDEYEPERPETiAPSMDIGnpSNGERAL 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113433 337 RLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKPKnPNAAQVCILSG 402
Cdd:COG0498 297 FALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEID-PDEPVVVLSTG 361
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
415-504 |
1.52e-17 |
|
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the pfam01842 domain.
Pssm-ID: 395467 [Multi-domain] Cd Length: 91 Bit Score: 77.71 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 415 ERADLGLNKEVFLSVTIPERPGSF-EALHNIITPRSITEFSYRYDNDDYANIYTSFVVkDRATELPLILQQISEQNMVAE 493
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALlTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIEL-SQAEDLDEFIERLNKLGYDYE 79
|
90
....*....|.
gi 19113433 494 DISDNELAKTH 504
Cdd:pfam00585 80 DLSDNEAAYEH 90
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
510-598 |
2.28e-16 |
|
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: 74.62 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 510 GGKSSVSKERLYRLDFPERPGALCKFLRSIKEVCSISLFHYRNCGGDIASVLAGLRVFDGQ-VEKLHSVLEEIGYNWVDE 588
Cdd:pfam00585 2 RALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQAEdLDEFIERLNKLGYDYEDL 81
|
90
....*....|
gi 19113433 589 TNNPVYLRYL 598
Cdd:pfam00585 82 SDNEAAYEHL 91
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
114-267 |
5.42e-13 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 70.80 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVP-VYLKREDLTPVFSFKIRGAhnKMA-SLDKQSLKNGVIACSAGNHAQGVA-YSARTlGVKATIV 190
Cdd:PRK08197 80 TPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGL--AVGvSRAKELGVKHLAMPTNGNAGAAWAaYAARA-GIRATIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANVLLhganFDIAKAECARLAKEQNLEV----IHPFDDPYVIAGQGTIGLEILHQIDLRKLDA 266
Cdd:PRK08197 157 MPADAPEITRLECALAGAELYL----VDGLISDAGKIVAEAVAEYgwfdVSTLKEPYRIEGKKTMGLELAEQLGWRLPDV 232
|
.
gi 19113433 267 I 267
Cdd:PRK08197 233 I 233
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
170-260 |
4.47e-12 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 67.98 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 170 GNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHpfDDPY------ 243
Cdd:PRK08206 125 GNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ--DTAWegyeei 202
|
90 100
....*....|....*....|
gi 19113433 244 ---VIAGQGTIGLEILHQID 260
Cdd:PRK08206 203 ptwIMQGYGTMADEAVEQLK 222
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
114-389 |
9.78e-12 |
|
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: 66.00 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQ-SLKNG--VIACSAGNHAQGVAYSARTLGVKATIV 190
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRgLLKPGttIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 191 MPQNTPEIKWRNVKRLGANV-LLHGANFD-----IAKAEcaRLAKEqnleviHP-------FDDPY-VIAGQGTIGLEIL 256
Cdd:cd01561 83 MPETMSEEKRKLLRALGAEViLTPEAEADgmkgaIAKAR--ELAAE------TPnafwlnqFENPAnPEAHYETTAPEIW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 257 HQIDlRKLDAIYCAVGgggliagiaT---------YVKRIAPHVKVIGVETFDAdalkkslkdkkrvtlkevGLFADGTA 327
Cdd:cd01561 155 EQLD-GKVDAFVAGVG---------TggtitgvarYLKEKNPNVRIVGVDPVGS------------------VLFSGGPP 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113433 328 V--KL--VGEEtfrLVSKN-----IDDVVLVDKDEICAAIKDVFLDTRSVVEPSGAMAVAGMKRYVAKHKP 389
Cdd:cd01561 207 GphKIegIGAG---FIPENldrslIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGP 274
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
115-386 |
1.65e-11 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 66.00 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 115 PLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNGVIAcSAGNHAQGVAYSARTLGVKATIVMPQN 194
Cdd:PRK08329 59 HLTPPITPTVKRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVFVSYN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 195 TPEIKWRNVKRLGANV-LLHGANFDIAKaECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDLrkLDAIYCAVGG 273
Cdd:PRK08329 138 ASKEKISLLSRLGAELhFVEGDRMEVHE-EAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGV--PDYAFVPVGS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 274 GGLIAGIATYVKR------IAPHVKVIGVETFDADALKKSLKDKKRVtlkevglfADGTAV--KLVGEETFRLVSKNIDD 345
Cdd:PRK08329 215 GTLFLGIWKGFKElhemgeISKMPKLVAVQAEGYESLCKRSKSENKL--------ADGIAIpePPRKEEMLRALEESNGF 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 19113433 346 VVLVDKDEICAAIKDV----FLdtrsvVEPSGAMAVAGMKRYVAK 386
Cdd:PRK08329 287 CISVGEEETRAALHWLrrmgFL-----VEPTSAVALAAYWKLLEE 326
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
114-380 |
2.35e-11 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 65.99 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVvISESTGVPVYLKREDLTPVFSFKIRGAHNKMA-SLDKQSlkNGVIACSAGNHAQGVA-YSARTlGVKATIVM 191
Cdd:PRK05638 67 TPLIRAR-ISEKLGENVYIKDETRNPTGSFRDRLATVAVSyGLPYAA--NGFIVASDGNAAASVAaYSARA-GKEAFVVV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 192 PQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDDPYVIAGQGTIGLEILHQIDLRK-------- 263
Cdd:PRK05638 143 PRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINPTHvivptgsg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 264 --LDAIYCAVGGGGLiagiatyVKRIAPHVKVIGVETFDADALKKS---LKDKKRVTlKEVGLFADGTAVKlvgEETFRL 338
Cdd:PRK05638 223 syLYSIYKGFKELLE-------IGVIEEIPKLIAVQTERCNPIASEilgNKTKCNET-KALGLYVKNPVMK---EYVSEA 291
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19113433 339 VSKNIDDVVLVDKDEICAAiKDVFLDTRSVVEPSGAMAVAGM 380
Cdd:PRK05638 292 IKESGGTAVVVNEEEIMAG-EKLLAKEGIFAELSSAVVMPAL 332
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
105-297 |
1.16e-10 |
|
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: 62.76 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 105 SNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNkM--ASLDKQSLKNG--VIACSAGNHAQGVAYSA 180
Cdd:COG0031 5 DSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALS-MieDAEKRGLLKPGgtIVEATSGNTGIGLAMVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 181 RTLGVKATIVMPQNTPEIKWRNVKRLGANVLL-------HGAnfdIAKAEcaRLAKEQNlEVIHP--FDDP------YVi 245
Cdd:COG0031 84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLtpgaegmKGA---IDKAE--ELAAETP-GAFWPnqFENPanpeahYE- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19113433 246 agqgTIGLEILHQIDLRkLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVE 297
Cdd:COG0031 157 ----TTGPEIWEQTDGK-VDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVE 203
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
106-301 |
8.35e-08 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 54.48 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 106 NVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQ-SLKNG--VIACSAGNHAQGVAYSART 182
Cdd:PRK10717 6 DVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRgLLKPGgtIVEGTAGNTGIGLALVAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 183 LGVKATIVMPQNTPEIKWRNVKRLGANVLL----------HGANFDIAKAEcarlakeqnlEVIHPFDDPYVIAGQ---- 248
Cdd:PRK10717 86 RGYKTVIVMPETQSQEKKDLLRALGAELVLvpaapyanpnNYVKGAGRLAE----------ELVASEPNGAIWANQfdnp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 249 -------GTIGLEILHQIDlRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDA 301
Cdd:PRK10717 156 anreahyETTGPEIWEQTD-GKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGS 214
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
114-271 |
1.31e-07 |
|
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: 53.65 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPvFSF---KIRgahnKMASLDKQSLKNG---VIacSAG----NHAQGVAYSARTL 183
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLTG-PAIggnKTR----KLEYLLADALAQGadtLV--TFGgaqsNHARATAAAAAKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 184 GVKATIVmpqntpeIKWRNVKRLGANVLL---HGANF------------DIAKAECARLAKEqnlevihpFDDPYVIAGQ 248
Cdd:COG2515 85 GLKCVLV-------LRGEEPTPLNGNLLLdrlLGAELhfvsrgeyrdrdEAMEAVAAELRAR--------GGKPYVIPEG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 19113433 249 GT----------IGLEILHQIDLR--KLDAIYCAV 271
Cdd:COG2515 150 GSnplgalgyveAAAELAAQLAELgvDFDYIVVAS 184
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
114-321 |
2.69e-07 |
|
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: 52.81 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISES--TGVPVYLKREDLTPVFSF---KIRgahnKMASLDKQSLKNG---VIACSA--GNHAQGVAYSARTL 183
Cdd:cd06449 1 TPIQYLPRLSEHlgGKVEIYAKRDDCNSGLAFggnKIR----KLEYLLPDALAKGadtLVTVGGiqSNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 184 GVKATIVM--PQNTPEIKWRNV------KRLGANVLLHGANFDIAKAECARLAKEqnlEVIHPFDDPYVI-AG-----QG 249
Cdd:cd06449 77 GLKCVLVQenWVPYSDAVYDRVgnillsRIMGADVRLVSAGFDIGIRKSFEEAAE---EVEAKGGKPYVIpAGgsehpLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 250 TIG-----LEILHQIDLR--KLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVE--TFDADALKKSLKdKKRVTLKEVG 320
Cdd:cd06449 154 GLGyvgfvLEIAQQEEELgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDasAKPEKTKAQVLR-IAQAKLAEEG 232
|
.
gi 19113433 321 L 321
Cdd:cd06449 233 L 233
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
92-391 |
4.35e-07 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 52.47 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 92 PDGtpdylrLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSL----KNGVIAC 167
Cdd:PLN03013 108 PDG------LNIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFispgKSVLVEP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 168 SAGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLL----HGANFDIAKAEcARLAKEQNLEVIHPFDDPY 243
Cdd:PLN03013 182 TSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLtdpaKGMTGAVQKAE-EILKNTPDAYMLQQFDNPA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 244 VIAGQ-GTIGLEILHQIDlRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLF 322
Cdd:PLN03013 261 NPKIHyETTGPEIWDDTK-GKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFI 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 323 ADGtavklvgeetfrLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVE-PSGAMAVAGMKryVAKhKPKN 391
Cdd:PLN03013 340 PKN------------LDQKIMDEVIAISSEEAIETAKQLALKEGLMVGiSSGAAAAAAIK--VAK-RPEN 394
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
102-391 |
5.43e-07 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 51.85 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 102 TLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSL----KNGVIACSAGNHAQGVA 177
Cdd:PLN02565 4 SIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLikpgESVLIEPTSGNTGIGLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 178 YSARTLGVKATIVMPQNTPEIKWRNVKRLGANVLL----HGANFDIAKAEcARLAKEQNLEVIHPFDDP------YVIAG 247
Cdd:PLN02565 84 FMAAAKGYKLIITMPASMSLERRIILLAFGAELVLtdpaKGMKGAVQKAE-EILAKTPNSYILQQFENPanpkihYETTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 248 ----QGTIGleilhqidlrKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFA 323
Cdd:PLN02565 163 peiwKGTGG----------KVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIP 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113433 324 DGTAVKLvgeetfrlvsknIDDVVLVDKDEICAAIKDVFLDTRSVVE-PSGAMAVAGMKryVAKhKPKN 391
Cdd:PLN02565 233 GVLDVDL------------LDEVVQVSSDEAIETAKLLALKEGLLVGiSSGAAAAAAIK--IAK-RPEN 286
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
114-271 |
2.04e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 50.22 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFS--FKIRgahnKMASLDKQSLKNG---VIACSA--GNHAQGVAYSARTLGVK 186
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGLALggNKTR----KLEFLLADALAQGadtLITAGAiqSNHARQTAAAAAKLGLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 187 ATIVMPQNTPEiKWRNVKRLGaNVLL------------HGANFD-IAKAECARLAKEQNlevihpfdDPYVIAGQG--TI 251
Cdd:PRK03910 92 CVLLLENPVPT-EAENYLANG-NVLLddlfgaeihvvpAGTDMDaQLEELAEELRAQGR--------RPYVIPVGGsnAL 161
|
170 180 190
....*....|....*....|....*....|
gi 19113433 252 G--------LEILHQIDLRKL--DAIYCAV 271
Cdd:PRK03910 162 GalgyvacaLEIAQQLAEGGVdfDAVVVAS 191
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
526-598 |
2.68e-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: 45.62 E-value: 2.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113433 526 PERPGALCKFLRSIkEVCSISLFHYRNCGGDIASVLAGLRVFDG--QVEKLHSVLEEIGYNWVDETNNPV---YLRYL 598
Cdd:cd04906 9 PERPGSFKKFCELI-GPRNITEFNYRYADEKDAHIFVGVSVANGaeELAELLEDLKSAGYEVVDLSDDELaktHLRYM 85
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
52-304 |
3.16e-06 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 49.57 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 52 SSIDCLEPKLQGIIEDNISPSTAQKEIsdikfNIPKEmlLPDgtpdylrLTLTSNVYEVIKETPLTKGVVISESTGVPVY 131
Cdd:PLN02556 12 SSIPPSSHTLRKLFSTVGSPSFAQRLR-----DLPKD--LPG-------TKIKTDASQLIGKTPLVYLNKVTEGCGAYIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 132 LKREDLTPVFSFKIRGAHNKMASLDKQSL----KNGVIACSAGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKRLG 207
Cdd:PLN02556 78 AKQEMFQPTSSIKDRPALAMIEDAEKKNLitpgKTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 208 ANVLLHganfDIAKAECARLAKEQNLEVIHP-------FDDPY-VIAGQGTIGLEILHQIdLRKLDAIYCAVGGGGLIAG 279
Cdd:PLN02556 158 AELVLT----DPTKGMGGTVKKAYELLESTPdafmlqqFSNPAnTQVHFETTGPEIWEDT-LGQVDIFVMGIGSGGTVSG 232
|
250 260
....*....|....*....|....*
gi 19113433 280 IATYVKRIAPHVKVIGVETFDADAL 304
Cdd:PLN02556 233 VGKYLKSKNPNVKIYGVEPAESNVL 257
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
113-403 |
5.96e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 48.58 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 113 ETPLTKGVvisestgvPVYLKREDLTPVFSFKIRGAHNKMASLDKQSLKNgVIACSAGNHAQGVA-YSARTlGVKATIVM 191
Cdd:PRK06450 58 RTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQ-ISEDSSGNAGASIAaYGAAA-GIEVKIFV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 192 PQNTPEIKWRNVKRLGANVL-LHGANFDIAKAecarlAKEQNL----EVIHP-FDDpyviaGQGTIGLEILHQIDLRKLD 265
Cdd:PRK06450 128 PETASGGKLKQIESYGAEVVrVRGSREDVAKA-----AENSGYyyasHVLQPqFRD-----GIRTLAYEIAKDLDWKIPN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 266 AIYCAVGGGGLIAGIATYVKR------IAPHVKVIGVETFDADALKKSLKDKKRVTLKEVGLFADGtavkLVGEETFRL- 338
Cdd:PRK06450 198 YVFIPVSAGTLLLGVYSGFKHlldsgvISEMPKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADA----LVSTRPFLLd 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113433 339 ----VSKNIDDVVLVDKDEICAAIKDVFLDTrSVVEPSGAMAVAGMKRYvakhKPKNPnaaqVCILSGA 403
Cdd:PRK06450 274 ymvkALSEYGECIVVSDNEIVEAWKELAKKG-LLVEYSSATVYAAYKKY----SVNDS----VLVLTGS 333
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
114-259 |
6.02e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 48.55 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGV-PVYLKREDLTPVFSFKIRGAHNKMasldKQSLKNG---VIACSAGNHAQGVAYSARTLGVKATI 189
Cdd:PRK06381 16 TPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHV----RRAMRLGysgITVGTCGNYGASIAYFARLYGLKAVI 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113433 190 VMPQNTPEIKWRNVKRLGANVLLHGANFDIAKAECARLAKEQNLEVIHPFDD-PYV-IAGQGTIGLEILHQI 259
Cdd:PRK06381 92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVnSVVdIEAYSAIAYEIYEAL 163
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
96-211 |
3.50e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 46.95 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 96 PDYLRLTLTSNVYEVIKETPLTKG----VVISESTGVP--VYLKREDLTPVFSFKIRGAHNKmASLDKQSLKNGVIA-CS 168
Cdd:PRK13802 309 PEFHKELATLNQRYVGRPSPLTEAprfaERVKEKTGLDarVFLKREDLNHTGAHKINNALGQ-ALLVKRMGKTRVIAeTG 387
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 19113433 169 AGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKR---LGANVL 211
Cdd:PRK13802 388 AGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARmrmLGAEVV 433
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
424-499 |
4.74e-05 |
|
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: 42.15 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 424 EVFLSVTIPERPGsfeALH---NIITPR-SITEFSYRYDNDDYANIYTSFVVKDRatELPLILQQISEQNMVAEDISDNE 499
Cdd:cd04907 1 ERLFRFEFPERPG---ALKkflNELLPKwNITLFHYRNQGSDYGRVLVGIQVPDA--DLDELKERLDALGYPYQEETDNP 75
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
75-210 |
7.57e-05 |
|
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: 45.22 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 75 QKEISDIKFniPKEMLlpdgtpDYLRltltsnvYEVIKETPLTKGVVISEST-GVPVYLKREDLTPVFSFKIrgaHNKMA 153
Cdd:cd06446 11 SKERYDPDF--PEELR------ELYK-------DYVGRPTPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKI---NNALG 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113433 154 S--LDKQSLKNGVIA-CSAGNHAQGVAYSARTLGVKATIVMPQNTPEIKWRNVKR---LGANV 210
Cdd:cd06446 73 QalLAKRMGKKRVIAeTGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRmelLGAEV 135
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
114-271 |
1.55e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 44.80 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 114 TPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKmASLDKQSLKNGVIA-CSAGNHAQGVAYSARTLGVKATIVMP 192
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQ-ALLAKRMGKTRIIAeTGAGQHGVATATACALFGLKCTIFMG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 193 QNTPEIKWRNVKR---LGANVllhganfdIAKAECARLAKEQNLEVI--------------------HPFddPYVIAG-Q 248
Cdd:PRK13803 351 EEDIKRQALNVERmklLGANV--------IPVLSGSKTLKDAVNEAIrdwvasvpdthyligsavgpHPY--PEMVAYfQ 420
|
170 180
....*....|....*....|....*.
gi 19113433 249 GTIGLEI---LHQIDLRKLDAIYCAV 271
Cdd:PRK13803 421 SVIGEEAkeqLKEQTGKLPDAIIACV 446
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
131-260 |
2.35e-04 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 44.03 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 131 YLKREDLTPVFSFKIRGAH------NKMASLDKQSLknGVIACSAGNHAQGV-AYSARTlGVKATIVMPQNTPEI-KWRN 202
Cdd:PLN02569 153 WVKHCGISHTGSFKDLGMTvlvsqvNRLRKMAKPVV--GVGCASTGDTSAALsAYCAAA-GIPSIVFLPADKISIaQLVQ 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113433 203 VKRLGANVLLHGANFDiakaECARLAKEQNLEVihPFDD-----PYVIAGQGTIGLEILHQID 260
Cdd:PLN02569 230 PIANGALVLSIDTDFD----GCMRLIREVTAEL--PIYLanslnSLRLEGQKTAAIEILQQFD 286
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
112-210 |
2.94e-04 |
|
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 272987 Cd Length: 385 Bit Score: 43.50 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 112 KETPLTKGVVISESTGVP-VYLKREDLTPVFSFKIRGAHNKmASLDKQSLKNGVIA-CSAGNHAQGVAYSARTLGVKATI 189
Cdd:TIGR00263 49 RPTPLTFAPNLTEALGGAkIYLKREDLNHTGAHKINNALGQ-ALLAKRMGKKRIIAeTGAGQHGVATATAAALLGLDCEV 127
|
90 100
....*....|....*....|....
gi 19113433 190 VMPQNTPEIKWRNVKR---LGANV 210
Cdd:TIGR00263 128 YMGAEDVERQKPNVFRmelLGAKV 151
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
109-210 |
1.06e-03 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 41.90 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 109 EVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAhnkmASLDKQSLKNGVIAC-------SAGNHAQGVAYSAR 181
Cdd:PLN02356 49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVA----VKIIEEALESGQLFPggvvtegSAGSTAISLATVAP 124
|
90 100
....*....|....*....|....*....
gi 19113433 182 TLGVKATIVMPQNTPEIKWRNVKRLGANV 210
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATV 153
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
100-415 |
1.32e-03 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 41.14 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 100 RLTLTSNVYEVIKETPLTKGVVISESTGVPVYLKREDLTPVFSFKIRGAHNKMASLDKQSL----KNGVIACSAGNHAQG 175
Cdd:PLN00011 4 RCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLitpgKSTLIEATAGNTGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 176 VAYSARTLGVKATIVMPqNTPEIKWRNVKR-LGANVLLH----GANFDIAKAEcARLAKEQNLEVIHPFDDPYVIAGQ-G 249
Cdd:PLN00011 84 LACIGAARGYKVILVMP-STMSLERRIILRaLGAEVHLTdqsiGLKGMLEKAE-EILSKTPGGYIPQQFENPANPEIHyR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 250 TIGLEILHQiDLRKLDAIYCAVGGGGLIAGIATYVKRIAPHVKVIGVETFDADALkkSLKDKKRVTLKEVGlfadgtavk 329
Cdd:PLN00011 162 TTGPEIWRD-SAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVL--SGGQPGPHLIQGIG--------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 330 lVGEETFRLVSKNIDDVVLVDKDEICAAIKDVFLDTRSVVE-PSGAMAVAGMKryVAKhKPKNPNAAQVCIL-SG----- 402
Cdd:PLN00011 230 -SGIIPFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGiSSGAAAAAALK--VAK-RPENAGKLIVVIFpSGgeryl 305
|
330
....*....|...
gi 19113433 403 ANMDFDRLRFIAE 415
Cdd:PLN00011 306 STKLFESVRYEAE 318
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
110-210 |
1.83e-03 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 40.89 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 110 VIKETPLTKGVVISE------STGVPVYLKREDLTPVFSFKIRGAHNKmASLDKQSLKNGVIACS-AGNHAQGVAYSART 182
Cdd:PLN02618 63 VGRETPLYFAERLTEhykradGEGPEIYLKREDLNHTGAHKINNAVAQ-ALLAKRLGKKRIIAETgAGQHGVATATVCAR 141
|
90 100 110
....*....|....*....|....*....|.
gi 19113433 183 LGVKATIVMPQNTPEIKWRNVKR---LGANV 210
Cdd:PLN02618 142 FGLECIVYMGAQDMERQALNVFRmrlLGAEV 172
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
112-210 |
4.45e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 39.85 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113433 112 KETPLTKGVVISES-TGVPVYLKREDLTPVfsfkirGAH---NKM--ASLDKQSLKNGVIA-CSAGNHAQGVAYSARTLG 184
Cdd:PRK13028 61 RPTPLYHAKRLSEElGGAQIYLKREDLNHT------GAHkinNCLgqALLAKRMGKKRLIAeTGAGQHGVATATAAALFG 134
|
90 100
....*....|....*....|....*....
gi 19113433 185 VKATIVMPQNTPEIKWRNV---KRLGANV 210
Cdd:PRK13028 135 LECEIYMGEVDIERQHPNVfrmKLLGAEV 163
|
|
| |
