|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
13-513 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 986.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 13 GAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQ 92
Cdd:PRK09224 2 GADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 93 GVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALE 172
Cdd:PRK09224 82 GVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAME 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 173 LLQQDAH-LDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDET 251
Cdd:PRK09224 162 ILQQHPHpLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERC 331
Cdd:PRK09224 242 FRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAERA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 332 ELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSD 411
Cdd:PRK09224 322 ELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDLSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 412 DEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHE-PDFET 490
Cdd:PRK09224 402 DELAKLHVRYMVGGRPPKPLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADePEFEA 481
|
490 500
....*....|....*....|...
gi 16131630 491 RLNELGYDCHDETNNPAFRFFLA 513
Cdd:PRK09224 482 FLDELGYPYWDETDNPAYRLFLA 504
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
15-512 |
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: 899.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 15 EYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:TIGR01124 1 DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 95 AFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:TIGR01124 81 AFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQDA-HLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFR 253
Cdd:TIGR01124 161 RQVAnPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 254 LCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERCEL 333
Cdd:TIGR01124 241 LCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 334 GEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGlEERKEILQMLNDGGYSVVDLSDDE 413
Cdd:TIGR01124 321 GEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNP-QERQEILARLNDGGYSVVDLTDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 414 MAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHEPD-FETRL 492
Cdd:TIGR01124 400 LAKLHVRYMVGGRPPHVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDqFEQFL 479
|
490 500
....*....|....*....|
gi 16131630 493 NELGYDCHDETNNPAFRFFL 512
Cdd:TIGR01124 480 AELGYRYHDETNNPAYRLFL 499
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
1-513 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 657.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 1 MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAH 80
Cdd:PRK12483 7 VSPTTIAPRAALLADYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 81 GVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHP 160
Cdd:PRK12483 87 GVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 161 MVIAGQGTLALELL-QQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFA 239
Cdd:PRK12483 167 DVIAGQGTVAMEILrQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 240 EGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANV 319
Cdd:PRK12483 247 DGVAVAQIGEHTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 320 NFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQML 399
Cdd:PRK12483 327 NFDRLRHVAERAELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 400 NDGGYSVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAF 479
Cdd:PRK12483 407 RAQGFPVLDLTDDELAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGL 486
|
490 500 510
....*....|....*....|....*....|....*
gi 16131630 480 ELGDHE-PDFETRLNELGYDCHDETNNPAFRFFLA 513
Cdd:PRK12483 487 QVPEDErAALDAALAALGYPYWEETGNPAYRLFLG 521
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
2-512 |
1.49e-168 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 489.05 E-value: 1.49e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 2 ADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHG 81
Cdd:PLN02550 80 TNEAENGSIPEAMEYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 82 VITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPM 161
Cdd:PLN02550 160 VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 162 VIAGQGTLALELLQQ-DAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAE 240
Cdd:PLN02550 240 VIAGQGTVGMEIVRQhQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFAD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 241 GVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVN 320
Cdd:PLN02550 320 GVAVKEVGEETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMN 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 321 FHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGlEERKEILQMLN 400
Cdd:PLN02550 400 FDRLRIVTELADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHTE-QELQALKKRME 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 401 DGGYSVVDLSDDEMAKLHVRYMVGGRpSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFE 480
Cdd:PLN02550 479 SAQLRTVNLTSNDLVKDHLRYLMGGR-AIVKDELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQ 557
|
490 500 510
....*....|....*....|....*....|...
gi 16131630 481 LGDHEPD-FETRLNELGYDCHDETNNPAFRFFL 512
Cdd:PLN02550 558 VPPEEMQeFKSRANALGYEYQDECDNEAFQLLM 590
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
22-336 |
1.57e-142 |
|
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: 412.89 E-value: 1.57e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 22 RAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARL 101
Cdd:COG1171 15 AARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 102 GVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLD 181
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPDLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 182 RVFVPvgggglaagvavlI-------------KQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIG 248
Cdd:COG1171 175 AVFVP-------------VggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 249 DETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYiaLHNIRGERLAHILSGANVNFHGLRYVS 328
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG--KERLKGKRVVVVLSGGNIDPDRLAEIL 319
|
....*...
gi 16131630 329 ERCELGEQ 336
Cdd:COG1171 320 ERGLVGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
17-320 |
2.30e-138 |
|
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: 401.48 E-value: 2.30e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:cd01562 1 LEDILAAAARIKPVVrrTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 95 AFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRL 254
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131630 255 CQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAlhNIRGERLAHILSGANVN 320
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKL--DLKGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
25-415 |
8.61e-100 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 307.12 E-value: 8.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 25 VYEAAQV-------TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFS 97
Cdd:PRK08639 12 IDKAAKRlkdvvpeTPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 98 SARLGVKALIVMPTATADIKVDAVRGFGG---EVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:PRK08639 92 CRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQDAHL---DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDET 251
Cdd:PRK08639 172 EQLEKEgspDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAlhNIRGERLAHILSGANVNFHGLRYVSERC 331
Cdd:PRK08639 252 FEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKD--EIKGKTVVCVISGGNNDIERMPEIKERS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 332 ELGEQREALLAVTIPEEKG---SFLKfcQLLG-GRSVTEFNYRFADAKN-ACIFVGVRLSR-----GLEERkeilqmLND 401
Cdd:PRK08639 330 LIYEGLKHYFIVNFPQRPGalrEFLD--DVLGpNDDITRFEYLKKNNREtGPVLVGIELKDaedydGLIER------MEA 401
|
410
....*....|....
gi 16131630 402 GGYSVVDLSDDEMA 415
Cdd:PRK08639 402 FGPSYIDINPNEPL 415
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
32-407 |
4.20e-85 |
|
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: 267.77 E-value: 4.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPT 111
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGG 191
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 192 LAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAIC 271
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 272 AAMKDLFEDVRAVAEPSGALALAGMkkyiaLH---NIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEE 348
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAAL-----LEqkvDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131630 349 KGSFLKFCQLL---GGRSVTEFNYRFAdAKNACIFVGVRLS---RGLEERKEILQMLNDGGYSVV 407
Cdd:TIGR01127 316 PGALYHLLESIaeaRANIVKIDHDRLS-KEIPPGFAMVEITletRGKEHLDEILKILRDMGYNFY 379
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
29-339 |
1.98e-81 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 256.59 E-value: 1.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIV 108
Cdd:PRK08638 25 IRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALLGIDGKVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 109 MPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVG 188
Cdd:PRK08638 105 MPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIVPIG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSD 268
Cdd:PRK08638 185 GGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSED 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131630 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNfhgLRYVSERCELGEQREA 339
Cdd:PRK08638 265 EIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVD---LSRVSQITGHVVAADA 332
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
32-406 |
6.21e-72 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 234.40 E-value: 6.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPT 111
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGG 191
Cdd:PRK07334 104 FTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 192 LAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALdagHPVDLPRVG-LFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAI 270
Cdd:PRK07334 184 LISGMATAAKALKPDIEIIGVQTELYPSMYAAI---KGVALPCGGsTIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 271 CAAMKDLFEDVRAVAEPSGALALAGMKKYIALhnIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKG 350
Cdd:PRK07334 261 EQAVSLLLEIEKTVVEGAGAAGLAALLAYPER--FRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLRVDIRDRPG 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131630 351 SFLKFCQLLG--GRSVTEFNYR--FAD--AKNACIFVgVRLSRGLEERKEILQMLNDGGYSV 406
Cdd:PRK07334 339 ALARVTALIGeaGANIIEVSHQrlFTDlpAKGAELEL-VIETRDAAHLQEVIAALRAAGFEA 399
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
32-316 |
5.04e-71 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 228.35 E-value: 5.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPT 111
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQ-QGFTWVPPFDHPMVIAGQGTLALELL-QQDAHLDRVFVPVGG 189
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILeQLGGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 190 GGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRI-GDETFRLCQEYLDDIITVDSD 268
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16131630 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSG 316
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
17-319 |
1.73e-69 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 225.23 E-value: 1.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:PRK07476 3 LADIYRARRRIAGRVrrTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 95 AFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:PRK07476 83 AYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAE----GVAVK-RIgd 249
Cdd:PRK07476 163 EALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLDnRY-- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131630 250 eTFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAgmkkyiALHN----IRGERLAHILSGANV 319
Cdd:PRK07476 241 -TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIA------ALLAgkiaARDGPIVVVVSGANI 307
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
31-325 |
4.51e-67 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 218.79 E-value: 4.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGG 190
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 191 GLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVA--VKRiGDETFRLCQEYLDDIITVDSD 268
Cdd:PRK06815 180 GLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVEP-GAITFPLCQQLIDQKVLVSEE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131630 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHniRGERLAHILSGANVNFHGLR 325
Cdd:PRK06815 259 EIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY--QGKKVAVVLCGKNIVLEKYL 313
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
29-320 |
2.88e-63 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 209.10 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIV 108
Cdd:PRK07048 22 AHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 109 MPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVG 188
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALFVCLG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAG--HPVDLPRVglFAEGVAVKRIGDETFRLCQEYLDDIITVD 266
Cdd:PRK07048 182 GGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGeiVHIDTPRT--IADGAQTQHLGNYTFPIIRRLVDDIVTVS 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16131630 267 SDAICAAMKDLFEDVRAVAEPSGALALAGMKKyiALHNIRGERLAHILSGANVN 320
Cdd:PRK07048 260 DAELVDAMRFFAERMKIVVEPTGCLGAAAALR--GKVPLKGKRVGVIISGGNVD 311
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
32-316 |
2.71e-61 |
|
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: 201.20 E-value: 2.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHG--VITASAGNHAQGVAFSSARLGVKALIVM 109
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 110 PTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQ-GFTWVPPFDHPMVIAGQGTLALELLQQ--DAHLDRVFVP 186
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQlgGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 187 VGGGGLAAGVAVLIKQLMPQIKVIAVEAEdsaclkaaldaghpvdlprvglfaegvavkrigdetfrlcqeylddIITVD 266
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16131630 267 SDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNiRGERLAHILSG 316
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTG 243
|
|
| PLN02970 |
PLN02970 |
serine racemase |
29-324 |
3.02e-58 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 196.05 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIV 108
Cdd:PLN02970 25 IHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 109 MPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVG 188
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPIS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQLMPQIKVIAVE---AEDSACLKAaldAGHPVDLPRVGLFAEGVAVkRIGDETFRLCQEYLDDIITV 265
Cdd:PLN02970 185 GGGLISGIALAAKAIKPSIKIIAAEpkgADDAAQSKA---AGEIITLPVTNTIADGLRA-SLGDLTWPVVRDLVDDVITV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131630 266 DSDAICAAMKDLFEDVRAVAEPSGALALAGM------KKYIALHnirGERLAHILSGANVNFHGL 324
Cdd:PLN02970 261 DDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsdsfrSNPAWKG---CKNVGIVLSGGNVDLGVL 322
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
17-320 |
5.92e-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: 184.29 E-value: 5.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:TIGR02991 3 LQDIERAAARISGRVeeTPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 95 AFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:TIGR02991 83 AYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAE--GVAVKRIGDETF 252
Cdd:TIGR02991 163 EQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131630 253 RLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMkkyIALHNIRGERLAHILSGANVN 320
Cdd:TIGR02991 243 AMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL---LAGKIKNPGPCAVIVSGRNID 307
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
48-320 |
3.88e-53 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 182.08 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 48 ILVKREDRQPVHSFKLRGAYAMMagLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGE 127
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 128 VLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKqlmPQI 207
Cdd:PRK08246 117 VVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFE---GRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 208 KVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEP 287
Cdd:PRK08246 194 RVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEP 273
|
250 260 270
....*....|....*....|....*....|....*...
gi 16131630 288 SGALALAgmkkyiALHNIR-----GERLAHILSGANVN 320
Cdd:PRK08246 274 GAATALA------ALLSGAyvpapGERVAVVLCGANTD 305
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
22-321 |
9.51e-51 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 175.95 E-value: 9.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 22 RAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQ-KAHGVITASAGNHAQGVAFSSAR 100
Cdd:PRK06110 12 AAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 101 LGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFdHPMVIAGQGTLALELLQQDAHL 180
Cdd:PRK06110 92 HGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 181 DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVkRIGD-ETFRLCQEYL 259
Cdd:PRK06110 171 DVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMAC-RTPDpEALEVIRAGA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131630 260 DDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALhnIRGERLAHILSGANVNF 321
Cdd:PRK06110 250 DRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERER--LAGKRVGLVLSGGNIDR 309
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
338-422 |
4.77e-47 |
|
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: 158.09 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 338 EALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKL 417
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 16131630 418 HVRYM 422
Cdd:cd04906 81 HLRYM 85
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
32-320 |
3.14e-43 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 156.71 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSsrldnvILVKREDRQPVHSFKLRGAY-AMMAGLtEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK08813 40 TPLHYAERFG------VWLKLENLQRTGSYKVRGALnALLAGL-ERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLqqdAHL-DRVFVPVGG 189
Cdd:PRK08813 113 HGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELA---AHApDVVIVPIGG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 190 GGLAAGVAVLIKQlmPQIKVIAVEAEDSACLKAALdAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDA 269
Cdd:PRK08813 190 GGLASGVALALKS--QGVRVVGAQVEGVDSMARAI-RGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAE 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16131630 270 ICAAMKDLFEDVRAVAEPSGALALAGMKKyialhnIRGERLAHILSGANVN 320
Cdd:PRK08813 267 LRETLVRLALEEHVIAEGAGALALAAGRR------VSGKRKCAVVSGGNID 311
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
32-320 |
2.18e-41 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 151.46 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQK-AHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANfDEAKAKAIElSQQQGFTWVPPFDHPMVIAGQGTLALELLQQ-DAHLDRVFVPVGG 189
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILTNTR-QEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQlGFSPDAIFASCGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 190 GGLAAGVAVLIKQLMPQIKVIAVE---AEDSAclkAALDAGHPVDLPRV-GLFAEGVAVKRIGDETFRLCQEyLDDIITV 265
Cdd:PRK06608 182 GGLISGTYLAKELISPTSLLIGSEplnANDAY---LSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKK-LDDFYLV 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16131630 266 DSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNiRGERLAHILSGANVN 320
Cdd:PRK06608 258 EEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQS-KPQKLLVILSGGNID 311
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
433-512 |
1.01e-38 |
|
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: 135.76 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 433 ERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHE-PDFETRLNELGYDCHDETNNPAFRFF 511
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADlDELKERLDALGYPYQEETDNPAYKLF 80
|
.
gi 16131630 512 L 512
Cdd:cd04907 81 L 81
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
424-512 |
1.84e-37 |
|
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: 132.79 E-value: 1.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 424 GGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHE--PDFETRLNELGYDCHD 501
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQAEdlDEFIERLNKLGYDYED 80
|
90
....*....|.
gi 16131630 502 ETNNPAFRFFL 512
Cdd:pfam00585 81 LSDNEAAYEHL 91
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
329-419 |
1.95e-34 |
|
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: 124.70 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 329 ERCELGEQREALLAVTIPEEKGSFLKFCQLLGGR-SVTEFNYRFADAKNACIFVGVRLSRGlEERKEILQMLNDGGYSVV 407
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRnNITLFEYRKHGDKNGCVLVGIELSQA-EDLDEFIERLNKLGYDYE 79
|
90
....*....|..
gi 16131630 408 DLSDDEMAKLHV 419
Cdd:pfam00585 80 DLSDNEAAYEHL 91
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
31-294 |
8.79e-30 |
|
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: 118.94 E-value: 8.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRG--AYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIV 108
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGigHLCQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 109 MPTATADIKVDAVRGFGGEVLLHGAN-FDEAKAKAIEL-SQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVP 186
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELaENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 187 VGGGGLAAGVAVLIKQL----MPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYldDI 262
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLerngWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEH--NI 238
|
250 260 270
....*....|....*....|....*....|....*
gi 16131630 263 ITV---DSDAIcAAMKDLFEDVRAVAEPSGALALA 294
Cdd:cd06448 239 KSEvvsDRDAV-QACLRFADDERILVEPACGAALA 272
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
32-326 |
6.72e-27 |
|
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: 110.76 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNV-ILVKREDRQPVHSFKLRGAYAMMAGLTEEqKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAKEL-GVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTwVPPFDHPMVIAGQGTLALELLQQ-DAHL-DRVFVPVG 188
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIY-LSNSLNPYRLEGQKTIAFEIAEQlGWEVpDYVVVPVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQL--------MPqiKVIAVEAEDSACLKAALDAG----HPVDLPRVglFAEGVavkRIGD-----ET 251
Cdd:cd01563 181 NGGNITAIWKGFKELkelglidrLP--RMVGVQAEGAAPIVRAFKEGkddiEPVENPET--IATAI---RIGNpasgpKA 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131630 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNI-RGERLAHILSGanvnfHGLRY 326
Cdd:cd01563 254 LRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIdKGERVVVVLTG-----HGLKD 324
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
436-501 |
5.41e-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: 97.96 E-value: 5.41e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131630 436 YSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHE--PDFETRLNELGYDCHD 501
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDREdlAELKERLEALGYPYVD 68
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
341-408 |
6.61e-23 |
|
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153157 [Multi-domain] Cd Length: 68 Bit Score: 91.80 E-value: 6.61e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131630 341 LAVTIPEEKGSFLKFCQLLGG-RSVTEFNYRFADAKNACIFVGVRLSRGlEERKEILQMLNDGGYSVVD 408
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPpRNITEFHYRNQGGDEARVLVGIQVPDR-EDLAELKERLEALGYPYVD 68
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
31-301 |
3.59e-22 |
|
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: 98.35 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAgLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:COG0498 66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVS-LALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 -TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFdHPMVIAGQGTLALELLQQ-DAHLDRVFVP-- 186
Cdd:COG0498 145 eGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQlGRVPDWVVVPtg 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 187 -------VGGGGLAAGVAVLIKQLMpqiKVIAVEAEDSA-CLKA------------------ALDAGHPVDLPRVgLFAe 240
Cdd:COG0498 224 nggnilaGYKAFKELKELGLIDRLP---RLIAVQATGCNpILTAfetgrdeyeperpetiapSMDIGNPSNGERA-LFA- 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131630 241 gvaVKRIGDetfrlcqeyldDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIA 301
Cdd:COG0498 299 ---LRESGG-----------TAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLRE 345
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
1-314 |
1.25e-20 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 93.79 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 1 MADSQPLSGA------PEGAEYLRAVLRA-PVYeaaQVTPLQKMEKLSSRLD-NVILVKRED-RQPVHSFK-LRGAYAM- 69
Cdd:PRK08206 10 IADNKPYDGAdlpllsQEEAKKARAFHQSfPGY---APTPLVALPDLAAELGvGSILVKDESyRFGLNAFKaLGGAYAVa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 70 ---------------MAGLTEEQKAH-----GVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVL 129
Cdd:PRK08206 87 rllaeklgldiselsFEELTSGEVREklgdiTFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 130 LHGANFDEAKAKAIELSQQQGftWV------------PPFDhpmVIAGQGTLALELLQQ-DAHLDR---VFVPVGGGGLA 193
Cdd:PRK08206 167 ITDGNYDDSVRLAAQEAQENG--WVvvqdtawegyeeIPTW---IMQGYGTMADEAVEQlKEMGVPpthVFLQAGVGSLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 194 AGVAVLIKQLMPQ--IKVIAVEAEDSACL-KAALDaGHPV----DLPRV--GLfAEGvAVKRIGdetFRLCQEYLDDIIT 264
Cdd:PRK08206 242 GAVLGYFAEVYGEqrPHFVVVEPDQADCLyQSAVD-GKPVavtgDMDTImaGL-ACG-EPNPLA---WEILRNCADAFIS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16131630 265 VDSDAICAAMKDLFE----DVRAVAEPSGALALAGMkkYIALHNIRGERLAHIL 314
Cdd:PRK08206 316 CPDEVAALGMRILANplggDPPIVSGESGAVGLGAL--AALMTDPDYQELREKL 367
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
31-322 |
1.60e-17 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 83.72 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 31 VTPLQKmeklssRLDNVILvKREDRQPVHSFKLRGAYAMMAGLTEEqKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK08329 64 ITPTVK------RSIKVYF-KLDYLQPTGSFKDRGTYVTVAKLKEE-GINEVVIDSSGNAALSLALYSLSEGIKVHVFVS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEvlLHGANFDEAKA--KAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVG 188
Cdd:PRK08329 136 YNASKEKISLLSRLGAE--LHFVEGDRMEVheEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQL--MPQI----KVIAVEAE--DSACLKAAldaghpvdlpRVGLFAEGVAV---KRIgDETFRLCQE 257
Cdd:PRK08329 214 SGTLFLGIWKGFKELheMGEIskmpKLVAVQAEgyESLCKRSK----------SENKLADGIAIpepPRK-EEMLRALEE 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131630 258 YLDDIITVDSDAICAAMKDLFEDVRAVaEPSGALALAGMKKYIALHNIRGERLAHI-LSGANVNFH 322
Cdd:PRK08329 283 SNGFCISVGEEETRAALHWLRRMGFLV-EPTSAVALAAYWKLLEEGLIEGGSKVLLpLSGSGLKNL 347
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
32-367 |
1.39e-16 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 82.17 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKmEKLSSRLDNVILVKREDRQPVHSFKLRGA-YAMMAGLteEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLAtVAVSYGL--PYAANGFIVASDGNAAASVAAYSARAGKEAFVVVP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQdAHLDRVFVPVGGG 190
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEE-INPTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 191 GLAAGVAVLIKQL--------MPqiKVIAVEAEDSACLKAALdAGHPV---DLPRVGLFAEGVAVKRIGDETFRlcqEYL 259
Cdd:PRK05638 223 SYLYSIYKGFKELleigvieeIP--KLIAVQTERCNPIASEI-LGNKTkcnETKALGLYVKNPVMKEYVSEAIK---ESG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 260 DDIITVDSDAICAAMKDLFEDvRAVAEPSGALALAGMKKYIALHNI-RGERLAHILSGanvnfHGLRYVSErcelgEQRE 338
Cdd:PRK05638 297 GTAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTG-----SGLKGYGE-----GGRE 365
|
330 340
....*....|....*....|....*....
gi 16131630 339 ALlavTIPEEKGSFLKfcqLLGGRSVTEF 367
Cdd:PRK05638 366 KF---TIGGTKLEILK---ILSEREMYGY 388
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
32-299 |
4.71e-16 |
|
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: 78.71 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVIT-------ASAGNHAQGVAFSSARLGVK 104
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMI----EDAEKRGLLKpgttiiePTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 105 ALIVMPTATADIKVDAVRGFGGEVLL----HGANFDEAKAKAIELSQQQ-GFTWVPPFDHPM-VIAGQGTLALELLQQ-D 177
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETpNAFWLNQFENPAnPEAHYETTAPEIWEQlD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 178 AHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVdlprvglfaEGVAVKRIGDetfRLCQE 257
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKI---------EGIGAGFIPE---NLDRS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16131630 258 YLDDIITV-DSDAIcAAMKDLFEDVRAVAEPSGALALAGMKKY 299
Cdd:cd01561 227 LIDEVVRVsDEEAF-AMARRLAREEGLLVGGSSGAAVAAALKL 268
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
24-326 |
9.93e-14 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 72.73 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 24 PVYEAAQV-------TPLQKMEKLSSRLD-NVILVKREDRQPVHSFKLRGAyAMMAGLTEEQKAHGVITASAGNHAQGVA 95
Cdd:PRK08197 65 PVRDPEHIvslgegmTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGL-AVGVSRAKELGVKHLAMPTNGNAGAAWA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 96 FSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQ 175
Cdd:PRK08197 144 AYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 176 Q------DAhldrVFVPVGGGGLAAGVAVLIKQL---------MPqiKVIAVEAEDSACLKAALDAG--HPVDLPRVGLF 238
Cdd:PRK08197 224 QlgwrlpDV----ILYPTGGGVGLIGIWKAFDELealgwiggkRP--RLVAVQAEGCAPIVKAWEEGkeESEFWEDAHTV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 239 AEGVAV-KRIGDEtfrlcqEYLDDI-------ITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRG-ER 309
Cdd:PRK08197 298 AFGIRVpKALGDF------LVLDAVretggcaIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGdER 371
|
330
....*....|....*..
gi 16131630 310 LAHILSGAnvnfhGLRY 326
Cdd:PRK08197 372 VVLFNTGS-----GLKY 383
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
32-309 |
1.19e-12 |
|
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: 68.54 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVIT-------ASAGNHAQGVAFSSARLGVK 104
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMI----EDAEKRGLLKpggtiveATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 105 ALIVMPTATADIKVDAVRGFGGEVLL--HGANFDEAKAKAIELSQQQGFTWVP--------PFDHpmviagQGTLALELL 174
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAFWPnqfenpanPEAH------YETTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 175 QQ-DAHLD----------------RVFvpvgggglaagvavliKQLMPQIKVIAVEAEDSACLKAALDAGHPVdlprvgl 237
Cdd:COG0031 164 EQtDGKVDafvagvgtggtitgvgRYL----------------KERNPDIKIVAVEPEGSPLLSGGEPGPHKI------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 238 faEGVAVKRIGDeTFRLcqEYLDDIITV-DSDAIcAAMKDLfedvrAVAE-----PSGALALAGMKKYIAL----HNI-- 305
Cdd:COG0031 221 --EGIGAGFVPK-ILDP--SLIDEVITVsDEEAF-AMARRL-----AREEgilvgISSGAAVAAALRLAKRlgpgKTIvt 289
|
....*...
gi 16131630 306 ----RGER 309
Cdd:COG0031 290 ilpdSGER 297
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
32-160 |
2.11e-06 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 49.86 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVITA-------SAGNHAQGVAFSSARLGVK 104
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII----WDAEKRGLLKPggtivegTAGNTGIGLALVAAARGYK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131630 105 ALIVMPTATADIKVDAVRGFGGEVLL----------HGANFDEAKAKAIELSQQQGFTWVPPFDHP 160
Cdd:PRK10717 90 TVIVMPETQSQEKKDLLRALGAELVLvpaapyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNP 155
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
32-299 |
2.19e-06 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 49.73 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVilvkredrQPVHSFKLRGAYAMMAGLTEeQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPT 111
Cdd:PRK06450 59 TPLIKKGNIWFKLDFL--------NPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 112 ATADIKVDAVRGFGGEVL-LHGANFDEAKAkaielSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHL--DRVFVPVG 188
Cdd:PRK06450 130 TASGGKLKQIESYGAEVVrVRGSREDVAKA-----AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKipNYVFIPVS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 189 GGGLAAGVAVLIKQL--------MPqiKVIAVEAEDSACLKAALDaGHPVDLP-RVGLFAEGVAVKR--IGDETFRLCQE 257
Cdd:PRK06450 205 AGTLLLGVYSGFKHLldsgviseMP--KIVAVQTEQVSPLCAKFK-GISYTPPdKVTSIADALVSTRpfLLDYMVKALSE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16131630 258 YlDDIITVDSDAICAAMKDLfEDVRAVAEPSGALALAGMKKY 299
Cdd:PRK06450 282 Y-GECIVVSDNEIVEAWKEL-AKKGLLVEYSSATVYAAYKKY 321
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
32-130 |
5.36e-06 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 48.33 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGlTEE----QKAHGVITASAGNHAQGVAFSSARLGVKALI 107
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ-AEKrgeiKPGDTLIEATSGNTGIALAMIAAIKGYRMKL 91
|
90 100
....*....|....*....|...
gi 16131630 108 VMPTATADIKVDAVRGFGGEVLL 130
Cdd:PRK11761 92 IMPENMSQERRAAMRAYGAELIL 114
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
32-130 |
7.72e-06 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 48.03 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVITA--------SAGNHAQGVAFSSARLGV 103
Cdd:PLN02556 60 TPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMI----EDAEKKNLITPgkttliepTSGNMGISLAFMAAMKGY 135
|
90 100
....*....|....*....|....*..
gi 16131630 104 KALIVMPTATADIKVDAVRGFGGEVLL 130
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVL 162
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
433-505 |
7.78e-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: 44.08 E-value: 7.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131630 433 ERLYSFEFPESPGALLRFLNTLGTYwNISLFHYRSHGTDYGRVLAAFELGDHEPDFET---RLNELGYDCHDETNN 505
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPR-NITEFNYRYADEKDAHIFVGVSVANGAEELAElleDLKSAGYEVVDLSDD 75
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
32-186 |
8.79e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 47.78 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLD-NVILVKREDRQPVHSFKLRGAYAMMaGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMP 110
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHV-RRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131630 111 TATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQG-FTWVPPFDHPMV-IAGQGTLALELLQQDAHL-DRVFVP 186
Cdd:PRK06381 95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGiYDANPGSVNSVVdIEAYSAIAYEIYEALGDVpDAVAVP 173
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
32-186 |
3.21e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.98 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHS--FKLRG-AYAMMAGLteEQKAHGVITASA--GNHAQGVAFSSARLGVKAL 106
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGLALggNKTRKlEFLLADAL--AQGADTLITAGAiqSNHARQTAAAAAKLGLKCV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 107 IVM--PTATADIKVDAvRG-------FGGEVLL--HGANFDEAKAKAIELSQQQGFTwvppfdhPMVIAGQGT------- 168
Cdd:PRK03910 94 LLLenPVPTEAENYLA-NGnvllddlFGAEIHVvpAGTDMDAQLEELAEELRAQGRR-------PYVIPVGGSnalgalg 165
|
170 180
....*....|....*....|....*
gi 16131630 169 ---LALELLQQ----DAHLDRVFVP 186
Cdd:PRK03910 166 yvaCALEIAQQlaegGVDFDAVVVA 190
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
18-297 |
1.11e-04 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 44.22 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 18 RAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMA-----GLTEEQKAhGVITASAGNHAQ 92
Cdd:PLN00011 4 RCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKdaedkGLITPGKS-TLIEATAGNTGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 93 GVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLH----GANFDEAKAKAIeLSQQQGFTWVPPFDHPMVIAGQ-G 167
Cdd:PLN00011 83 GLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTdqsiGLKGMLEKAEEI-LSKTPGGYIPQQFENPANPEIHyR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 168 TLALELLQQDA-HLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVdlprvglfaEGVAVkr 246
Cdd:PLN00011 162 TTGPEIWRDSAgKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLI---------QGIGS-- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16131630 247 iGDETFRLCQEYLDDIITVDS-DAICAAMKDLFEDVRAVAEPSGALALAGMK 297
Cdd:PLN00011 231 -GIIPFNLDLTIVDEIIQVTGeEAIETAKLLALKEGLLVGISSGAAAAAALK 281
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
32-214 |
1.32e-04 |
|
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: 43.95 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNV--ILVKREDRQPVHSF---KLRgAYAMMAGLTEEQKAHGVITASA--GNHAQGVAFSSARLGVK 104
Cdd:cd06449 1 TPIQYLPRLSEHLGGKveIYAKRDDCNSGLAFggnKIR-KLEYLLPDALAKGADTLVTVGGiqSNHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 105 ALIVM--PTATADIKVDAV------RGFGGEVLLHGANFD----EAKAKAIELSQQQGFT--WVPP--FDHPMVIAGQGT 168
Cdd:cd06449 80 CVLVQenWVPYSDAVYDRVgnillsRIMGADVRLVSAGFDigirKSFEEAAEEVEAKGGKpyVIPAggSEHPLGGLGYVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131630 169 LALELLQQDAHL----DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEA 214
Cdd:cd06449 160 FVLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDA 209
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
32-130 |
1.66e-04 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 43.76 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAglteEQKAHGVITA--------SAGNHAQGVAFSSARLGV 103
Cdd:PLN02565 16 TPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMIT----DAEEKGLIKPgesvliepTSGNTGIGLAFMAAAKGY 91
|
90 100
....*....|....*....|....*..
gi 16131630 104 KALIVMPTATADIKVDAVRGFGGEVLL 130
Cdd:PLN02565 92 KLIITMPASMSLERRIILLAFGAELVL 118
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
32-297 |
4.96e-04 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 42.46 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAglTEEQKA------HGVITASAGNHAQGVAFSSARLGVKA 105
Cdd:PLN03013 124 TPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVT--DAEQKGfispgkSVLVEPTSGNTGIGLAFIAASRGYRL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 106 LIVMPTATADIKVDAVRGFGGEVLL----HGANFDEAKAKAIELSQQQGFTwVPPFDHPMVIAGQ-GTLALELLQQDAHL 180
Cdd:PLN03013 202 ILTMPASMSMERRVLLKAFGAELVLtdpaKGMTGAVQKAEEILKNTPDAYM-LQQFDNPANPKIHyETTGPEIWDDTKGK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 181 DRVFVPVGGGGLAAGVAVL-IKQLMPQIKVIAVEAEDSACLKAALDAGHPVdlprvglfaEGVAVKRIGDEtfrLCQEYL 259
Cdd:PLN03013 281 VDIFVAGIGTGGTITGVGRfIKEKNPKTQVIGVEPTESDILSGGKPGPHKI---------QGIGAGFIPKN---LDQKIM 348
|
250 260 270
....*....|....*....|....*....|....*....
gi 16131630 260 DDIITVDS-DAICAAMKDLFEDVRAVAEPSGALALAGMK 297
Cdd:PLN03013 349 DEVIAISSeEAIETAKQLALKEGLMVGISSGAAAAAAIK 387
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
28-186 |
2.51e-03 |
|
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: 40.16 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 28 AAQVTPLQKMEKLSSRLDNVILVKREDRqpVHSF----KLRG-----AYAmmagltEEQKAHGVITASAG--NHAQGVAF 96
Cdd:COG2515 8 AFLPTPLQPLPRLSAALGVELWIKRDDL--TGPAiggnKTRKleyllADA------LAQGADTLVTFGGAqsNHARATAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131630 97 SSARLGVKALIVMPTATADIKVDAV---RGFGGEVLLHGANF----DEAKAKAIELSQQQGFTwvppfdhPMVIAGQGT- 168
Cdd:COG2515 80 AAAKLGLKCVLVLRGEEPTPLNGNLlldRLLGAELHFVSRGEyrdrDEAMEAVAAELRARGGK-------PYVIPEGGSn 152
|
170 180 190
....*....|....*....|....*....|.
gi 16131630 169 ---------LALELLQQDAHL----DRVFVP 186
Cdd:COG2515 153 plgalgyveAAAELAAQLAELgvdfDYIVVA 183
|
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