|
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: 986.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 13 GAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQ 92
Cdd:PRK09224 2 GADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 93 GVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALE 172
Cdd:PRK09224 82 GVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAME 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 173 LLQQDSH-LDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDET 251
Cdd:PRK09224 162 ILQQHPHpLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEET 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSGANVNFHGLRYVSERC 331
Cdd:PRK09224 242 FRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAERA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 332 ELGEQREALLAVTIPEEKGSFLKFCQLLGGRMVTEFNYRFADAKNACIFVGVRVSQGLEERKEIITQLCDGGYSVVDLSD 411
Cdd:PRK09224 322 ELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSRGQEERAEIIAQLRAHGYPVVDLSD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 412 DEMAKLHVRYMVGGRPSKPLQERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHE-PDFET 490
Cdd:PRK09224 402 DELAKLHVRYMVGGRPPKPLDERLYRFEFPERPGALLKFLSTLGTHWNISLFHYRNHGADYGRVLAGFQVPDADePEFEA 481
|
490 500
....*....|....*....|...
gi 16767181 491 RLHELGYECHDESNNPAFRFFLA 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: 880.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 15 EYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:TIGR01124 1 DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 95 AFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:TIGR01124 81 AFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQD-SHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFR 253
Cdd:TIGR01124 161 RQVaNPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 254 LCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSGANVNFHGLRYVSERCEL 333
Cdd:TIGR01124 241 LCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 334 GEQREALLAVTIPEEKGSFLKFCQLLGGRMVTEFNYRFADAKNACIFVGVRVSQGlEERKEIITQLCDGGYSVVDLSDDE 413
Cdd:TIGR01124 321 GEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNP-QERQEILARLNDGGYSVVDLTDDE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 414 MAKLHVRYMVGGRPSKPLQERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHEPD-FETRL 492
Cdd:TIGR01124 400 LAKLHVRYMVGGRPPHVENERLYSFEFPERPGALLRFLNTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDqFEQFL 479
|
490 500
....*....|....*....|
gi 16767181 493 HELGYECHDESNNPAFRFFL 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: 656.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 1 MAESQPLSVAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAH 80
Cdd:PRK12483 7 VSPTTIAPRAALLADYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 81 GVITASAGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHP 160
Cdd:PRK12483 87 GVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 161 MVIAGQGTLALELL-QQDSHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFA 239
Cdd:PRK12483 167 DVIAGQGTVAMEILrQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 240 EGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSGANV 319
Cdd:PRK12483 247 DGVAVAQIGEHTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 320 NFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRMVTEFNYRFADAKNACIFVGVRVSQGLEERKEIITQL 399
Cdd:PRK12483 327 NFDRLRHVAERAELGEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDPRAQLLASL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 400 CDGGYSVVDLSDDEMAKLHVRYMVGGRPSKPLQERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAF 479
Cdd:PRK12483 407 RAQGFPVLDLTDDELAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLGPRWNISLFHYRNHGAADGRVLAGL 486
|
490 500 510
....*....|....*....|....*....|....*
gi 16767181 480 ELGDHE-PDFETRLHELGYECHDESNNPAFRFFLA 513
Cdd:PRK12483 487 QVPEDErAALDAALAALGYPYWEETGNPAYRLFLG 521
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
10-512 |
3.44e-164 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 477.88 E-value: 3.44e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 10 APEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGN 89
Cdd:PLN02550 88 IPEAMEYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 90 HAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTL 169
Cdd:PLN02550 168 HAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 170 ALELLQQ-DSHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIG 248
Cdd:PLN02550 248 GMEIVRQhQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVG 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 249 DETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSGANVNFHGLRYVS 328
Cdd:PLN02550 328 EETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVT 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 329 ERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRMVTEFNYRFADAKNACIF--VGVRVSQGLEERKEiitQLCDGGYSV 406
Cdd:PLN02550 408 ELADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLysVGVHTEQELQALKK---RMESAQLRT 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 407 VDLSDDEMAKLHVRYMVGGRPSKPlQERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHEP 486
Cdd:PLN02550 485 VNLTSNDLVKDHLRYLMGGRAIVK-DELLYRFVFPERPGALMKFLDAFSPRWNISLFHYRGQGETGANVLVGIQVPPEEM 563
|
490 500
....*....|....*....|....*..
gi 16767181 487 D-FETRLHELGYECHDESNNPAFRFFL 512
Cdd:PLN02550 564 QeFKSRANALGYEYQDECDNEAFQLLM 590
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
22-336 |
1.30e-143 |
|
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: 415.59 E-value: 1.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 22 RAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARL 101
Cdd:COG1171 15 AARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 102 GVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLD 181
Cdd:COG1171 95 GIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPDLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 182 RVFVPvgggglaagvavlI-------------KQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIG 248
Cdd:COG1171 175 AVFVP-------------VggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 249 DETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYiaQHNIRGERLAHVLSGANVNFHGLRYVS 328
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG--KERLKGKRVVVVLSGGNIDPDRLAEIL 319
|
....*...
gi 16767181 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 |
9.21e-139 |
|
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: 402.25 E-value: 9.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:cd01562 1 LEDILAAAARIKPVVrrTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 95 AFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQDSHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFRL 254
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16767181 255 CQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHniRGERLAHVLSGANVN 320
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
25-330 |
4.92e-100 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 307.50 E-value: 4.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 25 VYEAAQV-------TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFS 97
Cdd:PRK08639 12 IDKAAKRlkdvvpeTPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 98 SARLGVKSLIVMPKATADIKVDAVRGFGG---EVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:PRK08639 92 CRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQDSHL---DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDET 251
Cdd:PRK08639 172 EQLEKEgspDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16767181 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQhnIRGERLAHVLSGANVNFHGLRYVSER 330
Cdd:PRK08639 252 FEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDE--IKGKTVVCVISGGNNDIERMPEIKER 328
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
32-407 |
6.52e-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: 267.38 E-value: 6.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMPK 111
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVGGGG 191
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 192 LAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAIC 271
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 272 AAMKDLFEDVRAVAEPSGALALAGMKKyiAQHNIRGERLAHVLSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGS 351
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLE--QKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16767181 352 FLKFCQLL---GGRMVTEFNYRFA---DAKNACIFVGVRVsQGLEERKEIITQLCDGGYSVV 407
Cdd:TIGR01127 319 LYHLLESIaeaRANIVKIDHDRLSkeiPPGFAMVEITLET-RGKEHLDEILKILRDMGYNFY 379
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
29-339 |
4.70e-82 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 258.13 E-value: 4.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIV 108
Cdd:PRK08638 25 IRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALLGIDGKVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 109 MPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVG 188
Cdd:PRK08638 105 MPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIVPIG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSD 268
Cdd:PRK08638 185 GGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSED 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16767181 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSGANVNfhgLRYVSERCELGEQREA 339
Cdd:PRK08638 265 EIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVD---LSRVSQITGHVVAADA 332
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
32-316 |
2.23e-72 |
|
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: 231.82 E-value: 2.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMPK 111
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQ-QGFTWVPPFDHPMVIAGQGTLALELL-QQDSHLDRVFVPVGG 189
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILeQLGGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 190 GGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRI-GDETFRLCQEYLDDIITVDSD 268
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16767181 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRGERLAHVLSG 316
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
32-406 |
6.08e-71 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 231.71 E-value: 6.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMPK 111
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 112 ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVGGGG 191
Cdd:PRK07334 104 FTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 192 LAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALeagHPVDLPRVG-LFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAI 270
Cdd:PRK07334 184 LISGMATAAKALKPDIEIIGVQTELYPSMYAAI---KGVALPCGGsTIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 271 CAAMKDLFEDVRAVAEPSGALALAGMKKYiaQHNIRGERLAHVLSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKG 350
Cdd:PRK07334 261 EQAVSLLLEIEKTVVEGAGAAGLAALLAY--PERFRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLRVDIRDRPG 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16767181 351 SFLKFCQLLG--GRMVTEFNYR--FAD--AKNACIFVgVRVSQGLEERKEIITQLCDGGYSV 406
Cdd:PRK07334 339 ALARVTALIGeaGANIIEVSHQrlFTDlpAKGAELEL-VIETRDAAHLQEVIAALRAAGFEA 399
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
17-319 |
2.48e-68 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 222.15 E-value: 2.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:PRK07476 3 LADIYRARRRIAGRVrrTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 95 AFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:PRK07476 83 AYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQDSHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAE----GVAVK-RIgd 249
Cdd:PRK07476 163 EALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLDnRY-- 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16767181 250 eTFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGmkkyIAQHNI--RGERLAHVLSGANV 319
Cdd:PRK07476 241 -TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAA----LLAGKIaaRDGPIVVVVSGANI 307
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
31-325 |
6.04e-68 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 221.10 E-value: 6.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 KATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVGGG 190
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 191 GLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVA--VKRiGDETFRLCQEYLDDIITVDSD 268
Cdd:PRK06815 180 GLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVEP-GAITFPLCQQLIDQKVLVSEE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16767181 269 AICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHniRGERLAHVLSGANVNFHGLR 325
Cdd:PRK06815 259 EIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY--QGKKVAVVLCGKNIVLEKYL 313
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
29-320 |
8.79e-64 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 210.26 E-value: 8.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIV 108
Cdd:PRK07048 22 AHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 109 MPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVG 188
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALFVCLG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAG--HPVDLPRVglFAEGVAVKRIGDETFRLCQEYLDDIITVD 266
Cdd:PRK07048 182 GGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGeiVHIDTPRT--IADGAQTQHLGNYTFPIIRRLVDDIVTVS 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16767181 267 SDAICAAMKDLFEDVRAVAEPSGALALAGMKKyiAQHNIRGERLAHVLSGANVN 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 |
4.61e-62 |
|
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: 203.13 E-value: 4.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHG--VITASAGNHAQGVAFSSARLGVKSLIVM 109
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 110 PKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQ-GFTWVPPFDHPMVIAGQGTLALELLQQ--DSHLDRVFVP 186
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQlgGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 187 VGGGGLAAGVAVLIKQLMPQIKVIAVEAEdsaclkaaleaghpvdlprvglfaegvavkrigdetfrlcqeylddIITVD 266
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16767181 267 SDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNiRGERLAHVLSG 316
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG-KGKTVVVILTG 243
|
|
| PLN02970 |
PLN02970 |
serine racemase |
29-324 |
2.80e-60 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 201.45 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 29 AQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIV 108
Cdd:PLN02970 25 IHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 109 MPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVG 188
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPIS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQLMPQIKVIAVE---AEDSAclkAALEAGHPVDLPRVGLFAEGVAVkRIGDETFRLCQEYLDDIITV 265
Cdd:PLN02970 185 GGGLISGIALAAKAIKPSIKIIAAEpkgADDAA---QSKAAGEIITLPVTNTIADGLRA-SLGDLTWPVVRDLVDDVITV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16767181 266 DSDAICAAMKDLFEDVRAVAEPSGALALAGM------KKYIAQHnirGERLAHVLSGANVNFHGL 324
Cdd:PLN02970 261 DDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsdsfrSNPAWKG---CKNVGIVLSGGNVDLGVL 322
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
48-320 |
1.90e-53 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 182.85 E-value: 1.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 48 ILVKREDRQPVHSFKLRGAYAMMagLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGE 127
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 128 VLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVGGGGLAAGVAVLIKqlmPQI 207
Cdd:PRK08246 117 VVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFE---GRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 208 KVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEP 287
Cdd:PRK08246 194 RVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEP 273
|
250 260 270
....*....|....*....|....*....|....*
gi 16767181 288 SGALALAGM--KKYIAQhniRGERLAHVLSGANVN 320
Cdd:PRK08246 274 GAATALAALlsGAYVPA---PGERVAVVLCGANTD 305
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
17-320 |
2.85e-53 |
|
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: 182.74 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 17 LRAVLRAPVYEAAQV--TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGV 94
Cdd:TIGR02991 3 LQDIERAAARISGRVeeTPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 95 AFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELL 174
Cdd:TIGR02991 83 AYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQDSHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAE--GVAVKRIGDETF 252
Cdd:TIGR02991 163 EQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVTF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16767181 253 RLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMkkyIAQHNIRGERLAHVLSGANVN 320
Cdd:TIGR02991 243 AMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL---LAGKIKNPGPCAVIVSGRNID 307
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
22-321 |
1.02e-52 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 181.35 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 22 RAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQ-KAHGVITASAGNHAQGVAFSSAR 100
Cdd:PRK06110 12 AAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 101 LGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFdHPMVIAGQGTLALELLQQDSHL 180
Cdd:PRK06110 92 HGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 181 DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVkRIGD-ETFRLCQEYL 259
Cdd:PRK06110 171 DVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMAC-RTPDpEALEVIRAGA 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16767181 260 DDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQhnIRGERLAHVLSGANVNF 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 |
5.30e-46 |
|
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: 155.40 E-value: 5.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 338 EALLAVTIPEEKGSFLKFCQLLGGRMVTEFNYRFADAKNACIFVGVRVSQGLEERKEIITQLCDGGYSVVDLSDDEMAKL 417
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAEELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 16767181 418 HVRYM 422
Cdd:cd04906 81 HLRYM 85
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
3-320 |
7.56e-44 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 158.64 E-value: 7.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 3 ESQPLSVAPEGAEYLRAVLRAPVYEAAqvTPLQKMEKLSsrldnvILVKREDRQPVHSFKLRGAY-AMMAGLtEEQKAHG 81
Cdd:PRK08813 13 EPDVGDVAVSVADVLAAQARLRRYLSP--TPLHYAERFG------VWLKLENLQRTGSYKVRGALnALLAGL-ERGDERP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 82 VITASAGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPM 161
Cdd:PRK08813 84 VICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 162 VIAGQGTLALELLQQDShlDRVFVPVGGGGLAAGVAVLIKQlmPQIKVIAVEAEDSACLKAALEaGHPVDLPRVGLFAEG 241
Cdd:PRK08813 164 VIAGQGTVGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16767181 242 VAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAgmkkyiAQHNIRGERLAHVLSGANVN 320
Cdd:PRK08813 239 VKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALA------AGRRVSGKRKCAVVSGGNID 311
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
32-320 |
1.87e-41 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 151.46 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQK-AHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 KATADIKVDAVRGFGGEVLLHGANfDEAKAKAIElAQQQGFTWVPPFDHPMVIAGQGTLALELLQQ-DSHLDRVFVPVGG 189
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILTNTR-QEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQlGFSPDAIFASCGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 190 GGLAAGVAVLIKQLMPQIKVIAVE---AEDSAclkAALEAGHPVDLPRV-GLFAEGVAVKRIGDETFRLCQEyLDDIITV 265
Cdd:PRK06608 182 GGLISGTYLAKELISPTSLLIGSEplnANDAY---LSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKK-LDDFYLV 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16767181 266 DSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNiRGERLAHVLSGANVN 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 |
1.07e-37 |
|
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: 133.06 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 433 ERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHE-PDFETRLHELGYECHDESNNPAFRFF 511
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNELLPKWNITLFHYRNQGSDYGRVLVGIQVPDADlDELKERLDALGYPYQEETDNPAYKLF 80
|
.
gi 16767181 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 |
4.05e-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: 132.02 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 424 GGRPSKPLQERLYSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHE--PDFETRLHELGYECHD 501
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNNITLFEYRKHGDKNGCVLVGIELSQAEdlDEFIERLNKLGYDYED 80
|
90
....*....|.
gi 16767181 502 ESNNPAFRFFL 512
Cdd:pfam00585 81 LSDNEAAYEHL 91
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
329-419 |
1.22e-35 |
|
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: 127.78 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 329 ERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRM-VTEFNYRFADAKNACIFVGVRVSQGlEERKEIITQLCDGGYSVV 407
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNnITLFEYRKHGDKNGCVLVGIELSQA-EDLDEFIERLNKLGYDYE 79
|
90
....*....|..
gi 16767181 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 |
6.61e-29 |
|
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: 116.24 E-value: 6.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRG--AYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIV 108
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGigHLCQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 109 MPKATADIKVDAVRGFGGEVLLHGAN-FDEAKAKAIELAQQQ-GFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVP 186
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 187 VGGGGLAAGVAVLIKQL----MPQIKVIAVEAEDSACLKAALEAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYldDI 262
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLerngWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEH--NI 238
|
250 260 270
....*....|....*....|....*....|....*
gi 16767181 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 |
2.34e-28 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 115.00 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNV-ILVKREDRQPVHSFKLRGAYAMMAGLTEEqKAHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAKEL-GVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 KATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTwVPPFDHPMVIAGQGTLALELLQQ-DSHL-DRVFVPVG 188
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIY-LSNSLNPYRLEGQKTIAFEIAEQlGWEVpDYVVVPVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQL--------MPqiKVIAVEAEDSACLKAALEAG----HPVDLPRVglFAEGVavkRIGD-----ET 251
Cdd:cd01563 181 NGGNITAIWKGFKELkelglidrLP--RMVGVQAEGAAPIVRAFKEGkddiEPVENPET--IATAI---RIGNpasgpKA 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16767181 252 FRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNI-RGERLAHVLSGanvnfHGLRY 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 |
1.43e-24 |
|
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: 96.81 E-value: 1.43e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16767181 436 YSFEFPESPGALLKFLHTLGTHWNISLFHYRSHGTDYGRVLAAFELGDHE--PDFETRLHELGYECHD 501
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRNITEFHYRNQGGDEARVLVGIQVPDREdlAELKERLEALGYPYVD 68
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
31-309 |
1.35e-23 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 102.59 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 31 VTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAgLTEEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:COG0498 66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVS-LALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 K-ATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFdHPMVIAGQGTLALELLQQ-DSHLDRVFVP-- 186
Cdd:COG0498 145 EgKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQlGRVPDWVVVPtg 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 187 -------VGGGGLAAGVAVLIKQLMpqiKVIAVEAEDSACLKAALEAGH-------------------PVDLPRVgLFAe 240
Cdd:COG0498 224 nggnilaGYKAFKELKELGLIDRLP---RLIAVQATGCNPILTAFETGRdeyeperpetiapsmdignPSNGERA-LFA- 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 241 gvaVKRIGDetfrlcqeyldDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNI-RGER 309
Cdd:COG0498 299 ---LRESGG-----------TAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIdPDEP 354
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
341-408 |
5.61e-22 |
|
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: 89.49 E-value: 5.61e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16767181 341 LAVTIPEEKGSFLKFCQLLGGRM-VTEFNYRFADAKNACIFVGVRVSQGlEERKEIITQLCDGGYSVVD 408
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGPPRnITEFHYRNQGGDEARVLVGIQVPDR-EDLAELKERLEALGYPYVD 68
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
26-295 |
1.49e-21 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 96.49 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 26 YEAAQVTPLQKMEKLSSRLD-NVILVKRED-RQPVHSFK-LRGAYAM----------------MAGLTEEQKAH-----G 81
Cdd:PRK08206 39 FPGYAPTPLVALPDLAAELGvGSILVKDESyRFGLNAFKaLGGAYAVarllaeklgldiselsFEELTSGEVREklgdiT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 82 VITASAGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGftWV------- 154
Cdd:PRK08206 119 FATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENG--WVvvqdtaw 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 155 -----PPFDhpmVIAGQGTLALELLQQ-DSHLDR---VFVPVGGGGLAAGVAVLIKQLMPQ--IKVIAVEAEDSACLKAA 223
Cdd:PRK08206 197 egyeeIPTW---IMQGYGTMADEAVEQlKEMGVPpthVFLQAGVGSLAGAVLGYFAEVYGEqrPHFVVVEPDQADCLYQS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 224 LEAGHPV----DLPRV--GLfAEGvAVKRIGdetFRLCQEYLDDIITVDSDAICAAMKDLFE----DVRAVAEPSGALAL 293
Cdd:PRK08206 274 AVDGKPVavtgDMDTImaGL-ACG-EPNPLA---WEILRNCADAFISCPDEVAALGMRILANplggDPPIVSGESGAVGL 348
|
..
gi 16767181 294 AG 295
Cdd:PRK08206 349 GA 350
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
30-176 |
1.95e-19 |
|
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.
Pssm-ID: 274631 Cd Length: 396 Bit Score: 90.16 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 30 QVTPLQKMEKLSSRLD-NVILVKRED-RQPVHSFK-LRGAYAM----------------MAGLTEEQ--KAHGVI---TA 85
Cdd:TIGR03528 40 QPTPLAELDNLAKHLGvGSILVKDESyRFGLNAFKvLGGSYAIgkylaeklgkdiselsFEKLKSNEirEKLGDItfvTA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 86 SAGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGF------TWVPPFDH 159
Cdd:TIGR03528 120 TDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGAECTITDLNYDDAVRLAWKMAQENGWvmvqdtAWEGYEKI 199
|
170
....*....|....*...
gi 16767181 160 PMVI-AGQGTLALELLQQ 176
Cdd:TIGR03528 200 PTWImQGYGTLALEALEQ 217
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
32-303 |
9.37e-18 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 83.72 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVIT-------ASAGNHAQGVAFSSARLGVK 104
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMI----EDAEKRGLLKpgttiiePTSGNTGIGLAMVAAAKGYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 105 SLIVMPKATADIKVDAVRGFGGEVLL----HGANFDEAKAKAIELAQQQ-GFTWVPPFDHPM-VIAGQGTLALELLQQ-D 177
Cdd:cd01561 79 FIIVMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETpNAFWLNQFENPAnPEAHYETTAPEIWEQlD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 178 SHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALEAGHPVdlprvglfaEGVAVKRIGDetfRLCQE 257
Cdd:cd01561 159 GKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKI---------EGIGAGFIPE---NLDRS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16767181 258 YLDDIITV-DSDAIcAAMKDLFEDVRAVAEPSGALALAGMKKYIAQH 303
Cdd:cd01561 227 LIDEVVRVsDEEAF-AMARRLAREEGLLVGGSSGAAVAAALKLAKRL 272
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
32-325 |
2.86e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 84.09 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKmEKLSSRLDNVILVKREDRQPVHSFKLRGA-YAMMAGLteEQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLAtVAVSYGL--PYAANGFIVASDGNAAASVAAYSARAGKEAFVVVP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 KATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQ--DSHldrVFVPVG 188
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEinPTH---VIVPTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQL--------MPqiKVIAVEAEdsACLKAALEA-GHPV---DLPRVGLFAEGVAVKRIGDETFRlcq 256
Cdd:PRK05638 221 SGSYLYSIYKGFKELleigvieeIP--KLIAVQTE--RCNPIASEIlGNKTkcnETKALGLYVKNPVMKEYVSEAIK--- 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 257 EYLDDIITVDSDAICAAMKDLFEDvRAVAEPSGALALAGMKKYIAQHNI-RGERLAHVLSGanvnfHGLR 325
Cdd:PRK05638 294 ESGGTAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIeKGDKVVLVVTG-----SGLK 357
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
31-322 |
1.60e-16 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 81.03 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 31 VTPLQKmeklssRLDNVILvKREDRQPVHSFKLRGAYAMMAGLTEEqKAHGVITASAGNHAQGVAFSSARLGVKSLIVMP 110
Cdd:PRK08329 64 ITPTVK------RSIKVYF-KLDYLQPTGSFKDRGTYVTVAKLKEE-GINEVVIDSSGNAALSLALYSLSEGIKVHVFVS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 111 KATADIKVDAVRGFGGEvlLHGANFDEAKA--KAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHLDRVFVPVG 188
Cdd:PRK08329 136 YNASKEKISLLSRLGAE--LHFVEGDRMEVheEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQL--MPQI----KVIAVEAE--DSACLKAAleaghpvdlpRVGLFAEGVAV---KRIgDETFRLCQE 257
Cdd:PRK08329 214 SGTLFLGIWKGFKELheMGEIskmpKLVAVQAEgyESLCKRSK----------SENKLADGIAIpepPRK-EEMLRALEE 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16767181 258 YLDDIITVDSDAICAAMKDLFEDVRAVaEPSGALALAGMKKYIAQHNIRGERLAHV-LSGANVNFH 322
Cdd:PRK08329 283 SNGFCISVGEEETRAALHWLRRMGFLV-EPTSAVALAAYWKLLEEGLIEGGSKVLLpLSGSGLKNL 347
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
31-176 |
1.87e-16 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 81.09 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 31 VTPLQKMEKLSSRLD-NVILVKRED-RQPVHSFK-LRGAYAM----------------MAGLTEEQ-----KAHGVITAS 86
Cdd:TIGR01747 22 PTPLCALDHLANLLGlKKILVKDESkRFGLNAFKmLGGSYAIaqylaeklhldietlsFEHLKNDAigekmGQATFATAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 87 AGNHAQGVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQ-----------QGFTWVP 155
Cdd:TIGR01747 102 DGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQMAQQhgwvvvqdtawEGYEKIP 181
|
170 180
....*....|....*....|.
gi 16767181 156 PFdhpmVIAGQGTLALELLQQ 176
Cdd:TIGR01747 182 TW----IMQGYATLADEAVEQ 198
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
24-326 |
7.79e-16 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 79.27 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 24 PVYEAAQV-------TPLQKMEKLSSRLD-NVILVKREDRQPVHSFKLRGAyAMMAGLTEEQKAHGVITASAGNHAQGVA 95
Cdd:PRK08197 65 PVRDPEHIvslgegmTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGL-AVGVSRAKELGVKHLAMPTNGNAGAAWA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 96 FSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQGFTWVPPFDHPMVIAGQGTLALELLQ 175
Cdd:PRK08197 144 AYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 176 QdshL-----DRVFVPVGGGGLAAGVAVLIKQL---------MPqiKVIAVEAEDSACLKAALEAG--HPVDLPRVGLFA 239
Cdd:PRK08197 224 Q---LgwrlpDVILYPTGGGVGLIGIWKAFDELealgwiggkRP--RLVAVQAEGCAPIVKAWEEGkeESEFWEDAHTVA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 240 EGVAV-KRIGDEtfrlcqEYLDDI-------ITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIAQHNIRG-ERL 310
Cdd:PRK08197 299 FGIRVpKALGDF------LVLDAVretggcaIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGdERV 372
|
330
....*....|....*.
gi 16767181 311 AHVLSGAnvnfhGLRY 326
Cdd:PRK08197 373 VLFNTGS-----GLKY 383
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
32-309 |
5.03e-15 |
|
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: 75.86 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVIT-------ASAGNHAQGVAFSSARLGVK 104
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMI----EDAEKRGLLKpggtiveATSGNTGIGLAMVAAAKGYR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 105 SLIVMPKATADIKVDAVRGFGGEVLL--HGANFDEAKAKAIELAQQQGFTWVP--------PFDHpmviagQGTLALELL 174
Cdd:COG0031 90 LILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAFWPnqfenpanPEAH------YETTGPEIW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 175 QQ-DSHLD----------------RVFvpvgggglaagvavliKQLMPQIKVIAVEAEDSACLKAALEAGHPVdlprvgl 237
Cdd:COG0031 164 EQtDGKVDafvagvgtggtitgvgRYL----------------KERNPDIKIVAVEPEGSPLLSGGEPGPHKI------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 238 faEGVAVKRIGDeTFRLcqEYLDDIITV-DSDAIcAAMKDLfedvrAVAE-----PSGALALAGMKKYIAQ----HNI-- 305
Cdd:COG0031 221 --EGIGAGFVPK-ILDP--SLIDEVITVsDEEAF-AMARRL-----AREEgilvgISSGAAVAAALRLAKRlgpgKTIvt 289
|
....*...
gi 16767181 306 ----RGER 309
Cdd:COG0031 290 ilpdSGER 297
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
32-299 |
6.21e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.27 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVilvkredrQPVHSFKLRGAYAMMAGLTEeQKAHGVITASAGNHAQGVAFSSARLGVKSLIVMPK 111
Cdd:PRK06450 59 TPLIKKGNIWFKLDFL--------NPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 112 ATADIKVDAVRGFGGEVL-LHGANFDEAKAkaielAQQQGFTWVPPFDHPMVIAGQGTLALELLQQDSHL--DRVFVPVG 188
Cdd:PRK06450 130 TASGGKLKQIESYGAEVVrVRGSREDVAKA-----AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKipNYVFIPVS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 189 GGGLAAGVAVLIKQL--------MPqiKVIAVEAEDSACLKAALEaGHPVDLP-RVGLFAEGVAVKR--IGDETFRLCQE 257
Cdd:PRK06450 205 AGTLLLGVYSGFKHLldsgviseMP--KIVAVQTEQVSPLCAKFK-GISYTPPdKVTSIADALVSTRpfLLDYMVKALSE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16767181 258 YlDDIITVDSDAICAAMKDLfEDVRAVAEPSGALALAGMKKY 299
Cdd:PRK06450 282 Y-GECIVVSDNEIVEAWKEL-AKKGLLVEYSSATVYAAYKKY 321
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
32-160 |
1.53e-06 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 50.24 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVITA-------SAGNHAQGVAFSSARLGVK 104
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII----WDAEKRGLLKPggtivegTAGNTGIGLALVAAARGYK 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16767181 105 SLIVMPKATADIKVDAVRGFGGEVLL----------HGANFDEAKAKAIELAQQQGFTWVPPFDHP 160
Cdd:PRK10717 90 TVIVMPETQSQEKKDLLRALGAELVLvpaapyanpnNYVKGAGRLAEELVASEPNGAIWANQFDNP 155
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
32-186 |
2.50e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 49.32 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLD-NVILVKREDRQPVHSFKLRGAY-----AMMAGLTeeqkahGVITASAGNHAQGVAFSSARLGVKS 105
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEahvrrAMRLGYS------GITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 106 LIVMPKATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELAQQQG-FTWVPPFDHPMV-IAGQGTLALELLQQDSHL-DR 182
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGiYDANPGSVNSVVdIEAYSAIAYEIYEALGDVpDA 169
|
....
gi 16767181 183 VFVP 186
Cdd:PRK06381 170 VAVP 173
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
433-505 |
5.06e-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: 44.46 E-value: 5.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16767181 433 ERLYSFEFPESPGALLKFLHTLGTHwNISLFHYRSHGTDYGRVLAAFELGDHEPDFET---RLHELGYECHDESNN 505
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPR-NITEFNYRYADEKDAHIFVGVSVANGAEELAElleDLKSAGYEVVDLSDD 75
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
32-130 |
5.81e-06 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 47.95 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGlTEE----QKAHGVITASAGNHAQGVAFSSARLGVKSLI 107
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ-AEKrgeiKPGDTLIEATSGNTGIALAMIAAIKGYRMKL 91
|
90 100
....*....|....*....|...
gi 16767181 108 VMPKATADIKVDAVRGFGGEVLL 130
Cdd:PRK11761 92 IMPENMSQERRAAMRAYGAELIL 114
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
32-130 |
1.59e-05 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 47.26 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMagltEEQKAHGVITA--------SAGNHAQGVAFSSARLGV 103
Cdd:PLN02556 60 TPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMI----EDAEKKNLITPgkttliepTSGNMGISLAFMAAMKGY 135
|
90 100
....*....|....*....|....*..
gi 16767181 104 KSLIVMPKATADIKVDAVRGFGGEVLL 130
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVL 162
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
32-186 |
7.51e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 44.82 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHS--FKLRG-AYAMMAGLteEQKAHGVITASA--GNHAQGVAFSSARLGVKSL 106
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGLALggNKTRKlEFLLADAL--AQGADTLITAGAiqSNHARQTAAAAAKLGLKCV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 107 IVMPKATADikVDAVRGFGGEVLL------------HGANFDEAKAKAIELAQQQGFTwvppfdhPMVIAGQGT------ 168
Cdd:PRK03910 94 LLLENPVPT--EAENYLANGNVLLddlfgaeihvvpAGTDMDAQLEELAEELRAQGRR-------PYVIPVGGSnalgal 164
|
170 180
....*....|....*....|....*.
gi 16767181 169 ----LALELLQQ----DSHLDRVFVP 186
Cdd:PRK03910 165 gyvaCALEIAQQlaegGVDFDAVVVA 190
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
32-130 |
3.00e-04 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 42.99 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAglteEQKAHGVITA--------SAGNHAQGVAFSSARLGV 103
Cdd:PLN02565 16 TPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMIT----DAEEKGLIKPgesvliepTSGNTGIGLAFMAAAKGY 91
|
90 100
....*....|....*....|....*..
gi 16767181 104 KSLIVMPKATADIKVDAVRGFGGEVLL 130
Cdd:PLN02565 92 KLIITMPASMSLERRIILLAFGAELVL 118
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
18-130 |
4.75e-04 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 42.30 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 18 RAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMA-----GLTEEQKAhGVITASAGNHAQ 92
Cdd:PLN00011 4 RCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKdaedkGLITPGKS-TLIEATAGNTGI 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 16767181 93 GVAFSSARLGVKSLIVMPKATADIKVDAVRGFGGEVLL 130
Cdd:PLN00011 83 GLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHL 120
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
32-214 |
4.88e-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: 42.41 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNV--ILVKREDRQPVHSF---KLRgAYAMMAGLTEEQKAHGVITASA--GNHAQGVAFSSARLGVK 104
Cdd:cd06449 1 TPIQYLPRLSEHLGGKveIYAKRDDCNSGLAFggnKIR-KLEYLLPDALAKGADTLVTVGGiqSNHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 105 SLIVMPK--ATADIKVDAV------RGFGGEVLLHGANFD----EAKAKAIELAQQQGFT--WVPP--FDHPMVIAGQGT 168
Cdd:cd06449 80 CVLVQENwvPYSDAVYDRVgnillsRIMGADVRLVSAGFDigirKSFEEAAEEVEAKGGKpyVIPAggSEHPLGGLGYVG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16767181 169 LALELLQQDSHL----DRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEA 214
Cdd:cd06449 160 FVLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDA 209
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
32-297 |
5.56e-04 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 42.46 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 32 TPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAglTEEQKA------HGVITASAGNHAQGVAFSSARLGVKS 105
Cdd:PLN03013 124 TPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVT--DAEQKGfispgkSVLVEPTSGNTGIGLAFIAASRGYRL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 106 LIVMPKATADIKVDAVRGFGGEVLLH--GANFDEAKAKAIELAQQQGFTW-VPPFDHPMVIAGQ-GTLALELLQQDSHLD 181
Cdd:PLN03013 202 ILTMPASMSMERRVLLKAFGAELVLTdpAKGMTGAVQKAEEILKNTPDAYmLQQFDNPANPKIHyETTGPEIWDDTKGKV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 182 RVFVPVGGGGLAAGVAVL-IKQLMPQIKVIAVEAEDSACLKAALEAGHPVdlprvglfaEGVAVKRIGDEtfrLCQEYLD 260
Cdd:PLN03013 282 DIFVAGIGTGGTITGVGRfIKEKNPKTQVIGVEPTESDILSGGKPGPHKI---------QGIGAGFIPKN---LDQKIMD 349
|
250 260 270
....*....|....*....|....*....|....*...
gi 16767181 261 DIITVDS-DAICAAMKDLFEDVRAVAEPSGALALAGMK 297
Cdd:PLN03013 350 EVIAISSeEAIETAKQLALKEGLMVGISSGAAAAAAIK 387
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
28-186 |
1.26e-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: 40.93 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 28 AAQVTPLQKMEKLSSRLDNVILVKREDRqpVHSF----KLRG-----AYAmmagltEEQKAHGVITASAG--NHAQGVAF 96
Cdd:COG2515 8 AFLPTPLQPLPRLSAALGVELWIKRDDL--TGPAiggnKTRKleyllADA------LAQGADTLVTFGGAqsNHARATAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16767181 97 SSARLGVKSLIVMPKATADIKVDAV---RGFGGEVLLHGANF----DEAKAKAIELAQQQGFTwvppfdhPMVIAGQGT- 168
Cdd:COG2515 80 AAAKLGLKCVLVLRGEEPTPLNGNLlldRLLGAELHFVSRGEyrdrDEAMEAVAAELRARGGK-------PYVIPEGGSn 152
|
170 180 190
....*....|....*....|....*....|.
gi 16767181 169 ---------LALELLQQ----DSHLDRVFVP 186
Cdd:COG2515 153 plgalgyveAAAELAAQlaelGVDFDYIVVA 183
|
|
| |
