|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
10-510 |
0e+00 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 896.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 10 SAIDYLRSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHA 89
Cdd:PRK09224 1 MGADYLRKILTARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 90 QGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGL 169
Cdd:PRK09224 81 QGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 170 ELVQQKPD-LDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDE 248
Cdd:PRK09224 161 EILQQHPHpLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 249 TFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSGANVNFHTLRFVSER 328
Cdd:PRK09224 241 TFRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAER 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 329 CEIGEKREALLAVTIAEQKGSFLKFCEILGNRAVTEFNYRHSDDKQACIFVGVRIS-GSAEKSEIIKDLQQNGYDVADLS 407
Cdd:PRK09224 321 AELGEQREALLAVTIPEEPGSFLKFCELLGGRNVTEFNYRYADAKEAHIFVGVQLSrGQEERAEIIAQLRAHGYPVVDLS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 408 DDDIAKTHIRYMVGGRASSIQYEQLYSFEFPEQKGALLKFLQML-TNWDISLFHYRAHGADYGDILAAFALNQGDEVELN 486
Cdd:PRK09224 401 DDELAKLHVRYMVGGRPPKPLDERLYRFEFPERPGALLKFLSTLgTHWNISLFHYRNHGADYGRVLAGFQVPDADEPEFE 480
|
490 500
....*....|....*....|....
gi 749034310 487 RHLEQLGYRFQNVSESPAYQYFLK 510
Cdd:PRK09224 481 AFLDELGYPYWDETDNPAYRLFLA 504
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
13-509 |
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: 777.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 13 DYLRSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGV 92
Cdd:TIGR01124 1 DYLRAILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 93 ALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELV 172
Cdd:TIGR01124 81 AFSAARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 173 QQKP-DLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFR 251
Cdd:TIGR01124 161 RQVAnPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 252 LCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSGANVNFHTLRFVSERCEI 331
Cdd:TIGR01124 241 LCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSERCEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 332 GEKREALLAVTIAEQKGSFLKFCEILGNRAVTEFNYRHSDDKQACIFVGVRISGSAEKSEIIKDLQQNGYDVADLSDDDI 411
Cdd:TIGR01124 321 GEQREALLAVTIPEQPGSFLKFCELLGNRNITEFNYRYADRKDAHIFVGVQLSNPQERQEILARLNDGGYSVVDLTDDEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 412 AKTHIRYMVGGRASSIQYEQLYSFEFPEQKGALLKFL-QMLTNWDISLFHYRAHGADYGDILAAFALNQGDEVELNRHLE 490
Cdd:TIGR01124 401 AKLHVRYMVGGRPPHVENERLYSFEFPERPGALLRFLnTLQGYWNISLFHYRNHGADYGRVLAGFQVPDHEPDQFEQFLA 480
|
490
....*....|....*....
gi 749034310 491 QLGYRFQNVSESPAYQYFL 509
Cdd:TIGR01124 481 ELGYRYHDETNNPAYRLFL 499
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
13-509 |
0e+00 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 603.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 13 DYLRSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGV 92
Cdd:PRK12483 21 DYLRKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 93 ALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELV 172
Cdd:PRK12483 101 ALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 173 QQKPD-LDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFR 251
Cdd:PRK12483 181 RQHPGpLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 252 LCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSGANVNFHTLRFVSERCEI 331
Cdd:PRK12483 261 LCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNFDRLRHVAERAEL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 332 GEKREALLAVTIAEQKGSFLKFCEILGNRAVTEFNYRHSDDKQACIFVGVRISGSAE-KSEIIKDLQQNGYDVADLSDDD 410
Cdd:PRK12483 341 GEQREAIIAVTIPEQPGSFKAFCAALGKRQITEFNYRYADAREAHLFVGVQTHPRHDpRAQLLASLRAQGFPVLDLTDDE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 411 IAKTHIRYMVGGRASSIQYEQLYSFEFPEQKGALLKFLQML-TNWDISLFHYRAHGADYGDILAAFALNQGDEVELNRHL 489
Cdd:PRK12483 421 LAKLHIRHMVGGRAPLAHDERLFRFEFPERPGALMKFLSRLgPRWNISLFHYRNHGAADGRVLAGLQVPEDERAALDAAL 500
|
490 500
....*....|....*....|
gi 749034310 490 EQLGYRFQNVSESPAYQYFL 509
Cdd:PRK12483 501 AALGYPYWEETGNPAYRLFL 520
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
10-510 |
1.12e-167 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 486.74 E-value: 1.12e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 10 SAIDYLRSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHA 89
Cdd:PLN02550 90 EAMEYLTNILSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 90 QGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGL 169
Cdd:PLN02550 170 QGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGM 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 170 ELVQQKPD-LDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDE 248
Cdd:PLN02550 250 EIVRQHQGpLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 249 TFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSGANVNFHTLRFVSER 328
Cdd:PLN02550 330 TFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVTEL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 329 CEIGEKREALLAVTIAEQKGSFLKFCEILGNRAVTEFNYRHSDDKQACIFVGVRISGSAEKSEIIKDLQQNGYDVADLSD 408
Cdd:PLN02550 410 ADVGRQQEAVLATFMPEEPGSFKRFCELVGPMNITEFKYRYSSEKEALVLYSVGVHTEQELQALKKRMESAQLRTVNLTS 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 409 DDIAKTHIRYMVGGRAsSIQYEQLYSFEFPEQKGALLKFLQMLT-NWDISLFHYRAHGADYGDILAAFALNQGDEVELNR 487
Cdd:PLN02550 490 NDLVKDHLRYLMGGRA-IVKDELLYRFVFPERPGALMKFLDAFSpRWNISLFHYRGQGETGANVLVGIQVPPEEMQEFKS 568
|
490 500
....*....|....*....|...
gi 749034310 488 HLEQLGYRFQNVSESPAYQYFLK 510
Cdd:PLN02550 569 RANALGYEYQDECDNEAFQLLMH 591
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
2-334 |
1.18e-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: 1.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 2 MNETQHSQSAIDYLRSIlssnIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVI 81
Cdd:COG1171 1 MTALMPTLADIEAAAAR----IAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 82 AASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVI 161
Cdd:COG1171 77 AASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 162 AGQGTIGLELVQQKPDLDYVFIPVggggliagiaVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIA 241
Cdd:COG1171 157 AGQGTIALEILEQLPDLDAVFVPVggggliagvaAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 242 VKRIGDETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYvkEHQLQDKNLACILSGANVNFHT 321
Cdd:COG1171 237 VGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG--KERLKGKRVVVVLSGGNIDPDR 314
|
330
....*....|...
gi 749034310 322 LRFVSERCEIGEK 334
Cdd:COG1171 315 LAEILERGLVGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
15-318 |
1.07e-132 |
|
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: 386.84 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 15 LRSILSS--NIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGV 92
Cdd:cd01562 1 LEDILAAaaRIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 93 ALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELV 172
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 173 QQKPDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRL 252
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749034310 253 CQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHqlQDKNLACILSGANVN 318
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVLSGGNID 304
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
22-412 |
3.60e-96 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 297.49 E-value: 3.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 22 NIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGL 101
Cdd:PRK08639 18 RLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAYACRHLGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 102 RALIVMPQNTPAIKVDAVRGYGG---EVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQ---K 175
Cdd:PRK08639 98 PGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQlekE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 176 PDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRLCQQ 255
Cdd:PRK08639 178 GSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 256 YVDDVVLVDNDEICASMkLIFENVRAI-SEPSGAASLAGLKKYVKEhqLQDKNLACILSGANVNFHTLRFVSERCEIGEK 334
Cdd:PRK08639 258 VVDDVVLVPEGAVCTTI-LELYNKEGIvAEPAGALSIAALELYKDE--IKGKTVVCVISGGNNDIERMPEIKERSLIYEG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 335 REALLAVTIAEQKG---SFLKfcEILG-NRAVTEFNY--RHSDDKQACIfVGVRISGSAEKSEIIKDLQQNGYDVADLSD 408
Cdd:PRK08639 335 LKHYFIVNFPQRPGalrEFLD--DVLGpNDDITRFEYlkKNNRETGPVL-VGIELKDAEDYDGLIERMEAFGPSYIDINP 411
|
....
gi 749034310 409 DDIA 412
Cdd:PRK08639 412 NEPL 415
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
30-403 |
3.11e-90 |
|
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: 280.86 E-value: 3.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMPQ 109
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 110 NTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPVGGGG 189
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 190 LIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRLCQQYVDDVVLVDNDEIC 269
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 270 ASMKLIFENVRAISEPSGAASLAGLKKYVKEhqLQDKNLACILSGANVNFHTLRFVSERCEIGEKREALLAVTIAEQKGS 349
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVD--VKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPDRPGA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 350 FLKFCEILG-NRA-VTEFNYRHSDDKQACIFVGVRIS----GSAEKSEIIKDLQQNGYDV 403
Cdd:TIGR01127 319 LYHLLESIAeARAnIVKIDHDRLSKEIPPGFAMVEITletrGKEHLDEILKILRDMGYNF 378
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
16-337 |
5.39e-84 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 263.13 E-value: 5.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 16 RSILSSNIYdlaqVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALS 95
Cdd:PRK08638 18 KQRLAGRIR----KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVALS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 96 AKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQK 175
Cdd:PRK08638 94 CALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 176 PDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRLCQQ 255
Cdd:PRK08638 174 WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 256 YVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSGANVNfhtLRFVSERCEIGEKR 335
Cdd:PRK08638 254 LVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVD---LSRVSQITGHVVAA 330
|
..
gi 749034310 336 EA 337
Cdd:PRK08638 331 DA 332
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
30-359 |
7.45e-76 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 244.42 E-value: 7.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMPQ 109
Cdd:PRK07334 24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 110 NTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPVGGGG 189
Cdd:PRK07334 104 FTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGGGG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 190 LIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTdlerVG--LFADGIAVKRIGDETFRLCQQYVDDVVLVDNDE 267
Cdd:PRK07334 184 LISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALP----CGgsTIAEGIAVKQPGQLTLEIVRRLVDDILLVSEAD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 268 ICASMKLIFENVRAISEPSGAASLAGLKKYvkEHQLQDKNLACILSGANVNFHTLRFVSERCEIGEKREALLAVTIAEQK 347
Cdd:PRK07334 260 IEQAVSLLLEIEKTVVEGAGAAGLAALLAY--PERFRGRKVGLVLSGGNIDTRLLANVLLRGLVRAGRLARLRVDIRDRP 337
|
330
....*....|..
gi 749034310 348 GSFLKFCEILGN 359
Cdd:PRK07334 338 GALARVTALIGE 349
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
30-314 |
1.35e-73 |
|
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: 234.90 E-value: 1.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMPQ 109
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 110 NTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTEL-GMTFIHPFDSPAVIAGQGTIGLELV-QQKPDLDYVFIPVGG 187
Cdd:pfam00291 88 DAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILeQLGGDPDAVVVPVGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 188 GGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRI-GDETFRLCQQYVDDVVLVDND 266
Cdd:pfam00291 168 GGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTVSDE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 749034310 267 EICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQDKNLACILSG 314
Cdd:pfam00291 248 EALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
29-323 |
5.05e-72 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 231.51 E-value: 5.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 29 VTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMP 108
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 109 QNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPVGGG 188
Cdd:PRK06815 100 EQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 189 GLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIA--VKRiGDETFRLCQQYVDDVVLVDND 266
Cdd:PRK06815 180 GLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVEP-GAITFPLCQQLIDQKVLVSEE 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 749034310 267 EICASMKLIFENVRAISEPSGAASLAGLKKYVKEHqlQDKNLACILSGANVNFHTLR 323
Cdd:PRK06815 259 EIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY--QGKKVAVVLCGKNIVLEKYL 313
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
23-322 |
5.41e-68 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 221.43 E-value: 5.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 23 IYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLR 102
Cdd:PRK07048 18 LAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 103 ALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVF 182
Cdd:PRK07048 98 ATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 183 IPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRLCQQYVDDVVL 262
Cdd:PRK07048 178 VCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTFPIIRRLVDDIVT 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749034310 263 VDNDEICASMKLIFENVRAISEPSGAASLAGLKKyvKEHQLQDKNLACILSGANV---NFHTL 322
Cdd:PRK07048 258 VSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR--GKVPLKGKRVGVIISGGNVdlaRFAAL 318
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
30-314 |
8.71e-66 |
|
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: 212.76 E-value: 8.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAG--VIAASAGNHAQGVALSAKHLGLRALIVM 107
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 108 PQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTEL-GMTFIHPFDSPAVIAGQGTIGLELVQQ--KPDLDYVFIP 184
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQlgGQKPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 185 VGGGGLIAGIAVLIKQVMPNIKVIGVEskdsaclyhalkqgqptdlervglfADGIAVKrigDEtfrlcqqyvddvvlvd 264
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVE-------------------------PEVVTVS---DE---------------- 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 749034310 265 ndEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHqLQDKNLACILSG 314
Cdd:cd00640 197 --EALEAIRLLAREEGILVEPSSAAALAAALKLAKKL-GKGKTVVVILTG 243
|
|
| PLN02970 |
PLN02970 |
serine racemase |
1-322 |
5.71e-65 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 213.77 E-value: 5.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 1 MMNETQHsqsAIDyLRSIL--SSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEA 78
Cdd:PLN02970 1 EAASEKY---AAD-LSSIReaRKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 79 GVIAASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSP 158
Cdd:PLN02970 77 GVVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 159 AVIAGQGTIGLELVQQKPDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFAD 238
Cdd:PLN02970 157 RVISGQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 239 GIAVkRIGDETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGL------KKYVKEHQlqdKNLACIL 312
Cdd:PLN02970 237 GLRA-SLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsdsfrSNPAWKGC---KNVGIVL 312
|
330
....*....|
gi 749034310 313 SGANVNFHTL 322
Cdd:PLN02970 313 SGGNVDLGVL 322
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
23-317 |
3.15e-64 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 211.36 E-value: 3.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 23 IYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLR 102
Cdd:PRK07476 13 IAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 103 ALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVF 182
Cdd:PRK07476 93 ATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALPDVATVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 183 IPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFAD----GIAVK-RIgdeTFRLCQQYV 257
Cdd:PRK07476 173 VPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslggGIGLDnRY---TFAMCRALL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749034310 258 DDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLkkyvKEHQL--QDKNLACILSGANV 317
Cdd:PRK07476 250 DDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAAL----LAGKIaaRDGPIVVVVSGANI 307
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
30-318 |
1.45e-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: 185.83 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMPQ 109
Cdd:TIGR02991 20 TPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMSE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 110 NTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPVGGGG 189
Cdd:TIGR02991 100 LVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQMPDLATVLVPLSGGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 190 LIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAvKRIGDE---TFRLCQQYVDDVVLVDND 266
Cdd:TIGR02991 180 LASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLG-GGIGLDnrvTFAMCKALLDEIVLVSEA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 749034310 267 EICASMKLIFENVRAISEPSGAASLAGLkkyVKEHQLQDKNLACILSGANVN 318
Cdd:TIGR02991 259 EIAAGIRHAYAEEREIVEGAGAVGIAAL---LAGKIKNPGPCAVIVSGRNID 307
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
46-322 |
1.89e-53 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 182.85 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 46 IFIKREDRQPVHSFKLRGAFAMIsnLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGE 125
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 126 VLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPVGGGGLIAGIAVLIKqvmPNI 205
Cdd:PRK08246 117 VVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIAAWFE---GRA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 206 KVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGDETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEP 285
Cdd:PRK08246 194 RVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEP 273
|
250 260 270
....*....|....*....|....*....|....*....
gi 749034310 286 SGAASLAGL--KKYVKEhqlQDKNLACILSGANVNFHTL 322
Cdd:PRK08246 274 GAATALAALlsGAYVPA---PGERVAVVLCGANTDPATL 309
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
336-419 |
3.09e-43 |
|
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: 148.08 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 336 EALLAVTIAEQKGSFLKFCEILGNRAVTEFNYRHSDDKQACIFVGVRISGSA-EKSEIIKDLQQNGYDVADLSDDDIAKT 414
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAeELAELLEDLKSAGYEVVDLSDDELAKT 80
|
....*
gi 749034310 415 HIRYM 419
Cdd:cd04906 81 HLRYM 85
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
30-318 |
4.99e-41 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 150.55 E-value: 4.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQkmekLSERLGnsIFIKREDRQPVHSFKLRGAF-AMISNLSKAQKEAgVIAASAGNHAQGVALSAKHLGLRALIVMP 108
Cdd:PRK08813 40 TPLH----YAERFG--VWLKLENLQRTGSYKVRGALnALLAGLERGDERP-VICASAGNHAQGVAWSAYRLGVQAITVMP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 109 QNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLdyVFIPVGGG 188
Cdd:PRK08813 113 HGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPDV--VIVPIGGG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 189 GLIAGIAVLIKQvmPNIKVIGVESKDSACLYHALKqGQPTDLERVGLFADGIAVKRIGDETFRLCQQYVDDVVLVDNDEI 268
Cdd:PRK08813 191 GLASGVALALKS--QGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAEL 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 749034310 269 CASM-KLIFENvRAISEPSGAASLAGLKKyvkehqLQDKNLACILSGANVN 318
Cdd:PRK08813 268 RETLvRLALEE-HVIAEGAGALALAAGRR------VSGKRKCAVVSGGNID 311
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
38-332 |
1.59e-40 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 148.60 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 38 LSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKE-AGVIAASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKV 116
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 117 DAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFdSPAVIAGQGTIGLELVQQKPDLDYVFIPVgGGGLIAGIAV 196
Cdd:PRK06110 110 AAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPI-GMGSGICGAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 197 LIKQVMP-NIKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVkRIGD-ETFRLCQQYVDDVVLVDNDEICASMKL 274
Cdd:PRK06110 188 AARDALGlKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMAC-RTPDpEALEVIRAGADRIVRVTDDEVAAAMRA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 749034310 275 IFENVRAISEPSGAASLAGLKKyvKEHQLQDKNLACILSGANVNFHTLRFVSERCEIG 332
Cdd:PRK06110 267 YFTDTHNVAEGAGAAALAAALQ--ERERLAGKRVGLVLSGGNIDRAVFARVLAGAAAE 322
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
30-318 |
2.32e-40 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 148.77 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLskaqKEAG-----VIAASAGNHAQGVALSAKHLGLRAL 104
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLEL----KEQGklpdkIVAYSTGNHGQAVAYASKLFGIKTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 105 IVMPQNTPAIKVDAVRGYGGEVLLYGANfDEAKAKAIElSTELGMTFIHPFDSPAVIAGQGTIGLELVQQ-KPDLDYVFI 183
Cdd:PRK06608 100 IYLPLNTSKVKQQAALYYGGEVILTNTR-QEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQlGFSPDAIFA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 184 PVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACLYHALKQGQPTDLERV-GLFADGIAVKRIGDETFRLCQQyVDDVVL 262
Cdd:PRK06608 178 SCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKK-LDDFYL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 749034310 263 VDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEhQLQDKNLACILSGANVN 318
Cdd:PRK06608 257 VEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKT-QSKPQKLLVILSGGNID 311
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
30-300 |
6.42e-31 |
|
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: 122.32 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLG-NSIFIKREDRQPVHSFKLRGA-FAMisnlSKAqKEAG---VIAASAGNHAQGVALSAKHLGLRAL 104
Cdd:cd01563 23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMtVAV----SKA-KELGvkaVACASTGNTSASLAAYAARAGIKCV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 105 IVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHpFDSPAVIAGQGTIGLELVQQ----KPdlDY 180
Cdd:cd01563 98 VFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQlgweVP--DY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 181 VFIPVGGGG---------LIAGIAVLIKQvMPniKVIGVESKDSACLYHALKQGQ--PTDLERVGLFADGIavkRIGD-- 247
Cdd:cd01563 175 VVVPVGNGGnitaiwkgfKELKELGLIDR-LP--RMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAI---RIGNpa 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 749034310 248 ---ETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKE 300
Cdd:cd01563 249 sgpKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE 304
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
22-316 |
1.18e-30 |
|
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: 123.00 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 22 NIYDL-AQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISnLSKAQKEAGVIAASAGNHAQGVALSAKHLG 100
Cdd:COG0498 58 KAVSLgEGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVS-LALERGAKTIVCASSGNGSAALAAYAARAG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 101 LRALIVMPQN-TPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFdSPAVIAGQGTIGLELVQQ---KP 176
Cdd:COG0498 137 IEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQlgrVP 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 177 DldYVFIPV----------GGGGLIAGIAVLIKqvMPniKVIGVESKDSACLYHALKQGQ-------------------P 227
Cdd:COG0498 216 D--WVVVPTgnggnilagyKAFKELKELGLIDR--LP--RLIAVQATGCNPILTAFETGRdeyeperpetiapsmdignP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 228 TDLERVgLFA----DGIAVkRIGDEtfrlcqqyvddvvlvdndEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQL 303
Cdd:COG0498 290 SNGERA-LFAlresGGTAV-AVSDE------------------EILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEI 349
|
330
....*....|...
gi 749034310 304 QDKNLACILSGAN 316
Cdd:COG0498 350 DPDEPVVVLSTGH 362
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
29-292 |
1.38e-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: 118.17 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 29 VTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSK--AQKEAGVIAASAGNHAQGVALSAKHLGLRALIV 106
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKqgLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 107 MPQNTPAIKVDAVRGYGGEVLLYGAN-FDEAKAKAIEL-STELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVfip 184
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELaENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 185 vggggliagiAVLIKQV----MPN-------------IKVIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKRIGD 247
Cdd:cd06448 158 ----------DAIVCSVggggLLNgivqglerngwgdIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 749034310 248 ETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLA 292
Cdd:cd06448 228 QALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALA 272
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
327-416 |
7.10e-28 |
|
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: 106.60 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 327 ERCEIGEKREALLAVTIAEQKGSFLKFCEILGNRA-VTEFNYRHSDDKQACIFVGVRISGSAEKSEIIKDLQQNGYDVAD 405
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRNnITLFEYRKHGDKNGCVLVGIELSQAEDLDEFIERLNKLGYDYED 80
|
90
....*....|.
gi 749034310 406 LSDDDIAKTHI 416
Cdd:pfam00585 81 LSDNEAAYEHL 91
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
430-509 |
8.10e-28 |
|
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: 106.10 E-value: 8.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 430 EQLYSFEFPEQKGALLKFLQ-MLTNWDISLFHYRAHGADYGDILAAFALNQGDEVELNRHLEQLGYRFQNVSESPAYQYF 508
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNeLLPKWNITLFHYRNQGSDYGRVLVGIQVPDADLDELKERLDALGYPYQEETDNPAYKLF 80
|
.
gi 749034310 509 L 509
Cdd:cd04907 81 L 81
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
421-509 |
1.50e-23 |
|
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the pfam01842 domain.
Pssm-ID: 395467 [Multi-domain] Cd Length: 91 Bit Score: 94.65 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 421 GGRASSIQYEQLYSFEFPEQKGALLKFLQMLTN-WDISLFHYRAHGADYGDILAAFALNQGDEV-ELNRHLEQLGYRFQN 498
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGrNNITLFEYRKHGDKNGCVLVGIELSQAEDLdEFIERLNKLGYDYED 80
|
90
....*....|.
gi 749034310 499 VSESPAYQYFL 509
Cdd:pfam00585 81 LSDNEAAYEHL 91
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
339-405 |
1.76e-20 |
|
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: 85.25 E-value: 1.76e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749034310 339 LAVTIAEQKGSFLKFCEILG-NRAVTEFNYRHSDDKQACIFVGVRISGSAEKSEIIKDLQQNGYDVAD 405
Cdd:cd04885 1 FAVTFPERPGALKKFLELLGpPRNITEFHYRNQGGDEARVLVGIQVPDREDLAELKERLEALGYPYVD 68
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
8-174 |
8.09e-19 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 88.40 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 8 SQSAIDYLRSILSSniYDLAQVTPLQKMEKLSERLG-NSIFIKRED-RQPVHSFK-LRGAFAM-----------ISNLS- 72
Cdd:PRK08206 25 SQEEAKKARAFHQS--FPGYAPTPLVALPDLAAELGvGSILVKDESyRFGLNAFKaLGGAYAVarllaeklgldISELSf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 73 ------KAQKEAG---VIAASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIEL 143
Cdd:PRK08206 103 eeltsgEVREKLGditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 749034310 144 STELGMTFIH----------PFDspaVIAGQGTIGLELVQQ 174
Cdd:PRK08206 183 AQENGWVVVQdtawegyeeiPTW---IMQGYGTMADEAVEQ 220
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
433-498 |
1.05e-18 |
|
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: 80.24 E-value: 1.05e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749034310 433 YSFEFPEQKGALLKFLQML-TNWDISLFHYRAHGADYGDILAAFALNQGDEV-ELNRHLEQLGYRFQN 498
Cdd:cd04885 1 FAVTFPERPGALKKFLELLgPPRNITEFHYRNQGGDEARVLVGIQVPDREDLaELKERLEALGYPYVD 68
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
30-225 |
1.72e-17 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 82.95 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKA---QKEAGVIAASAGNHAQGVALSAKHLGLRALIV 106
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRgllKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 107 MPQNTPAIKVDAVRGYGGEVLL----YGANFDEAKAKAIELSTELGMTFI-HPFDSPA-VIAGQGTIGLELVQQKPD-LD 179
Cdd:cd01561 83 MPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETPNAFWlNQFENPAnPEAHYETTAPEIWEQLDGkVD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749034310 180 YVFIPV---------GGGgliagiavlIKQVMPNIKVIGVESKDSAcLYHALKQG 225
Cdd:cd01561 163 AFVAGVgtggtitgvARY---------LKEKNPNVRIVGVDPVGSV-LFSGGPPG 207
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
30-174 |
4.58e-17 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 83.13 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLG-NSIFIKREDRQPVHSFKLRGAFAMISnlsKAqKEAGV--IA-ASAGNHAQGVALSAKHLGLRALI 105
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVS---RA-KELGVkhLAmPTNGNAGAAWAAYAARAGIRATI 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749034310 106 VMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQ 174
Cdd:PRK08197 156 FMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQ 224
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
17-314 |
6.89e-16 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 78.58 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 17 SILSSNIYDLAQ-VTPLQKMEKLSERLG-NSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEAgVIAASAGNHAQGVAL 94
Cdd:TIGR00260 9 PVTEKDLVDLGEgVTPLFRAPALAANVGiKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDT-VLCASTGNTGAAAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 95 SAKHLGLRALIVMPQN-TPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELsteLGMTFIHPFDS----PAVIAGQGTIGL 169
Cdd:TIGR00260 88 YAGKAGLKVVVLYPAGkISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQL---FEDKPALGLNSansiPYRLEGQKTYAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 170 ELVQQ--KPDLDYVFIPVGGG-------GLIAGIAVLIKQVMPniKVIGVESKDSACLYHA-LKQGQPTDLERVGLFADG 239
Cdd:TIGR00260 165 EAVEQlgWEAPDKVVVPVPNSgnfgaiwKGFKEKKMLGLDSLP--VKRGIQAEGAADIVRAfLEGGQWEPIETPETLSTA 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749034310 240 IAVKRI--GDETFRLCQQYVDDVVLVDNDEICASMKLIFENVRAISEPSGAASLAGLKKYVKEHQLQ-DKNLACILSG 314
Cdd:TIGR00260 243 MDIGNPanWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADpAERVVCALTG 320
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
30-218 |
1.15e-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: 77.40 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKA---QKEAGVIAASAGNHAQGVALSAKHLGLRALIV 106
Cdd:COG0031 14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRgllKPGGTIVEATSGNTGIGLAMVAAAKGYRLILV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 107 MPQNTPAIKVDAVRGYGGEVLLYGA--NFDEAKAKAIELSTEL-GMTFIHPFDSPA-VIAGQGTIGLELVQQ-KPDLDYV 181
Cdd:COG0031 94 MPETMSKERRALLRAYGAEVVLTPGaeGMKGAIDKAEELAAETpGAFWPNQFENPAnPEAHYETTGPEIWEQtDGKVDAF 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 749034310 182 FIPVggggliagiavlIKQVMPNIKVIGVESKDSACL 218
Cdd:COG0031 174 VAGVgtggtitgvgryLKERNPDIKIVAVEPEGSPLL 210
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
30-174 |
1.92e-15 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 78.32 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKmEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISN-LSKAQKeaGVIAASAGNHAQGVALSAKHLGLRALIVMP 108
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYgLPYAAN--GFIVASDGNAAASVAAYSARAGKEAFVVVP 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749034310 109 QNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQ 174
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEE 209
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
29-320 |
3.57e-14 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 73.71 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 29 VTPLQKmeklserLGNSIFIKREDRQPVHSFKLRGAFAMISNLskaqKEAG---VIAASAGNHAQGVALSAKHLGLRALI 105
Cdd:PRK08329 64 ITPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGineVVIDSSGNAALSLALYSLSEGIKVHV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 106 VMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIAGQGTIGLELVQQKPDLDYVFIPV 185
Cdd:PRK08329 133 FVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 186 GGGGLIAGIAVLIKQV--MPNI----KVIGVESK--DSAClyhalKQGQptdleRVGLFADGIAV---KRIgDETFRLCQ 254
Cdd:PRK08329 213 GSGTLFLGIWKGFKELheMGEIskmpKLVAVQAEgyESLC-----KRSK-----SENKLADGIAIpepPRK-EEMLRALE 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749034310 255 QYVDDVVLVDNDEICASMKLIFeNVRAISEPSGAASLAGLKKYVKEHQLQDKNLACI-LSGANVNFH 320
Cdd:PRK08329 282 ESNGFCISVGEEETRAALHWLR-RMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLpLSGSGLKNL 347
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
15-185 |
3.69e-13 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 70.51 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 15 LRSILSSNIYDLAQVTPLQKMEKLSERLG-NSIFIKREDRQPVHSFKLRGAFAMISNlSKAQKEAGVIAASAGNHAQGVA 93
Cdd:PRK06381 1 MEEELSSSEEKPPGGTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRR-AMRLGYSGITVGTCGNYGASIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 94 LSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSPAVIA--GQGTIGLEL 171
Cdd:PRK06381 80 YFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEI 159
|
170
....*....|....*
gi 749034310 172 VQQKPDL-DYVFIPV 185
Cdd:PRK06381 160 YEALGDVpDAVAVPV 174
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
30-128 |
1.52e-09 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 59.49 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSK--AQKEAGVIA-ASAGNHAQGVALSAKHLGLRALIV 106
Cdd:PRK10717 14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKrgLLKPGGTIVeGTAGNTGIGLALVAAARGYKTVIV 93
|
90 100
....*....|....*....|..
gi 749034310 107 MPQNTPAIKVDAVRGYGGEVLL 128
Cdd:PRK10717 94 MPETQSQEKKDLLRALGAELVL 115
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
30-128 |
1.54e-08 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 56.03 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMIsnlsKAQKEAGVIA-------ASAGNhaQGVALS--AKHLG 100
Cdd:PRK11761 13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMI----VQAEKRGEIKpgdtlieATSGN--TGIALAmiAAIKG 86
|
90 100
....*....|....*....|....*...
gi 749034310 101 LRALIVMPQNTPAIKVDAVRGYGGEVLL 128
Cdd:PRK11761 87 YRMKLIMPENMSQERRAAMRAYGAELIL 114
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
30-210 |
1.50e-07 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 53.19 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGN--SIFIKREDRQPVHSF---KLRGAFAMISN-LSKAQKEAGVIAASAGNHAQGVALSAKHLGLRA 103
Cdd:cd06449 1 TPIQYLPRLSEHLGGkvEIYAKRDDCNSGLAFggnKIRKLEYLLPDaLAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 104 LIVM--PQNTPAIKVDAV------RGYGGEVLLYGANFDEAKAKAIE-LSTELGMTFIHPFDSPA-----VIAGQGTIG- 168
Cdd:cd06449 81 VLVQenWVPYSDAVYDRVgnillsRIMGADVRLVSAGFDIGIRKSFEeAAEEVEAKGGKPYVIPAggsehPLGGLGYVGf 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749034310 169 -LELVQQKPDL----DYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGV 210
Cdd:cd06449 161 vLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGI 207
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
6-227 |
1.50e-07 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 53.43 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 6 QHSQSAIDYLRSILSSNIYD----LAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSKAQ----KE 77
Cdd:PLN02556 32 SFAQRLRDLPKDLPGTKIKTdasqLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNlitpGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 78 AGVIAASAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYganfDEAKA------KAIELSTELGMTF 151
Cdd:PLN02556 112 TTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLT----DPTKGmggtvkKAYELLESTPDAF 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749034310 152 -IHPFDSPA-VIAGQGTIGLELVQQK-PDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSaclyHALKQGQP 227
Cdd:PLN02556 188 mLQQFSNPAnTQVHFETTGPEIWEDTlGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAES----NVLNGGKP 262
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
30-185 |
3.01e-07 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 52.10 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDR-QPVHS----FKLRGafamisNLSKAQKE-AGVIAASAG---NHAQGVALSAKHLG 100
Cdd:COG2515 12 TPLQPLPRLSAALGVELWIKRDDLtGPAIGgnktRKLEY------LLADALAQgADTLVTFGGaqsNHARATAAAAAKLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 101 LRALIVMP-----QNTPAIKVDavRGYGGEVLLYGANF-----DEAKAKAIELSTElgmtfihpFDSPAVIAGQGT---- 166
Cdd:COG2515 86 LKCVLVLRgeeptPLNGNLLLD--RLLGAELHFVSRGEyrdrdEAMEAVAAELRAR--------GGKPYVIPEGGSnplg 155
|
170 180
....*....|....*....|....*....
gi 749034310 167 ------IGLELVQQ----KPDLDYVFIPV 185
Cdd:COG2515 156 algyveAAAELAAQlaelGVDFDYIVVAS 184
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
43-297 |
1.48e-05 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 47.04 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 43 GNSIFIKREDRQPVHSFKLRGAFAMISNLskAQKEAGVIAA-SAGNHAQGVALSAKHLGLRALIVMPQNTPAIKVDAVRG 121
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYL--AEKGIKQISEdSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIES 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 122 YGGEVLLYGANFDEAkAKAIELStelGMTFIHPFDSPAVIAGQGTIGLELVQQ---KPDlDYVFIPVGGGGLIAGIAVLI 198
Cdd:PRK06450 142 YGAEVVRVRGSREDV-AKAAENS---GYYYASHVLQPQFRDGIRTLAYEIAKDldwKIP-NYVFIPVSAGTLLLGVYSGF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 199 KQV--------MPNIkvIGVESKDSACLYHALKQGQPTDLERVGLFADGIAVKR--IGDETFRLCQQYVDDVVLVDNDEI 268
Cdd:PRK06450 217 KHLldsgviseMPKI--VAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRpfLLDYMVKALSEYGECIVVSDNEIV 294
|
250 260
....*....|....*....|....*....
gi 749034310 269 CASMKLIFENVRAisEPSGAASLAGLKKY 297
Cdd:PRK06450 295 EAWKELAKKGLLV--EYSSATVYAAYKKY 321
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
30-184 |
2.67e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 46.73 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLS-ERLG-NSIFIKREDRQPVHSFKLRGAFAMISNLSKAQKEA----GVIAASAGNhaQGVALSA--KHLGL 101
Cdd:PLN02569 134 SNLFWAERLGkEFLGmNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGD--TSAALSAycAAAGI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 102 RALIVMPQNTPAI-KVDAVRGYGGEVLLYGANFDEAKAKAIELSTELGMTFIHPFDSpAVIAGQGTIGLELVQQ----KP 176
Cdd:PLN02569 212 PSIVFLPADKISIaQLVQPIANGALVLSIDTDFDGCMRLIREVTAELPIYLANSLNS-LRLEGQKTAAIEILQQfdweVP 290
|
....*...
gi 749034310 177 dlDYVFIP 184
Cdd:PLN02569 291 --DWVIVP 296
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
16-218 |
2.91e-05 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 46.07 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 16 RSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSK----AQKEAGVIAASAGNHAQG 91
Cdd:PLN02565 2 KSSIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEkgliKPGESVLIEPTSGNTGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 92 VALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLY--GANFDEAKAKAIELSTELGMTFI-HPFDSPA--VIAGQgT 166
Cdd:PLN02565 82 LAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdpAKGMKGAVQKAEEILAKTPNSYIlQQFENPAnpKIHYE-T 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749034310 167 IGLELVQ-QKPDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSACL 218
Cdd:PLN02565 161 TGPEIWKgTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVL 213
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
30-179 |
3.35e-05 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 45.98 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVhsfklrgafAMISNlsKAQK---------EAG---VIAASA--GNHA-QGVAL 94
Cdd:PRK03910 16 TPLEPLPRLSAALGPDIYIKRDDLTGL---------ALGGN--KTRKleflladalAQGadtLITAGAiqSNHArQTAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 95 SAKhLGLRALIVMPQNTPAikVDAVRGYGGEVLLY------------GANFDEAkakAIELSTEL---GMTfihpfdsPA 159
Cdd:PRK03910 85 AAK-LGLKCVLLLENPVPT--EAENYLANGNVLLDdlfgaeihvvpaGTDMDAQ---LEELAEELraqGRR-------PY 151
|
170 180 190
....*....|....*....|....*....|
gi 749034310 160 VIAGQG--TIG--------LELVQQKPDLD 179
Cdd:PRK03910 152 VIPVGGsnALGalgyvacaLEIAQQLAEGG 181
|
|
| ACT_ThrD-I_1 |
cd04906 |
First of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
430-502 |
8.08e-05 |
|
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: 41.38 E-value: 8.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749034310 430 EQLYSFEFPEQKGALLKFLQMLTNWDISLFHYRAHGADYGDILAAFALNQGDEvELNRHLEQL---GYRFQNVSES 502
Cdd:cd04906 1 EALLAVTIPERPGSFKKFCELIGPRNITEFNYRYADEKDAHIFVGVSVANGAE-ELAELLEDLksaGYEVVDLSDD 75
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
16-227 |
9.91e-05 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 44.61 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 16 RSILSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSK----AQKEAGVIAASAGNHAQG 91
Cdd:PLN00011 4 RCLIKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDkgliTPGKSTLIEATAGNTGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 92 VALSAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLL----YGANFDEAKAKAIeLSTELGMTFIHPFDSPAVIAGQ-GT 166
Cdd:PLN00011 84 LACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLtdqsIGLKGMLEKAEEI-LSKTPGGYIPQQFENPANPEIHyRT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749034310 167 IGLELVQQKP-DLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSAclyhALKQGQP 227
Cdd:PLN00011 163 TGPEIWRDSAgKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESA----VLSGGQP 220
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
19-295 |
1.05e-04 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 44.77 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 19 LSSNIYDLAQVTPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMISNLSK----AQKEAGVIAASAGNHAQGVAL 94
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQkgfiSPGKSVLVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 95 SAKHLGLRALIVMPQNTPAIKVDAVRGYGGEVLLYganfDEAKAK--AIELSTEL-----GMTFIHPFDSPAVIAGQ-GT 166
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLT----DPAKGMtgAVQKAEEIlkntpDAYMLQQFDNPANPKIHyET 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 167 IGLELVQQ-KPDLDYVFIPVGGGGLIAGIAVLIKQVMPNIKVIGVESKDSaclyHALKQGQPTDLERVGLFADGIAV--- 242
Cdd:PLN03013 269 TGPEIWDDtKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTES----DILSGGKPGPHKIQGIGAGFIPKnld 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 749034310 243 KRIGDETFRLCQQyvddvvlvdnDEICASMKLIFENVRAISEPSGAASLAGLK 295
Cdd:PLN03013 345 QKIMDEVIAISSE----------EAIETAKQLALKEGLMVGISSGAAAAAAIK 387
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
30-107 |
1.20e-03 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 40.98 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNS-IFIKREDRQPVHSFKLRGAFAMISnLSKAQKEAGVIAAS-AGNHAQGVALSAKHLGLRALIVM 107
Cdd:cd06446 35 TPLYRAKRLSEYLGGAkIYLKREDLNHTGAHKINNALGQAL-LAKRMGKKRVIAETgAGQHGVATATACALFGLECEIYM 113
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
30-107 |
1.91e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 40.95 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQPVHSFKLRGAFAMiSNLSKAQKEAGVIAAS-AGNHAQGVALSAKHLGLRALIVM 107
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQ-ALLAKRMGKTRIIAETgAGQHGVATATACALFGLKCTIFM 349
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
30-107 |
2.78e-03 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 39.87 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749034310 30 TPLQKMEKLSERLGNSIFIKREDRQ--PVHSFKLRG-AFAMISNLSKAQKEAGVIAASAGNHAQGVALSAKHLGLRALIV 106
Cdd:PRK14045 22 TPIQYLPNISRELGADVYVKRDDLTglGIGGNKIRKlEYLLGDALSRGADVVITVGAVHSNHAFVTGLAAKKLGLDAVLV 101
|
.
gi 749034310 107 M 107
Cdd:PRK14045 102 L 102
|
|
| |
