|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
4-319 |
0e+00 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 565.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 4 PTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQ 83
Cdd:PRK07048 6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 84 AIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKE 163
Cdd:PRK07048 86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 164 LLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTF 243
Cdd:PRK07048 166 LFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTF 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631 244 AIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK07048 246 PIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
6-309 |
1.09e-150 |
|
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: 424.98 E-value: 1.09e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 6 YGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAI 85
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 86 ALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL 165
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 166 EEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAI 245
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631 246 IRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVD 309
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
1-317 |
3.90e-144 |
|
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: 409.43 E-value: 3.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGN 80
Cdd:COG1171 3 ALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 81 HAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTS 160
Cdd:COG1171 83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 161 AKELLEEVGQLDALFVPlggggllsgsalaaRSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGE 240
Cdd:COG1171 163 ALEILEQLPDLDAVFVPvggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGE 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631 241 YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:COG1171 243 LTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEIL 319
|
|
| PLN02970 |
PLN02970 |
serine racemase |
5-318 |
1.72e-133 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 382.49 E-value: 1.72e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PLN02970 10 DLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PLN02970 90 LALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQhLGEYTFA 244
Cdd:PLN02970 170 LEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322631 245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL---LKKEELV--GKKVGIILSGGNVDMKRYATLIS 318
Cdd:PLN02970 249 VVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsdsFRSNPAWkgCKNVGIVLSGGNVDLGVLWESFS 327
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
1-316 |
2.29e-85 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 260.47 E-value: 2.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE-KRSKGVIAFSSG 79
Cdd:PRK06608 2 LLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQgKLPDKIVAYSTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 80 NHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIgrQLAAEHGFALIPPYDHPDVIAGQGT 159
Cdd:PRK06608 82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKA--KEDEEQGFYYIHPSDSDSTIAGAGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 160 SAKELLEEVG-QLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHIN-TPKTIADGAQTQH 237
Cdd:PRK06608 160 LCYEALQQLGfSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNySPNTIADGLKTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 238 LGEYTFAIIREnVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEElVGKKVGIILSGGNVDMKRYAT 315
Cdd:PRK06608 240 VSARTFEYLKK-LDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAvvNWLKTQS-KPQKLLVILSGGNIDPILYNE 317
|
.
gi 6322631 316 L 316
Cdd:PRK06608 318 L 318
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
5-317 |
3.04e-85 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 260.05 E-value: 3.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PRK08638 10 AIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK08638 90 VALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFA 244
Cdd:PRK08638 170 LEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322631 245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVE-----PTACLgFAGALlkKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:PRK08638 250 IVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEgagalATAAL-LSGKL--DQYIQNKKVVAIISGGNVDLSRVSQIT 324
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
23-317 |
1.64e-83 |
|
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: 256.98 E-value: 1.64e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 103 DAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGG 182
Cdd:TIGR01127 81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 183 LLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELV 262
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6322631 263 KCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKII 295
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
5-309 |
3.77e-79 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 246.73 E-value: 3.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PRK07334 6 TLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK07334 86 VAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAgNDGQQSFRSGSIVHINTpKTIADGAQTQHLGEYTFA 244
Cdd:PRK07334 166 LEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTEL-YPSMYAAIKGVALPCGG-STIAEGIAVKQPGQLTLE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322631 245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVD 309
Cdd:PRK07334 244 IVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNID 308
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
6-318 |
2.05e-77 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 239.59 E-value: 2.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 6 YGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAI 85
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 86 ALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL 165
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 166 EEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADG-AQTQHLGEYTFA 244
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGtAGGVEPGAITFP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631 245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLIS 318
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEAVS 317
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
15-312 |
1.92e-73 |
|
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: 235.01 E-value: 1.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 15 RIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNV 94
Cdd:TIGR01124 10 RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 95 PATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDA 173
Cdd:TIGR01124 90 KALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANpLDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 174 LFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDI 253
Cdd:TIGR01124 170 VFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631 254 LTVSDQELVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGlkKYVALHGIRGQTLVAILSGANMNFHR 310
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
16-305 |
2.31e-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: 228.35 E-value: 2.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVP 95
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 96 ATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAE-HGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDA 173
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 174 LFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQ-HLGEYTFAIIRENVDD 252
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6322631 253 ILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV--GKKVGIILSG 305
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELkgGDRVVVVLTG 295
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
8-323 |
1.83e-69 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 219.07 E-value: 1.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 8 DVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK07476 5 DIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 88 SAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEE 167
Cdd:PRK07476 85 AARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 168 VGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGaqtqhLG-------E 240
Cdd:PRK07476 165 LPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADS-----LGggigldnR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 241 YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISGK 320
Cdd:PRK07476 240 YTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIINGE 319
|
...
gi 6322631 321 EDG 323
Cdd:PRK07476 320 VAD 322
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
13-312 |
2.08e-66 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 216.97 E-value: 2.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 13 SNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLL 92
Cdd:PRK12483 28 AARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 93 NVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL-EEVGQL 171
Cdd:PRK12483 108 GVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILrQHPGPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 172 DALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVD 251
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVD 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631 252 DILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGA--LLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:PRK12483 268 EVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIkkYAEREGIEGQTLVAIDSGANVNFDR 330
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
8-314 |
5.87e-66 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 213.13 E-value: 5.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 8 DVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK08639 11 DIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 88 SAKLLNVPATIVMPEDAPALKVAATAGYGA---HIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK08639 91 ACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEVGQL---DALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEY 241
Cdd:PRK08639 171 LEQLEKEgspDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDL 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631 242 TFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYA 314
Cdd:PRK08639 251 TFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMP 323
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
22-312 |
1.85e-65 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 214.23 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK09224 20 ETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDALFVPLGG 180
Cdd:PRK09224 100 VTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PRK09224 180 GGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDE 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631 261 LVKCMHFLAERMKVVVEPTACLGFAGalLKK----EELVGKKVGIILSGGNVDMKR 312
Cdd:PRK09224 260 ICAAIKDVFEDTRSIAEPAGALALAG--LKKyvaqHGIEGETLVAILSGANMNFDR 313
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
23-306 |
4.05e-59 |
|
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: 190.03 E-value: 4.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE-KRSKGVIAF-SSGNHAQAIALSAKLLNVPATIVM 100
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEgKLPKGVIIEsTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 101 PEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAE-HGFALIPPYDHPDVIAGQGTSAKELLEEVGQ--LDALFVP 177
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 178 LGGGGLLSGSALAARSLSPGCKIFGVEPEagndgqqsfrsgsivhintpktiadgaqtqhlgeytfaiirenvddILTVS 257
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6322631 258 DQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIILSGG 306
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALkLAKKLGKGKTVVVILTGG 244
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
5-319 |
5.87e-57 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 186.98 E-value: 5.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:TIGR02991 2 TLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:TIGR02991 82 LAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIAD--GAQTQHLGEYT 242
Cdd:TIGR02991 162 VEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631 243 FAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVgIILSGGNVDMKRYATLISG 319
Cdd:TIGR02991 242 FAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGPCA-VIVSGRNIDMDLHKRIIDG 317
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
23-319 |
8.32e-56 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 184.04 E-value: 8.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEK-RSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK06110 22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNR-YTEDREQIGRqLAAEHGFALIPPYdHPDVIAGQGTSAKELLEEVGQLDALFVPLGG 180
Cdd:PRK06110 102 HGNSVEKNAAMRALGAELIEHGEdFQAAREEAAR-LAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPIGM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PRK06110 180 GSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDE 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322631 261 LVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK06110 260 VAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLAG 318
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
22-312 |
6.79e-53 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 182.81 E-value: 6.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PLN02550 109 ESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEV-GQLDALFVPLGG 180
Cdd:PLN02550 189 VTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHqGPLHAIFVPVGG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PLN02550 269 GGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDA 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6322631 261 LVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:PLN02550 349 ICASIKDMFEEKRSILEPAGALALAGaeAYCKYYGLKDENVVAITSGANMNFDR 402
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
1-309 |
2.27e-49 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 167.05 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMlNDRLGAQIYFKGENFQRVGAFKFRGAMNAVskLSDEKRSKGVIAFSSGN 80
Cdd:PRK08246 2 HAMITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 81 HAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRY-NRYTeDREQIGRQLAAEHGFALIPPYDHPDVIAGQGT 159
Cdd:PRK08246 79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVgAEYA-DALEAAQAFAAETGALLCHAYDQPEVLAGAGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 160 SAKELLEEVGQLDALFVPLGGGGLLSGSALAarsLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLG 239
Cdd:PRK08246 158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIAAW---FEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322631 240 EYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAgALL--KKEELVGKKVGIILSGGNVD 309
Cdd:PRK08246 235 EIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALA-ALLsgAYVPAPGERVAVVLCGANTD 305
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
8-318 |
9.68e-45 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 155.94 E-value: 9.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 8 DVLDASNRIKEYVNKTPVLTSrmlnDRLGaqIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK08813 25 DVLAAQARLRRYLSPTPLHYA----ERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 88 SAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEE 167
Cdd:PRK08813 99 SAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 168 VGqlDALFVPLGGGGLLSGSALAARslSPGCKIFGVEPEAGNDGQQSFRsGSIVHINTPKTIADGAQTQHLGEYTFAIIR 247
Cdd:PRK08813 179 AP--DVVIVPIGGGGLASGVALALK--SQGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCS 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631 248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAllkkEELVGKKVGIILSGGNVDMKRYATLIS 318
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAG----RRVSGKRKCAVVSGGNIDATVLATLLS 320
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
23-308 |
4.62e-24 |
|
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: 99.98 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQ-IYFKGENFQRVGAFKFRGAMNAVSKLSdEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:cd01563 23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAK-ELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIpPYDHPDVIAGQGTSAKELLEEVGQL--DALFVPLG 179
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS-NSLNPYRLEGQKTIAFEIAEQLGWEvpDYVVVPVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 180 GGGLLSGSALAARSLS--------PgcKIFGVEPEAGNDGQQSFRSG--SIVHINTPKTIADGAQ--TQHLGEYTFAIIR 247
Cdd:cd01563 181 NGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAAPIVRAFKEGkdDIEPVENPETIATAIRigNPASGPKALRAVR 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631 248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEElvgkkvGIILSGGNV 308
Cdd:cd01563 259 ESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE------GIIDKGERV 313
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
23-303 |
2.11e-22 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 96.42 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAfSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCA-SSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 103 D-APALKVAATAGYGAHIIRYN-RYtEDREQIGRQLAAEHGFALIPPYdHPDVIAGQGTSAKELLEEVGQL-DALFVP-- 177
Cdd:COG0498 146 GkVSPGQLAQMLTYGAHVIAVDgNF-DDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVpDWVVVPtg 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 178 -------LGGGGLLSGSALAARSLsPgcKIFGVEPEAGNDGQQSFRSG-SIVHINTPKTIADGAQTQH--LGEYTFAIIR 247
Cdd:COG0498 224 nggnilaGYKAFKELKELGLIDRL-P--RLIAVQATGCNPILTAFETGrDEYEPERPETIAPSMDIGNpsNGERALFALR 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631 248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIIL 303
Cdd:COG0498 301 ESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRkLREEGEIDPDEPVVV 357
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
22-307 |
3.08e-22 |
|
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: 94.67 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSK--GVIAFSSGNHAQAIALSAKLLNVPATIV 99
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEcvHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 100 MPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQL--AAEHGFALIPPYDHPDVIAGQGTSAKEL---LEEVGQLDAL 174
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElaENDPGPVYVHPFDDPLIWEGHSSMVDEIaqqLQSQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 175 FvplggggllsgsalaarsLSPG-------------------CKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQT 235
Cdd:cd06448 161 V------------------CSVGgggllngivqglerngwgdIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 236 QHLGEYTFAIIRENVDDILTVSDQELVK-CMHFLAERmKVVVEPtAC-----LGFAGALLK----KEELVGKKVGIILSG 305
Cdd:cd06448 223 KTVSSQALEYAQEHNIKSEVVSDRDAVQaCLRFADDE-RILVEP-ACgaalaVVYSGKILDlqleVLLTPLDNVVVVVCG 300
|
..
gi 6322631 306 GN 307
Cdd:cd06448 301 GS 302
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
23-177 |
1.01e-16 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 80.04 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGA-QIYFKGENFQRVGAFKFRGAMNAVSKlSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK08197 80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSR-AKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVG-QL-DALFVP 177
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGwRLpDVILYP 236
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
22-303 |
3.59e-15 |
|
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: 74.47 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALSAKLLNVPA 96
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDA--EKRgllKPGttIIEPTSGNTGIGLAMVAAAKGYRF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 97 TIVMPEDAPALKVAATAGYGAHIIR----YNRYTEDREQIGRQLAAEHGFALIP-PYDHPD-VIAGQGTSAKELLEEV-G 169
Cdd:cd01561 80 IIVMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETPNAFWLnQFENPAnPEAHYETTAPEIWEQLdG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 170 QLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEagndgqqsfrsGSIVHINTPKTiadGAQTQHLGE-YTFAII-R 247
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPV-----------GSVLFSGGPPG---PHKIEGIGAgFIPENLdR 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631 248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV-GKKVGIIL 303
Cdd:cd01561 226 SLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGpGKTIVTIL 282
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
23-305 |
4.58e-15 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 75.62 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLnDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKrSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:PRK05638 67 TPLIRARIS-EKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYA-ANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 103 DAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQlDALFVPLGGGG 182
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINP-THVIVPTGSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 183 LLSGSALAARSL-SPGC-----KIFGVEPEAGNDgqqsfrSGSIVHINTPK---TIADGAQTQH--LGEYTFAIIRENVD 251
Cdd:PRK05638 224 YLYSIYKGFKELlEIGVieeipKLIAVQTERCNP------IASEILGNKTKcneTKALGLYVKNpvMKEYVSEAIKESGG 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631 252 DILTVSDQELVKCMHFLAERmKVVVEPTACLGFAGALLKKEELV---GKKVGIILSG 305
Cdd:PRK05638 298 TAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYiekGDKVVLVVTG 353
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
34-307 |
2.34e-13 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 69.86 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 34 RLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAfSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATA 113
Cdd:PRK08329 69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 114 GYGA--HIIRYNRYTEDREQIgrQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGGLLSGSALAA 191
Cdd:PRK08329 148 RLGAelHFVEGDRMEVHEEAV--KFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGF 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 192 RSL------SPGCKIFGVEPEagndGQQSFRSGSivhiNTPKTIADGAQTQH--LGEYTFAIIRENVDDILTVSDQELVK 263
Cdd:PRK08329 226 KELhemgeiSKMPKLVAVQAE----GYESLCKRS----KSENKLADGIAIPEppRKEEMLRALEESNGFCISVGEEETRA 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6322631 264 CMHFLaERMKVVVEPTACLGFAG-ALLKKEELV--GKKVGIILSGGN 307
Cdd:PRK08329 298 ALHWL-RRMGFLVEPTSAVALAAyWKLLEEGLIegGSKVLLPLSGSG 343
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
23-306 |
3.10e-11 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 63.19 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLG-AQIYFKGENFQRVGAFKFRGAMNAVsKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK06381 16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHV-RRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTS--AKELLEEVGQL-DALFVPL 178
Cdd:PRK06381 95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDIEAYSaiAYEIYEALGDVpDAVAVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 179 GGGGLLSGSALAARSLSPGC------KIFGVEPEAGNDGQQSFRSGS--IVHINtPKTIADGAQTQHL-------GEYTF 243
Cdd:PRK06381 175 GNGTTLAGIYHGFRRLYDRGktsrmpRMIGVSTSGGNQIVESFKRGSseVVDLE-VDEIRETAVNEPLvsyrsfdGDNAL 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322631 244 AIIRENVDDILTVSDQELVKCMHFL--AERMKVVVEPTACLGFAGALLKKEELVGKKVgIILSGG 306
Cdd:PRK06381 254 EAIYDSHGYAFGFSDDEMVKYAELLrrMEGLNALPASASALAALVKYLKKNGVNDNVV-AVITGR 317
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
22-269 |
7.18e-10 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 59.51 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 22 KTPVLTSRMLNDRLG-AQIYFKGENfQRVG--AFKFRGAMNAVSKL------------------SDEKRSK-GVIAFSS- 78
Cdd:PRK08206 44 PTPLVALPDLAAELGvGSILVKDES-YRFGlnAFKALGGAYAVARLlaeklgldiselsfeeltSGEVREKlGDITFATa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 79 --GNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALI-----PPYDHP 151
Cdd:PRK08206 123 tdGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVqdtawEGYEEI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 152 --DVIAGQGTSAKELLEEVGQLDA----LFVPLGGGgllsgsalaarSLSPG-----CKIFG--------VEPEAGNDGQ 212
Cdd:PRK08206 203 ptWIMQGYGTMADEAVEQLKEMGVppthVFLQAGVG-----------SLAGAvlgyfAEVYGeqrphfvvVEPDQADCLY 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 213 QSFRSGSIVHI-------------NTPKTIAdgaqtqhlgeytFAIIRENVDDILTVSDQELVKCMHFLA 269
Cdd:PRK08206 272 QSAVDGKPVAVtgdmdtimaglacGEPNPLA------------WEILRNCADAFISCPDEVAALGMRILA 329
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
23-305 |
8.25e-10 |
|
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: 58.93 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 23 TPVLTSRMLNDRLGAQ-IYFKGENFQRVGAFKFRGAMNAVSKLSDEKRsKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:TIGR00260 23 TPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGN-DTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 102 EDAPAL-KVAATAGYGAHIIRYNRYTEDREQIGRQLAaEHGFAL-------IPPYdhpdvIAGQGTSAKELLEEVGQL-- 171
Cdd:TIGR00260 102 AGKISLgKLAQALGYNAEVVAIDGNFDDAQRLVKQLF-EDKPALglnsansIPYR-----LEGQKTYAFEAVEQLGWEap 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 172 DALFVPLGGGGLLSgsalaarSLSPGCKIF------------GVEPEAGNDGQQSFR-SGSIVHINTPKTIAD----GAQ 234
Cdd:TIGR00260 176 DKVVVPVPNSGNFG-------AIWKGFKEKkmlgldslpvkrGIQAEGAADIVRAFLeGGQWEPIETPETLSTamdiGNP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631 235 TQhlGEYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV---GKKVGIILSG 305
Cdd:TIGR00260 249 AN--WPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTadpAERVVCALTG 320
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
14-271 |
3.06e-08 |
|
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: 54.28 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 14 NRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALS 88
Cdd:COG0031 5 DSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDA--EKRgllKPGgtIVEATSGNTGIGLAMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 89 AKLLNVPATIVMPEDAPALKVAATAGYGAHIIRynryTEDREQIG------RQLAAEHGFALIP-PYDHPDVIAG--QGT 159
Cdd:COG0031 83 AAAKGYRLILVMPETMSKERRALLRAYGAEVVL----TPGAEGMKgaidkaEELAAETPGAFWPnQFENPANPEAhyETT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 160 sAKELLEEV-GQLDALFVPlggggllsgsalaaRSLSPGCKIFGVEPEagndgqqsfrsGSIVHintPKTIADGAQTQHL 238
Cdd:COG0031 159 -GPEIWEQTdGKVDAFVAGvgtggtitgvgrylKERNPDIKIVAVEPE-----------GSPLL---SGGEPGPHKIEGI 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 6322631 239 GEytfAII-----RENVDDILTVSDQELVKCMHFLAER 271
Cdd:COG0031 224 GA---GFVpkildPSLIDEVITVSDEEAFAMARRLARE 258
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
16-305 |
2.03e-07 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 51.66 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVN----KTPVLTsrmlndrlGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDeKRSKGVIAFSSGNHAQAIALSAKL 91
Cdd:PRK06450 48 IKHFISlgegRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 92 LNVPATIVMPEDAPALKVAATAGYGAHIIRYNrytEDREQIGRQlAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQL 171
Cdd:PRK06450 119 AGIEVKIFVPETASGGKLKQIESYGAEVVRVR---GSREDVAKA-AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 172 --DALFVPLGGGGLLSGSALAARSL------SPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQH--LGEY 241
Cdd:PRK06450 195 ipNYVFIPVSAGTLLLGVYSGFKHLldsgviSEMPKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRpfLLDY 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631 242 TFAIIRENVDDIlTVSDQELVKCMHFLAeRMKVVVEPTACLGFAGalLKKEElVGKKVgIILSG 305
Cdd:PRK06450 275 MVKALSEYGECI-VVSDNEIVEAWKELA-KKGLLVEYSSATVYAA--YKKYS-VNDSV-LVLTG 332
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
16-271 |
1.48e-05 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 45.73 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE---KRSKGVIAFSSGNHAQAIALSAKLL 92
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRgllKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 93 NVPATIVMPEDAPALKVAATAGYGAHIIrynrYTEDRE------QIGRQLAAE-HGFALIPPYDHPD-VIAGQGTSAKEL 164
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELI----LTPGEEgmkgaiDKAEELAAEtNKYVMLDQFENPAnPEAHYKTTGPEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 165 LEEV-GQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSgsivhintPKTIadgaqtQHLG-EYT 242
Cdd:TIGR01136 157 WRDTdGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPG--------PHKI------QGIGaGFI 222
|
250 260 270
....*....|....*....|....*....|
gi 6322631 243 FAII-RENVDDILTVSDQELVKCMHFLAER 271
Cdd:TIGR01136 223 PKILdLSLIDEVITVSDEDAIETARRLARE 252
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
16-120 |
1.56e-05 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 46.02 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALSAK 90
Cdd:PRK11761 6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQA--EKRgeiKPGdtLIEATSGNTGIALAMIAA 83
|
90 100 110
....*....|....*....|....*....|
gi 6322631 91 LLNVPATIVMPEDAPALKVAATAGYGAHII 120
Cdd:PRK11761 84 IKGYRMKLIMPENMSQERRAAMRAYGAELI 113
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
33-169 |
9.38e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 44.03 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 33 DRLGAQ------IYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSK----GVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:PLN02569 140 ERLGKEflgmndLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPA 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322631 103 DAPAL-KVAATAGYGAHIIRYNRYTEDREQIGRQLAAEhgfalIPPYD----HPDVIAGQGTSAKELLEEVG 169
Cdd:PLN02569 220 DKISIaQLVQPIANGALVLSIDTDFDGCMRLIREVTAE-----LPIYLanslNSLRLEGQKTAAIEILQQFD 286
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
16-303 |
1.58e-04 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 42.74 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVNKTPVLTsrmLN--DRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE---KRSKGVIAFSSGNHAQAIALSAK 90
Cdd:TIGR01139 1 ISELIGNTPLVR---LNriEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRgllKPGKTIVEPTSGNTGIALAMVAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 91 LLNVPATIVMPEDAPALKVAATAGYGAHIIrynrYTEDREQIG------RQLAAEHG--FALIPPYDHP-DVIAGQGTSA 161
Cdd:TIGR01139 78 ARGYKLILTMPETMSIERRKLLKAYGAELV----LTPGAEGMKgaiakaEEIAASTPnsYFMLQQFENPaNPEIHRKTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 162 KELLEEV-GQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEP---------EAGNDGQQSFRSGSIvhintPKtIAD 231
Cdd:TIGR01139 154 PEIWRDTdGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPaespvlsggKPGPHKIQGIGAGFI-----PK-NLN 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631 232 gaqtqhlgeytfaiiRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIIL 303
Cdd:TIGR01139 228 ---------------RSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALkLAKRPEPDKLIVVIL 285
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
245-298 |
1.37e-03 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 40.02 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6322631 245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKK 298
Cdd:cd06447 326 LMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKR 379
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
16-120 |
9.96e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 37.48 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631 16 IKEYVNK-TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMnAVSKLSDEKRSKGVIAFS-SGNHAQAIALSAKLLN 93
Cdd:PRK13803 264 LQNYAGRpTPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNAL-GQALLAKRMGKTRIIAETgAGQHGVATATACALFG 342
|
90 100 110
....*....|....*....|....*....|
gi 6322631 94 VPATIVMPED---APALKVAATAGYGAHII 120
Cdd:PRK13803 343 LKCTIFMGEEdikRQALNVERMKLLGANVI 372
|
|
|