|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-320 |
1.37e-139 |
|
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: 397.44 E-value: 1.37e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERG---CEHFVCSSAGNAGMAAAYAARKLGIPSTIV 86
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 87 VPSTTPALTIQRLKNEGATVKVVGETL-DEAIRVAKDLEKNNSGWVYVPPFDDPLIWEGHSSIVKELKETM--TEKPGAI 163
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 164 VLAVGGGGLLCGVVQGLAEVGWRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115497052 244 EVVSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQKLQGEgKLRTPLSSLVVIVCGGSNISLAQLVALKKQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
11-304 |
1.79e-52 |
|
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: 425586 [Multi-domain] Cd Length: 295 Bit Score: 174.42 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGIGHLCkMWAERGCE--HFVCSSAGNAGMAAAYAARKLGIPSTIVVP 88
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEGgkTVVEASSGNHGRALAAAAARLGLKVTIVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 89 STTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVLAVG 168
Cdd:pfam00291 87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLLCGVVQGLAEvGWRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGV-TTVAAQAMKVYREHPIFSEVVS 247
Cdd:pfam00291 167 GGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgFEPGALALDLLDEYVGEVVTVS 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 115497052 248 DQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQKLQGEgklrtplSSLVVIVCG 304
Cdd:pfam00291 246 DEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-------DRVVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine dehydratase [Amino acid transport and metabolism]; |
10-313 |
6.39e-47 |
|
Threonine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 224092 [Multi-domain] Cd Length: 347 Bit Score: 161.61 E-value: 6.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKmwAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:COG1171 25 PTPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGaynkLSSLSE--EEERAAGVIAASAGNHAQGVAYAAKRLGIKATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVL 165
Cdd:COG1171 103 VMPETTPKIKVDATRGYGAEVILHGDNFDDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILEQLPDLPDAVFV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 AVGGGGLLCGVVQGLAEVGWrDVPVITMETIGAESFHASTKAGKL-VTLPCITSVAKALGVTTVAAQAMKVYREHPIFSE 244
Cdd:COG1171 182 PVGGGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTFEILRELVDDIV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115497052 245 VVSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQKLQGEgklrtplsSLVVIVCGGsNISLAQL 313
Cdd:COG1171 261 LVDEDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGK--------TVVVILSGG-NIDFERL 320
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
10-308 |
5.71e-43 |
|
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: 149.94 E-value: 5.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGcehFVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:cd01562 17 RTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPATI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMtEKPGAIvl 165
Cdd:cd01562 94 VMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILEQV-PDLDAV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 avggggllcgvvqgLAEVG---------------WRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAA 230
Cdd:cd01562 170 --------------FVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 231 QAMKVYREHPifSEV--VSDQEAVAALEKFVDDEKILVEPACGAALAAVYSnviQKLQGEGKlrtplsSLVVIVCGGsNI 308
Cdd:cd01562 236 LTFEIIRKLV--DDVvtVSEDEIAAAMLLLFEREKLVAEPAGALALAALLS---GKLDLKGK------KVVVVLSGG-NI 303
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
11-305 |
9.54e-43 |
|
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: 147.66 E-value: 9.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERG---CEHFVCSSAGNAGMAAAYAARKLGIPSTIVV 87
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 88 PSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTE-KPGAIVla 166
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqKPDAVV-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 167 vggggllcgvvqglaevgwrdVPVITmetigaesfhASTkagklvtlpcITSVAKAL-----GVTTVAAQAmkvyrehpi 241
Cdd:cd00640 159 ---------------------VPVGG----------GGN----------IAGIARALkellpNVKVIGVEP--------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115497052 242 FSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQKLQGEgklrtplsSLVVIVCGG 305
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGK--------TVVVILTGG 244
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
11-310 |
2.49e-30 |
|
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: 118.31 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCehfVCSSAGNAGMAAAYAARKLGIPSTIV 86
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSEDQRQRGV---VAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 87 VPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELketMTEKP------ 160
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEI---MEDIPdvdtvi 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 161 ------GAIVLAVGGGGLLCGvvqglaevgwrDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMK 234
Cdd:TIGR01127 154 vpvgggGLISGVASAAKQINP-----------NVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFN 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115497052 235 VYREHPIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAVYSnviQKLQGEGKlrtplsSLVVIVCGGsNISL 310
Cdd:TIGR01127 223 IIKEYVDDVVTVDEEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGK------KIAVVLSGG-NIDL 288
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
10-321 |
2.08e-26 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 109.12 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCehfVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:PRK12483 37 ETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARGV---ITASAGNHAQGVALAAARLGVKAVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELketMTEKPGAIVL 165
Cdd:PRK12483 114 VMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 AVGGGGLLCGVVQGLAEVGW--RDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHpiFS 243
Cdd:PRK12483 190 IFVPVGGGGLIAGIAAYVKYvrPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHY--VD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 244 EV--VSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQK-LQGEgklrtplsSLVVIVcGGSNISLAQL--VALKK 318
Cdd:PRK12483 268 EVvtVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREgIEGQ--------TLVAID-SGANVNFDRLrhVAERA 338
|
...
gi 115497052 319 QLG 321
Cdd:PRK12483 339 ELG 341
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
10-321 |
2.67e-24 |
|
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: 102.89 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGI-GHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVP 88
Cdd:TIGR01124 17 ETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAyNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIVMP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 89 STTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVLAVG 168
Cdd:TIGR01124 97 ETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPVG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLLCgvvqGLAEVGWRDVP---VITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHPIFSEV 245
Cdd:TIGR01124 176 GGGLAA----GVAALIKQLMPeikVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDIVT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115497052 246 VSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQK-LQGEgklrtplsSLVVIVCgGSNISLAQL--VALKKQLG 321
Cdd:TIGR01124 252 VDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHgIRGQ--------TLVAILS-GANMNFHRLryVSERCELG 321
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
10-304 |
1.11e-22 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 97.90 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCehfVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:PRK09224 20 ETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIvl 165
Cdd:PRK09224 97 VMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAV-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 avggggllcgvvqgLAEVG---------------WRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAA 230
Cdd:PRK09224 174 --------------FVPVGgggliagvaayikqlRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115497052 231 QAMKVYREHpiFSEV--VSDQEAVAALEKFVDDEKILVEPAcGA-ALAAVYSNVIQ-KLQGEgklrtplsSLVVIVCG 304
Cdd:PRK09224 240 ETFRLCQEY--VDDVitVDTDEICAAIKDVFEDTRSIAEPA-GAlALAGLKKYVAQhGIEGE--------TLVAILSG 306
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
29-305 |
1.83e-22 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 95.41 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 29 LKLDSAQPSGSFKIRGIghLCKMWAER-GCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTPALTIQRLKNEGATVK 107
Cdd:PRK08246 41 LKLEHLQHTGSFKARGA--FNRLLAAPvPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 108 VVGETLDEAIRVAKDLEKnNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKP---------GAIVlavggggllcgvvq 178
Cdd:PRK08246 119 VVGAEYADALEAAQAFAA-ETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlvavgggGLIA-------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 179 GLAEVGWRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHPIFSEVVSDQEAVAALEKF 258
Cdd:PRK08246 184 GIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRAL 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 115497052 259 VDDEKILVEPACGAALAAVYSNVIQKLQGEgklrtplsSLVVIVCGG 305
Cdd:PRK08246 264 WEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
|
|
| PLN02970 |
PLN02970 |
serine racemase |
11-316 |
4.17e-21 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 92.05 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCehfVCSSAGNAGMAAAYAARKLGIPSTIV 86
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 87 VPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLeKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVLA 166
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARV-QQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 167 V--GGGGLLCGVVQGLAEvgwrDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGvTTVAAQAMKVYREhpIFSE 244
Cdd:PLN02970 184 SggGLISGIALAAKAIKP----SIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLR-ASLGDLTWPVVRD--LVDD 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115497052 245 V--VSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQ-KLQGEGKLRtplssLVVIVCGGsNISLAQLVAL 316
Cdd:PLN02970 257 VitVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRsNPAWKGCKN-----VGIVLSGG-NVDLGVLWES 325
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
10-307 |
5.62e-21 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 92.56 E-value: 5.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGcehFVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:PRK08639 25 ETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGaynaISQLSDEELAAG---VVCASAGNHAQGVAYACRHLGIPGVI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLK---NEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTE--KP 160
Cdd:PRK08639 102 FMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILEQLEKegSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 161 GAIVLAVGGGGLLCGVVQGLAEVGWRdVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHP 240
Cdd:PRK08639 181 DYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILKDVV 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 241 ifSEVVS-DQEAVAA--LEKFvDDEKILVEPAcGAALAAVYSNVIQKLQGegklrtplSSLVVIVCGGSN 307
Cdd:PRK08639 260 --DDVVLvPEGAVCTtiLELY-NKEGIVAEPA-GALSIAALELYKDEIKG--------KTVVCVISGGNN 317
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
9-275 |
1.42e-20 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 92.29 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 9 METPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGI-GHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 88 PSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKdLEKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVLAV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAK-QRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 168 GGGGLLCGVVQGLAEVGwRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHPIFSEVVS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260
....*....|....*....|....*...
gi 115497052 248 DQEAVAALEKFVDDEKILVEPACGAALA 275
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALA 373
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
10-277 |
1.12e-19 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 88.80 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCehfVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:PRK07334 23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGalnkLLLLTEEERARGV---IAMSAGNHAQGVAYHAQRLGIPATI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELketmtekpgaivl 165
Cdd:PRK07334 100 VMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 avggggllcgvvqgLAEVGWRDVPVIT--------------------METIG--AESFHASTKAGKLVTLPCITS-VAKA 222
Cdd:PRK07334 166 --------------LEDAPDLDTLVVPigggglisgmataakalkpdIEIIGvqTELYPSMYAAIKGVALPCGGStIAEG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 115497052 223 LGVTTVAAQAMKVYREHPIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAV 277
Cdd:PRK07334 232 IAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL 286
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
5-313 |
1.73e-19 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 87.06 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 5 RPLHMETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGcehFVCSSAGNAGMAAAYAARKLG 80
Cdd:PRK06815 15 RPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 81 IPSTIVVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKnNSGWVYVPPFDDPLIWEGHSSIVKELKETMtEKP 160
Cdd:PRK06815 92 IPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAE-QQGKVYISPYNDPQVIAGQGTIGMELVEQQ-PDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 161 GAIVLAVGGGGLLCGVVQGLAEVGwRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAK--ALGV-----TTVAAQAM 233
Cdd:PRK06815 170 DAVFVAVGGGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVepgaiTFPLCQQL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 234 ---KVyrehpifseVVSDQEAVAALEKFVDDEKILVEPACGAALAAvysnvIQKLQGEGKLRTplssLVVIVCgGSNISL 310
Cdd:PRK06815 249 idqKV---------LVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-----ALKLAPRYQGKK----VAVVLC-GKNIVL 309
|
...
gi 115497052 311 AQL 313
Cdd:PRK06815 310 EKY 312
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
10-312 |
3.77e-19 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 86.17 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEH-FVCSSAGNAGMAAAYAARKLGIPSTIVVP 88
Cdd:PRK07476 19 RTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARgVVTASTGNHGRALAYAARALGIRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 89 STTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMtekPGAIVLAVG 168
Cdd:PRK07476 99 RLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL---PDVATVLVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLLCGVVQGLAEVGWR-DVPVI--TMETiGAeSFHASTKAGKLVTLPCITSVAKALG--------VTTVAAQAMkvyr 237
Cdd:PRK07476 175 LSGGGLASGVAAAVKAIRpAIRVIgvSMER-GA-AMHASLAAGRPVQVEEVPTLADSLGggigldnrYTFAMCRAL---- 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115497052 238 ehpiFSEVV--SDQEAVAALEKFVDDEKILVEPACGAALAAVYsnviqklqgEGKLRTPLSSLVVIVCGGsNISLAQ 312
Cdd:PRK07476 249 ----LDDVVllDEAEIAAGIRHAYREERLVVEGAGAVGIAALL---------AGKIAARDGPIVVVVSGA-NIDMEL 311
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
10-310 |
7.59e-18 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 82.86 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGcehFVCSSAGNAGMAAAYAARKLGIPSTI 85
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 86 VVPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVL 165
Cdd:PRK08638 104 VMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIVP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 AVGGGGLLcgvvqGLAEVGWRDVPVITMETIGAESFH---ASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREhpIF 242
Cdd:PRK08638 183 IGGGGLIA-----GIAVALKSINPTIHIIGVQSENVHgmaASFYAGEITTHRTTGTLADGCDVSRPGNLTYEIVRE--LV 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497052 243 SEV--VSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQK-LQGEgklrtplsSLVVIVCGGsNISL 310
Cdd:PRK08638 256 DDIvlVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQyIQNK--------KVVAIISGG-NVDL 317
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
11-304 |
5.86e-17 |
|
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: 79.94 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGT-TAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPS 89
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGNTSASLAAYAARAGIKCVVFLPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 90 TTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsgWVYVPPFDDPLIWEGHSSIVKELKETM-TEKPGAIVLAVG 168
Cdd:cd01563 103 GKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLgWEVPDYVVVPVG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLLCGVVQG---LAEVGWRD-VP-VITMETIGAESFHASTKAGKLVTLP--CITSVAKALGVTTVA--AQAMKVYREH 239
Cdd:cd01563 181 NGGNITAIWKGfkeLKELGLIDrLPrMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRIGNPAsgPKALRAVRES 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115497052 240 PIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAVysnviQKLQGEGKLRTPlSSLVVIVCG 304
Cdd:cd01563 261 GGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGL-----KKLREEGIIDKG-ERVVVVLTG 319
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
10-311 |
4.94e-14 |
|
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: 71.42 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG-IGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVP 88
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 89 STTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMtekPGAIVLAVG 168
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADR-GLTMLPPFDHPDIVAGQGTLGLEVVEQM---PDLATVLVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLLCGVVQGLAEVGWR-DVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGVTTVAAQAMKVYREHPIFSEVV- 246
Cdd:TIGR02991 175 LSGGGLASGVAMAVKAARpDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALLDEIVl 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115497052 247 -SDQEAVAALEKFVDDEKILVEPACGAALAAVysnviqkLQGEGKLRTPLSSLVvivcGGSNISLA 311
Cdd:TIGR02991 255 vSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL-------LAGKIKNPGPCAVIV----SGRNIDMD 309
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
28-152 |
1.71e-12 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 67.34 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 28 YLKLDSAQPSGSFKIRGIGHLCKMWAERGCEH-FVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTPALTIQRLKNEGATV 106
Cdd:PRK08813 51 WLKLENLQRTGSYKVRGALNALLAGLERGDERpVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATV 130
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 115497052 107 KVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKEL 152
Cdd:PRK08813 131 RQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIEL 175
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-309 |
1.79e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 67.10 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRGI-GHLCKMwAERGC--EHFVCSSAGNAGMAAAYAARKLGIPSTIV 86
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVlNHLLEL-KEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 87 VPSTTPALTIQRLKNEGATVKVVgETLDEAIRVAKdlEKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKPGAIVLA 166
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAK--EDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 167 VGGGgllcgvvqGLAEVGWRDVPVI--TMETIGAESFHA-----STKAGKLVTLPCI-TSVAKALGVTTVAAQAMKVYRE 238
Cdd:PRK06608 179 CGGG--------GLISGTYLAKELIspTSLLIGSEPLNAndaylSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKK 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115497052 239 HPIFSEVVSDQEA--VAALEKFVddeKILVEPACGAALAAvysnVIQKLqgegKLRTPLSSLVVIVCGGsNIS 309
Cdd:PRK06608 251 LDDFYLVEEYEIYywTAWLTHLL---KVICEPSSAINMVA----VVNWL----KTQSKPQKLLVILSGG-NID 311
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
11-316 |
3.88e-11 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 63.11 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKMWAERGCEHFvcsSAGNAGMAAAYAARKLGIPSTIV 86
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIALSARLLGIPATIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 87 VPSTTPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKEtmtekpgaivla 166
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELFE------------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 167 vggggllcgvvqglaEVGWRDVPVITM--------------------ETIGAE---------SFHAstkaGKLVTLPCIT 217
Cdd:PRK07048 169 ---------------EVGPLDALFVCLggggllsgcalaaralspgcKVYGVEpeagndgqqSFRS----GEIVHIDTPR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 218 SVAKALGVTTVAAQAMKVYREHPIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAVYSNVIQkLQGegklrtplSS 297
Cdd:PRK07048 230 TIADGAQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP-LKG--------KR 300
|
330
....*....|....*....
gi 115497052 298 LVVIVCGGsNISLAQLVAL 316
Cdd:PRK07048 301 VGVIISGG-NVDLARFAAL 318
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
11-305 |
3.27e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 57.51 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVaGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPST 90
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 91 TPALTIQRLKNEGATVKVVGETLDEAIRVAKDLEKNNsGWVYVPPFDDPLIWEGHSSIVKELKETMTekPGAIVLAVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 171 GLLCGVVQGLAEVGWRDVPVITMETIGAESFHASTKAGKLVTLPCITSVAKALGV----TTVAAQAMKVYREHPIFSEVV 246
Cdd:PRK05638 223 SYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIASEILGNKTKCNETKALGLyvknPVMKEYVSEAIKESGGTAVVV 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 115497052 247 SDQEAVAAlEKFVDDEKILVEPACGAALAAVYsnviqKLQGEGKLRTPLSSLVVIVCGG 305
Cdd:PRK05638 303 NEEEIMAG-EKLLAKEGIFAELSSAVVMPALL-----KLGEEGYIEKGDKVVLVVTGSG 355
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-304 |
7.53e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 56.55 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAG-TTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPS 89
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 90 TTPALTIQRLKNEGATVKVVGETLDEAIR-VAKDLEKnnSGWVYVPPFDDPLIWEGHSSIVKELKETMT-EKPGAIVLAV 167
Cdd:PRK08197 160 DAPEITRLECALAGAELYLVDGLISDAGKiVAEAVAE--YGWFDVSTLKEPYRIEGKKTMGLELAEQLGwRLPDVILYPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 168 GGGGLLCGVVQGLAE---VGWRDVPVITMETIGAE-------SFHASTKAGKL----VTLPCITSVAKALGVTTVaaqaM 233
Cdd:PRK08197 238 GGGVGLIGIWKAFDEleaLGWIGGKRPRLVAVQAEgcapivkAWEEGKEESEFwedaHTVAFGIRVPKALGDFLV----L 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497052 234 KVYREHPIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAVysnviQKLQGEGKLRtPLSSLVVIVCG 304
Cdd:PRK08197 314 DAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA-----RQLRESGWLK-GDERVVLFNTG 378
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-313 |
1.41e-06 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 49.22 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 19 LSKVAGTTAYLKLDSAQPSGSFKIRG----IGHLCKmwAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTpal 94
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGglvyFDRLAR--RGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 95 tiQRLKNE-----GATVKVVGETLD----EAIRVAKDleknnSGWVYVPPFDDPLIwEGHSSIVKELketMTEKPGAivl 165
Cdd:PRK06110 105 --SVEKNAamralGAELIEHGEDFQaareEAARLAAE-----RGLHMVPSFHPDLV-RGVATYALEL---FRAVPDL--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 166 avggGGLLCGVVQG---LAEVGWRDVPVITMETIGAESFHA-----STKAGKLVTLPCITSVAKALGVTTVAAQAMKVYR 237
Cdd:PRK06110 171 ----DVVYVPIGMGsgiCGAIAARDALGLKTRIVGVVSAHApayalSFEAGRVVTTPVATTLADGMACRTPDPEALEVIR 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115497052 238 EHpiFSEV--VSDQEAVAALEKFVDDEKILVEPACGAALAAVysnviqkLQGEGKLRtplSSLVVIVCGGSNISLAQL 313
Cdd:PRK06110 247 AG--ADRIvrVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERLA---GKRVGLVLSGGNIDRAVF 312
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; |
21-276 |
2.31e-06 |
|
Threonine synthase [Amino acid transport and metabolism];
Pssm-ID: 223572 [Multi-domain] Cd Length: 411 Bit Score: 48.86 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 21 KVAGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPST-TPALTIQRL 99
Cdd:COG0498 90 GVLNDNLYVKELGHNPTGSFKDRGMTVLVSLAKELGAKTILCASSGNTGASAAAYAARAGLKVFVLYPKGkVSPGKLAQM 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 100 KNEGATVKVVGETLDEAIRVAKDLeKNNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEK-------P----GAIVLAVG 168
Cdd:COG0498 170 LTLGAHVIAVDGNFDDAQELVKEA-ANREGLLSAVNSINPYRLEGQKTYAFEIAEQLGWKapdhvvvPvgngGNLLAIYK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 169 GGGLlcgvvqgLAEVGW-----RDVPVitmETIGAESFHASTKAGKlvtlPCITSVAKAL--GVTTVAAQAMKVYREHPI 241
Cdd:COG0498 249 GFKE-------GLPIGKidkapNMNGV---QAEGFSPGVYAWKEGR----ETPETIAPAMdiGNPSNWERALFALRESGG 314
|
250 260 270
....*....|....*....|....*....|....*
gi 115497052 242 FSEVVSDQEAVAALEKFVDDEKILVEPACGAALAA 276
Cdd:COG0498 315 LAVAVSDEEILEAIKLLAEREGILIEPHSAVAVAA 349
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
24-154 |
2.08e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 45.59 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 24 GTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTPALTIQRLKNEG 103
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLG 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 115497052 104 ATVKVVG----ETLDEAIRVAKDleknnSGWVYVPPFDDPLIWEGHSSIVKELKE 154
Cdd:PRK08329 151 AELHFVEgdrmEVHEEAVKFSKR-----NNIPYVSHWLNPYFLEGTKTIAYEIYE 200
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
11-303 |
2.13e-05 |
|
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: 45.20 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 11 TPVRDSMTLSKVAGTTAYLKLDSAQPSGSFKIR-----------------------------GIGhLCkmwaergcehFV 61
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRialymiedaekrgllkpgttiieptsgntGIG-LA----------MV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 62 CssagnagmaaayaaRKLGIPSTIVVPSTTPALTIQRLKNEGATVKVVGETLDE----AIRVAKDLEKNNSGWVYVPPFD 137
Cdd:cd01561 72 A--------------AAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 138 DPLIWEGHSsivkelKETMTEkpgaIvlavggggllcgvvqglaevgWRDVPvitmetigaesfhastkaGKLVTLPC-- 215
Cdd:cd01561 138 NPANPEAHY------ETTAPE----I---------------------WEQLD------------------GKVDAFVAgv 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 216 -----ITSVAKAL-----GVTTVAAQAM------------------------KVYREHPIfSEV--VSDQEAVAALEKFV 259
Cdd:cd01561 169 gtggtITGVARYLkeknpNVRIVGVDPVgsvlfsggppgphkiegigagfipENLDRSLI-DEVvrVSDEEAFAMARRLA 247
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 115497052 260 DDEKILVEPACGAALAAVYsNVIQKLqGEGKLrtplssLVVIVC 303
Cdd:cd01561 248 REEGLLVGGSSGAAVAAAL-KLAKRL-GPGKT------IVTILP 283
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
28-277 |
3.60e-05 |
|
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: 44.68 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 28 YLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTPAL--TIQRLkNEGAT 105
Cdd:TIGR00260 41 YVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKISLgkLAQAL-GYNAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 106 VKVVGETLDEAIRVAKDLEKNNSGWVYVPPFDDPLIWEGHSSIVKE-LKETMTEKPGAIVLAVGGGGLLCGVVQGLAE-- 182
Cdd:TIGR00260 120 VVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEaVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEkk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 183 -VGWRDVPVitMETIGAESFH----ASTKAGKLVTLPCITSVAKAL--GVTTVAAQAMKVYREHPIFSEVVSDQEAVAAL 255
Cdd:TIGR00260 200 mLGLDSLPV--KRGIQAEGAAdivrAFLEGGQWEPIETPETLSTAMdiGNPANWPRALEAFRRSNGYAEDLSDEEILEAI 277
|
250 260
....*....|....*....|..
gi 115497052 256 EKFVDDEKILVEPACGAALAAV 277
Cdd:TIGR00260 278 KLLAREEGYFVEPHSAVAVAAL 299
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
10-160 |
1.64e-04 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 42.80 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 10 ETPVrdsmtlskVAGTTAYLKLDSAQPSGSFKIRGIGHLCKMWAERGCEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPS 89
Cdd:PRK06450 58 RTPL--------IKKGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPE 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497052 90 TTPALTIQRLKNEGATVKVVGETLDEAIRVAKdleknNSGWVYVPPFDDPLIWEGHSSIVKELKETMTEKP 160
Cdd:PRK06450 130 TASGGKLKQIESYGAEVVRVRGSREDVAKAAE-----NSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKI 195
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; |
19-303 |
4.11e-03 |
|
Cysteine synthase [Amino acid transport and metabolism];
Pssm-ID: 223110 [Multi-domain] Cd Length: 300 Bit Score: 38.29 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 19 LSKVAGTTAYLKLDSAQPSGSFKIRgIGH------LCKMWAERGcEHFVCSSAGNAGMAAAYAARKLGIPSTIVVPSTTP 92
Cdd:COG0031 20 LSPGTGVEIYAKLESFNPGGSVKDR-IALymiedaEKRGLLKPG-GTIVEATSGNTGIALAMVAAAKGYRLIIVMPETMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 93 ALTIQRLKNEGATVKVV---GETLDEAIRVAKDLEKNNSGWVYVPP-FDDPLIWEGHS-SIVKELKETMTEKPGAIvlav 167
Cdd:COG0031 98 QERRKLLRALGAEVILTpgaPGNMKGAIERAKELAAEIPGYAVWLNqFENPANPEAHYeTTGPEIWQQTDGKVDAF---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 168 ggggllcgvvqgLAEVGwrdvpvitmeTIGaesfhasTkagklvtlpcITSVAKAL-----GVTTVAAQA---------- 232
Cdd:COG0031 174 ------------VAGVG----------TGG-------T----------ITGVARYLkernpNVRIVAVDPegsvllsgge 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497052 233 --------------MKVYREHPIFSEVVSDQEAVAALEKFVDDEKILVEPACGAALAAvYSNVIQKLqGEGKlrtplsSL 298
Cdd:COG0031 215 gphkiegigagfvpENLDLDLIDEVIRVSDEEAIATARRLAREEGLLVGISSGAALAA-ALKLAKEL-PAGK------TI 286
|
....*
gi 115497052 299 VVIVC 303
Cdd:COG0031 287 VTILP 291
|
|
|