|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
8-332 |
0e+00 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 568.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 8 GDTLSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVAN 87
Cdd:PRK10717 5 EDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 88 ALGYRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKYADPNHFQHVSRRMAEET-----EGAIWAGQFDNIANRKAHIEG 162
Cdd:PRK10717 85 ARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANREAHYET 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 163 TAQELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNYFAHGELKAEGSSVAEGIGQGRITAN 242
Cdd:PRK10717 165 TGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQGRITAN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 243 LEGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLvsegRENPQVATILCDTGFRYLSTLYNAEW 322
Cdd:PRK10717 245 LEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAREL----GPGHTIVTILCDSGERYQSKLFNPDF 320
|
330
....*....|
gi 736904736 323 LRSKGLPVFD 332
Cdd:PRK10717 321 LREKGLPVPR 330
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-316 |
5.58e-148 |
|
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: 418.68 E-value: 5.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 1 MNITAPIgdtLSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGI 80
Cdd:COG0031 1 MRIYDSI---LELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 81 GIALVANALGYRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKyaDPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHI 160
Cdd:COG0031 78 GLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAE--GMKGAIDKAEELAAETPGAFWPNQFENPANPEAHY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 161 EGTAQELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNyfahGElkAEGSSVAEGIGQGRIT 240
Cdd:COG0031 156 ETTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLS----GG--EPGPHKIEGIGAGFVP 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 241 ANLEGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpqVATILCDTGFRYLST 316
Cdd:COG0031 230 KILDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKT----IVTILPDSGERYLST 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
15-315 |
3.30e-141 |
|
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: 401.12 E-value: 3.30e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQSKEKMDTLRALGAELVLVPPTKYADPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQELWHQTEGR 174
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 175 IDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNYFAHGELKaegssvAEGIGQGRITANLEGAPIDTQFRI 254
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHK------IEGIGAGFIPENLDRSLIDEVVRV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736904736 255 SDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpqVATILCDTGFRYLS 315
Cdd:cd01561 235 SDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKT----IVTILPDSGERYLS 291
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
11-316 |
5.55e-93 |
|
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: 279.17 E-value: 5.55e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 11 LSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANALG 90
Cdd:TIGR01136 2 EELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 91 YRTVIVMPDNQSKEKMDTLRALGAELVLVPP---TKYAdpnhfQHVSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQEL 167
Cdd:TIGR01136 82 YKLILTMPETMSLERRKLLRAYGAELILTPGeegMKGA-----IDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 168 WHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNYFAHGELKaegssvAEGIGQGRITANLEGAP 247
Cdd:TIGR01136 157 WRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHK------IQGIGAGFIPKILDLSL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736904736 248 IDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLvseGRENPQVATILCDTGFRYLST 316
Cdd:TIGR01136 231 IDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRL---ENADKVIVAILPDTGERYLST 296
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
9-338 |
3.32e-91 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 279.76 E-value: 3.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 9 DTLSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANA 88
Cdd:TIGR01137 4 NILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 89 LGYRTVIVMPDNQSKEKMDTLRALGAELVlVPPTKYA--DPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQE 166
Cdd:TIGR01137 84 KGYKCIIVLPEKMSSEKVDVLRALGAEIV-RTPTAAAfdSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 167 LWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALynyfAHGE-LKAEGSS--VAEGIGQGRITANL 243
Cdd:TIGR01137 163 ILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSIL----AQPEeLNQTGRTpyKVEGIGYDFIPTVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 244 EGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQlvsEGRENPQVATILCDTGFRYLSTLYNAEWL 323
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAED---ELQEGQRCVVLLPDSIRNYMTKFLNDEWM 315
|
330
....*....|....*
gi 736904736 324 RSKGLPVFDWLERGD 338
Cdd:TIGR01137 316 LDNGFLDDEDLTVKD 330
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
10-316 |
2.11e-88 |
|
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: 267.31 E-value: 2.11e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 10 TLSLIGNTPLVRLSGPSEAAGcDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANAL 89
Cdd:TIGR01139 1 ISELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 90 GYRTVIVMPDNQSKEKMDTLRALGAELVLVPPtkyadpnhfqhvSRRM------AEET-----EGAIWAGQFDNIANRKA 158
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPG------------AEGMkgaiakAEEIaastpNSYFMLQQFENPANPEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 159 HIEGTAQELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALynyFAHGElkaEGSSVAEGIGQGR 238
Cdd:TIGR01139 148 HRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV---LSGGK---PGPHKIQGIGAGF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736904736 239 ITANLEGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpqVATILCDTGFRYLST 316
Cdd:TIGR01139 222 IPKNLNRSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKL----IVVILPSTGERYLST 295
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
14-328 |
6.51e-86 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 265.32 E-value: 6.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 14 IGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANALGYRT 93
Cdd:PLN02356 51 IGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKC 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 94 VIVMPDNQSKEKMDTLRALGAELVLVPPTKYADPNHFQHVSRRMAEET-------------------------------- 141
Cdd:PLN02356 131 HVVIPDDVAIEKSQILEALGATVERVRPVSITHKDHYVNIARRRALEAnelaskrrkgsetdgihlektngciseeeken 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 142 -------EGAIWAGQFDNIANRKAHIEGTAQELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAAL 214
Cdd:PLN02356 211 slfssscTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 215 YNYFAHGEL----KAEG-------SSVAEGIGQGRITANLEGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVA 283
Cdd:PLN02356 291 FNKVTRGVMytreEAEGrrlknpfDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCV 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 736904736 284 GAIELGrQLVSEGRenpQVATILCDTGFRYLSTLYNAEWLRSKGL 328
Cdd:PLN02356 371 GAVRVA-QSLGPGH---TIVTILCDSGMRHLSKFHDPQYLSQHGL 411
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
13-316 |
1.34e-80 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 247.48 E-value: 1.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 13 LIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANALGYR 92
Cdd:PRK11761 9 TIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 93 TVIVMPDNQSKEKMDTLRALGAELVLVPPTK---YAdpnhfQHVSRRMAEETEGAIwAGQFDNIANRKAHIEGTAQELWH 169
Cdd:PRK11761 89 MKLIMPENMSQERRAAMRAYGAELILVPKEQgmeGA-----RDLALQMQAEGEGKV-LDQFANPDNPLAHYETTGPEIWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 170 QTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPhgaalynyfahgelkAEGSSVAeGI---GQGRITANLEGA 246
Cdd:PRK11761 163 QTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQP---------------EEGSSIP-GIrrwPEEYLPKIFDAS 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 247 PIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLvsegrENPQVATILCDTGFRYLST 316
Cdd:PRK11761 227 RVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-----PNAVIVAIICDRGDRYLST 291
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
17-308 |
2.91e-70 |
|
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: 218.92 E-value: 2.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELrPAGTVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLVPptkyADPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHIeGTAQELWHQTEG-RI 175
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVP----GDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 176 DGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGaalynyfahgelkaegssvaegigqgritanlegapidtqFRIS 255
Cdd:cd00640 155 DAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPEV----------------------------------------VTVS 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 736904736 256 DEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpqVATILCD 308
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKT----VVVILTG 243
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
13-308 |
1.60e-69 |
|
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: 219.10 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 13 LIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERgelRPAGTVIEGTAGNTGIGIALVANALGYR 92
Cdd:pfam00291 4 GIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 93 TVIVMPDNQSKEKMDTLRALGAELVLVPptkyADPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHiEGTAQELWHQTE 172
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVG----GDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGY-GTIGLEILEQLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 173 GRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGA-ALYNYFAHGEL--KAEGSSVAEGIGQGRITANLE----G 245
Cdd:pfam00291 156 GDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPvpVPVADTIADGLGVGDEPGALAldllD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736904736 246 APIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpQVATILCD 308
Cdd:pfam00291 236 EYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD---RVVVVLTG 295
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
11-316 |
1.50e-67 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 214.01 E-value: 1.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 11 LSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTVIEGTAGNTGIGIALVANALG 90
Cdd:TIGR01138 3 EQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 91 YRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKYADPNhfQHVSRRMAEETEGAIwAGQFDNIANRKAHIEGTAQELWHQ 170
Cdd:TIGR01138 83 YRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGA--RDLALELANRGEGKL-LDQFNNPDNPYAHYTSTGPEIWQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 171 TEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPhgaalynyfahgelkAEGSSVaEGIG---QGRITANLEGAP 247
Cdd:TIGR01138 160 TGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQP---------------EEGSSI-PGIRrwpTEYLPGIFDASL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736904736 248 IDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLvsegrENPQVATILCDTGFRYLST 316
Cdd:TIGR01138 224 VDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAREL-----PDAVVVAIICDRGDRYLST 287
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
9-317 |
3.49e-60 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 195.91 E-value: 3.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 9 DTLSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTV-IEGTAGNTGIGIALVAN 87
Cdd:PLN02565 8 DVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 88 ALGYRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKyADPNHFQHvSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQEL 167
Cdd:PLN02565 88 AKGYKLIITMPASMSLERRIILLAFGAELVLTDPAK-GMKGAVQK-AEEILAKTPNSYILQQFENPANPKIHYETTGPEI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 168 WHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNYFAHGELKaegssvAEGIGQGRITANLEGAP 247
Cdd:PLN02565 166 WKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHK------IQGIGAGFIPGVLDVDL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 248 IDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpQVATILCDTGFRYLSTL 317
Cdd:PLN02565 240 LDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGK---LIVVIFPSFGERYLSSV 306
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
9-330 |
1.56e-58 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 191.75 E-value: 1.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 9 DTLSLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPA-GTVIEGTAGNTGIGIALVAN 87
Cdd:PLN00011 10 DVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 88 ALGYRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKYAdpNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQEL 167
Cdd:PLN00011 90 ARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGL--KGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 168 WHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALynyFAHGElkaEGSSVAEGIGQGRITANLEGAP 247
Cdd:PLN00011 168 WRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAV---LSGGQ---PGPHLIQGIGSGIIPFNLDLTI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 248 IDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpQVATILCDTGFRYLST-LYNAEWLRSK 326
Cdd:PLN00011 242 VDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGK---LIVVIFPSGGERYLSTkLFESVRYEAE 318
|
....
gi 736904736 327 GLPV 330
Cdd:PLN00011 319 NLPI 322
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
13-317 |
1.80e-55 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 185.16 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 13 LIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTV-IEGTAGNTGIGIALVANALGY 91
Cdd:PLN02556 56 LIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTlIEPTSGNMGISLAFMAAMKGY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 92 RTVIVMPDNQSKEKMDTLRALGAELVLVPPTKYADPNHFQhvSRRMAEETEGAIWAGQFDNIANRKAHIEGTAQELWHQT 171
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKK--AYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 172 EGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPhgaALYNYFAHGElkaEGSSVAEGIGQGRITANLEGAPIDTQ 251
Cdd:PLN02556 214 LGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP---AESNVLNGGK---PGPHHITGNGVGFKPDILDMDVMEKV 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 252 FRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpQVATILCDTGFRYLSTL 317
Cdd:PLN02556 288 LEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPENKGK---LIVTVHPSFGERYLSSV 350
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
7-316 |
2.57e-55 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 186.52 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 7 IGDTLS-LIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGTV-IEGTAGNTGIGIAL 84
Cdd:PLN03013 113 IADNVSqLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 85 VANALGYRTVIVMPDNQSKEKMDTLRALGAELVLVPPTKyaDPNHFQHVSRRMAEETEGAIWAGQFDNIANRKAHIEGTA 164
Cdd:PLN03013 193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAK--GMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 165 QELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAALYNYFAHGELKaegssvAEGIGQGRITANLE 244
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHK------IQGIGAGFIPKNLD 344
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736904736 245 GAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRenpQVATILCDTGfRYLST 316
Cdd:PLN03013 345 QKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGK---LIAVSLFASG-RDIYT 412
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
17-239 |
9.66e-25 |
|
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: 102.04 E-value: 9.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR--DAEERgelrpAGTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALAslSEEER-----ARGVVAASAGNHAQGVAYAARLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQSKEKMDTLRALGAELVLVPPTkYADPnhfQHVSRRMAEEtEGAIW----------AGQfdnianrkahieGT- 163
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDT-YDDA---EAAAAELAEE-EGATFvhpfddpdviAGQ------------GTi 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736904736 164 AQELWHQTeGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAA-LYNYFAHGELKA--EGSSVAEGIGQGRI 239
Cdd:COG1171 163 ALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAaMYRSLAAGEPVTlpGVDTIADGLAVGRP 240
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
17-222 |
1.64e-22 |
|
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: 95.63 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEErgELRPAGtVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE--EERAKG-VVAASAGNHAQGVAYAAKLLGIPATIV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLVPPTkYADPnhfQHVSRRMAEETEG---------AIWAGQfdnianrkahieGT-AQE 166
Cdd:cd01562 95 MPETAPAAKVDATRAYGAEVVLYGED-FDEA---EAKARELAEEEGLtfihpfddpDVIAGQ------------GTiGLE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 736904736 167 LWHQTEGrIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGA-ALYNYFAHGE 222
Cdd:cd01562 159 ILEQVPD-LDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGApAMAQSLAAGK 214
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
17-307 |
1.01e-21 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 93.60 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR--DAEERGElrpagTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRllNEAQRQQ-----GVITASSGNHGQGVALAAKLAGIPVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQSKEKMDTLRALGAELVLVPptkyADPNHFQHVSRRMAEETeGAIWAGQFDN---IANrkahiEGT-AQELWHQ 170
Cdd:PRK06815 96 VYAPEQASAIKLDAIRALGAEVRLYG----GDALNAELAARRAAEQQ-GKVYISPYNDpqvIAG-----QGTiGMELVEQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 171 tEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDP-HGAALYNYFAHGELK--------AEGSsvAEGIGQGRITA 241
Cdd:PRK06815 166 -QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPaNSPSLYTSLEAGEIVevaeqptlSDGT--AGGVEPGAITF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 242 NLEGAPIDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLvsEGRenpQVATILC 307
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY--QGK---KVAVVLC 303
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
15-310 |
1.10e-19 |
|
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: 89.10 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERG----AKTIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQ-SKEKMDTLRALGAELVLVPPTkYADPnhfQHVSRRMAEETE----GAI-WAGqfdnianrkahIEGT---AQ 165
Cdd:COG0498 141 VFVPEGKvSPGQLAQMLTYGAHVIAVDGN-FDDA---QRLVKELAADEGlyavNSInPAR-----------LEGQktyAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 166 ELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKE-----KNSEI-RIALTDPHGAA-LYNYFAHGELKAE---GSSVAEGIg 235
Cdd:COG0498 206 EIAEQLGRVPDWVVVPTGNGGNILAGYKAFKElkelgLIDRLpRLIAVQATGCNpILTAFETGRDEYEperPETIAPSM- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 236 qgRI--TANLE----------GAPIdtqfRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAielgRQLVSEGRENPQVA 303
Cdd:COG0498 285 --DIgnPSNGEralfalresgGTAV----AVSDEEILEAIRLLARREGIFVEPATAVAVAGL----RKLREEGEIDPDEP 354
|
....*..
gi 736904736 304 TILCDTG 310
Cdd:COG0498 355 VVVLSTG 361
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
15-288 |
2.08e-16 |
|
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: 78.79 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAG-CDIWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRT 93
Cdd:cd01563 21 GNTPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELG----VKAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 94 VIVMPDNQSKEKMDTLRALGAELVLVPPTkyadpnhFQHVSRRMAEETEGAIWagqFDNIANRKAHIEGT---AQELWHQ 170
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEGN-------FDDALRLVRELAEENWI---YLSNSLNPYRLEGQktiAFEIAEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 171 TEGRI-DGFTCAAGTGGTIAGVGMGLKEknsEIRIALTD---------PHGAA-LYNYFAHGELKAEGSSVAEGIGQG-R 238
Cdd:cd01563 167 LGWEVpDYVVVPVGNGGNITAIWKGFKE---LKELGLIDrlprmvgvqAEGAApIVRAFKEGKDDIEPVENPETIATAiR 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736904736 239 ItanleGAPIDTQF-------------RISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIEL 288
Cdd:cd01563 244 I-----GNPASGPKalravresggtavAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKL 301
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
17-236 |
6.40e-15 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 75.56 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR----DAEERGelrpagtVIEGTAGNTGIGIALVANALGYR 92
Cdd:PRK09224 21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAqlteEQLARG-------VITASAGNHAQGVALSAARLGIK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 93 TVIVMPDNQSKEKMDTLRALGAELVLVPPTkYADPNhfQHvSRRMAEEtEGAIWAGQFDN---IANrkahiEGT-AQELW 168
Cdd:PRK09224 94 AVIVMPVTTPDIKVDAVRAFGGEVVLHGDS-FDEAY--AH-AIELAEE-EGLTFIHPFDDpdvIAG-----QGTiAMEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736904736 169 HQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHG-AALYNYFAHGE--------LKAEGSSVAEgIGQ 236
Cdd:PRK09224 164 QQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDsACLKAALEAGErvdlpqvgLFADGVAVKR-IGE 239
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
16-307 |
9.48e-15 |
|
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: 73.87 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 16 NTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRPAGtVIEGTAGNTGIGIALVANALGYRTVI 95
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECVH-VVCSSGGNAGLAAAYAARKLGVPCTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 96 VMPDNQSKEKMDTLRALGAELVLVPPTKYADPNHFQHvsrRMAEETEGAIWAGQFDNIANRKAH---IEGTAQELWHQte 172
Cdd:cd06448 80 VVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLRE---ELAENDPGPVYVHPFDDPLIWEGHssmVDEIAQQLQSQ-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 173 GRIDGFTCAAGTGGTIAGVGMGLKEKN-SEIRIALTDPHGAALYNY-FAHGELKA--EGSSVAEGIGQGRITAN-LEGA- 246
Cdd:cd06448 155 EKVDAIVCSVGGGGLLNGIVQGLERNGwGDIPVVAVETEGAHSLNAsLKAGKLVTlpKITSVATSLGAKTVSSQaLEYAq 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 247 --PIDTQFrISDEEGLVWVERLLRGEGLCLGLSSGINVAGA---IELGRQLVSEGRENPQVATILC 307
Cdd:cd06448 235 ehNIKSEV-VSDRDAVQACLRFADDERILVEPACGAALAVVysgKILDLQLEVLLTPLDNVVVVVC 299
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
17-258 |
1.23e-14 |
|
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: 74.01 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRpagTVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQR---GVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLvpptKYADPNHFQHVSRRMAEEtEGAIWAGQFDN---IANrkahiEGT-AQELWHQTe 172
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVIL----HGDDYDEAYAFATSLAEE-EGRVFVHPFDDefvMAG-----QGTiGLEIMEDI- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 173 GRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGA-ALYNYFAHGELKA--EGSSVAEGIG---QGRITANLEGA 246
Cdd:TIGR01127 147 PDVDTVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGApSMYESLREGKIKAveSVRTIADGIAvkkPGDLTFNIIKE 226
|
250
....*....|..
gi 736904736 247 PIDTQFRISDEE 258
Cdd:TIGR01127 227 YVDDVVTVDEEE 238
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
3-204 |
1.86e-14 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 74.06 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 3 ITAPIGDtlsLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAAL-WMIR---DAEERGelrpagtVIEGTAGNT 78
Cdd:PRK12483 27 LAARVYD---VARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYnKMARlpaEQLARG-------VITASAGNH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 79 GIGIALVANALGYRTVIVMPDNQSKEKMDTLRALGAELVLVP---PTKYAdpnHFQHVsrrmaEETEGAIWAGQFDN--- 152
Cdd:PRK12483 97 AQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGesfPDALA---HALKL-----AEEEGLTFVPPFDDpdv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 736904736 153 IANrkahiEGT-AQELWHQTEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRI 204
Cdd:PRK12483 169 IAG-----QGTvAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKV 216
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
17-190 |
5.11e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 69.03 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGelRPAGTVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLVPPTKYADpnhfqhvSRRMAEETEGAIWAGQFDN---IANrkahiEGT-AQELWHQTE 172
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILTNTRQEAE-------EKAKEDEEQGFYYIHPSDSdstIAG-----AGTlCYEALQQLG 169
|
170
....*....|....*...
gi 736904736 173 GRIDGFTCAAGTGGTIAG 190
Cdd:PRK06608 170 FSPDAIFASCGGGGLISG 187
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
17-231 |
1.15e-12 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 67.67 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGcDIWGKCEFANPGSSVKDRAALWMIRDAEErgelrPAGTVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:PRK08246 24 TPVLEADGAGFGPA-PVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLVpPTKYADPnhfQHVSRRMAEETeGAIWAGQFDNIANrkAHIEGTAQELWHQTEGRID 176
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVV-GAEYADA---LEAAQAFAAET-GALLCHAYDQPEV--LAGAGTLGLEIEEQAPGVD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 736904736 177 GFTCAAGTGGTIAGVGMGLKeknSEIRIALTDPHGA-ALYNYFAHGE-LKAEGSSVA 231
Cdd:PRK08246 171 TVLVAVGGGGLIAGIAAWFE---GRARVVAVEPEGApTLHAALAAGEpVDVPVSGIA 224
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
16-240 |
2.56e-12 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 67.23 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 16 NTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAAL--WMIRDAEERgelrpAGTVIEGTAGNTGIGIALVANALGYRT 93
Cdd:PRK07334 23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALnkLLLLTEEER-----ARGVIAMSAGNHAQGVAYHAQRLGIPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 94 VIVMPDNQSKEKMDTLRALGAELVLVPPTkYADPNHFqhvSRRMAEEtEG----------AIWAGQfdnianrkahieGT 163
Cdd:PRK07334 98 TIVMPRFTPTVKVERTRGFGAEVVLHGET-LDEARAH---ARELAEE-EGltfvhpyddpAVIAGQ------------GT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 164 -AQELWHQTeGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHG-AALYNYFAHGELKAEGSSVAEGIG---QGR 238
Cdd:PRK07334 161 vALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELyPSMYAAIKGVALPCGGSTIAEGIAvkqPGQ 239
|
..
gi 736904736 239 IT 240
Cdd:PRK07334 240 LT 241
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
26-222 |
4.52e-12 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 66.87 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 26 SEAAGCDIWGKCEFANPGSSVKDRAALWMI----RDAEERGelrpagtVIEGTAGNTGIGIALVANALGYRTVIVMPDNQ 101
Cdd:PLN02550 119 SERLGVKVLLKREDLQPVFSFKLRGAYNMMaklpKEQLDKG-------VICSSAGNHAQGVALSAQRLGCDAVIAMPVTT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 102 SKEKMDTLRALGAELVLVPPTKyadpNHFQHVSRRMAEEtEGAIWAGQFDN---IANrkahiEGT-AQELWHQTEGRIDG 177
Cdd:PLN02550 192 PEIKWQSVERLGATVVLVGDSY----DEAQAYAKQRALE-EGRTFIPPFDHpdvIAG-----QGTvGMEIVRQHQGPLHA 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 736904736 178 FTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGA-ALYNYFAHGE 222
Cdd:PLN02550 262 IFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDAnAMALSLHHGE 307
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
12-213 |
1.47e-11 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 64.83 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 12 SLIGNTPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR--DAEERgelrpAGTVIEGTAGNTGIGIALVANAL 89
Cdd:PRK08639 21 DVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISqlSDEEL-----AAGVVCASAGNHAQGVAYACRHL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 90 GYRTVIVMPDNQSKEKMDTLRALGA---ELVLVPPTkyadpnhF---QHVSRRMAEETeGAIWAGQFDN---IANrkahi 160
Cdd:PRK08639 96 GIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDT-------FddsAAAAQEYAEET-GATFIPPFDDpdvIAG----- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 161 EGT-AQELWHQ--TEGRIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGAA 213
Cdd:PRK08639 163 QGTvAVEILEQleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAA 218
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
15-197 |
2.38e-11 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 63.96 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAGCD-IWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRT 93
Cdd:PRK06381 14 GGTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLG----YSGITVGTCGNYGASIAYFARLYGLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 94 VIVMPDNQSKEKMDTLRALGAELVLVpPTKYADPNHFqhvSRRMAEETegaiwaGQFD-NIANRKAHIE-----GTAQEL 167
Cdd:PRK06381 90 VIFIPRSYSNSRVKEMEKYGAEIIYV-DGKYEEAVER---SRKFAKEN------GIYDaNPGSVNSVVDieaysAIAYEI 159
|
170 180 190
....*....|....*....|....*....|
gi 736904736 168 WHQTEGRIDGFTCAAGTGGTIAGVGMGLKE 197
Cdd:PRK06381 160 YEALGDVPDAVAVPVGNGTTLAGIYHGFRR 189
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
26-117 |
5.17e-11 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 62.70 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 26 SEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGElRPAGtVIEGTAGNTGIGIALVANALGYRTVIVMPDNQSKEK 105
Cdd:PRK06110 31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGP-RVRG-VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK 108
|
90
....*....|..
gi 736904736 106 MDTLRALGAELV 117
Cdd:PRK06110 109 NAAMRALGAELI 120
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
17-204 |
2.85e-10 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 60.52 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR---DAE-ERGelrpagtVIEGTAGNTGIGIALVANALGYR 92
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSsltDAEkRKG-------VVACSAGNHAQGVALSCALLGID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 93 TVIVMPDNQSKEKMDTLRALGAELVLVPPTkyadpnhFQHVSRRMAE--ETEGAIWAGQFDN---IANrkahiEGTA--- 164
Cdd:PRK08638 101 GKVVMPKGAPKSKVAATCGYGAEVVLHGDN-------FNDTIAKVEEivEEEGRTFIPPYDDpkvIAG-----QGTIgle 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 736904736 165 --QELWHqtegrIDGFTCAAGTGGTIAGVGMGLKEKNSEIRI 204
Cdd:PRK08638 169 ilEDLWD-----VDTVIVPIGGGGLIAGIAVALKSINPTIHI 205
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
15-204 |
2.02e-09 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 57.88 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAGCDIWGKCE----FANPGSsvKDRAALWMIRDAEERGelrpAGTVIegTAGntGIG------IAL 84
Cdd:COG2515 10 LPTPLQPLPRLSAALGVELWIKRDdltgPAIGGN--KTRKLEYLLADALAQG----ADTLV--TFG--GAQsnharaTAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 85 VANALGYRTVIVMPDNQSKEKMDTL---RALGAELVLVPPTKYADPN-HFQHVSRRMAEETEGA--IWAGQFDNIANrKA 158
Cdd:COG2515 80 AAAKLGLKCVLVLRGEEPTPLNGNLlldRLLGAELHFVSRGEYRDRDeAMEAVAAELRARGGKPyvIPEGGSNPLGA-LG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 736904736 159 HIEgTAQELWHQTEGRIDGFT---CAAGTGGTIAGVGMGLKEKNSEIRI 204
Cdd:COG2515 159 YVE-AAAELAAQLAELGVDFDyivVASGSGGTLAGLVAGLALLGSDTRV 206
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
17-258 |
2.80e-09 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 57.67 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR--DAEERgelrpAGTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLslSAQER-----ARGVVTASTGNHGRALAYAARALGIRAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVM----PDNqskeKMDTLRALGAELVLVPPTKyadpNHFQHVSRRMAEEtEGAIWAGQFDN---IANrkahiEGT-AQE 166
Cdd:PRK07476 95 ICMsrlvPAN----KVDAIRALGAEVRIVGRSQ----DDAQAEVERLVRE-EGLTMVPPFDDpriIAG-----QGTiGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 167 LWHQTEgriDGFTCAAGT--GGTIAGVGMGLKEKNSEIR-IALTDPHGAALYNYFAHGE--LKAEGSSVAEGIGQG---- 237
Cdd:PRK07476 161 ILEALP---DVATVLVPLsgGGLASGVAAAVKAIRPAIRvIGVSMERGAAMHASLAAGRpvQVEEVPTLADSLGGGigld 237
|
250 260
....*....|....*....|..
gi 736904736 238 -RITANLEGAPIDTQFRISDEE 258
Cdd:PRK07476 238 nRYTFAMCRALLDDVVLLDEAE 259
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
15-196 |
6.17e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 56.67 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRlsgpseaaGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKG----IKQISEDSSGNAGASIAAYGAAAGIEVK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQSKEKMDTLRALGAELVLVPPTKyadpnhfQHVSRrmAEETEGAIWAGQFDNIANRKAhIEGTAQELWHQTEGR 174
Cdd:PRK06450 125 IFVPETASGGKLKQIESYGAEVVRVRGSR-------EDVAK--AAENSGYYYASHVLQPQFRDG-IRTLAYEIAKDLDWK 194
|
170 180
....*....|....*....|...
gi 736904736 175 IDGFTCAAGTGGT-IAGVGMGLK 196
Cdd:PRK06450 195 IPNYVFIPVSAGTlLLGVYSGFK 217
|
|
| PLN02970 |
PLN02970 |
serine racemase |
17-212 |
4.22e-08 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 53.91 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIR----DAEERGelrpagtVIEGTAGNTGIGIALVANALGYR 92
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFslsdDQAEKG-------VVTHSSGNHAAALALAAKLRGIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 93 TVIVMPDNQSKEKMDTLRALGAELVLVPPTKYADpnhfQHVSRRMAEETeGAIWAGQFDN---IANrkahiEGT-AQELW 168
Cdd:PLN02970 101 AYIVVPKNAPACKVDAVIRYGGIITWCEPTVESR----EAVAARVQQET-GAVLIHPYNDgrvISG-----QGTiALEFL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 736904736 169 HQTEGrIDGFTCAAGTGGTIAGVGMGLKEKNSEIRIALTDPHGA 212
Cdd:PLN02970 171 EQVPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
17-190 |
1.62e-07 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 52.33 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSEAAGCDIWGKCE-FANPGSsVKDRAALWMIrdAEERGELRPAGtVIEGTAGNTGIGIALVANALGYRTVI 95
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCEnFQRMGA-FKFRGAYNAL--SQFSPEQRRAG-VVTFSSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 96 VMPDNQSKEKMDTLRALGAELVLVPPTKyadpNHFQHVSRRMAEETeGAIWAGQFDNianrkAHI---EGT-AQELWHQT 171
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYT----EDREEIGRRLAEER-GLTLIPPYDH-----PHViagQGTaAKELFEEV 170
|
170 180
....*....|....*....|
gi 736904736 172 eGRIDG-FTCAAGtGGTIAG 190
Cdd:PRK07048 171 -GPLDAlFVCLGG-GGLLSG 188
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
69-119 |
1.45e-06 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 49.49 E-value: 1.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 736904736 69 TVIEGTAGNTGIGIALVANALGYRTVIVMPDNQSKEKMDTLRALGAELVLV 119
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT 168
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
15-312 |
3.62e-06 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 48.27 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRlSGPSEAAGCDIWGKCEFANPGSSVKDRAALWMIRDAEERGELRpagtVIEGTAGNTGIGIALVANALGYRTV 94
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 95 IVMPDNQSKEKMDTLRALGAELVlvpptKYADP--NHFQHVSRRmaEETEGAIWAGQFDNIANrkahIEG---TAQELWH 169
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKII-----RYGESvdEAIEYAEEL--ARLNGLYNVTPEYNIIG----LEGqktIAFELWE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 170 QTEGriDGFTCAAGTGGTIAGVGMGLKE--KNSEIR-----IALTDPHGAALYNYFaHG------ELKAEGSSVAEGIGQ 236
Cdd:PRK05638 209 EINP--THVIVPTGSGSYLYSIYKGFKEllEIGVIEeipklIAVQTERCNPIASEI-LGnktkcnETKALGLYVKNPVMK 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736904736 237 GRITANLEGApiDTQFRISDEEGLVWVERLLRGEGLCLGLSSGINVAGAIELGRQLVSEGRENpqVATILCDTGFR 312
Cdd:PRK05638 286 EYVSEAIKES--GGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEKGDK--VVLVVTGSGLK 357
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
9-119 |
8.30e-06 |
|
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: 46.99 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 9 DTLSLI-GNTPLVRLSGPSEAAGCD-IWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVA 86
Cdd:TIGR00260 14 DLVDLGeGVTPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELG----NDTVLCASTGNTGAAAAAYA 89
|
90 100 110
....*....|....*....|....*....|....
gi 736904736 87 NALGYRTVIVMPDNQ-SKEKMDTLRALGAELVLV 119
Cdd:TIGR00260 90 GKAGLKVVVLYPAGKiSLGKLAQALGYNAEVVAI 123
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
17-119 |
1.17e-05 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 46.74 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSgpseaagCDIWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRTVIV 96
Cdd:PRK08329 65 TPTVKRS-------IKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEG----INEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100
....*....|....*....|...
gi 736904736 97 MPDNQSKEKMDTLRALGAELVLV 119
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFV 156
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
15-119 |
2.24e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 45.76 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 15 GNTPLVRLSGPSEAAGCD-IWGKCEFANPGSSVKDRAALWMIRDAEERGelrpAGTVIEGTAGNTGIGIALVANALGYRT 93
Cdd:PRK08197 78 GMTPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLAVGVSRAKELG----VKHLAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100
....*....|....*....|....*.
gi 736904736 94 VIVMPDNQSKEKMDTLRALGAELVLV 119
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLV 179
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
17-291 |
2.72e-04 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 42.02 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 17 TPLVRLSGPSE--AAGCDIWGKCEFANPGSSV---KDRAALWMIRDAEERGelrpAGTVIE--GTAGNTGIGIALVANAL 89
Cdd:cd06449 1 TPIQYLPRLSEhlGGKVEIYAKRDDCNSGLAFggnKIRKLEYLLPDALAKG----ADTLVTvgGIQSNHTRQVAAVAAKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 90 GYRTVIVM--PDNQSKEKMDT------LRALGAELVLVPPTKYADPNHFQHVSRRMAEETEG---AIWAGQFDNIANRKA 158
Cdd:cd06449 77 GLKCVLVQenWVPYSDAVYDRvgnillSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGkpyVIPAGGSEHPLGGLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 159 HIeGTAQELWHQTEG---RIDGFTCAAGTGGTIAGVGMGLKEKNSEIRI------ALTDPHGAALYNyFAHGELKAEGSS 229
Cdd:cd06449 157 YV-GFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVigidasAKPEKTKAQVLR-IAQAKLAEEGLE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736904736 230 VAEgigqgritanlEGAPIDTQFR-----ISDEEGLVWVERLLRGEGLCLG-LSSGINVAGAIELGRQ 291
Cdd:cd06449 235 VKE-----------EDVVLDDDYAapeygIPNDETIEAIKLCARLEGIITDpVYEGKSMQGMIDLVRN 291
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
33-114 |
3.60e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 41.92 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 33 IWGKCEFANPGSSVKDRAALWMIRDAEERGELRPagtVIEGTAGNTGIGIALVANALGYRTVIVMPDNQSKEKMDTLRAL 112
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHW 126
|
..
gi 736904736 113 GA 114
Cdd:PRK08813 127 GA 128
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
51-118 |
4.00e-04 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 41.82 E-value: 4.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736904736 51 ALWMIRDAeerGELRPAGTVIEgTAGNTGIGIALV--ANALGYRTVIVMPDNQSKEKM-DTLRALGAELVL 118
Cdd:cd08290 134 AYRLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEELkERLKALGADHVL 200
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
69-117 |
1.73e-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: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 736904736 69 TVIEGTAGNTGIGIALVANALGYRTVIVMPDNQSKEKMDTLRALGAELV 117
Cdd:cd06447 136 SIAVGSTGNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVV 184
|
|
| MDR2 |
cd08268 |
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
40-119 |
9.43e-03 |
|
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176229 [Multi-domain] Cd Length: 328 Bit Score: 37.58 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736904736 40 ANPGSSVKDRAALWMIRDA-----EERGELRPAGTVIEgTAGNTGIGIALV--ANALGYRTVIVmpdNQSKEKMDTLRAL 112
Cdd:cd08268 113 LPDGLSFVEAAALWMQYLTaygalVELAGLRPGDSVLI-TAASSSVGLAAIqiANAAGATVIAT---TRTSEKRDALLAL 188
|
....*..
gi 736904736 113 GAELVLV 119
Cdd:cd08268 189 GAAHVIV 195
|
|
| |
