|
Name |
Accession |
Description |
Interval |
E-value |
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
25-340 |
1.98e-147 |
|
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: 419.69 E-value: 1.98e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 25 IEAYRDWLPVsAKTPVITLHEGATPLIPVPTIAERIGkGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICAST 104
Cdd:cd01563 1 LWRYRELLPV-TEDDIVSLGEGNTPLVRAPRLGERLG-GKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACAST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 105 GNTSAAAAAYARRAGMRAFVLIPDGYvAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVNPYRLQGQK 184
Cdd:cd01563 79 GNTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNPYRLEGQK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 185 TAAFEIVDVLG-EAPDWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPLV--------YDTTVSDPNT 255
Cdd:cd01563 158 TIAFEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVrafkegkdDIEPVENPET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 256 IATAIRIGNPVNRAKAMAVREASDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDE--VPAGATVVCVL 333
Cdd:cd01563 238 IATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
|
....*..
gi 78170182 334 TGNGLKD 340
Cdd:cd01563 318 TGHGLKD 324
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
20-368 |
7.23e-137 |
|
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: 395.34 E-value: 7.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 20 DWPGLIeAYRDWLPVSAKTPVITLHEGATPLIPVPTIAERIGKgvRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAV 99
Cdd:COG0498 40 SRRGLW-RYRELLPFDDEEKAVSLGEGGTPLVKAPRLADELGK--NLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 100 ICASTGNTSAAAAAYARRAGMRAFVLIPDGYVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVNPYR 179
Cdd:COG0498 117 VCASSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINPAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 180 LQGQKTAAFEIVDVLGEAPDWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPLVYDT-------TVSD 252
Cdd:COG0498 197 LEGQKTYAFEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELGLIDRLPRLIAVQATGCNPILTAFetgrdeyEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 253 PNTIATAIRIGNPVNRAKAMAVREASDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDE--VPAGATVV 330
Cdd:COG0498 277 PETIAPSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVV 356
|
330 340 350
....*....|....*....|....*....|....*...
gi 78170182 331 CVLTGNGLKDPDCAINNNDAAFHTdLNPDLETVAKVMG 368
Cdd:COG0498 357 VLSTGHGLKFPDAVREALGGEPLA-VPPDLEAVKAAVE 393
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
25-342 |
4.66e-131 |
|
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: 378.26 E-value: 4.66e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 25 IEAYRDWLPVSaKTPVITLHEGATPLIPVPTIAERIGkGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICAST 104
Cdd:TIGR00260 1 VWRYREFLPVT-EKDLVDLGEGVTPLFRAPALAANVG-IKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCAST 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 105 GNTSAAAAAYARRAGMRAFVLIPDGYVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN--PYRLQG 182
Cdd:TIGR00260 79 GNTGAAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANsiPYRLEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 183 QKTAAFEIVDVLG-EAPDWLCIPMGNAGNITAYWMGFQEYHQAGHSrSLPRMMGFQASGSAPLV-------YDTTVSDPN 254
Cdd:TIGR00260 159 QKTYAFEAVEQLGwEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGLD-SLPVKRGIQAEGAADIVrafleggQWEPIETPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 255 TIATAIRIGNPVNRAKAMAVREASDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLK--RKDEVPAGATVVCV 332
Cdd:TIGR00260 238 TLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKlvEKGTADPAERVVCA 317
|
330
....*....|
gi 78170182 333 LTGNGLKDPD 342
Cdd:TIGR00260 318 LTGNGLKDPE 327
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
41-335 |
1.02e-65 |
|
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: 210.24 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 41 ITLHEGATPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEaGCEA--VICASTGNTSAAAAAYARRA 118
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKE-GEGGktVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 119 GMRAFVLIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFP-VTLVNSV-NPYRLQGQKTAAFEIVDVLGE 196
Cdd:pfam00291 78 GLKVTIVVPED-APPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPgAYYINQYdNPLNIEGYGTIGLEILEQLGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 197 APDWLCIPMGNAGNITAYWMGFQEyhqaghSRSLPRMMGFQASGSAPLV------YDTTVSDPNTIATAIRIGNPVNRaK 270
Cdd:pfam00291 157 DPDAVVVPVGGGGLIAGIARGLKE------LGPDVRVIGVEPEGAPALArslaagRPVPVPVADTIADGLGVGDEPGA-L 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78170182 271 AMAVREASDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGL-LKRKDEVPAGATVVCVLTG 335
Cdd:pfam00291 230 ALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
9-360 |
4.15e-65 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 214.29 E-value: 4.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 9 RRRFTANPVMQDWP--GLIEAYRDW-LPVSAKTPVITLHEGATPLIpvptIAERIGKGV----RVFVKYDGLNPTGSFKD 81
Cdd:PLN02569 92 RALFDSRVGKTTWPygSGVWSKKEWvLPEIDDDDIVSLFEGNSNLF----WAERLGKEFlgmnDLWVKHCGISHTGSFKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 82 RGMTMAISKAKEAG-----CEAVICASTGNTSAAAAAYARRAGMRAFVLIPDGYVAQGKLAQALVYGAEVLAIRGNFDRA 156
Cdd:PLN02569 168 LGMTVLVSQVNRLRkmakpVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSIDTDFDGC 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 157 LDIVREAADQFPVTLVNSVNPYRLQGQKTAAFEIVDVLG-EAPDWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMG 235
Cdd:PLN02569 248 MRLIREVTAELPIYLANSLNSLRLEGQKTAAIEILQQFDwEVPDWVIVPGGNLGNIYAFYKGFKMCKELGLVDRLPRLVC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 236 FQASGSAPLV--YDT------TVSDPNTIATAIRIGNPVNRAKA-MAVREaSDGAFLDVTDEEIINAyKLLGGGEGIFCE 306
Cdd:PLN02569 328 AQAANANPLYraYKSgweefkPVKANPTFASAIQIGDPVSIDRAvYALKE-SNGIVEEATEEELMDA-QAEADKTGMFLC 405
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 78170182 307 PASAASVAGLLKRKDEVPAGAT--VVCVLTGNGLKdpdcaINNNDAAFHTDLNPDL 360
Cdd:PLN02569 406 PHTGVALAALKKLRASGVIGPTdrTVVVSTAHGLK-----FTQSKIDYHSKEIPDM 456
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
48-335 |
3.48e-57 |
|
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: 186.57 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA---VICASTGNTSAAAAAYARRAGMRAFV 124
Cdd:cd00640 1 TPLVRLKRLSKLGG--ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgvIIESTGGNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 125 LIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFP-VTLVNS-VNPYRLQGQKTAAFEIV-DVLGEAPDWL 201
Cdd:cd00640 79 VMPEG-ASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPgAYYVNQfDNPANIAGQGTIGLEILeQLGGQKPDAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 202 CIPMGNAGNITAYWMGFQEYHqaghsrSLPRMMGFQAsgsaplvydttvsdpntiatairignpvnrakamavreasdgA 281
Cdd:cd00640 158 VVPVGGGGNIAGIARALKELL------PNVKVIGVEP------------------------------------------E 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 78170182 282 FLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTG 335
Cdd:cd00640 190 VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTG 243
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
28-342 |
2.46e-52 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 178.27 E-value: 2.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 28 YRDWLPVSAKTPVITLHEGATPLIPVPTIAERIGKGvRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICASTGNT 107
Cdd:PRK08197 60 YHELLPVRDPEHIVSLGEGMTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 108 SAAAAAYARRAGMRAFVLIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQ---FPV-TLvnsVNPYRLQGQ 183
Cdd:PRK08197 139 GAAWAAYAARAGIRATIFMPAD-APEITRLECALAGAELYLVDGLISDAGKIVAEAVAEygwFDVsTL---KEPYRIEGK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 184 KTAAFEIVDVLG-EAPDWLCIPMGNAGNITAYWMGFQEYHQAGH-SRSLPRMMGFQASGSAPLVY----DTTVS----DP 253
Cdd:PRK08197 215 KTMGLELAEQLGwRLPDVILYPTGGGVGLIGIWKAFDELEALGWiGGKRPRLVAVQAEGCAPIVKaweeGKEESefweDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 254 NTIATAIRIGNPV-NRAKAMAVREaSDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLK-RKD-EVPAGATVV 330
Cdd:PRK08197 295 HTVAFGIRVPKALgDFLVLDAVRE-TGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQlRESgWLKGDERVV 373
|
330
....*....|..
gi 78170182 331 CVLTGNGLKDPD 342
Cdd:PRK08197 374 LFNTGSGLKYPD 385
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
28-341 |
4.64e-45 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 160.36 E-value: 4.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 28 YRDWLPVSAKtpVITLHEGATPLIPVpTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICASTGNT 107
Cdd:PRK05638 49 YKELLPQVKK--IISLGEGGTPLIRA-RISEKLG--ENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 108 SAAAAAYARRAGMRAFVLIPDgYVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSV-NPYRLQGQKTA 186
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPR-KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEyNIIGLEGQKTI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 187 AFEIVDVLGeaPDWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPL---VYDTTVSDPNTIATAIRIG 263
Cdd:PRK05638 203 AFELWEEIN--PTHVIVPTGSGSYLYSIYKGFKELLEIGVIEEIPKLIAVQTERCNPIaseILGNKTKCNETKALGLYVK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 264 NPVNRAKAMAVREASDGAFLDVTDEEIINAYKLLgGGEGIFCEPASAASVAGLLKRKDE--VPAGATVVCVLTGNGLKDP 341
Cdd:PRK05638 281 NPVMKEYVSEAIKESGGTAVVVNEEEIMAGEKLL-AKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGSGLKGY 359
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
28-339 |
6.45e-40 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 144.58 E-value: 6.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 28 YRDWLPVSAKTpVITLHEGATPLIPVPtiaerigkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICASTGNT 107
Cdd:PRK08329 46 YIDYLPVDEEF-LPHLTPPITPTVKRS---------IKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 108 SAAAAAYARRAGMRAFVLIPDgYVAQGKLAQALVYGAEVLAIRGnfDRALdiVREAADQFP----VTLVNS-VNPYRLQG 182
Cdd:PRK08329 116 ALSLALYSLSEGIKVHVFVSY-NASKEKISLLSRLGAELHFVEG--DRME--VHEEAVKFSkrnnIPYVSHwLNPYFLEG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 183 QKTAAFEIVDVLGeAPDWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPLVYDTtvSDPNTIATAIRI 262
Cdd:PRK08329 191 TKTIAYEIYEQIG-VPDYAFVPVGSGTLFLGIWKGFKELHEMGEISKMPKLVAVQAEGYESLCKRS--KSENKLADGIAI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78170182 263 GNPVNRAKAMAVREASDGAFLDVTDEEIINAYKLLgGGEGIFCEPASAASVAGLLKRKDE--VPAGATVVCVLTGNGLK 339
Cdd:PRK08329 268 PEPPRKEEMLRALEESNGFCISVGEEETRAALHWL-RRMGFLVEPTSAVALAAYWKLLEEglIEGGSKVLLPLSGSGLK 345
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
46-335 |
3.23e-37 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 136.37 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 46 GATPLIPVPTIAERIGKGvRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICASTGNTSAAAAAYARRAGMRAFVL 125
Cdd:PRK06381 14 GGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 126 IPDGYvAQGKLAQALVYGAEVLAIRGNFDRALDIVREAA------DQFPvtlvNSVNP-YRLQGQKTAAFEIVDVLGEAP 198
Cdd:PRK06381 93 IPRSY-SNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAkengiyDANP----GSVNSvVDIEAYSAIAYEIYEALGDVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 199 DWLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPLV--YDTTVSDPNTIATAIRIGNPVNRA------- 269
Cdd:PRK06381 168 DAVAVPVGNGTTLAGIYHGFRRLYDRGKTSRMPRMIGVSTSGGNQIVesFKRGSSEVVDLEVDEIRETAVNEPlvsyrsf 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78170182 270 ---KAMAVREASDGAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTG 335
Cdd:PRK06381 248 dgdNALEAIYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVITG 316
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
41-339 |
3.54e-27 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 109.82 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 41 ITLHEGATPLIpvptiaerigKGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEAVICASTGNTSAAAAAYARRAGM 120
Cdd:PRK06450 52 ISLGEGRTPLI----------KKGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 121 RAFVLIPDGyVAQGKLAQALVYGAEVLAIRGNFDralDIVREAADQFPVTLVNSVNPYRLQGQKTAAFEIVDVLG-EAPD 199
Cdd:PRK06450 122 EVKIFVPET-ASGGKLKQIESYGAEVVRVRGSRE---DVAKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDwKIPN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 200 WLCIPMGNAGNITAYWMGFQEYHQAGHSRSLPRMMGFQASGSAPL---VYDTTVSDPN---TIATAIRIGNPVNRAKAM- 272
Cdd:PRK06450 198 YVFIPVSAGTLLLGVYSGFKHLLDSGVISEMPKIVAVQTEQVSPLcakFKGISYTPPDkvtSIADALVSTRPFLLDYMVk 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78170182 273 AVREASDGafLDVTDEEIINAYKLLgGGEGIFCEPASAASVAGLLKRKDEVPagatvVCVLTGNGLK 339
Cdd:PRK06450 278 ALSEYGEC--IVVSDNEIVEAWKEL-AKKGLLVEYSSATVYAAYKKYSVNDS-----VLVLTGSGLK 336
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
48-335 |
1.48e-24 |
|
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: 102.42 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA-VICASTGN----------------Tsaa 110
Cdd:COG1171 25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRGAYNALASLSEEERARgVVAASAGNhaqgvayaarllgipaT--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 111 aaayarragmrafVLIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVNPYRL-QGQKTAAFE 189
Cdd:COG1171 100 -------------IVMPET-APAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDViAGQGTIALE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 190 IVDVLGEaPDWLCIPMGN----AGNITAYWmgfqeyhqagHSRSLPRMMGFQASGSAPLvYD-------TTVSDPNTIAT 258
Cdd:COG1171 166 ILEQLPD-LDAVFVPVGGggliAGVAAALK----------ALSPDIRVIGVEPEGAAAM-YRslaagepVTLPGVDTIAD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78170182 259 AIRIGNPVNRAKAMaVREASDGaFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVpAGATVVCVLTG 335
Cdd:COG1171 234 GLAVGRPGELTFEI-LRDLVDD-IVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERL-KGKRVVVVLSG 307
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
48-335 |
7.31e-24 |
|
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: 99.87 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA-VICASTGNTSAAAAAYARRAGMRAFVLI 126
Cdd:cd01562 18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAASAGNHAQGVAYAAKLLGIPATIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 127 PDGYVAQgKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIVDVLGEaPDWLCIPM 205
Cdd:cd01562 96 PETAPAA-KVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDdPDVIAGQGTIGLEILEQVPD-LDAVFVPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 206 GN----AGNITAywmgfqeyhqAGHSRSLPRMMGFQASGSAPLVYD------TTVSDPNTIATAIRIGNPVNRAKAMAvR 275
Cdd:cd01562 174 GGggliAGIATA----------VKALSPNTKVIGVEPEGAPAMAQSlaagkpVTLPEVDTIADGLAVKRPGELTFEII-R 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 276 EASDGAFLdVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVpAGATVVCVLTG 335
Cdd:cd01562 243 KLVDDVVT-VSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL-KGKKVVVVLSG 300
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
46-333 |
1.21e-12 |
|
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: 67.54 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 46 GATPLIPVPTIAEriGKGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAG--------CE----------AVICASTGnt 107
Cdd:cd01561 1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGllkpgttiIEptsgntgiglAMVAAAKG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 108 saaaaayarragmRAFVLIPDGYVAQGKLAQALVYGAEVL----AIRGNFDRALDIVREAADQFPvtlvNSV------NP 177
Cdd:cd01561 77 -------------YRFIIVMPETMSEEKRKLLRALGAEVIltpeAEADGMKGAIAKARELAAETP----NAFwlnqfeNP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 178 YRLQG-QKTAAFEIVDVLGEAPDWLCIPMGNAGNITAYWMGFQEyhqagHSRSLpRMMGFQASGSAPLVYDttvSDPNTI 256
Cdd:cd01561 140 ANPEAhYETTAPEIWEQLDGKVDAFVAGVGTGGTITGVARYLKE-----KNPNV-RIVGVDPVGSVLFSGG---PPGPHK 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78170182 257 ATAIRIGnpvnRAKAMAVREASDGaFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVL 333
Cdd:cd01561 211 IEGIGAG----FIPENLDRSLIDE-VVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTIL 282
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
46-339 |
2.00e-11 |
|
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: 63.91 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 46 GATPLIPVPTIAEriGKGVRVFVKYDGLNPTGSFKDR-GMTMaISKAKEAGcE-----AVICASTGNTsaaaaayarrag 119
Cdd:COG0031 12 GNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRiALSM-IEDAEKRG-LlkpggTIVEATSGNTgiglamv-aaak 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 120 mraFVL-IPDGyVAQGKLAQALVYGAEV------LAIRGNFDRALDIVREA-----ADQFpvtlVNSVNP--YRlqgqKT 185
Cdd:COG0031 87 gyrLILvMPET-MSKERRALLRAYGAEVvltpgaEGMKGAIDKAEELAAETpgafwPNQF----ENPANPeaHY----ET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 186 AAFEIVDVLGEAPDWLCIPMGNAGNITaywmgfqeyhqaGHSRSL----P--RMMGFQASGSAplVYDTTVSDPNTIAta 259
Cdd:COG0031 158 TGPEIWEQTDGKVDAFVAGVGTGGTIT------------GVGRYLkernPdiKIVAVEPEGSP--LLSGGEPGPHKIE-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 260 iRIGNPVnrakamaVREASDGAFLD----VTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTG 335
Cdd:COG0031 222 -GIGAGF-------VPKILDPSLIDevitVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPD 293
|
....
gi 78170182 336 NGLK 339
Cdd:COG0031 294 SGER 297
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
50-209 |
2.19e-11 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 64.26 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 50 LIPVPT-IAERIGkgvrVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCE-AVICASTGNTSAAAAAYARRAGMRAFVLIP 127
Cdd:PRK08813 37 LSPTPLhYAERFG----VWLKLENLQRTGSYKVRGALNALLAGLERGDErPVICASAGNHAQGVAWSAYRLGVQAITVMP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 128 DGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSV-NPYRLQGQKTAAFEIVdvlGEAPDWLCIPMG 206
Cdd:PRK08813 113 HG-APQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFdDPDVIAGQGTVGIELA---AHAPDVVIVPIG 188
|
...
gi 78170182 207 NAG 209
Cdd:PRK08813 189 GGG 191
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
47-349 |
9.70e-11 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 62.90 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 47 ATPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISK-AKEAGCEAVICASTGNTsaaaaayarragmrafvl 125
Cdd:PRK08639 25 ETPLQRNDYLSEKYG--ANVYLKREDLQPVRSYKLRGAYNAISQlSDEELAAGVVCASAGNH------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 126 ipdgyvAQG-----------------------KLAQALVYGAEVLAIR--G-NFDRALDIVREAADQFPVTLVNSV-NPY 178
Cdd:PRK08639 85 ------AQGvayacrhlgipgvifmpvttpqqKIDQVRFFGGEFVEIVlvGdTFDDSAAAAQEYAEETGATFIPPFdDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 179 RLQGQKTAAFEIVDVLGEA--PDWLCIPMGNAG---NITAYwmgFQEYHQAghsrslPRMMGFQASGSAPLvydttvsdp 253
Cdd:PRK08639 159 VIAGQGTVAVEILEQLEKEgsPDYVFVPVGGGGlisGVTTY---LKERSPK------TKIIGVEPAGAASM--------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 254 ntiATAIRIGNPV------NRAKAMAVREASDGAF---------LDVTDE-----EIINAYKLlgggEGIFCEPASAASV 313
Cdd:PRK08639 221 ---KAALEAGKPVtlekidKFVDGAAVARVGDLTFeilkdvvddVVLVPEgavctTILELYNK----EGIVAEPAGALSI 293
|
330 340 350
....*....|....*....|....*....|....*.
gi 78170182 314 AGLLKRKDEVPaGATVVCVLTGnglkdpdcaiNNND 349
Cdd:PRK08639 294 AALELYKDEIK-GKTVVCVISG----------GNND 318
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
48-369 |
2.20e-10 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 61.29 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIgKGvRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCE-AVICASTGNTSAAAAAYARRAGMRAFVLI 126
Cdd:PRK08638 28 TPLPRSNYLSERC-KG-EIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRkGVVACSAGNHAQGVALSCALLGIDGKVVM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 127 PDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIVDVLGEApDWLCIPM 205
Cdd:PRK08638 106 PKG-APKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDdPKVIAGQGTIGLEILEDLWDV-DTVIVPI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 206 GNAGNITAYWMGFQEYHQAGHsrslprMMGFQAS---GSAPLVYD---TTVSDPNTIATAIRIGNPVNRAKAMaVREASD 279
Cdd:PRK08638 184 GGGGLIAGIAVALKSINPTIH------IIGVQSEnvhGMAASFYAgeiTTHRTTGTLADGCDVSRPGNLTYEI-VRELVD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 280 GAFLdVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRK-DEVPAGATVVCVLTGNglkdpdcainnndaafhtdlNP 358
Cdd:PRK08638 257 DIVL-VSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKlDQYIQNKKVVAIISGG--------------------NV 315
|
330
....*....|.
gi 78170182 359 DLETVAKVMGF 369
Cdd:PRK08638 316 DLSRVSQITGH 326
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
48-335 |
3.72e-08 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 54.25 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISK----AKEAGceaVICASTGNTSAAAAAYARRAGMRAF 123
Cdd:PRK07048 25 TPVLTSRTADARTG--AQVFFKCENFQRMGAFKFRGAYNALSQfspeQRRAG---VVTFSSGNHAQAIALSARLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 124 VLIPDGYVAqGKLAQALVYGAEVLAirgnFDRALD----IVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIVDVLGEAp 198
Cdd:PRK07048 100 IVMPQDAPA-AKVAATRGYGGEVVT----YDRYTEdreeIGRRLAEERGLTLIPPYDhPHVIAGQGTAAKELFEEVGPL- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 199 DWLCIPMGNAGNITAywmgfqeyhQAGHSRSL-PRMM-----------GFQASGSAPLVydtTVSDPNTIATAIR---IG 263
Cdd:PRK07048 174 DALFVCLGGGGLLSG---------CALAARALsPGCKvygvepeagndGQQSFRSGEIV---HIDTPRTIADGAQtqhLG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78170182 264 N---PVnrakamaVREASDgAFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPaGATVVCVLTG 335
Cdd:PRK07048 242 NytfPI-------IRRLVD-DIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLK-GKRVGVIISG 307
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
63-335 |
8.69e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 53.24 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 63 GVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGC--EAVICASTGNTSAAAAAYARRAGMRAFVLIPDgYVAQGKLAQAL 140
Cdd:PRK06608 37 GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPL-NTSKVKQQAAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 141 VYGAEVL--AIRGNFDRAldiVREAADQFPVTLVNSVNPYRLQGQKTAAFEIVDVLGEAPDWLCIPMGNAGNITAYWMgf 218
Cdd:PRK06608 116 YYGGEVIltNTRQEAEEK---AKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGTYL-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 219 qeyhqAGHSRSLPRMMgfqaSGSAPL-VYDTTVS-----------DPNTIATAirignpvnrAKAMAVREAS-------D 279
Cdd:PRK06608 191 -----AKELISPTSLL----IGSEPLnANDAYLSlknnkiyrlnySPNTIADG---------LKTLSVSARTfeylkklD 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78170182 280 GaFLDVTDEEIinAY------KLLgggeGIFCEPASA---ASVAGLLKRKDevpAGATVVCVLTG 335
Cdd:PRK06608 253 D-FYLVEEYEI--YYwtawltHLL----KVICEPSSAinmVAVVNWLKTQS---KPQKLLVILSG 307
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
4-339 |
1.25e-07 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 53.07 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 4 LFQNLRRRFTANPVMQDWP--GLIEAYrdwlpvsaktpvitlheGATPLIPVPTIAEriGKGVRVFVKYDGLNPTGSFKD 81
Cdd:PLN02356 25 LLCNSRKRKTKKPLSKKKPrnGLIDAI-----------------GNTPLIRINSLSE--ATGCEILGKCEFLNPGGSVKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 82 RGMTMAISKAKEAG---CEAVIC-ASTGNTSAAAAAYARRAGMRAFVLIPDGY-VAQGKLAQALvyGAEVLAIR----GN 152
Cdd:PLN02356 86 RVAVKIIEEALESGqlfPGGVVTeGSAGSTAISLATVAPAYGCKCHVVIPDDVaIEKSQILEAL--GATVERVRpvsiTH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 153 FDRALDIVREAADQfpvtlVNSVNPYRLQGQKTAAFEIVDVLGEAPD---------------WLCIPMGNAGNITAYWMG 217
Cdd:PLN02356 164 KDHYVNIARRRALE-----ANELASKRRKGSETDGIHLEKTNGCISEeekenslfsssctggFFADQFENLANFRAHYEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 218 F--QEYHQ------------------AGHSRSL----PRMMGFQASGSAPLVYDTT---VSDPNTIATAIRIGNP----- 265
Cdd:PLN02356 239 TgpEIWEQtqgnldafvaaagtggtlAGVSRFLqeknPNIKCFLIDPPGSGLFNKVtrgVMYTREEAEGRRLKNPfdtit 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78170182 266 ----VNRAKAMAVREASDGAFLDvTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTGNGLK 339
Cdd:PLN02356 319 egigINRLTQNFLMAKLDGAFRG-TDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMR 395
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
48-335 |
2.64e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 52.20 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRG----MTMAISKAKEAGceaVICASTGNTSAAAAAYARRAGMRAF 123
Cdd:PRK07334 24 TPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGalnkLLLLTEEERARG---VIAMSAGNHAQGVAYHAQRLGIPAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 124 VLIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIvdvLGEAP--DW 200
Cdd:PRK07334 99 IVMPRF-TPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDdPAVIAGQGTVALEM---LEDAPdlDT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 201 LCIPMGNAGNI----TAywmgfqeyhqAGHSRSLPRMMGFQASgSAPLVYDTTVSDP-----NTIATAIRIGNPVNRAKA 271
Cdd:PRK07334 175 LVVPIGGGGLIsgmaTA----------AKALKPDIEIIGVQTE-LYPSMYAAIKGVAlpcggSTIAEGIAVKQPGQLTLE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78170182 272 MAVREASDgaFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVpAGATVVCVLTG 335
Cdd:PRK07334 244 IVRRLVDD--ILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERF-RGRKVGLVLSG 304
|
|
| cysteate_syn |
TIGR03844 |
cysteate synthase; Members of this family are cysteate synthase, an enzyme of alternate ... |
10-339 |
3.79e-07 |
|
cysteate synthase; Members of this family are cysteate synthase, an enzyme of alternate pathway to sulfopyruvate, a precursor of coenzyme M. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Energy metabolism, Methanogenesis]
Pssm-ID: 163556 Cd Length: 398 Bit Score: 51.66 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 10 RRFTanpvMQDWPGlIEAYRDWLPVSAKTPvitlhegaTPLIPVPTIAERIGKGVR------VFVKY----DGLNPTGSF 79
Cdd:TIGR03844 34 RQLT----LRDLPG-IFRYYDWLPVTGHLR--------TRGGPVTYKSEGLARELGlsdlyiTFSGYwperGAFMRTCSF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 80 KDRGMTMAISKAKEAGCEAVICASTGNTSAAAAAYARRAGMRAFVLIPDGyvAQGKLAQAlVYGAEVL--AIRGNFDRAL 157
Cdd:TIGR03844 101 KELEALPTMQRLKERGGKTLVVASAGNTGRAFAEVSAITGQPVILVVPKS--SADRLWTT-EPASSVLlvTVDGDYTDAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 158 DIVRE--AADQFpVTLVNSVNPYRLQGQKTAAFEIVDVLGEAPDWLCIPMGNA-GNITAYWMGFQEYHQAGHSRSLPRMM 234
Cdd:TIGR03844 178 ALADRiaTLPGF-VPEGGARNVARRDGMGTVMLDAAVTIGSLPDHYFQAVGSGtGGIAAWEAAMRLIEDGRFGSKLPRLH 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 235 GFQASGSAPLV---------YDTTVSDPNTIATAIRIGNPV--NRAKAMAVR-------EASDGAFLDVTDEEIINAYKL 296
Cdd:TIGR03844 257 LAQNLPFVPMVnawqegrreIIPESDMPDAENSIEEVYSDVltNRTPPYGVTggvfdalIATGGQMYGVSNKEAVSAGKL 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 78170182 297 LGGGEGIFCEPASAASVAGLLK--RKDEVPAGATVVCVLTGNGLK 339
Cdd:TIGR03844 337 FEESEGIDILPAAAVAVAALVKavESGFIGPDDDILLNITGGGYK 381
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
48-106 |
4.32e-07 |
|
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: 51.15 E-value: 4.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78170182 48 TPLIPVPTIAERigKGVRVFVKYDGLNPTGSFKDRGM----TMAISKAKeAGCEAVICASTGN 106
Cdd:cd06448 2 TPLIESTALSKT--AGCNVFLKLENLQPSGSFKIRGIghlcQKSAKQGL-NECVHVVCSSGGN 61
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
63-335 |
5.41e-07 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 50.85 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 63 GVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCE-AVICASTGNTSAAAAAYARRAGMRAFVLIPDGyVAQGKLAQALV 141
Cdd:PRK06815 34 GCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQqGVITASSGNHGQGVALAAKLAGIPVTVYAPEQ-ASAIKLDAIRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 142 YGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIVDVLGEaPDWLCIPMGNAGNITaywmGFQE 220
Cdd:PRK06815 113 LGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNdPQVIAGQGTIGMELVEQQPD-LDAVFVAVGGGGLIS----GIAT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 221 YHQAGHSRSlpRMMGFQASGSAPLVYDT------------TVSD-------PNTIATAIrignpvnrakamaVREASDGA 281
Cdd:PRK06815 188 YLKTLSPKT--EIIGCWPANSPSLYTSLeageivevaeqpTLSDgtaggvePGAITFPL-------------CQQLIDQK 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 78170182 282 FLdVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVpAGATVVCVLTG 335
Cdd:PRK06815 253 VL-VSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVAVVLCG 304
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
48-342 |
1.23e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 49.58 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA-VICASTGNTSAAAAAYARRAGMRAFV-- 124
Cdd:PRK07476 20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRGATNALLSLSAQERARgVVTASTGNHGRALAYAARALGIRATIcm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 125 --LIPDGYVAQgklAQALvyGAEVLAIRGNFDRALDIVREAADQFPVTLVNSV-NPYRLQGQKTAAFEIVDVLGEApDWL 201
Cdd:PRK07476 98 srLVPANKVDA---IRAL--GAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFdDPRIIAGQGTIGLEILEALPDV-ATV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 202 CIPMGNAGNItaywmgfqeyhqAGhsrslprmMGFQASGSAPLVYDTTVSDPNTIATA--IRIGNPV------------- 266
Cdd:PRK07476 172 LVPLSGGGLA------------SG--------VAAAVKAIRPAIRVIGVSMERGAAMHasLAAGRPVqveevptladslg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 267 ------NRAKAMAVREASDGAFLdVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVcVLTGNGLkD 340
Cdd:PRK07476 232 ggigldNRYTFAMCRALLDDVVL-LDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVV-VVSGANI-D 308
|
..
gi 78170182 341 PD 342
Cdd:PRK07476 309 ME 310
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
34-335 |
3.22e-06 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 48.41 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 34 VSAKTPVITLHEGATPLIPVPTIAeriGKGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGcEAVICASTGNTSAAAAA 113
Cdd:PRK08246 10 VRAAAQRIAPHIRRTPVLEADGAG---FGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPVPA-AGVVAASGGNAGLAVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 114 YARRAGMRAFVLIPdGYVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQKTAAFEIVD 192
Cdd:PRK08246 86 AAAALGVPATVFVP-ETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDqPEVLAGAGTLGLEIEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 193 VLGEaPDWLCIPMGNAGNI--TAYWMGfqeyhqaGHSrslpRMMGFQASGSaplvydttvsdpNTIATAIRIGNPVN--- 267
Cdd:PRK08246 165 QAPG-VDTVLVAVGGGGLIagIAAWFE-------GRA----RVVAVEPEGA------------PTLHAALAAGEPVDvpv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 268 ---RAKAMAVREASDGAF----------LDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLT 334
Cdd:PRK08246 221 sgiAADSLGARRVGEIAFalarahvvtsVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGERVAVVLC 300
|
.
gi 78170182 335 G 335
Cdd:PRK08246 301 G 301
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
282-340 |
5.83e-06 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 47.92 E-value: 5.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 78170182 282 FLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTGNGLKD 340
Cdd:cd06446 303 YVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKD 361
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
48-335 |
7.75e-06 |
|
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: 47.03 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGKGVRVFVKYDGLNPTGSF---KDRGMTMAISKAKEAGCEAVI-CASTGNTSAAAAAYARRAGMRAF 123
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVEIYAKRDDCNSGLAFggnKIRKLEYLLPDALAKGADTLVtVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 124 VLI--------PDGYVAQGKLAQALVYGAEV--------LAIRGNFDRALDIVREAADQ-FPVTLVNSVNPYRLQGQKTA 186
Cdd:cd06449 81 VLVqenwvpysDAVYDRVGNILLSRIMGADVrlvsagfdIGIRKSFEEAAEEVEAKGGKpYVIPAGGSEHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 187 AFEIVD---VLGEAPDWLCIPMGNAGNITAYWMGFQEYHQAghsrslPRMMGFQASGSaPLVYDTTVsdpntiatairig 263
Cdd:cd06449 161 VLEIAQqeeELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQ------RRVIGIDASAK-PEKTKAQV------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 264 npVNRAKAMAVREASDGAFLDVT-------------DEEIINAYKLLGGGEGIFCEPA-SAASVAGL--LKRKDEVPAGA 327
Cdd:cd06449 221 --LRIAQAKLAEEGLEVKEEDVVldddyaapeygipNDETIEAIKLCARLEGIITDPVyEGKSMQGMidLVRNGEFKEGS 298
|
....*...
gi 78170182 328 TVVCVLTG 335
Cdd:cd06449 299 KVLFIHLG 306
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
48-327 |
1.10e-05 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 47.22 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGM-TMAISKAKEAGCEAVICASTGNTSAAAAAYARRAGMRAFVLI 126
Cdd:PLN02550 110 SPLQLAKKLSERLG--VKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 127 PdgyVAQGKLAQALV--YGAEVLAIRGNFDRALDIVREAADQFPVTLVNSV-NPYRLQGQKTAAFEIVDVLGEAPDWLCI 203
Cdd:PLN02550 188 P---VTTPEIKWQSVerLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFdHPDVIAGQGTVGMEIVRQHQGPLHAIFV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 204 PMGNAGNITaywmGFQEYHQaghsRSLPRMmgfQASGSAPlvydttvSDPNTIATAIRIGnpvNRAKAMAVREASDGAFL 283
Cdd:PLN02550 265 PVGGGGLIA----GIAAYVK----RVRPEV---KIIGVEP-------SDANAMALSLHHG---ERVMLDQVGGFADGVAV 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 78170182 284 DVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEV--PAGA 327
Cdd:PLN02550 324 KEVGEETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSIlePAGA 369
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
47-335 |
2.00e-05 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 45.76 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 47 ATPLIPVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA--VICASTGNTSAAAAAYARRAGMRAFV 124
Cdd:PRK06110 21 PTPQYRWPLLAERLG--CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVrgVISATRGNHGQSVAFAARRHGLAATI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 125 LIPDGYVAQgKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVNPYRLQGQKTAAFEIvdvLGEAP--DWLC 202
Cdd:PRK06110 99 VVPHGNSVE-KNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFHPDLVRGVATYALEL---FRAVPdlDVVY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 203 IPMGNAGNITAywmgfqeyhqAGHSRSL----PRMMGFQASGsAPLVYD-----TTVSDP--NTIA--TAIRIgnPVNRA 269
Cdd:PRK06110 175 VPIGMGSGICG----------AIAARDAlglkTRIVGVVSAH-APAYALsfeagRVVTTPvaTTLAdgMACRT--PDPEA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78170182 270 KAMAVREASDgaFLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVpAGATVVCVLTG 335
Cdd:PRK06110 242 LEVIRAGADR--IVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERL-AGKRVGLVLSG 304
|
|
| Thr-synth_2 |
cd01560 |
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ... |
75-218 |
3.45e-05 |
|
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.
Pssm-ID: 107203 [Multi-domain] Cd Length: 460 Bit Score: 45.69 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 75 PTGSFKDrgmtMAIS--------KAKEAGCEAVI-CASTGNT-SAAAAAYARRAGMRAFVLIPDGYVAQGKLAQALVYGA 144
Cdd:cd01560 106 PTLAFKD----MALQflgrlleyFLKRRNERITIlVATSGDTgSAAIEGFRGKPNVDVVVLYPKGGVSPIQELQMTTLPA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 145 E---VLAIRGNFDRALDIVREA-ADQ-FPVTL----VNSVNPYRLQGQKT----AAFEIV-DVLGEAPDwLCIPMGNAGN 210
Cdd:cd01560 182 DnvhVVAVEGDFDDCQSLVKALfADEdFNKKLklssANSINWARILAQIVyyfyAYLQLLkRGEGEKVE-FSVPTGNFGN 260
|
170
....*....|..
gi 78170182 211 ITAYW----MGF 218
Cdd:cd01560 261 ILAGYyakkMGL 272
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
285-369 |
4.17e-05 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 45.06 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 285 VTDEEIINAYKLLGGGEGIFcePA--SAASVAGLLKRKDEVPAGATVVCVLTGNGLKdpdcainnndaafhtdlnpDLET 362
Cdd:PRK04346 330 ITDDEALEAFQLLSRLEGII--PAleSSHALAYALKLAPTLGKDQIIVVNLSGRGDK-------------------DVFT 388
|
....*..
gi 78170182 363 VAKVMGF 369
Cdd:PRK04346 389 VAKLLGV 395
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
48-106 |
4.48e-04 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 42.05 E-value: 4.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 48 TPLIPVPTIAERIGKgvRVFVKYDGLNPTGSFKDRGMTMAISKAKEAGCEA-VICASTGN 106
Cdd:PRK09224 21 TPLEKAPKLSARLGN--QVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARgVITASAGN 78
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
285-347 |
5.38e-04 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 41.78 E-value: 5.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78170182 285 VTDEEIINAYKLLGGGEGIFcePA--SAASVAGLLKRKDEVPAGATVVCVLTGNGLKDPDCAINN 347
Cdd:PRK13028 334 ATDEEALDAFFLLSRTEGII--PAleSSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEM 396
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
46-332 |
5.39e-04 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 41.40 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 46 GATPLIPVPTIAEriGKGVRVFVKYDGLNPTGSFKDRGMTMAISKAKEAG----CEAVICASTGNTSAAAAAYARRAGMR 121
Cdd:PRK11761 11 GNTPLVKLQRLPP--DRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGeikpGDTLIEATSGNTGIALAMIAAIKGYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 122 AFVLIPDGYVAQGKLAQAlVYGAEVL------AIRGNFDRALDIVREAA----DQFpvtlVNSVNPYrlqgqktAAFEiv 191
Cdd:PRK11761 89 MKLIMPENMSQERRAAMR-AYGAELIlvpkeqGMEGARDLALQMQAEGEgkvlDQF----ANPDNPL-------AHYE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 192 dvlGEAPD-W---------LCIPMGNAGNITaywmgfqeyhqaGHSRSLP------RMMGFQ-ASGSA------------ 242
Cdd:PRK11761 155 ---TTGPEiWrqtegrithFVSSMGTTGTIM------------GVSRYLKeqnpavQIVGLQpEEGSSipgirrwpeeyl 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 243 PLVYDTTVSDpntiataiRIgnpvnrakamavreasdgafLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDE 322
Cdd:PRK11761 220 PKIFDASRVD--------RV--------------------LDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARE 271
|
330
....*....|
gi 78170182 323 VPaGATVVCV 332
Cdd:PRK11761 272 NP-NAVIVAI 280
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
282-345 |
6.07e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 41.72 E-value: 6.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78170182 282 FLDVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLKRKDEVPAGATVVCVLTGNGLKDPDCAI 345
Cdd:PRK13803 539 YTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLK 602
|
|
| PLN02970 |
PLN02970 |
serine racemase |
26-335 |
7.23e-04 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 41.20 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 26 EAYRDWLPVSAKTPVITlhegatplipVPTIAERIGkgVRVFVKYDGLNPTGSFKDRGMTMAI-SKAKEAGCEAVICAST 104
Cdd:PLN02970 16 EARKRIAPFIHRTPVLT----------SSSLDALAG--RSLFFKCECFQKGGAFKFRGACNAIfSLSDDQAEKGVVTHSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 105 GNTSAAAAAYARRAGMRAFVLIPDGyVAQGKLAQALVYGAEVLAIRGNFDRALDIVREAADQFPVTLVNSVN-PYRLQGQ 183
Cdd:PLN02970 84 GNHAAALALAAKLRGIPAYIVVPKN-APACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNdGRVISGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 184 KTAAFEIVDVLGEApDWLCIPMGNAGNITAYwmgfqeyhqAGHSRSLP---RMMGFQASG------SAPLVYDTTVSDPN 254
Cdd:PLN02970 163 GTIALEFLEQVPEL-DVIIVPISGGGLISGI---------ALAAKAIKpsiKIIAAEPKGaddaaqSKAAGEIITLPVTN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78170182 255 TIATAIR--IGN---PVnrakamaVREASDGAFLdVTDEEIINAYKLLGGGEGIFCEPASAASVAGLLK---RKDEVPAG 326
Cdd:PLN02970 233 TIADGLRasLGDltwPV-------VRDLVDDVIT-VDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSdsfRSNPAWKG 304
|
330
....*....|
gi 78170182 327 ATVV-CVLTG 335
Cdd:PLN02970 305 CKNVgIVLSG 314
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
282-346 |
4.28e-03 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 38.97 E-value: 4.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78170182 282 FLDVTDEEIINAYKLLGGGEGIFcePASAAS--VAGLLKRKDEVPAGATVVCVLTGNGLKDPDCAIN 346
Cdd:PLN02618 340 YYSVTDEEALEAFQRLSRLEGII--PALETShaLAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIK 404
|
|
| |
