|
Name |
Accession |
Description |
Interval |
E-value |
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
6-320 |
2.12e-162 |
|
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: 456.67 E-value: 2.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPVTDqTPALTLHEGNTPLIHLPKLSEQLG-IELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTG 84
Cdd:cd01563 1 LWRYRELLPVTE-DDIVSLGEGNTPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 85 NTSAAAAAYAARANMKCIVIIPNGKiAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIEGQKT 164
Cdd:cd01563 80 NTSASLAAYAARAGIKCVVFLPAGK-ALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSNSLNPYRLEGQKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 165 AAFEVCEQLG-EAPDVLAIPVGNAGNITAYWKGFKEYHEKNG-TGLPKMRGFEAEGAAAIVRN--------EVIENPETI 234
Cdd:cd01563 159 IAFEIAEQLGwEVPDYVVVPVGNGGNITAIWKGFKELKELGLiDRLPRMVGVQAEGAAPIVRAfkegkddiEPVENPETI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 235 ATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLT 314
Cdd:cd01563 239 ATAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVLT 318
|
....*.
gi 906393278 315 GNGLKD 320
Cdd:cd01563 319 GHGLKD 324
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
6-322 |
2.63e-158 |
|
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: 446.44 E-value: 2.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPVTdQTPALTLHEGNTPLIHLPKLSEQLGI-ELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTG 84
Cdd:TIGR00260 1 VWRYREFLPVT-EKDLVDLGEGVTPLFRAPALAANVGIkNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 85 NTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN--PYRIEGQ 162
Cdd:TIGR00260 80 NTGAAAAAYAGKAGLKVVVLYPAGKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANsiPYRLEGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 163 KTAAFEVCEQLG-EAPDVLAIPVGNAGNITAYWKGFKEYHEKNGTGLPKMRGFEAEGAAAIVRN-------EVIENPETI 234
Cdd:TIGR00260 160 KTYAFEAVEQLGwEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGLDSLPVKRGIQAEGAADIVRAfleggqwEPIETPETL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 235 ATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLT 314
Cdd:TIGR00260 240 STAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADPAERVVCALT 319
|
....*...
gi 906393278 315 GNGLKDPN 322
Cdd:TIGR00260 320 GNGLKDPE 327
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
1-347 |
1.69e-146 |
|
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: 419.22 E-value: 1.69e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 1 MWKglihqYKEFLPVTDQTPALTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMC 80
Cdd:COG0498 44 LWR-----YRELLPFDDEEKAVSLGEGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVC 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 81 ASTGNTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIE 160
Cdd:COG0498 119 ASSGNGSAALAAYAARAGIEVFVFVPEGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINPARLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 161 GQKTAAFEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHEKNGTG-LPKMRGFEAEGAAAIVR-------NEVIENPE 232
Cdd:COG0498 199 GQKTYAFEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELGLIDrLPRLIAVQATGCNPILTafetgrdEYEPERPE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 233 TIATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAV 312
Cdd:COG0498 279 TIAPSMDIGNPSNGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVL 358
|
330 340 350
....*....|....*....|....*....|....*
gi 906393278 313 LTGNGLKDPNTAVDISEIKPVTLPTDEDSILEYVK 347
Cdd:COG0498 359 STGHGLKFPDAVREALGGEPLAVPPDLEAVKAAVE 393
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
10-347 |
2.48e-78 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 248.19 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 10 KEF-LPVTDQTPALTLHEGNTPLIHLPKLS-EQLGI-ELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGN-----DTIMCA 81
Cdd:PLN02569 114 KEWvLPEIDDDDIVSLFEGNSNLFWAERLGkEFLGMnDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKmakpvVGVGCA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 82 STGNTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIEG 161
Cdd:PLN02569 194 STGDTSAALSAYCAAAGIPSIVFLPADKISIAQLVQPIANGALVLSIDTDFDGCMRLIREVTAELPIYLANSLNSLRLEG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 162 QKTAAFEVCEQLG-EAPDVLAIPVGNAGNITAYWKGFKEYHEkngTGL----PKMRGFEAEGAAAIVR---------NEV 227
Cdd:PLN02569 274 QKTAAIEILQQFDwEVPDWVIVPGGNLGNIYAFYKGFKMCKE---LGLvdrlPRLVCAQAANANPLYRayksgweefKPV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 228 IENPeTIATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAyQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGS 307
Cdd:PLN02569 351 KANP-TFASAIQIGDPVSIDRAVYALKESNGIVEEATEEELMDA-QAEADKTGMFLCPHTGVALAALKKLRASGVIGPTD 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 906393278 308 KVVAVLTGNGLKDPNTAVDI--SEIK---------PVTLPTDEDSILEYVK 347
Cdd:PLN02569 429 RTVVVSTAHGLKFTQSKIDYhsKEIPdmacrfanpPVSVKADFGSVMDVLK 479
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
22-315 |
5.21e-76 |
|
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: 236.05 E-value: 5.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 22 LTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEE-GNDTIMCASTGNTSAAAAAYAARANMK 100
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGeGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 101 CIVIIPNGKIAfGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSP-IALVNSV-NPYRIEGQKTAAFEVCEQLGEAPD 178
Cdd:pfam00291 81 VTIVVPEDAPP-GKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPgAYYINQYdNPLNIEGYGTIGLEILEQLGGDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 179 VLAIPVGNAGNITAYWKGFKEyheknGTGLPKMRGFEAEGAAAIV------RNEVIENPETIATAIRIGNPASwDKAVKA 252
Cdd:pfam00291 160 AVVVPVGGGGLIAGIARGLKE-----LGPDVRVIGVEPEGAPALArslaagRPVPVPVADTIADGLGVGDEPG-ALALDL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 906393278 253 AEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGvLKQVKSGEIPKGSKVVAVLTG 315
Cdd:pfam00291 234 LDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAA-LKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
29-315 |
8.04e-66 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 208.14 E-value: 8.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEG---NDTIMCASTGNTSAAAAAYAARANMKCIVII 105
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 106 PNGKiAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIA-LVNS-VNPYRIEGQKTAAFEVCEQLGE-APDVLAI 182
Cdd:cd00640 81 PEGA-SPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAyYVNQfDNPANIAGQGTIGLEILEQLGGqKPDAVVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 183 PVGNAGNITAYWKGFKEYHEKngtglPKMRGFEAEgaaaivrnevienpetiatairignpaswdkavkaaeesngkIDE 262
Cdd:cd00640 160 PVGGGGNIAGIARALKELLPN-----VKVIGVEPE------------------------------------------VVT 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 906393278 263 VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVLTG 315
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAK--KLGKGKTVVVILTG 243
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
1-323 |
2.33e-63 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 206.78 E-value: 2.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 1 MWKglihqYKEFLPVTDQTPALTLHEGNTPLIHLPKLSEQLGI-ELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIM 79
Cdd:PRK08197 57 LWR-----YHELLPVRDPEHIVSLGEGMTPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 80 CASTGNTSAAAAAYAARANMKCIVIIPNGKIAFGKLAQAVmYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYR 158
Cdd:PRK08197 132 MPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECAL-AGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKePYR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 159 IEGQKTAAFEVCEQLG-EAPDVLAIPVGNAGNITAYWKGFKEYHEKN--GTGLPKMRGFEAEGAAAIVR--------NEV 227
Cdd:PRK08197 211 IEGKKTMGLELAEQLGwRLPDVILYPTGGGVGLIGIWKAFDELEALGwiGGKRPRLVAVQAEGCAPIVKaweegkeeSEF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 228 IENPETIATAIRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKGS 307
Cdd:PRK08197 291 WEDAHTVAFGIRVPKALGDFLVLDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGDE 370
|
330
....*....|....*.
gi 906393278 308 KVVAVLTGNGLKDPNT 323
Cdd:PRK08197 371 RVVLFNTGSGLKYPDT 386
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
6-321 |
2.50e-53 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 181.93 E-value: 2.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPVTDQTpaLTLHEGNTPLIHlPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTGN 85
Cdd:PRK05638 46 VWRYKELLPQVKKI--ISLGEGGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 86 TSAAAAAYAARANMKCIVIIPNgKIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSpiALVNSVNPYRI---EGQ 162
Cdd:PRK05638 123 AAASVAAYSARAGKEAFVVVPR-KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN--GLYNVTPEYNIiglEGQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 163 KTAAFEVCEQLGeaPDVLAIPVGNAGNITAYWKGFKEYHEKNGTG-LPKMRGFEAEGAAAIVrNEVIENP----ETIATA 237
Cdd:PRK05638 200 KTIAFELWEEIN--PTHVIVPTGSGSYLYSIYKGFKELLEIGVIEeIPKLIAVQTERCNPIA-SEILGNKtkcnETKALG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 238 IRIGNPASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARvEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLTGNG 317
Cdd:PRK05638 277 LYVKNPVMKEYVSEAIKESGGTAVVVNEEEIMAGEKLLAK-EGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTGSG 355
|
....
gi 906393278 318 LKDP 321
Cdd:PRK05638 356 LKGY 359
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
6-319 |
1.71e-47 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 163.84 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPVTDQ-TPALTLheGNTPLIhlpklseQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTG 84
Cdd:PRK08329 43 MRRYIDYLPVDEEfLPHLTP--PITPTV-------KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 85 NTSAAAAAYAARANMKCIVIIPNGKIAfGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNS-VNPYRIEGQK 163
Cdd:PRK08329 114 NAALSLALYSLSEGIKVHVFVSYNASK-EKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHwLNPYFLEGTK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 164 TAAFEVCEQLGeAPDVLAIPVGNAGNITAYWKGFKEYHE-KNGTGLPKMRGFEAEGAAAIVRNEVIENpeTIATAIRIGN 242
Cdd:PRK08329 193 TIAYEIYEQIG-VPDYAFVPVGSGTLFLGIWKGFKELHEmGEISKMPKLVAVQAEGYESLCKRSKSEN--KLADGIAIPE 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906393278 243 PASWDKAVKAAEESNGKIDEVTDDEILHAYQLIARVeGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLTGNGLK 319
Cdd:PRK08329 270 PPRKEEMLRALEESNGFCISVGEEETRAALHWLRRM-GFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLK 345
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
27-315 |
2.89e-43 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 152.17 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGI-ELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVII 105
Cdd:PRK06381 14 GGTPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 106 PNGkIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVN--SVNP-YRIEGQKTAAFEVCEQLGEAPDVLAI 182
Cdd:PRK06381 94 PRS-YSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANpgSVNSvVDIEAYSAIAYEIYEALGDVPDAVAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 183 PVGNAGNITAYWKGFKEYHEKNGTG-LPKMRGFEAEGAAAIV------RNEVIE-NPETIA-TAirIGNP-ASW-----D 247
Cdd:PRK06381 173 PVGNGTTLAGIYHGFRRLYDRGKTSrMPRMIGVSTSGGNQIVesfkrgSSEVVDlEVDEIReTA--VNEPlVSYrsfdgD 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 248 KAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKgsKVVAVLTG 315
Cdd:PRK06381 251 NALEAIYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVND--NVVAVITG 316
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
29-315 |
7.65e-34 |
|
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: 127.07 E-value: 7.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAK-AKEEGNDTIMCASTGN---------TSaaaaayaarAN 98
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASlSEEERARGVVAASAGNhaqgvayaaRL---------LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 99 MKCIVIIPNGkIAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYR-IEGQKTAAFEVCEQLGEaP 177
Cdd:COG1171 96 IPATIVMPET-APAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDvIAGQGTIALEILEQLPD-L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 178 DVLAIPVGN----AGnITAYWKGFKeyhekngtglPKMR--GFEAEGAAAIVR----NEVIENPE--TIATAIRIG--NP 243
Cdd:COG1171 174 DAVFVPVGGggliAG-VAAALKALS----------PDIRviGVEPEGAAAMYRslaaGEPVTLPGvdTIADGLAVGrpGE 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906393278 244 ASWDKAVKAAEEsngkIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQvksGEIPKGSKVVAVLTG 315
Cdd:COG1171 243 LTFEILRDLVDD----IVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGKRVVVVLSG 307
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
29-315 |
1.22e-31 |
|
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: 120.67 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDT-IMCASTGNTSAAAAAYAARANMKCIVIIPN 107
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAASAGNHAQGVAYAAKLLGIPATIVMPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 108 GKIAFgKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEaPDVLAIPVGN 186
Cdd:cd01562 98 TAPAA-KVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDdPDVIAGQGTIGLEILEQVPD-LDAVFVPVGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 187 AG---NITAYWKGFKeyhekngtglPKMR--GFEAEGAAAIVR----NEVIENPE--TIATAIRIGNP-ASWDKAVKAae 254
Cdd:cd01562 176 GGliaGIATAVKALS----------PNTKviGVEPEGAPAMAQslaaGKPVTLPEvdTIADGLAVKRPgELTFEIIRK-- 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906393278 255 esngKIDE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSgeiPKGSKVVAVLTG 315
Cdd:cd01562 244 ----LVDDvvtVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSG 300
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
22-319 |
1.05e-24 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 102.51 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 22 LTLHEGNTPLIHlpklseqlGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKC 101
Cdd:PRK06450 52 ISLGEGRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPNgKIAFGKLAQAVMYGAEIIAIDGNFDDalkiVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCEQLG-EAPDV 179
Cdd:PRK06450 124 KIFVPE-TASGGKLKQIESYGAEVVRVRGSRED----VAKAAENSGYYYASHVlQPQFRDGIRTLAYEIAKDLDwKIPNY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 180 LAIPVGNAGNITAYWKGFKEYHEKNGTG-LPKMRGFEAEGAA---AIVRNEVIENPE---TIATAIRIGNPASWDKAVKA 252
Cdd:PRK06450 199 VFIPVSAGTLLLGVYSGFKHLLDSGVISeMPKIVAVQTEQVSplcAKFKGISYTPPDkvtSIADALVSTRPFLLDYMVKA 278
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 906393278 253 AEEsNGKIDEVTDDEILHAYQLIARvEGVFAEPGSCASIAGvLKQVKSGEipkgskVVAVLTGNGLK 319
Cdd:PRK06450 279 LSE-YGECIVVSDNEIVEAWKELAK-KGLLVEYSSATVYAA-YKKYSVND------SVLVLTGSGLK 336
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
27-313 |
5.47e-24 |
|
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: 99.51 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEG----NDTIMCASTGNTSAAAAAYAARANMKCI 102
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGllkpGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 103 VIIPNgKIAFGKLAQAVMYGAEIIAIDGNFDD----ALKIVRSICEKSPIALV-----NSVNPyriEG-QKTAAFEVCEQ 172
Cdd:cd01561 81 IVMPE-TMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWlnqfeNPANP---EAhYETTAPEIWEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 173 LGEAPDVLAIPVGNAGNITAYWKGFKEYHekngtglPKMR--GFEAEGAAAIVRNEVienPETIATAIRIGN-PASWDKA 249
Cdd:cd01561 157 LDGKVDAFVAGVGTGGTITGVARYLKEKN-------PNVRivGVDPVGSVLFSGGPP---GPHKIEGIGAGFiPENLDRS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 250 VkaaeesngkIDE---VTDDE-ILHAYQLIARvEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVL 313
Cdd:cd01561 227 L---------IDEvvrVSDEEaFAMARRLARE-EGLLVGGSSGAAVAAALKLAK--RLGPGKTIVTIL 282
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
27-319 |
1.83e-21 |
|
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: 92.80 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDR---GMVMAvakAKEEG----NDTIMCASTGNTSAAAAAYAARANM 99
Cdd:COG0031 12 GNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRialSMIED---AEKRGllkpGGTIVEATSGNTGIGLAMVAAAKGY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 100 KCIVIIPNG----KIafgKLAQAvmYGAEIIAIDG--NFDDALKIVRSICEKSPialvNSV------NPYRIEG-QKTAA 166
Cdd:COG0031 89 RLILVMPETmskeRR---ALLRA--YGAEVVLTPGaeGMKGAIDKAEELAAETP----GAFwpnqfeNPANPEAhYETTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 167 FEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHekngtglPKMR--GFEAEGAAaivrneVIENPETIATAIR-IGN- 242
Cdd:COG0031 160 PEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERN-------PDIKivAVEPEGSP------LLSGGEPGPHKIEgIGAg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 243 --PASWDKAVkaaeesngkIDE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVLTGNG 317
Cdd:COG0031 227 fvPKILDPSL---------IDEvitVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAK--RLGPGKTIVTILPDSG 295
|
..
gi 906393278 318 LK 319
Cdd:COG0031 296 ER 297
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
29-315 |
2.95e-19 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 87.94 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAK-AKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVII-- 105
Cdd:PRK08639 26 TPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQlSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFMpv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 106 --PNGKI----AFGKlaQAVmygaEIIAIDGNFDDALKIVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCEQLGEA-- 176
Cdd:PRK08639 106 ttPQQKIdqvrFFGG--EFV----EIVLVGDTFDDSAAAAQEYAEETGATFIPPFdDPDVIAGQGTVAVEILEQLEKEgs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 177 PDVLAIPVGNAG---NITAYwkgFKEYHEKNgtglpKMRGFEAEGA----AAIVRNEVIENPET------IATAiRIGnp 243
Cdd:PRK08639 180 PDYVFVPVGGGGlisGVTTY---LKERSPKT-----KIIGVEPAGAasmkAALEAGKPVTLEKIdkfvdgAAVA-RVG-- 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 906393278 244 aswDKAVKAAEESNGKIDEVTDD----EILHAYQliarVEGVFAEPGSCASIAgVLKQVKSgEIpKGSKVVAVLTG 315
Cdd:PRK08639 249 ---DLTFEILKDVVDDVVLVPEGavctTILELYN----KEGIVAEPAGALSIA-ALELYKD-EI-KGKTVVCVISG 314
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
27-325 |
9.96e-16 |
|
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: 76.49 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGN----DTIMCASTGNTSAAAAAYAARANMKCI 102
Cdd:TIGR01138 7 GNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEikpgDVLIEATSGNTGIALAMIAALKGYRMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 103 VIIPNGKIAFGKLAQAVmYGAEII------AIDGNFDDALKIVRSICEKSPIALVNSVNPYriEGQKTAAFEVCEQLGEA 176
Cdd:TIGR01138 87 LLMPDNMSQERKAAMRA-YGAELIlvtkeeGMEGARDLALELANRGEGKLLDQFNNPDNPY--AHYTSTGPEIWQQTGGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 177 PDVLAIPVGNAGNITAYWKGFKEYHEK-NGTGLPKMRGFEAEGaaaivrnevienpetiataIRignpaSWDKAVKAAEE 255
Cdd:TIGR01138 164 ITHFVSSMGTTGTIMGVSRFLKEQNPPvQIVGLQPEEGSSIPG-------------------IR-----RWPTEYLPGIF 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 906393278 256 SNGKIDEVTDDEILHAYQL---IARVEGVFAEPGSCASIAGVLKQVKsgEIPKGSkVVAVLTGNGLKDPNTAV 325
Cdd:TIGR01138 220 DASLVDRVLDIHQRDAENTmreLAVREGIFCGVSSGGAVAAALRLAR--ELPDAV-VVAIICDRGDRYLSTGV 289
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
27-317 |
4.18e-15 |
|
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: 74.62 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDR---GMVM-AVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCI 102
Cdd:TIGR01136 6 GNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRialSMILdAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 103 VIIP-NGKIAFGKLAQAvmYGAEIIAIDGN--FDDALKIVRSICEKSPIALV-----NSVNPYriEGQKTAAFEVCEQLG 174
Cdd:TIGR01136 86 LTMPeTMSLERRKLLRA--YGAELILTPGEegMKGAIDKAEELAAETNKYVMldqfeNPANPE--AHYKTTGPEIWRDTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 175 EAPDVLAIPVGNAGNITAYWKGFKEYhekngtgLPKMRGFEAEGAAAIVRNEVIENPETIAtaiRIGN---PASWDKAVk 251
Cdd:TIGR01136 162 GRIDHFVAGVGTGGTITGVGRYLKEQ-------NPNIQIVAVEPAESPVLSGGEPGPHKIQ---GIGAgfiPKILDLSL- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 252 aaeesngkIDEV----TDDEILHAYQLiARVEGVFAEPGSCASIAGVLkQVKSGEIPKGSKVVAVLTGNG 317
Cdd:TIGR01136 231 --------IDEVitvsDEDAIETARRL-AREEGILVGISSGAAVAAAL-KLAKRLENADKVIVAILPDTG 290
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
29-323 |
4.80e-15 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 75.19 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGN--DTIMCASTGNTSAAAAAYAARANMKCIVIIP 106
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 107 NgKIAFGKLAQAVMYGAEIIAIDGNfDDALKIVRSICEKSPIALVNSVNPYRIEGQKTAAFEVCEQLGEAPDVLAIPVGN 186
Cdd:PRK06608 104 L-NTSKVKQQAALYYGGEVILTNTR-QEAEEKAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASCGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 187 AGNITAywkgfkEYHEKNGTG-LPKMRGFE---AEGAAAIVRNEVI----ENPETIATAIRigNPASWDKAVkaaeESNG 258
Cdd:PRK06608 182 GGLISG------TYLAKELISpTSLLIGSEplnANDAYLSLKNNKIyrlnYSPNTIADGLK--TLSVSARTF----EYLK 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 259 KID---EVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIPKgsKVVAVLTGnGLKDPNT 323
Cdd:PRK06608 250 KLDdfyLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKPQ--KLLVILSG-GNIDPIL 314
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
28-331 |
2.12e-14 |
|
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: 73.10 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 28 NTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGM---VMAVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVI 104
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIghlCQKSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPN--GKIAFGKLAQavmYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSV---NPYRIEGQKTAAFEVCEQLGEA--P 177
Cdd:cd06448 81 VPEstKPRVVEKLRD---EGATVVVHGKVWWEADNYLREELAENDPGPVYVHpfdDPLIWEGHSSMVDEIAQQLQSQekV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 178 DVLAIPVGNAGNITAYWKGFKEYHEKNGTGLpkmrGFEAEGA----AAIVRNEVIENPETIATAIRIGNPASWDKAVKAA 253
Cdd:cd06448 158 DAIVCSVGGGGLLNGIVQGLERNGWGDIPVV----AVETEGAhslnASLKAGKLVTLPKITSVATSLGAKTVSSQALEYA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 254 EESNGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGV------LKQVKSGEIPKGSKVVAVLTGNGlkdpNTAVDI 327
Cdd:cd06448 234 QEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVysgkilDLQLEVLLTPLDNVVVVVCGGSN----ITLEQL 309
|
....
gi 906393278 328 SEIK 331
Cdd:cd06448 310 KEYK 313
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
29-315 |
6.11e-14 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 71.65 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRG----MVMAVAKAKEEGndtIMCASTGNTSAAAAAYAARANMKCIVI 104
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPNGKIAFgKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEaPDVLAIP 183
Cdd:PRK06815 98 APEQASAI-KLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNdPQVIAGQGTIGMELVEQQPD-LDAVFVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 184 VGNAG---NITAYWKGFKeyhekngtglPKMR--GFEAEGAAAIVRN----EVIENPE--TIATairiGNPASWDKAVKA 252
Cdd:PRK06815 176 VGGGGlisGIATYLKTLS----------PKTEiiGCWPANSPSLYTSleagEIVEVAEqpTLSD----GTAGGVEPGAIT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 906393278 253 AEESNGKIDE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGeipKGSKVVAVLTG 315
Cdd:PRK06815 242 FPLCQQLIDQkvlVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY---QGKKVAVVLCG 304
|
|
| Thr-synth_2 |
cd01560 |
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ... |
25-192 |
3.21e-13 |
|
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: 70.35 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 25 HEGNTPLihlPKLSEQLGI-EL-HvktegvNPTGSFKDRGM-----VMAVAKAKEEGNDTIMCASTGNT-SAAAAAYAAR 96
Cdd:cd01560 84 HPDIAPL---VQLGDNLYVlELfH------GPTLAFKDMALqflgrLLEYFLKRRNERITILVATSGDTgSAAIEGFRGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 97 ANMKCIVIIPNGKIAfgKLAQAVMYGA-----EIIAIDGNFDDALKIVRSI------CEKSPIALVNSVNPYRIEGQKT- 164
Cdd:cd01560 155 PNVDVVVLYPKGGVS--PIQELQMTTLpadnvHVVAVEGDFDDCQSLVKALfadedfNKKLKLSSANSINWARILAQIVy 232
|
170 180 190
....*....|....*....|....*....|.
gi 906393278 165 ---AAFEVCEQLGEAPDVLAIPVGNAGNITA 192
Cdd:cd01560 233 yfyAYLQLLKRGEGEKVEFSVPTGNFGNILA 263
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
29-332 |
4.47e-13 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 69.27 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHlpklSEQLGIELhvKTEGVNPTGSFKDRGMVMAVAKAKEEGND-TIMCASTGNTSAAAAAYAARANMKCIVIIPN 107
Cdd:PRK08813 40 TPLHY----AERFGVWL--KLENLQRTGSYKVRGALNALLAGLERGDErPVICASAGNHAQGVAWSAYRLGVQAITVMPH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 108 GKIAfGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCeqlGEAPDVLAIPVGN 186
Cdd:PRK08813 114 GAPQ-TKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFdDPDVIAGQGTVGIELA---AHAPDVVIVPIGG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 187 AGNITAYWKGFKEyhekngTGLpKMRGFEAEGAAAI---VRNEV--IENPETIATAIRIGNPASWDKAVKAAEESNGKId 261
Cdd:PRK08813 190 GGLASGVALALKS------QGV-RVVGAQVEGVDSMaraIRGDLreIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVI- 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906393278 262 eVTDDEILHAYQLIARVEGVFAEPGSCASIAgvlkqvkSGEIPKGSKVVAVLTGNGLKDPNTAVDISEIKP 332
Cdd:PRK08813 262 -VREAELRETLVRLALEEHVIAEGAGALALA-------AGRRVSGKRKCAVVSGGNIDATVLATLLSEVRP 324
|
|
| PLN02970 |
PLN02970 |
serine racemase |
29-317 |
9.70e-13 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 68.17 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKA-KEEGNDTIMCASTGNTSAAAAAYAARANMKCIVIIPN 107
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLsDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVVPK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 108 GKIAFgKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEApDVLAIPVGN 186
Cdd:PLN02970 108 NAPAC-KVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNdGRVISGQGTIALEFLEQVPEL-DVIIVPISG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 187 AGNIT---AYWKGFKeyhekngtglPKMRGFEAEGAAA------IVRNEVIENPE--TIATAIR--IGnPASWdKAVKaa 253
Cdd:PLN02970 186 GGLISgiaLAAKAIK----------PSIKIIAAEPKGAddaaqsKAAGEIITLPVtnTIADGLRasLG-DLTW-PVVR-- 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 254 eesnGKIDE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVL-KQVKSGEIPKGSKVVAVLTGNG 317
Cdd:PLN02970 252 ----DLVDDvitVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsDSFRSNPAWKGCKNVGIVLSGG 315
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
29-334 |
5.38e-12 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 65.91 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRG----MVMAVAKAKEEGndtIMCASTGNTSAAAAAYAARANMKCIVI 104
Cdd:PRK08638 28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPNGKiAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEAPDVLaIP 183
Cdd:PRK08638 105 MPKGA-PKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDdPKVIAGQGTIGLEILEDLWDVDTVI-VP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 184 VGNAGNITAYWKGFKEYHekngtglPKMR--GFEAEG----AAAIVRNEVIENPE--TIATAIRIGNPAswDKAVKAAEE 255
Cdd:PRK08638 183 IGGGGLIAGIAVALKSIN-------PTIHiiGVQSENvhgmAASFYAGEITTHRTtgTLADGCDVSRPG--NLTYEIVRE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 256 SNGKIDEVTDDEILHAYQ-LIARVEGVFAEPGSCASIAgvlkqVKSGEIP---KGSKVVAVLTGNGlkdpntaVDISEIK 331
Cdd:PRK08638 254 LVDDIVLVSEDEIRNAMKdLIQRNKVVTEGAGALATAA-----LLSGKLDqyiQNKKVVAIISGGN-------VDLSRVS 321
|
...
gi 906393278 332 PVT 334
Cdd:PRK08638 322 QIT 324
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
29-315 |
1.37e-11 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 64.65 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAK-AKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVIIPN 107
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQfSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATIVMPQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 108 GKIAfGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEApDVLAIPVGN 186
Cdd:PRK07048 105 DAPA-AKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDhPHVIAGQGTAAKELFEEVGPL-DALFVCLGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 187 AGNITaywkgfkeyheknGTGL------PKMRGFEAEGAAA-----------IVRnevIENPETIATAirignpaswdka 249
Cdd:PRK07048 183 GGLLS-------------GCALaaralsPGCKVYGVEPEAGndgqqsfrsgeIVH---IDTPRTIADG------------ 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 250 vkAAEESNGK------------IDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGeipKGSKVVAVLTG 315
Cdd:PRK07048 235 --AQTQHLGNytfpiirrlvddIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPL---KGKRVGVIISG 307
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
29-315 |
1.37e-10 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 61.55 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDT--IMCASTGNTSAAAAAYAARANMKCIVIIP 106
Cdd:PRK06110 22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVrgVISATRGNHGQSVAFAARRHGLAATIVVP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 107 NGKiAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVNPYRIEGQKTAAFEVceqLGEAP--DVLAIPV 184
Cdd:PRK06110 102 HGN-SVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSFHPDLVRGVATYALEL---FRAVPdlDVVYVPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 185 GNAGNITAYwkgfkeYHEKNGTGLpKMR--GFEAEGAAA----IVRNEVIENP--ETIA--TAIRIGNPASWDKAVKAAE 254
Cdd:PRK06110 178 GMGSGICGA------IAARDALGL-KTRivGVVSAHAPAyalsFEAGRVVTTPvaTTLAdgMACRTPDPEALEVIRAGAD 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906393278 255 EsngkIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQvksGEIPKGSKVVAVLTG 315
Cdd:PRK06110 251 R----IVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQE---RERLAGKRVGLVLSG 304
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
29-315 |
1.98e-10 |
|
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: 60.90 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLG--IELHVKTEGVNPTGSF---KDRGMVMAVAKAKEEGNDTIMCAS--TGNTSAAAAAYAARANMKC 101
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGLAFggnKIRKLEYLLPDALAKGADTLVTVGgiQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPN------------GKIAFGKL--AQAVMYGAEI-IAIDGNFDDALKIVRSICEKS-PIALVNSVNPYRIEGQKTA 165
Cdd:cd06449 81 VLVQENwvpysdavydrvGNILLSRImgADVRLVSAGFdIGIRKSFEEAAEEVEAKGGKPyVIPAGGSEHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 166 AFEV---CEQLGEAPDVLAIPVGNAGNITAYWKGFKEYhekngtglpkMRGFEAEGAAAIVRNEVienpeTIATAIRIGN 242
Cdd:cd06449 161 VLEIaqqEEELGFKFDSIVVCSVTGSTHAGLSVGLAAL----------GRQRRVIGIDASAKPEK-----TKAQVLRIAQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 243 PASWDKAVKAAEESNGKIDE-------VTDDEILHAYQLIARVEGVFAEPGSCA-SIAGVLKQVKSGEIPKGSKVVAVLT 314
Cdd:cd06449 226 AKLAEEGLEVKEEDVVLDDDyaapeygIPNDETIEAIKLCARLEGIITDPVYEGkSMQGMIDLVRNGEFKEGSKVLFIHL 305
|
.
gi 906393278 315 G 315
Cdd:cd06449 306 G 306
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
29-315 |
2.29e-10 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 61.74 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRG----MVMAVAKAKEEGndtIMCASTGNTSAAAAAYAARANMKCIVI 104
Cdd:PRK12483 38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARG---VITASAGNHAQGVALAAARLGVKAVIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPNGKIAFgKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCEQLGEAPDVLAIP 183
Cdd:PRK12483 115 MPRTTPQL-KVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFdDPDVIAGQGTVAMEILRQHPGPLDAIFVP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 184 VGNAG---NITAYWKGFKeyhekngtglPKMR--GFEAEG----AAAIVRNEVIENPE--TIATAIrignpaswdkAVKA 252
Cdd:PRK12483 194 VGGGGliaGIAAYVKYVR----------PEIKviGVEPDDsnclQAALAAGERVVLGQvgLFADGV----------AVAQ 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 906393278 253 AEESNGKI-----DE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEIpKGSKVVAVLTG 315
Cdd:PRK12483 254 IGEHTFELcrhyvDEvvtVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGI-EGQTLVAIDSG 323
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
29-181 |
4.38e-10 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 59.98 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGND-TIMCASTGNTSAAAAAYAARANMKCIV---- 103
Cdd:PRK07476 20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERArGVVTASTGNHGRALAYAARALGIRATIcmsr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 104 IIPNGKIAfgklaqAV-MYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCEQLGEAPDVLA 181
Cdd:PRK07476 100 LVPANKVD------AIrALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFdDPRIIAGQGTIGLEILEALPDVATVLV 173
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
28-315 |
9.05e-10 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 59.52 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 28 NTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRG----MVMAVAKAKEEGndtIMCASTGNTSAAAAAYAARANMKCIV 103
Cdd:PRK07334 23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGalnkLLLLTEEERARG---VIAMSAGNHAQGVAYHAQRLGIPATI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 104 IIPNGKiAFGKLAQAVMYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVceqLGEAP--DVL 180
Cdd:PRK07334 100 VMPRFT-PTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDdPAVIAGQGTVALEM---LEDAPdlDTL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 181 AIPVGNAGNI----TAYwKGFKeyhekngtglPKMR--GFEAEGAAAIVrNEVIENP-----ETIATAIRIGNPASWDKA 249
Cdd:PRK07334 176 VVPIGGGGLIsgmaTAA-KALK----------PDIEiiGVQTELYPSMY-AAIKGVAlpcggSTIAEGIAVKQPGQLTLE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906393278 250 VKAAeesngKIDE---VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQvksGEIPKGSKVVAVLTG 315
Cdd:PRK07334 244 IVRR-----LVDDillVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY---PERFRGRKVGLVLSG 304
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
17-309 |
1.83e-09 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 58.12 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 17 DQTPALTLHEGNTPLIHLPKLSEQLG--IELHVKTEGVNPTGSF---KDRGMVMAVAKAKEEGNDTIMcaSTG----NTS 87
Cdd:PRK12390 4 QKFPRYPLTFGPTPIHPLKRLSAHLGgkVELYAKREDCNSGLAFggnKTRKLEYLVPDALAQGADTLV--SIGgvqsNHT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 88 AAAAAYAARANMKCIVIIPN------------GKIAFGKLAqavmyGAEIIAIDGNFD--------DALKIVRSICEKS- 146
Cdd:PRK12390 82 RQVAAVAAHLGMKCVLVQENwvnyedavydrvGNILLSRIM-----GADVRLVPDGFDigirksweDALEDVRAAGGKPy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 147 PIALVNSVNPYRIEGQKTAAFEVCEQ---LGEAPD--VLAIPVGN--AGNITaywkGFKeyheknGTGLP-KMRGFEAEG 218
Cdd:PRK12390 157 AIPAGASDHPLGGLGFVGFAEEVRAQeaeLGFKFDyiVVCSVTGStqAGMVV----GFA------ADGRArRVIGIDASA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 219 AAAIVRNEVIENPETIATAIRIGNPASwDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEP---GScaSIAGVL 295
Cdd:PRK12390 227 KPEQTRAQVLRIARNTAELVELGRDIT-EDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPvyeGK--SMHGMI 303
|
330
....*....|....
gi 906393278 296 KQVKSGEIPKGSKV 309
Cdd:PRK12390 304 DLVRKGEFPEGSKV 317
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
29-195 |
2.27e-09 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 58.78 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAK-AKEEGNDTIMCASTGNTSAAAAAYAARANMKCIVIIP- 106
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKlPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPv 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 107 -NGKIAFgklaQAV-MYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSV-NPYRIEGQKTAAFEVCEQLGEAPDVLAIP 183
Cdd:PLN02550 190 tTPEIKW----QSVeRLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFdHPDVIAGQGTVGMEIVRQHQGPLHAIFVP 265
|
170
....*....|....*
gi 906393278 184 VGNAG---NITAYWK 195
Cdd:PLN02550 266 VGGGGliaGIAAYVK 280
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
27-313 |
2.98e-09 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 57.56 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDR---GMVM-AVAKAKEEGNDTIMCASTGNTSAAAAAYAARANMKCI 102
Cdd:PRK10717 12 GNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRaalNIIWdAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 103 VIIPNG----KIAFGKLaqavmYGAEIIAIDG----NFDDALKIVRSICEKSPIALVNSV-------NPYRIEGQ-KTAA 166
Cdd:PRK10717 92 IVMPETqsqeKKDLLRA-----LGAELVLVPAapyaNPNNYVKGAGRLAEELVASEPNGAiwanqfdNPANREAHyETTG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 167 FEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHEKNGTGLPkmrgfEAEGAAAI--VRNEVIENP-ETIATAIRIGN- 242
Cdd:PRK10717 167 PEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLA-----DPTGSALYsyYKTGELKAEgSSITEGIGQGRi 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906393278 243 PASWDKAvkaaeesngKIDE---VTDDEILH-AYQLIaRVEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVL 313
Cdd:PRK10717 242 TANLEGA---------PIDDairIPDEEALStAYRLL-EEEGLCLGGSSGINVAAALRLAR--ELGPGHTIVTIL 304
|
|
| cysteate_syn |
TIGR03844 |
cysteate synthase; Members of this family are cysteate synthase, an enzyme of alternate ... |
6-333 |
6.07e-09 |
|
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: 57.05 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPV-----TDQTPALTLHEGntplihlpkLSEQLGI-ELHVKTEGVNP-------TGSFKDRGMVMAVAKAKE 72
Cdd:TIGR03844 44 IFRYYDWLPVtghlrTRGGPVTYKSEG---------LARELGLsDLYITFSGYWPergafmrTCSFKELEALPTMQRLKE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 73 EGNDTIMCASTGNTSAAAAAYAARANMKCIVIIPngKIAFGKL-----AQAVMygaeIIAIDGNFDDALKIVRSICEKSP 147
Cdd:TIGR03844 115 RGGKTLVVASAGNTGRAFAEVSAITGQPVILVVP--KSSADRLwttepASSVL----LVTVDGDYTDAIALADRIATLPG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 148 I-ALVNSVNPYRIEGQKTAAFEVCEQLGEAPDVLAIPVGNA-GNITAyWKG----------------------------F 197
Cdd:TIGR03844 189 FvPEGGARNVARRDGMGTVMLDAAVTIGSLPDHYFQAVGSGtGGIAA-WEAamrliedgrfgsklprlhlaqnlpfvpmV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 198 KEYHEKNGTGLPKMRGFEAEGAAAIVRNEVIEN---PETIATAIRignpaswdKAVKAaeeSNGKIDEVTDDEILHAYQL 274
Cdd:TIGR03844 268 NAWQEGRREIIPESDMPDAENSIEEVYSDVLTNrtpPYGVTGGVF--------DALIA---TGGQMYGVSNKEAVSAGKL 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 906393278 275 IARVEGVFAEPGSCASIAGVLKQVKSGEIPKGSKVVAVLTGNGLKDPNTAVDISEIKPV 333
Cdd:TIGR03844 337 FEESEGIDILPAAAVAVAALVKAVESGFIGPDDDILLNITGGGYKRLREDLPRYQIEPD 395
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
29-315 |
7.57e-09 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 57.07 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRG----MVMAVAKAKEEGndtIMCASTGNTSAAAAAYAARANMKCIVI 104
Cdd:PRK09224 21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARG---VITASAGNHAQGVALSAARLGIKAVIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPNG----KI----AFGklAQAVMYGAeiiaidgNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGE 175
Cdd:PRK09224 98 MPVTtpdiKVdavrAFG--GEVVLHGD-------SFDEAYAHAIELAEEEGLTFIHPFDdPDVIAGQGTIAMEILQQHPH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 176 APDVLAIPVGNAG---NITAYWKGFKeyhekngtglPKMR--GFEAEGAAAIVRnevienpetiatAIRIGNPASWDK-- 248
Cdd:PRK09224 169 PLDAVFVPVGGGGliaGVAAYIKQLR----------PEIKviGVEPEDSACLKA------------ALEAGERVDLPQvg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 249 ------AVK-AAEES----NGKIDE---VTDDEIlhayqlIARVEGVF------AEPGSCASIAGVLKQVKSGEIpKGSK 308
Cdd:PRK09224 227 lfadgvAVKrIGEETfrlcQEYVDDvitVDTDEI------CAAIKDVFedtrsiAEPAGALALAGLKKYVAQHGI-EGET 299
|
....*..
gi 906393278 309 VVAVLTG 315
Cdd:PRK09224 300 LVAILSG 306
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
20-315 |
1.24e-08 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 55.61 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 20 PALTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNP--TGSFKDRGMVMAVAKAKEEGNDTI----------------MCA 81
Cdd:PRK03910 7 PRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGlaLGGNKTRKLEFLLADALAQGADTLitagaiqsnharqtaaAAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 82 STGntsaaaaayaaranMKCIVIIPNGKIAFGKLAQAV-------MYGAEIIAIDGNfDDALKIVRSICEKspialvnsv 154
Cdd:PRK03910 87 KLG--------------LKCVLLLENPVPTEAENYLANgnvllddLFGAEIHVVPAG-TDMDAQLEELAEE--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 155 npYRIEGQK------------------TAAFEVCEQL---GEAPDVLAIPVGNAGNITAYWKGFKEYHEKngtglPKMRG 213
Cdd:PRK03910 143 --LRAQGRRpyvipvggsnalgalgyvACALEIAQQLaegGVDFDAVVVASGSGGTHAGLAAGLAALGPD-----IPVIG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 214 FEAEGAAAIVRNEVIENPETIATAIRIGNPASwDKAVKAAEESNGKIDEVTDDEILHAYQLIARVEGVFAEP---GScaS 290
Cdd:PRK03910 216 VTVSRSAAEQEPKVAKLAQATAELLGLPTEIP-RADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPvytGK--A 292
|
330 340
....*....|....*....|....*
gi 906393278 291 IAGVLKQVKSGEIPKGSKVVAVLTG 315
Cdd:PRK03910 293 MAGLIDLIRQGRFKKGGNVLFIHTG 317
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
27-126 |
2.02e-08 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 54.88 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEG----NDTIMCASTGNTSAAAAAYAARANMKCI 102
Cdd:PRK11761 11 GNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGeikpGDTLIEATSGNTGIALAMIAAIKGYRMK 90
|
90 100
....*....|....*....|....
gi 906393278 103 VIIPNGKIAFGKLAQAVmYGAEII 126
Cdd:PRK11761 91 LIMPENMSQERRAAMRA-YGAELI 113
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
14-107 |
4.08e-08 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 54.61 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 14 PVTDQTPALTLHE--GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGN----DTIMCASTGNTS 87
Cdd:PLN02356 37 PLSKKKPRNGLIDaiGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQlfpgGVVTEGSAGSTA 116
|
90 100
....*....|....*....|
gi 906393278 88 AAAAAYAARANMKCIVIIPN 107
Cdd:PLN02356 117 ISLATVAPAYGCKCHVVIPD 136
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
29-331 |
6.47e-08 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 53.99 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQL------GIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMCAS-TGNTSAAAAAYAARANMKC 101
Cdd:PLN02618 67 TPLYFAERLTEHYkradgeGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETgAGQHGVATATVCARFGLEC 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPNGKIAFGKLAQAVM--YGAEIIAI---DGNFDDAL-KIVR---SICEKSPIALVNSVNPY----------RIEGQ 162
Cdd:PLN02618 147 IVYMGAQDMERQALNVFRMrlLGAEVRPVhsgTATLKDATsEAIRdwvTNVETTHYILGSVAGPHpypmmvrdfhSVIGK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 163 KTAAfEVCEQLGEAPDVLAIPVGNAGNITAYwkgFKEYHEKNGTglpKMRGFEAEG--------AAAIVRNEV------- 227
Cdd:PLN02618 227 ETRR-QAMEKWGGKPDVLVACVGGGSNAMGL---FHEFIDDEDV---RLIGVEAAGfgldsgkhAATLTKGEVgvlhgam 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 228 ----------IENPETIATAIR---IGNPASWDKAVKAAEesngkIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGV 294
Cdd:PLN02618 300 syllqdedgqIIEPHSISAGLDypgVGPEHSFLKDTGRAE-----YYSVTDEEALEAFQRLSRLEGIIPALETSHALAYL 374
|
330 340 350
....*....|....*....|....*....|....*..
gi 906393278 295 LKQVKSgeIPKGSKVVAVLTGNGLKDPNTAVDISEIK 331
Cdd:PLN02618 375 EKLCPT--LPDGTKVVVNCSGRGDKDVNTAIKYLQVS 409
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
29-137 |
2.22e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 52.19 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGI-ELHVKTEGVN-PTGSFKDRGMVMAVAK--AKEEGND---------------------TIMCAST 83
Cdd:PRK08206 45 TPLVALPDLAAELGVgSILVKDESYRfGLNAFKALGGAYAVARllAEKLGLDiselsfeeltsgevreklgdiTFATATD 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 906393278 84 GNTSAAAAAYAARANMKCIVIIPNGkIAFGKLAQAVMYGAEIIAIDGNFDDALK 137
Cdd:PRK08206 125 GNHGRGVAWAAQQLGQKAVIYMPKG-SSEERVDAIRALGAECIITDGNYDDSVR 177
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
27-317 |
8.24e-07 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 50.00 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEE-----GNDTIMCASTGNTSAAAAAYAARANMKC 101
Cdd:PLN00011 16 GNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKglitpGKSTLIEATAGNTGIGLACIGAARGYKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPNG-----KIAFGKLAQAVMYGAEIIAIDGNFDDAlkivRSICEKSPIALV-----NSVNP---YRIEGQktaafE 168
Cdd:PLN00011 96 ILVMPSTmslerRIILRALGAEVHLTDQSIGLKGMLEKA----EEILSKTPGGYIpqqfeNPANPeihYRTTGP-----E 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 169 VCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYHEKngtglPKMRGFEAEGAAAIVRNEviENPETIATairIGN---PAS 245
Cdd:PLN00011 167 IWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKD-----IKVCVVEPVESAVLSGGQ--PGPHLIQG---IGSgiiPFN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906393278 246 WDKAVKaaeesnGKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEipKGSKVVAVLTGNG 317
Cdd:PLN00011 237 LDLTIV------DEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPE--NAGKLIVVIFPSG 300
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
29-320 |
1.24e-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: 49.84 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQL-GIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMcASTG------NTSaaaaAYAARANMKC 101
Cdd:cd06446 35 TPLYRAKRLSEYLgGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKRVI-AETGagqhgvATA----TACALFGLEC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIpnGKIAFGKLAQAV----MYGAEI-----------IAIDGNFDDALKIVRSIcekspIALVNSV---NPYR---IE 160
Cdd:cd06446 110 EIYM--GAVDVERQPLNVfrmeLLGAEVvpvpsgsgtlkDAISEAIRDWVTNVEDT-----HYLLGSVvgpHPYPnmvRD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 161 GQKTAAFEVCEQL----GEAPDVLAIPVG---NAGNITAYWKGFKEyhekngtglPKMRGFEAEG--------AAAIVRN 225
Cdd:cd06446 183 FQSVIGEEAKKQIlekeGELPDVVIACVGggsNAAGLFYPFINDKD---------VKLIGVEAGGcgletgghAAYLFGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 226 EV-----------------IENPETIATAIR---IGNPASWDKAVKAAEesngkIDEVTDDEILHAYQLIARVEGVFAEP 285
Cdd:cd06446 254 TAgvlhglkmytlqdedgqIVPPHSISAGLDypgVGPEHAYLKDSGRVE-----YVAVTDEEALEAFKLLARTEGIIPAL 328
|
330 340 350
....*....|....*....|....*....|....*
gi 906393278 286 GSCASIAGVLKQVKsgEIPKGSKVVAVLTGNGLKD 320
Cdd:cd06446 329 ESSHAIAYAIKLAK--KLGKEKVIVVNLSGRGDKD 361
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
6-317 |
1.51e-06 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 49.57 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 6 IHQYKEFLPVTDQTPALTLHEGNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEE-----GNDTIMC 80
Cdd:PLN02556 37 LRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKnlitpGKTTLIE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 81 ASTGNTSAAAAAYAARANMKCIVIIPngkiAFGKLAQAVM---YGAEIIAID--GNFDDALKIVRSICEKSPIA--LVNS 153
Cdd:PLN02556 117 PTSGNMGISLAFMAAMKGYKMILTMP----SYTSLERRVTmraFGAELVLTDptKGMGGTVKKAYELLESTPDAfmLQQF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 154 VNPYRIEGQ-KTAAFEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKeyhEKNgtglPKMRGFEAEGAAAIVRNEVIENPE 232
Cdd:PLN02556 193 SNPANTQVHfETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLK---SKN----PNVKIYGVEPAESNVLNGGKPGPH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 233 TIaTAIRIG-NPASWDKAVKAaeesngKIDEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEiPKGSKVVA 311
Cdd:PLN02556 266 HI-TGNGVGfKPDILDMDVME------KVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPE-NKGKLIVT 337
|
....*.
gi 906393278 312 VLTGNG 317
Cdd:PLN02556 338 VHPSFG 343
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
29-332 |
2.71e-06 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 49.04 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEEGNDTIMcAST--GNTSAAAAAYAARANMKCIVIIp 106
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRII-AETgaGQHGVATATACALFGLKCTIFM- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 107 nGKIAFGKLAQAV----MYGAEIIAI---DGNFDDAL-KIVR--SICEKSPIALVNSV---NPY--------RIEGQKTA 165
Cdd:PRK13803 350 -GEEDIKRQALNVermkLLGANVIPVlsgSKTLKDAVnEAIRdwVASVPDTHYLIGSAvgpHPYpemvayfqSVIGEEAK 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 166 AfEVCEQLGEAPDVLAIPVGNAGNITAYWKGFKEYhekngtGLPKMRGFEAEG--------AAAIV--RNEVIENPETIA 235
Cdd:PRK13803 429 E-QLKEQTGKLPDAIIACVGGGSNAIGIFYHFLDD------PSVKLIGVEAGGkgvntgehAATIKkgRKGVLHGSMTYL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 236 TAIRIGN-------PASWDKAVKAAEESN----GKID--EVTDDEILHAYQLIARVEGVFAEPGSCASIAgVLKQVKsGE 302
Cdd:PRK13803 502 MQDENGQilephsiSAGLDYPGIGPMHANlfetGRAIytSVTDEEALDAFKLLAKLEGIIPALESSHALA-YLKEGR-KK 579
|
330 340 350
....*....|....*....|....*....|
gi 906393278 303 IPKGSKVVAVLTGNGLKDPNTAVDISEIKP 332
Cdd:PRK13803 580 FKKKDIVIVNLSGRGDKDIPTLKEYFENLP 609
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
29-315 |
5.91e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 44.18 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 29 TPLIHLPkLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAkAKEEGNDTIMCASTGNTSAAAAAYAARANMKCIV----I 104
Cdd:PRK08246 24 TPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRLL-AAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVfvpeT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 105 IPNGKIAfgKLAQavmYGAEIIAIDGNFDDALKIVRSICEKSPIALVNSVN-PYRIEGQKTAAFEVCEQLGEaPDVLAIP 183
Cdd:PRK08246 102 APPAKVA--RLRA---LGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDqPEVLAGAGTLGLEIEEQAPG-VDTVLVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 184 VGNAGNI--TAYWKGfkeyhekngtGLPKMRGFEAEGAAAIVR-----NEVIENPETIAT----AIRIGNPAsWDKAVKA 252
Cdd:PRK08246 176 VGGGGLIagIAAWFE----------GRARVVAVEPEGAPTLHAalaagEPVDVPVSGIAAdslgARRVGEIA-FALARAH 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 906393278 253 AEESNgkidEVTDDEILHAYQLIARVEGVFAEPGSCASIAGVLkqvkSG--EIPKGSKVVAVLTG 315
Cdd:PRK08246 245 VVTSV----LVSDEAIIAARRALWEELRLAVEPGAATALAALL----SGayVPAPGERVAVVLCG 301
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
27-199 |
4.19e-04 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 41.83 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEE-----GNDTIMCASTGNTSAAAAAYAARANMKC 101
Cdd:PLN02565 14 GKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKglikpGESVLIEPTSGNTGIGLAFMAAAKGYKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPnGKIAFGKLAQAVMYGAEIIAIDG--NFDDALKIVRSICEKSPIALV-----NSVNPyRIEGQKTAAfEVCEQLG 174
Cdd:PLN02565 94 IITMP-ASMSLERRIILLAFGAELVLTDPakGMKGAVQKAEEILAKTPNSYIlqqfeNPANP-KIHYETTGP-EIWKGTG 170
|
170 180
....*....|....*....|....*
gi 906393278 175 EAPDVLAIPVGNAGNITAYWKGFKE 199
Cdd:PLN02565 171 GKVDAFVSGIGTGGTITGAGKYLKE 195
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
27-313 |
7.74e-04 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 41.30 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 27 GNTPLIHLPKLSEQLGIELHVKTEGVNPTGSFKDRGMVMAVAKAKEE-----GNDTIMCASTGNTSAAAAAYAARANMKC 101
Cdd:PLN03013 122 GKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKgfispGKSVLVEPTSGNTGIGLAFIAASRGYRL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 102 IVIIPnGKIAFGKLAQAVMYGAEIIAID--GNFDDALKIVRSICEKSPIALV-----NSVNPyRIEGQKTAAfEVCEQLG 174
Cdd:PLN03013 202 ILTMP-ASMSMERRVLLKAFGAELVLTDpaKGMTGAVQKAEEILKNTPDAYMlqqfdNPANP-KIHYETTGP-EIWDDTK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906393278 175 EAPDVLAIPVGNAGNITAYWKGFKeyhEKNgtglPKMRGFEAEGAAAIVRNEVIENPETIATAIRIGNPASWDKAVkaae 254
Cdd:PLN03013 279 GKVDIFVAGIGTGGTITGVGRFIK---EKN----PKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKI---- 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 906393278 255 esngkIDEV---TDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKSGEipKGSKVVAVL 313
Cdd:PLN03013 348 -----MDEViaiSSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPE--NAGKLIAVS 402
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
263-331 |
1.88e-03 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 39.66 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906393278 263 VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVLTGNGLKDPNTAVDISEIK 331
Cdd:PRK04346 330 ITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAP--TLGKDQIIVVNLSGRGDKDVFTVAKLLGVI 396
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
263-320 |
7.99e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 37.92 E-value: 7.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 906393278 263 VTDDEILHAYQLIARVEGVFAEPGSCASIAGVLKQVKsgEIPKGSKVVAVLTGNGLKD 320
Cdd:PRK13028 334 ATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAP--ELSKDETILVNLSGRGDKD 389
|
|
| |
