|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
2-451 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 815.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 2 IHGKSLEAWCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESD 81
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 82 IVPLPKLQRRLLEEAGKTGEaqlpaaGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSA 161
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIP------GRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 162 HAFFGRHRIAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACH 241
Cdd:COG3048 155 RAFFSQYSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 242 FVDDENSPQLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLL 321
Cdd:COG3048 235 FVDDENSRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 322 GVYTGLHDQVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGM 401
Cdd:COG3048 315 GLATGLHDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGP 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490435089 402 VCVLRDA--AYLDRIGVTpARFARATHLVWGTGGSMVPDSEFAAHVDKGRAL 451
Cdd:COG3048 395 LRLLGSAgqAYLERHGLT-EKMANATHLVWATGGSMVPEEEMEAYLAKGKAL 445
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
5-452 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 775.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 5 KSLEAWCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVP 84
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 85 LPKLQRRLLEEAGKtgeaqlPAAGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAF 164
Cdd:PRK02991 81 IPAMQKALEKEYGQ------PISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 165 FGRHRIAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVD 244
Cdd:PRK02991 155 FSQYSIAVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 245 DENSPQLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVY 324
Cdd:PRK02991 235 DENSRTLFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 325 TGLHDQVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCV 404
Cdd:PRK02991 315 TGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 490435089 405 LRDAAYLDRIGVTPaRFARATHLVWGTGGSMVPDSEFAAHVDKGRALQ 452
Cdd:PRK02991 395 CASVAYLQRHGLSE-QLKNATHLVWATGGSMVPEEEMEQYLAKGRALL 441
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
10-444 |
0e+00 |
|
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a pyridoxal-phosphate enzyme that converts D-serine to pyruvate and NH3. This enzyme is also called D-serine dehydratase and D-serine deaminase and was previously designated EC 4.2.1.14. It is homologous to an enzyme that acts on threonine and may itself act weakly on threonine. [Energy metabolism, Amino acids and amines]
Pssm-ID: 211710 Cd Length: 431 Bit Score: 652.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 10 WCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVPLPKLQ 89
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 90 RRLLEEAgktgeaQLPAAGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAFFGRHR 169
Cdd:TIGR02035 81 KRLEKEY------QQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 170 IAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSP 249
Cdd:TIGR02035 155 IAVGSTGNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 250 QLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVYTGLHD 329
Cdd:TIGR02035 235 TLFLGYAVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 330 QVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLR-DA 408
Cdd:TIGR02035 315 QISVQDIGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCAsEV 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 490435089 409 AYLDRIGVTPARFARATHLVWGTGGSMVPDSEFAAH 444
Cdd:TIGR02035 395 SYRYMHGFSAEQLRNATHLVWATGGGMVPEEEMNAY 430
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
28-438 |
0e+00 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 637.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 28 WFNPGIAPAATALAdvGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVPLPKLQRRLLEEAGKtgeaqlPAA 107
Cdd:cd06447 3 WKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQ------PIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 108 GALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAFFGRHRIAVGSTGNLGLSIGIMSA 187
Cdd:cd06447 75 GRLLLKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 188 KLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSPQLFLGYAVAAERLAGQLQ 267
Cdd:cd06447 155 ALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 268 RAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVYTGLHDQVSVQDFGIDNVTAADGL 347
Cdd:cd06447 235 ELGIKVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 348 AVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLRDAAYlDRIGVTPARFARATHL 427
Cdd:cd06447 315 AVGRPSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEG-KRYVRLGYRMENATHI 393
|
410
....*....|.
gi 490435089 428 VWGTGGSMVPD 438
Cdd:cd06447 394 VWATGGSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
108-406 |
1.49e-30 |
|
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: 119.72 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 108 GALWLKTDNALPiSGSIKARGGIHEVLWHAERlalqagliregddyaalasdsahafFGRHRIAVGSTGNLGLSIGIMSA 187
Cdd:pfam00291 22 VDVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------------EGGKTVVEASSGNHGRALAAAAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 188 KLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSPQLFLGYAVAAERLAGQLq 267
Cdd:pfam00291 76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 268 raGVRVDAehplfVYLPCGVGGGPGGVAFGLKRVFGDaVHCIFAEPTHSPCMLLGVYTGLHDQVSVQDfgidnvTAADGL 347
Cdd:pfam00291 155 --GGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPALARSLAAGRPVPVPVAD------TIADGL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 348 AVGR-PSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLR 406
Cdd:pfam00291 221 GVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALA 280
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
2-451 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 815.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 2 IHGKSLEAWCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESD 81
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 82 IVPLPKLQRRLLEEAGKTGEaqlpaaGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSA 161
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIP------GRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 162 HAFFGRHRIAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACH 241
Cdd:COG3048 155 RAFFSQYSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 242 FVDDENSPQLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLL 321
Cdd:COG3048 235 FVDDENSRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 322 GVYTGLHDQVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGM 401
Cdd:COG3048 315 GLATGLHDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGP 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490435089 402 VCVLRDA--AYLDRIGVTpARFARATHLVWGTGGSMVPDSEFAAHVDKGRAL 451
Cdd:COG3048 395 LRLLGSAgqAYLERHGLT-EKMANATHLVWATGGSMVPEEEMEAYLAKGKAL 445
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
5-452 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 775.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 5 KSLEAWCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVP 84
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 85 LPKLQRRLLEEAGKtgeaqlPAAGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAF 164
Cdd:PRK02991 81 IPAMQKALEKEYGQ------PISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 165 FGRHRIAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVD 244
Cdd:PRK02991 155 FSQYSIAVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 245 DENSPQLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVY 324
Cdd:PRK02991 235 DENSRTLFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 325 TGLHDQVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCV 404
Cdd:PRK02991 315 TGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRV 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 490435089 405 LRDAAYLDRIGVTPaRFARATHLVWGTGGSMVPDSEFAAHVDKGRALQ 452
Cdd:PRK02991 395 CASVAYLQRHGLSE-QLKNATHLVWATGGSMVPEEEMEQYLAKGRALL 441
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
10-444 |
0e+00 |
|
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a pyridoxal-phosphate enzyme that converts D-serine to pyruvate and NH3. This enzyme is also called D-serine dehydratase and D-serine deaminase and was previously designated EC 4.2.1.14. It is homologous to an enzyme that acts on threonine and may itself act weakly on threonine. [Energy metabolism, Amino acids and amines]
Pssm-ID: 211710 Cd Length: 431 Bit Score: 652.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 10 WCASHPLIRDLVALRETSWFNPGIAPAATALADVGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVPLPKLQ 89
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 90 RRLLEEAgktgeaQLPAAGALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAFFGRHR 169
Cdd:TIGR02035 81 KRLEKEY------QQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 170 IAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSP 249
Cdd:TIGR02035 155 IAVGSTGNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 250 QLFLGYAVAAERLAGQLQRAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVYTGLHD 329
Cdd:TIGR02035 235 TLFLGYAVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 330 QVSVQDFGIDNVTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLR-DA 408
Cdd:TIGR02035 315 QISVQDIGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCAsEV 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 490435089 409 AYLDRIGVTPARFARATHLVWGTGGSMVPDSEFAAH 444
Cdd:TIGR02035 395 SYRYMHGFSAEQLRNATHLVWATGGGMVPEEEMNAY 430
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
28-438 |
0e+00 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 637.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 28 WFNPGIAPAATALAdvGLGADDVADASARLQRFAPYIAKVFPETAAAGGIIESDIVPLPKLQRRLLEEAGKtgeaqlPAA 107
Cdd:cd06447 3 WKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQ------PIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 108 GALWLKTDNALPISGSIKARGGIHEVLWHAERLALQAGLIREGDDYAALASDSAHAFFGRHRIAVGSTGNLGLSIGIMSA 187
Cdd:cd06447 75 GRLLLKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 188 KLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSPQLFLGYAVAAERLAGQLQ 267
Cdd:cd06447 155 ALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 268 RAGVRVDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDAVHCIFAEPTHSPCMLLGVYTGLHDQVSVQDFGIDNVTAADGL 347
Cdd:cd06447 235 ELGIKVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 348 AVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLRDAAYlDRIGVTPARFARATHL 427
Cdd:cd06447 315 AVGRPSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEG-KRYVRLGYRMENATHI 393
|
410
....*....|.
gi 490435089 428 VWGTGGSMVPD 438
Cdd:cd06447 394 VWATGGSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
108-406 |
1.49e-30 |
|
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: 119.72 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 108 GALWLKTDNALPiSGSIKARGGIHEVLWHAERlalqagliregddyaalasdsahafFGRHRIAVGSTGNLGLSIGIMSA 187
Cdd:pfam00291 22 VDVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------------EGGKTVVEASSGNHGRALAAAAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 188 KLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSPQLFLGYAVAAERLAGQLq 267
Cdd:pfam00291 76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 268 raGVRVDAehplfVYLPCGVGGGPGGVAFGLKRVFGDaVHCIFAEPTHSPCMLLGVYTGLHDQVSVQDfgidnvTAADGL 347
Cdd:pfam00291 155 --GGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPALARSLAAGRPVPVPVAD------TIADGL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 348 AVGR-PSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVCVLR 406
Cdd:pfam00291 221 GVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALA 280
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
110-433 |
2.96e-25 |
|
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: 103.75 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 110 LWLKTDNALPiSGSIKARGGIHEVLwhaerLALQAGLIREGddyaalasdsahaffgrhRIAVGSTGNLGLSIGIMSAKL 189
Cdd:cd00640 17 IYLKLEFLNP-TGSFKDRGALNLIL-----LAEEEGKLPKG------------------VIIESTGGNTGIALAAAAARL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 190 GFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPACHFVDDENSPQLFLGYAVAAERLAGQLqra 269
Cdd:cd00640 73 GLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 270 gvrvDAEHPLFVYLPCGVGGGPGGVAFGLKRVFGDaVHCIFAEPthspcmllgvytglhdqvsvqdfgidnvtaadglav 349
Cdd:cd00640 150 ----GGQKPDAVVVPVGGGGNIAGIARALKELLPN-VKVIGVEP------------------------------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 350 grpsgfvgkamqrlidGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMVcvlrdaAYLDRIGvtparfARATHLVW 429
Cdd:cd00640 189 ----------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAAL------KLAKKLG------KGKTVVVI 240
|
....
gi 490435089 430 GTGG 433
Cdd:cd00640 241 LTGG 244
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
108-398 |
1.02e-12 |
|
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: 68.91 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 108 GALWLKTDNALPIsGSIKARGGIHEVLWHAERlALQAGLIregddyAAlasdsahaffgrhriavgSTGNLGLSIGIMSA 187
Cdd:COG1171 39 AEVYLKLENLQPT-GSFKLRGAYNALASLSEE-ERARGVV------AA------------------SAGNHAQGVAYAAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 188 KLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPAcHFVDDENSPQLFLGYAVAAERLAGQLQ 267
Cdd:COG1171 93 LLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGA-TFVHPFDDPDVIAGQGTIALEILEQLP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 268 ragvRVDAehplfVYLPCgvgggpggvafG-----------LKRVfGDAVHCIFAEPTHSPCMLLGVYTGLHDQVSVQDf 336
Cdd:COG1171 172 ----DLDA-----VFVPV-----------GgggliagvaaaLKAL-SPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVD- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490435089 337 gidnvTAADGLAVGRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGV 398
Cdd:COG1171 230 -----TIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL 286
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
110-401 |
1.44e-10 |
|
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: 62.12 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 110 LWLKTDNaLPISGSIKARGGIHEvLWHAERLALQAGLIregddyAAlasdsahaffgrhriavgSTGNLGLSIGIMSAKL 189
Cdd:cd01562 34 VYLKCEN-LQKTGSFKIRGAYNK-LLSLSEEERAKGVV------AA------------------SAGNHAQGVAYAAKLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 190 GFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRrEAASDPACHFVDDENSPQLFLGYAVAAERLAGQLQRa 269
Cdd:cd01562 88 GIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKAR-ELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQVPD- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 270 gvrVDAehplfVYLPCGVGGGPGGVAFGLKRVFGDaVHCIFAEPTHSPCMLLGVYTGlhdqvSVQDFGIDNvTAADGLAV 349
Cdd:cd01562 166 ---LDA-----VFVPVGGGGLIAGIATAVKALSPN-TKVIGVEPEGAPAMAQSLAAG-----KPVTLPEVD-TIADGLAV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490435089 350 GRPSGFVGKAMQRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGM 401
Cdd:cd01562 231 KRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAAL 282
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
170-409 |
1.64e-05 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 46.61 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 170 IAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDySVAVEQGRREAASDPACHFVDDENSP 249
Cdd:PRK06815 71 VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGD-ALNAELAARRAAEQQGKVYISPYNDP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 250 QLFLGYAVAAERLAGQLQragvRVDAehplfVYLPCGVGGGPGGVAFGLKRVfGDAVHCIFAEPTHSPCMLLGVYTGLHD 329
Cdd:PRK06815 150 QVIAGQGTIGMELVEQQP----DLDA-----VFVAVGGGGLISGIATYLKTL-SPKTEIIGCWPANSPSLYTSLEAGEIV 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 330 QVSVQDfgidnvTAADGLAVGRPSGFVGKAM-QRLIDGYYTVSDEALFRLLALAHDDEGLRLEPSALAGVPGMvcvLRDA 408
Cdd:PRK06815 220 EVAEQP------TLSDGTAGGVEPGAITFPLcQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAA---LKLA 290
|
.
gi 490435089 409 A 409
Cdd:PRK06815 291 P 291
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
101-246 |
3.89e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 45.33 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 101 EAQLPAAGALWLKTDNaLPISGSIKARGGIHEVLWHAERLAlqagliregddyaalasdsahaffgrhRIAVGSTGNLGL 180
Cdd:PRK08246 30 DGAGFGPAPVWLKLEH-LQHTGSFKARGAFNRLLAAPVPAA---------------------------GVVAASGGNAGL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490435089 181 SIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDPA--CHFVDDE 246
Cdd:PRK08246 82 AVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGAllCHAYDQP 149
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
111-243 |
1.28e-03 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 40.75 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 111 WLKTDNALPIsGSIKARGGIHEVLWHAERLALQAGLIregddyaalasdSAhaffgrhriavgSTGNLGLSIGIMSAKLG 190
Cdd:PRK06110 39 WVKHENHTPT-GAFKVRGGLVYFDRLARRGPRVRGVI------------SA------------TRGNHGQSVAFAARRHG 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490435089 191 FQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRREAASDpACHFV 243
Cdd:PRK06110 94 LAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAER-GLHMV 145
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
82-398 |
1.43e-03 |
|
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: 40.65 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 82 IVPLPKLQRRLLeeagktgeaqlpaAGALWLKTDNALPiSGSIKARGgihevlwhaerlalqagliregddyAALASDSA 161
Cdd:cd01563 25 LVRAPRLGERLG-------------GKNLYVKDEGLNP-TGSFKDRG-------------------------MTVAVSKA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 162 HAFfGRHRIAVGSTGNLGLSIGIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRrEAASDPACH 241
Cdd:cd01563 66 KEL-GVKAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVR-ELAEENWIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 242 FVDDENSpqLFL-GYAVAAERLAGQLqragvrvDAEHPLFVYLPCGVGGGPGGVAFGLK------------RVFGdavhc 308
Cdd:cd01563 144 LSNSLNP--YRLeGQKTIAFEIAEQL-------GWEVPDYVVVPVGNGGNITAIWKGFKelkelglidrlpRMVG----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 309 ifAEPTHSPCMLLGVYTGLHDQVSVQDFGidnvTAADGLAVGRP-SGFVGKAMQRLIDGYY-TVSDEALFRLLALAHDDE 386
Cdd:cd01563 210 --VQAEGAAPIVRAFKEGKDDIEPVENPE----TIATAIRIGNPaSGPKALRAVRESGGTAvAVSDEEILEAQKLLARTE 283
|
330
....*....|....*
gi 490435089 387 GLRLEPS---ALAGV 398
Cdd:cd01563 284 GIFVEPAsaaSLAGL 298
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
104-275 |
3.59e-03 |
|
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: 39.20 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 104 LPAAGA-LWLKTDNALPiSGSIKARGgihevLWHAERLALQAGLiregddyaalaSDSAHAFfgrhriaVGSTGNLGLSI 182
Cdd:cd06448 11 SKTAGCnVFLKLENLQP-SGSFKIRG-----IGHLCQKSAKQGL-----------NECVHVV-------CSSGGNAGLAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490435089 183 GIMSAKLGFQATVHMSADARQWKKDRLRASGVTVVEHASDYSVAVEQGRRE-AASDPACHFVDDENSPQLFLGYAVAAER 261
Cdd:cd06448 67 AYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElAENDPGPVYVHPFDDPLIWEGHSSMVDE 146
|
170
....*....|....
gi 490435089 262 LAGQLQrAGVRVDA 275
Cdd:cd06448 147 IAQQLQ-SQEKVDA 159
|
|
| |
