|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 905.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 1 MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESE 80
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 81 LVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQ 160
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 161 YSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDEN 240
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 241 SRTLFLGYSVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGL 320
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 321 HDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCAS 400
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15832499 401 V--SYQQMHGFSaEQLRNATHLVWATGGGMVPEEEMEQYLAKGR 442
Cdd:COG3048 401 AgqAYLERHGLT-EKMANATHLVWATGGSMVPEEEMEAYLAKGK 443
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
6-442 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 893.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 6 MNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIP 85
Cdd:PRK02991 3 INKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVAIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 86 AMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAV 165
Cdd:PRK02991 83 AMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSIAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 166 GSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLF 245
Cdd:PRK02991 163 GSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 246 LGYSVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQIS 325
Cdd:PRK02991 243 LGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 326 VQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQ 405
Cdd:PRK02991 323 VQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASVAYLQ 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 15832499 406 MHGFSaEQLRNATHLVWATGGGMVPEEEMEQYLAKGR 442
Cdd:PRK02991 403 RHGLS-EQLKNATHLVWATGGSMVPEEEMEQYLAKGR 438
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
9-438 |
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: 809.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 9 LIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQ 88
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 89 KRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAVGST 168
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 169 GNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGY 248
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 249 SVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQD 328
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 329 IGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCAS-VSYQQMH 407
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASeVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|.
gi 15832499 408 GFSAEQLRNATHLVWATGGGMVPEEEMEQYL 438
Cdd:TIGR02035 401 GFSAEQLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
25-431 |
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: 734.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 25 TTWFNPGTTSLAEGLPyvGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLL 104
Cdd:cd06447 1 IFWKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 105 LKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGF 184
Cdd:cd06447 79 LKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 185 KVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAEQGR 264
Cdd:cd06447 159 KVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 265 IVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGR 344
Cdd:cd06447 239 KVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 345 ASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHgFSAEQLRNATHLVWAT 424
Cdd:cd06447 319 PSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKRYV-RLGYRMENATHIVWAT 397
|
....*..
gi 15832499 425 GGGMVPE 431
Cdd:cd06447 398 GGSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
73-393 |
1.37e-41 |
|
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: 149.38 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 73 TGGIIESELVAIPamqkRLEKEYQQPIsgqlLLKKDSHLPiSGSIKARGGIYEVLAHAEKlaleaglltleddyskllsp 152
Cdd:pfam00291 2 SLGIGPTPLVRLP----RLSKELGVDV----YLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 153 efkqfFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPN 232
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 233 CFFIDDENSRTLFLGYSVAGQRLKAQfaeQGRIVDAdnplfVYLPCGVGGGPGGVAFGLKLAFGDhVHCFFAEPTHSPCM 312
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQ---LGGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 313 LLGVHTGLHDQISVQDigidnlTAADGLAVGRASG-FVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGM 391
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDEPGaLALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
..
gi 15832499 392 AG 393
Cdd:pfam00291 273 AA 274
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 905.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 1 MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESE 80
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 81 LVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQ 160
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 161 YSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDEN 240
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 241 SRTLFLGYSVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGL 320
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 321 HDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCAS 400
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15832499 401 V--SYQQMHGFSaEQLRNATHLVWATGGGMVPEEEMEQYLAKGR 442
Cdd:COG3048 401 AgqAYLERHGLT-EKMANATHLVWATGGSMVPEEEMEAYLAKGK 443
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
6-442 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 893.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 6 MNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIP 85
Cdd:PRK02991 3 INKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVAIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 86 AMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAV 165
Cdd:PRK02991 83 AMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSIAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 166 GSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLF 245
Cdd:PRK02991 163 GSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 246 LGYSVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQIS 325
Cdd:PRK02991 243 LGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQIS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 326 VQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQ 405
Cdd:PRK02991 323 VQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASVAYLQ 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 15832499 406 MHGFSaEQLRNATHLVWATGGGMVPEEEMEQYLAKGR 442
Cdd:PRK02991 403 RHGLS-EQLKNATHLVWATGGSMVPEEEMEQYLAKGR 438
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
9-438 |
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: 809.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 9 LIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQ 88
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 89 KRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAVGST 168
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 169 GNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGY 248
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 249 SVAGQRLKAQFAEQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQD 328
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 329 IGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCAS-VSYQQMH 407
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASeVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|.
gi 15832499 408 GFSAEQLRNATHLVWATGGGMVPEEEMEQYL 438
Cdd:TIGR02035 401 GFSAEQLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
25-431 |
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: 734.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 25 TTWFNPGTTSLAEGLPyvGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLL 104
Cdd:cd06447 1 IFWKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 105 LKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLEDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGF 184
Cdd:cd06447 79 LKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 185 KVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAEQGR 264
Cdd:cd06447 159 KVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 265 IVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGR 344
Cdd:cd06447 239 KVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 345 ASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHgFSAEQLRNATHLVWAT 424
Cdd:cd06447 319 PSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKRYV-RLGYRMENATHIVWAT 397
|
....*..
gi 15832499 425 GGGMVPE 431
Cdd:cd06447 398 GGSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
73-393 |
1.37e-41 |
|
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: 149.38 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 73 TGGIIESELVAIPamqkRLEKEYQQPIsgqlLLKKDSHLPiSGSIKARGGIYEVLAHAEKlaleaglltleddyskllsp 152
Cdd:pfam00291 2 SLGIGPTPLVRLP----RLSKELGVDV----YLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 153 efkqfFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPN 232
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 233 CFFIDDENSRTLFLGYSVAGQRLKAQfaeQGRIVDAdnplfVYLPCGVGGGPGGVAFGLKLAFGDhVHCFFAEPTHSPCM 312
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQ---LGGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 313 LLGVHTGLHDQISVQDigidnlTAADGLAVGRASG-FVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGM 391
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDEPGaLALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
..
gi 15832499 392 AG 393
Cdd:pfam00291 273 AA 274
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
89-426 |
1.47e-32 |
|
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: 123.39 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 89 KRLEKEYqqpiSGQLLLKKDSHLPiSGSIKARGGIYEVLAHAEKLALEAGLltleddyskllspefkqffsqysIAVGST 168
Cdd:cd00640 7 KRLSKLG----GANIYLKLEFLNP-TGSFKDRGALNLILLAEEEGKLPKGV-----------------------IIESTG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 169 GNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGY 248
Cdd:cd00640 59 GNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 249 SVAGQRLKAQFAEQgrivdadNPLFVYLPCGVGGGPGGVAFGLKlAFGDHVHCFFAEPthspcmllgvhtglhdqisvqd 328
Cdd:cd00640 139 GTIGLEILEQLGGQ-------KPDAVVVPVGGGGNIAGIARALK-ELLPNVKVIGVEP---------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 329 igidnltaadglavgrasgfvgramerlldGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCasvsyqqmhg 408
Cdd:cd00640 189 ------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA---------- 228
|
330
....*....|....*...
gi 15832499 409 fsAEQLRNATHLVWATGG 426
Cdd:cd00640 229 --KKLGKGKTVVVILTGG 244
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
47-402 |
3.35e-13 |
|
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: 69.82 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 47 QDVQDAHARLSrfapylakafpetaatGGIIESELVAIPAMQKRLEKEyqqpisgqLLLKKDsHLPISGSIKARGGiYEV 126
Cdd:cd01562 2 EDILAAAARIK----------------PVVRRTPLLTSPTLSELLGAE--------VYLKCE-NLQKTGSFKIRGA-YNK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 127 LAHAEKLALEAGLltleddyskllspefkqffsqysIAVgSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHG 206
Cdd:cd01562 56 LLSLSEEERAKGV-----------------------VAA-SAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYG 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 207 VTVVEYEQDYGVAVEEGRKAAQsDPNCFFI---DDEnsrtlflgYSVAGQRLKA-QFAEQGRIVDAdnplfVYLPCGVGG 282
Cdd:cd01562 112 AEVVLYGEDFDEAEAKARELAE-EEGLTFIhpfDDP--------DVIAGQGTIGlEILEQVPDLDA-----VFVPVGGGG 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 283 GPGGVAFGLKlAFGDHVHCFFAEPTHSPCMLLGVHTGlhdqiSVQDIGIDNlTAADGLAVGRASGFVGRAMERLLDGFYT 362
Cdd:cd01562 178 LIAGIATAVK-ALSPNTKVIGVEPEGAPAMAQSLAAG-----KPVTLPEVD-TIADGLAVKRPGELTFEIIRKLVDDVVT 250
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15832499 363 LSDQTMYDMLGWLAQEEGIRLEPSALAGMAG---------PQRVCASVS 402
Cdd:cd01562 251 VSEDEIAAAMLLLFEREKLVAEPAGALALAAllsgkldlkGKKVVVVLS 299
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
44-393 |
3.13e-11 |
|
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: 64.29 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 44 LTEQDVQDAHARLSRFapylakafpetaatggIIESELVAIPAMQKRLEkeyqqpisGQLLLKKDSHLPIsGSIKARGGI 123
Cdd:COG1171 6 PTLADIEAAAARIAGV----------------VRRTPLLRSPTLSERLG--------AEVYLKLENLQPT-GSFKLRGAY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 124 YEVLAHAEKlALEAGLltleddyskllspefkqffsqysIAVgSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLR 203
Cdd:COG1171 61 NALASLSEE-ERARGV-----------------------VAA-SAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 204 SHGVTVVEYEQDYGVAVEEGRKAAQsDPNCFFIDDENSRTLFLGYSVAGqrlkAQFAEQGRIVDAdnplfVYLPCGVGGG 283
Cdd:COG1171 116 AYGAEVVLHGDTYDDAEAAAAELAE-EEGATFVHPFDDPDVIAGQGTIA----LEILEQLPDLDA-----VFVPVGGGGL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 284 PGGVAFGLKlAFGDHVHCFFAEPTHSPCMLLGVHTGlhdQIsVQDIGIDnlTAADGLAVGRASGFVGRAMERLLDGFYTL 363
Cdd:COG1171 186 IAGVAAALK-ALSPDIRVIGVEPEGAAAMYRSLAAG---EP-VTLPGVD--TIADGLAVGRPGELTFEILRDLVDDIVTV 258
|
330 340 350
....*....|....*....|....*....|
gi 15832499 364 SDQTMYDMLGWLAQEEGIRLEPSALAGMAG 393
Cdd:COG1171 259 SEDEIAAAMRLLLERTKIVVEPAGAAALAA 288
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
163-393 |
9.73e-09 |
|
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: 56.45 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 163 IAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDP-------NCFF 235
Cdd:cd01563 73 VACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWiylsnslNPYR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 236 IddENSRTlfLGYSVAGQrlkaqfaeqgriVDADNPLFVYLPCGVGGGPGGVAFGLK----LAFGDHVHCFFA-EPTHSP 310
Cdd:cd01563 153 L--EGQKT--IAFEIAEQ------------LGWEVPDYVVVPVGNGGNITAIWKGFKelkeLGLIDRLPRMVGvQAEGAA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 311 CMLLGVHTGLHDQISVQDIgidnLTAADGLAVGR-ASGF-VGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSAL 388
Cdd:cd01563 217 PIVRAFKEGKDDIEPVENP----ETIATAIRIGNpASGPkALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASA 292
|
....*
gi 15832499 389 AGMAG 393
Cdd:cd01563 293 ASLAG 297
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
101-228 |
8.62e-06 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 47.38 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 101 GQLLLKKDsHLPISGSIKARGGiyevlahAEKLaleaglltleddysKLLSPEFKQffsqYSIAVGSTGNLGLSIGIMSA 180
Cdd:PRK06815 35 CEVYLKCE-HLQHTGSFKFRGA-------SNKL--------------RLLNEAQRQ----QGVITASSGNHGQGVALAAK 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15832499 181 RIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQ 228
Cdd:PRK06815 89 LAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAE 136
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
89-393 |
6.49e-05 |
|
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: 44.81 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 89 KRLEKEyqqpISGQLLLKKDSHLPiSGSIKARGgiYEVLAHaekLALEAGLLTleddyskllspefkqffsqysIAVGST 168
Cdd:COG0498 73 PRLADE----LGKNLYVKEEGHNP-TGSFKDRA--MQVAVS---LALERGAKT---------------------IVCASS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 169 GNLGLSIGIMSARIGFKVTVHMSAD--ARAwKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQsDPNCFFiddENSRTLF- 245
Cdd:COG0498 122 GNGSAALAAYAARAGIEVFVFVPEGkvSPG-QLAQMLTYGAHVIAVDGNFDDAQRLVKELAA-DEGLYA---VNSINPAr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 246 -LGYSVAGQRLKAQFAEQGRIV-----DADNPLFVYLpcgvgggpggvAFGLKLAFGDHVHC---FFAEPTHSPCMLLGV 316
Cdd:COG0498 197 lEGQKTYAFEIAEQLGRVPDWVvvptgNGGNILAGYK-----------AFKELKELGLIDRLprlIAVQATGCNPILTAF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 317 HTGlHDQISVQDigidNLTAADGLAVGRASGFvgramERLLD-------GFYTLSDQTMYDMLGWLAQEEGIRLEPSALA 389
Cdd:COG0498 266 ETG-RDEYEPER----PETIAPSMDIGNPSNG-----ERALFalresggTAVAVSDEEILEAIRLLARREGIFVEPATAV 335
|
....
gi 15832499 390 GMAG 393
Cdd:COG0498 336 AVAG 339
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
110-228 |
1.27e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 43.79 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832499 110 HLPISGSIKARGGIYEVLAHAEKlalEAGlltleddyskllspefkqffsqysIAVGSTGNLGLSIGIMSARIGFKVTVH 189
Cdd:PRK08246 45 HLQHTGSFKARGAFNRLLAAPVP---AAG------------------------VVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 15832499 190 MSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQ 228
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAA 136
|
|
| |
