|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
5-450 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 786.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 5 IYGKPLDAWLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESP 84
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 85 LIEVPLFADALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRK 164
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 165 HSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDEN 244
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 245 STTLFLGYAVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGL 324
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 325 HEKLAVQDFGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKE 404
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1431888003 405 A-RGYRARMALDDaAMRNATHVIWATGGGMVPEAQMSVYLQTGRAAL 450
Cdd:COG3048 401 AgQAYLERHGLTE-KMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
8-450 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 744.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 8 KPLDAWLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIE 87
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 88 VPLFADALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSI 167
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 168 AVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTT 247
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 248 LFLGYAVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEK 327
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 328 LAVQDFGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEArG 407
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASV-A 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1431888003 408 YRARMALDDaAMRNATHVIWATGGGMVPEAQMSVYLQTGRAAL 450
Cdd:PRK02991 400 YLQRHGLSE-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 ... |
13-443 |
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: 650.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 13 WLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIEVPLFA 92
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 93 DALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSIAVGST 172
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 173 GNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTTLFLGY 252
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 253 AVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEKLAVQD 332
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 333 FGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEARGYRARM 412
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASEVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|.
gi 1431888003 413 ALDDAAMRNATHVIWATGGGMVPEAQMSVYL 443
Cdd:TIGR02035 401 GFSAEQLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
31-436 |
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: 620.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 31 WFNPAVAPLVDAMDdiPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIEVPLFADALSRRYKVEAPRRLLLK 110
Cdd:cd06447 3 WKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 111 QDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSIAVGSTGNLGTSIGIASATLGFTT 190
Cdd:cd06447 81 ADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 191 TVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTTLFLGYAVAGERLKRQLDLANVPV 270
Cdd:cd06447 161 TVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 271 DAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEKLAVQDFGIDNLTAADGLAVGRPS 350
Cdd:cd06447 241 DAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 351 GFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEARGYraRMALDDAAMRNATHVIWATG 430
Cdd:cd06447 321 GLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGK--RYVRLGYRMENATHIVWATG 398
|
....*.
gi 1431888003 431 GGMVPE 436
Cdd:cd06447 399 GSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
79-395 |
2.36e-34 |
|
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: 130.12 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 79 GVIESPLIEVPlfadALSRRYKVeaprRLLLKQDSHLPvSGSIKARGGIYEVLFHAEQLAIRHgllnegddyrmlatdac 158
Cdd:pfam00291 4 GIGPTPLVRLP----RLSKELGV----DVYLKLESLNP-TGSFKDRGALNLLLRLKEGEGGKT----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 159 ralfrkhsIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCH 238
Cdd:pfam00291 58 --------VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 239 FVDDENSTTLFLGYAVAGERLKRQLdlaNVPVDAghplfVYLPCGVGGGPGGVAFGLKLAFGDaVHCVFAEPTHSPCMLM 318
Cdd:pfam00291 130 YINQYDNPLNIEGYGTIGLEILEQL---GGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPALAR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 319 GVLTGLHEKLAVQDfgidnlTAADGLAVGR-PSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPS---ALAG 394
Cdd:pfam00291 201 SLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSsaaALAA 274
|
.
gi 1431888003 395 A 395
Cdd:pfam00291 275 L 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
5-450 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 786.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 5 IYGKPLDAWLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESP 84
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 85 LIEVPLFADALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRK 164
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 165 HSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDEN 244
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 245 STTLFLGYAVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGL 324
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 325 HEKLAVQDFGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKE 404
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1431888003 405 A-RGYRARMALDDaAMRNATHVIWATGGGMVPEAQMSVYLQTGRAAL 450
Cdd:COG3048 401 AgQAYLERHGLTE-KMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
8-450 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 744.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 8 KPLDAWLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIE 87
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 88 VPLFADALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSI 167
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 168 AVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTT 247
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 248 LFLGYAVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEK 327
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 328 LAVQDFGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEArG 407
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASV-A 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1431888003 408 YRARMALDDaAMRNATHVIWATGGGMVPEAQMSVYLQTGRAAL 450
Cdd:PRK02991 400 YLQRHGLSE-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 ... |
13-443 |
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: 650.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 13 WLRDYPLLRPLMELQPVEWFNPAVAPLVDAMDDIPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIEVPLFA 92
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 93 DALSRRYKVEAPRRLLLKQDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSIAVGST 172
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 173 GNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTTLFLGY 252
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 253 AVAGERLKRQLDLANVPVDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEKLAVQD 332
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 333 FGIDNLTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEARGYRARM 412
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASEVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|.
gi 1431888003 413 ALDDAAMRNATHVIWATGGGMVPEAQMSVYL 443
Cdd:TIGR02035 401 GFSAEQLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
31-436 |
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: 620.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 31 WFNPAVAPLVDAMDdiPLDASDVADASARLQRFAPLLAQTFDDVREAGGVIESPLIEVPLFADALSRRYKVEAPRRLLLK 110
Cdd:cd06447 3 WKNPNYGKPAEALA--PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 111 QDSHLPVSGSIKARGGIYEVLFHAEQLAIRHGLLNEGDDYRMLATDACRALFRKHSIAVGSTGNLGTSIGIASATLGFTT 190
Cdd:cd06447 81 ADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 191 TVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDDENSTTLFLGYAVAGERLKRQLDLANVPV 270
Cdd:cd06447 161 TVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 271 DAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDAVHCVFAEPTHSPCMLMGVLTGLHEKLAVQDFGIDNLTAADGLAVGRPS 350
Cdd:cd06447 241 DAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 351 GFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPSALAGAPGFARVSKEARGYraRMALDDAAMRNATHVIWATG 430
Cdd:cd06447 321 GLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGK--RYVRLGYRMENATHIVWATG 398
|
....*.
gi 1431888003 431 GGMVPE 436
Cdd:cd06447 399 GSMVPE 404
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
79-395 |
2.36e-34 |
|
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: 130.12 E-value: 2.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 79 GVIESPLIEVPlfadALSRRYKVeaprRLLLKQDSHLPvSGSIKARGGIYEVLFHAEQLAIRHgllnegddyrmlatdac 158
Cdd:pfam00291 4 GIGPTPLVRLP----RLSKELGV----DVYLKLESLNP-TGSFKDRGALNLLLRLKEGEGGKT----------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 159 ralfrkhsIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCH 238
Cdd:pfam00291 58 --------VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 239 FVDDENSTTLFLGYAVAGERLKRQLdlaNVPVDAghplfVYLPCGVGGGPGGVAFGLKLAFGDaVHCVFAEPTHSPCMLM 318
Cdd:pfam00291 130 YINQYDNPLNIEGYGTIGLEILEQL---GGDPDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPALAR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 319 GVLTGLHEKLAVQDfgidnlTAADGLAVGR-PSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQAIRLEPS---ALAG 394
Cdd:pfam00291 201 SLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSsaaALAA 274
|
.
gi 1431888003 395 A 395
Cdd:pfam00291 275 L 275
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
83-431 |
4.30e-29 |
|
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: 114.15 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 83 SPLIEvplfADALSRRYKVeaprRLLLKQDSHLPvSGSIKARGGIYEVLFHAEQLAIRHGLlnegddyrmlatdacralf 162
Cdd:cd00640 1 TPLVR----LKRLSKLGGA----NIYLKLEFLNP-TGSFKDRGALNLILLAEEEGKLPKGV------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 163 rkhsIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLCHFVDD 242
Cdd:cd00640 53 ----IIESTGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 243 ENSTTLFLGYAVAGERLKRQLdlanvpvDAGHPLFVYLPCGVGGGPGGVAFGLKLAFGDaVHCVFAEPthspcmlmgvlt 322
Cdd:cd00640 129 FDNPANIAGQGTIGLEILEQL-------GGQKPDAVVVPVGGGGNIAGIARALKELLPN-VKVIGVEP------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 323 glheklavqdfgidnltaadglavgrpsgfvgramqrmidGYYTIDDRELYALLALMADTQAIRLEPS---ALAGApgfa 399
Cdd:cd00640 189 ----------------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSsaaALAAA---- 224
|
330 340 350
....*....|....*....|....*....|..
gi 1431888003 400 rvskeargyrarMALDDAAMRNATHVIWATGG 431
Cdd:cd00640 225 ------------LKLAKKLGKGKTVVVILTGG 244
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
71-399 |
2.46e-16 |
|
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: 79.45 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 71 FDDVREA-----GGVIESPLIEvplfADALSRRYKVEaprrLLLKQDSHLPVsGSIKARGGIYevlfhaeqlAIRHgLLN 145
Cdd:cd01562 1 LEDILAAaarikPVVRRTPLLT----SPTLSELLGAE----VYLKCENLQKT-GSFKIRGAYN---------KLLS-LSE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 146 EGddyrmlatdacralfRKHSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIE 225
Cdd:cd01562 62 EE---------------RAKGVVAASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 226 SGRRLASND--PLCHFVDDENsttLFLGYAVAGERLKRQLDlanvPVDAghplfVYLPCGVGGGPGGVAFGLKlAFGDAV 303
Cdd:cd01562 127 KARELAEEEglTFIHPFDDPD---VIAGQGTIGLEILEQVP----DLDA-----VFVPVGGGGLIAGIATAVK-ALSPNT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 304 HCVFAEPTHSPCMLMGVLTGLHEKLAVQDfgidnlTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQ 383
Cdd:cd01562 194 KVIGVEPEGAPAMAQSLAAGKPVTLPEVD------TIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFERE 267
|
330
....*....|....*.
gi 1431888003 384 AIRLEPsalAGAPGFA 399
Cdd:cd01562 268 KLVAEP---AGALALA 280
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
70-399 |
1.20e-13 |
|
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: 71.61 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 70 TFDDVREA-----GGVIESPLIEVPlfadALSRRYKveapRRLLLKQDSHLPVsGSIKARGGIYevlfhaeqlAIRHglL 144
Cdd:COG1171 7 TLADIEAAaariaGVVRRTPLLRSP----TLSERLG----AEVYLKLENLQPT-GSFKLRGAYN---------ALAS--L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 145 NEGDdyrmlatdacralfRKHSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAI 224
Cdd:COG1171 67 SEEE--------------RARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 225 ESGRRLASNDPLcHFVDDENSTTLFLGYAVAGERLKRQLDlanvPVDAghplfVYLPCGVGGGPGGVAFGLKlAFGDAVH 304
Cdd:COG1171 133 AAAAELAEEEGA-TFVHPFDDPDVIAGQGTIALEILEQLP----DLDA-----VFVPVGGGGLIAGVAAALK-ALSPDIR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 305 CVFAEPTHSPCMLMGVLTGLHEKLAVQDfgidnlTAADGLAVGRPSGFVGRAMQRMIDGYYTIDDRELYALLALMADTQA 384
Cdd:COG1171 202 VIGVEPEGAAAMYRSLAAGEPVTLPGVD------TIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTK 275
|
330
....*....|....*
gi 1431888003 385 IRLEPsalAGAPGFA 399
Cdd:COG1171 276 IVVEP---AGAAALA 287
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
69-410 |
2.37e-10 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 61.63 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 69 QTFDDVREAGGVIESPLIEVPL-FADALSRRYKVEAprrlLLKQDsHLPVSGSIKARGGIYEV-LFHAEQlairhgllne 146
Cdd:PRK06815 2 TLFDAILEAHQRLRPQVRVTPLeHSPLLSQHTGCEV----YLKCE-HLQHTGSFKFRGASNKLrLLNEAQ---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 147 gddyrmlatdacralfRKHSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIES 226
Cdd:PRK06815 67 ----------------RQQGVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 227 GRRLASNDPLChFVDDENSTTLFLGYAVAGERLKRQ---LDLANVPVDAGhplfvylpcgvgGGPGGVAFGLKlAFGDAV 303
Cdd:PRK06815 131 ARRAAEQQGKV-YISPYNDPQVIAGQGTIGMELVEQqpdLDAVFVAVGGG------------GLISGIATYLK-TLSPKT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 304 HCVFAEPTHSPCMLMGVLTGLHEKLAVQDfgidnlTAADGLAVGRPSGFVGRAM-QRMIDGYYTIDDRELYALLALMADT 382
Cdd:PRK06815 197 EIIGCWPANSPSLYTSLEAGEIVEVAEQP------TLSDGTAGGVEPGAITFPLcQQLIDQKVLVSEEEIKEAMRLIAET 270
|
330 340
....*....|....*....|....*...
gi 1431888003 383 QAIRLEPSALAGAPGFARVSKEARGYRA 410
Cdd:PRK06815 271 DRWLIEGAAGVALAAALKLAPRYQGKKV 298
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
62-235 |
1.22e-07 |
|
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: 53.37 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 62 RFAPLLAQTFDDVREAG-GVieSPLIEvplfADALSRRYKVEaprRLLLKQDSHLPvSGSIKARGgIYEVLFHAEQLAIR 140
Cdd:cd01563 3 RYRELLPVTEDDIVSLGeGN--TPLVR----APRLGERLGGK---NLYVKDEGLNP-TGSFKDRG-MTVAVSKAKELGVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 141 HgllnegddyrmlatdacralfrkhsIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDY 220
Cdd:cd01563 72 A-------------------------VACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNF 126
|
170
....*....|....*
gi 1431888003 221 GEAIESGRRLASNDP 235
Cdd:cd01563 127 DDALRLVRELAEENW 141
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
45-243 |
2.10e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 46.10 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 45 DIPLDASDVADASarlQRFAPLLAQTfddvreaggviesPLIEVPLFAdalsrrykvEAPRRLLLKQDsHLPVSGSIKAR 124
Cdd:PRK08246 2 HAMITRSDVRAAA---QRIAPHIRRT-------------PVLEADGAG---------FGPAPVWLKLE-HLQHTGSFKAR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 125 GGIYevlfhaeqlairhgllnegddyRMLATDAcralfRKHSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKD 204
Cdd:PRK08246 56 GAFN----------------------RLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1431888003 205 RLRAHGVTVIEYAGDYGEAIESGRRLASNDP--LCHFVDDE 243
Cdd:PRK08246 109 RLRALGAEVVVVGAEYADALEAAQAFAAETGalLCHAYDQP 149
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
109-240 |
6.55e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 41.52 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 109 LKQDSHLPVsGSIKARGGIyeVLFHAeqlairhgLLNEGDDYRMLATdACRalfrkhsiavgstGNLGTSIGIASATLGF 188
Cdd:PRK06110 40 VKHENHTPT-GAFKVRGGL--VYFDR--------LARRGPRVRGVIS-ATR-------------GNHGQSVAFAARRHGL 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1431888003 189 TTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLASNDPLcHFV 240
Cdd:PRK06110 95 AATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGL-HMV 145
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
60-395 |
9.70e-04 |
|
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: 41.34 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 60 LQRFAPLLAqtFDDVREA-----GGViesPLIEVPLFADALSRRykveaprrLLLKQDSHLPvSGSIKARGgiyevlfha 134
Cdd:COG0498 44 LWRYRELLP--FDDEEKAvslgeGGT---PLVKAPRLADELGKN--------LYVKEEGHNP-TGSFKDRA--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 135 EQLAIRHgLLNEGDDyrmlatdacralfrkhSIAVGSTGNLGTSIGIASATLGFTTTVHMSAD--ARQWKKdRLRAHGVT 212
Cdd:COG0498 101 MQVAVSL-ALERGAK----------------TIVCASSGNGSAALAAYAARAGIEVFVFVPEGkvSPGQLA-QMLTYGAH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 213 VIEYAGDYGEAIESGRRLASNDPLcHFVddeNSTTLF--LGYAVAG----ERLKRQLDLANVPV-DAGHPLFVYLpcgvg 285
Cdd:COG0498 163 VIAVDGNFDDAQRLVKELAADEGL-YAV---NSINPArlEGQKTYAfeiaEQLGRVPDWVVVPTgNGGNILAGYK----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 286 ggpggvAFGLKLAFGDAVHC---VFAEPTHSPCMLMGVLTGLHEKLAVQDfgidnLTAADGLAVGRPSGF--VGRAMQRM 360
Cdd:COG0498 234 ------AFKELKELGLIDRLprlIAVQATGCNPILTAFETGRDEYEPERP-----ETIAPSMDIGNPSNGerALFALRES 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 1431888003 361 IDGYYTIDDRELYALLALMADTQAIRLEPS---ALAGA 395
Cdd:COG0498 303 GGTAVAVSDEEILEAIRLLARREGIFVEPAtavAVAGL 340
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
84-235 |
1.62e-03 |
|
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: 40.19 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 84 PLIEVPLFADALsrrykveaPRRLLLKQDSHLPvSGSIKARGGIYEVLfHAEqlaiRHGLLNEGDdyrmlatdacralfr 163
Cdd:cd01561 4 PLVRLNRLSPGT--------GAEIYAKLEFFNP-GGSVKDRIALYMIE-DAE----KRGLLKPGT--------------- 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431888003 164 khSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVI----EYAGDYGEAIESGRRLASNDP 235
Cdd:cd01561 55 --TIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVIltpeAEADGMKGAIAKARELAAETP 128
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
82-231 |
1.64e-03 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 40.63 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 82 ESPLIEVPlfadALSRRYKVEAprrLLLKQDSHLPVSGSIKARGGIYEVlfhAEQLAIRHGLLNEGDDYRMLATDACRAL 161
Cdd:PRK08206 44 PTPLVALP----DLAAELGVGS---ILVKDESYRFGLNAFKALGGAYAV---ARLLAEKLGLDISELSFEELTSGEVREK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431888003 162 FRKHSIAVGSTGNLGTSIGIASATLGFTTTVHMSADARQWKKDRLRAHGVTVIEYAGDYGEAIESGRRLA 231
Cdd:PRK08206 114 LGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEA 183
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
167-231 |
6.43e-03 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 38.53 E-value: 6.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431888003 167 IAVGSTGNLGTSIGIASATLGFTTTVHMSadaRQWKKDR---LRAHGVTVIEYAGDYGEAIESGRRLA 231
Cdd:PRK06381 66 ITVGTCGNYGASIAYFARLYGLKAVIFIP---RSYSNSRvkeMEKYGAEIIYVDGKYEEAVERSRKFA 130
|
|
| |
