|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
1-431 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 706.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 1 MNVDALIEKYPEVKTMQELKPFFWRNPDYGKKA----DLSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLID 76
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAeglpYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 77 LPYMKARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGI 156
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 157 AVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYD 236
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 237 LFLGYSVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDK 316
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 317 ISVYDIGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIM------DQS 390
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPvrvcasVAY 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 951374585 391 LENLSADFPMKNANHIVWATGGSMVPKEDMDRYLEIGREEL 431
Cdd:PRK02991 401 LQRHGLSEQLKNATHLVWATGGSMVPEEEMEQYLAKGRALL 441
|
|
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-431 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 682.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 1 MNVDALIEKYPEVKTMQELKPFFWRNPDYGKKAD----LSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLID 76
Cdd:COG3048 4 KTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEalpdVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESPLVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 77 LPYMKARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGI 156
Cdd:COG3048 84 IPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQYSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 157 AVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYD 236
Cdd:COG3048 164 AVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDENSRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 237 LFLGYSVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDK 316
Cdd:COG3048 244 LFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGLHDK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 317 ISVYDIGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSLENLSA 396
Cdd:COG3048 324 ISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGSAGQ 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 951374585 397 DF--------PMKNANHIVWATGGSMVPKEDMDRYLEIGREEL 431
Cdd:COG3048 404 AYlerhglteKMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
23-417 |
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: 662.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 23 FWRNPDYGKKADLS--IGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLIDLPYMKARLNKSFTNEIEGGLYLKA 100
Cdd:cd06447 2 FWKNPNYGKPAEALapLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLLKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 101 DNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGIAVGSTGNLGLSIGIVAQRLGFRTS 180
Cdd:cd06447 82 DSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFKVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 181 VHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYDLFLGYSVAALRLQAQLKSQGIKVD 260
Cdd:cd06447 162 VHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIKVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 261 KDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDKISVYDIGIDGTTKADGLAVGRASR 340
Cdd:cd06447 242 AEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRPSG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 341 IAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSLENLSAD------FPMKNANHIVWATGGSM 414
Cdd:cd06447 322 LVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKryvrlgYRMENATHIVWATGGSM 401
|
...
gi 951374585 415 VPK 417
Cdd:cd06447 402 VPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
6-424 |
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: 527.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 6 LIEKYPEVKTMQELKPFFWRNP----DYGKKADLSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLIDLPYMK 81
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPgttsLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 82 ARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGIAVGST 161
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 162 GNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYDLFLGY 241
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 242 SVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDKISVYD 321
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 322 IGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFT---------IMDQSLE 392
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAgpvrvcaseVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|..
gi 951374585 393 NLSADfPMKNANHIVWATGGSMVPKEDMDRYL 424
Cdd:TIGR02035 401 GFSAE-QLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
66-384 |
1.42e-38 |
|
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: 140.91 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 66 THGILESPLIDLPYMKARLNksftneieGGLYLKADNYLPiSGSIKSRGGIYEVLKFAEKvaiqeggliyednyavlask 145
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELG--------VDVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 146 kyhdlFAKYGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPM 225
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 226 TYFIDDEGSYDLFLGYSVAALRLQAQLksqGIKVDkdhplFVYLPAGVGGSPSGVTFGLKKvLGENAHAIFAEPTHIPSV 305
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQL---GGDPD-----AVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 306 TLGMVTGLNDKISVYDigidgtTKADGLAVGR-ASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGF 384
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
1-431 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 706.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 1 MNVDALIEKYPEVKTMQELKPFFWRNPDYGKKA----DLSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLID 76
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAeglpYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 77 LPYMKARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGI 156
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 157 AVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYD 236
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 237 LFLGYSVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDK 316
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 317 ISVYDIGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIM------DQS 390
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPvrvcasVAY 400
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 951374585 391 LENLSADFPMKNANHIVWATGGSMVPKEDMDRYLEIGREEL 431
Cdd:PRK02991 401 LQRHGLSEQLKNATHLVWATGGSMVPEEEMEQYLAKGRALL 441
|
|
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-431 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 682.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 1 MNVDALIEKYPEVKTMQELKPFFWRNPDYGKKAD----LSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLID 76
Cdd:COG3048 4 KTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEalpdVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESPLVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 77 LPYMKARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGI 156
Cdd:COG3048 84 IPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQYSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 157 AVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYD 236
Cdd:COG3048 164 AVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDENSRD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 237 LFLGYSVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDK 316
Cdd:COG3048 244 LFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGLHDK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 317 ISVYDIGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSLENLSA 396
Cdd:COG3048 324 ISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGSAGQ 403
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 951374585 397 DF--------PMKNANHIVWATGGSMVPKEDMDRYLEIGREEL 431
Cdd:COG3048 404 AYlerhglteKMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
23-417 |
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: 662.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 23 FWRNPDYGKKADLS--IGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLIDLPYMKARLNKSFTNEIEGGLYLKA 100
Cdd:cd06447 2 FWKNPNYGKPAEALapLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLLKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 101 DNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGIAVGSTGNLGLSIGIVAQRLGFRTS 180
Cdd:cd06447 82 DSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFKVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 181 VHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYDLFLGYSVAALRLQAQLKSQGIKVD 260
Cdd:cd06447 162 VHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIKVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 261 KDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDKISVYDIGIDGTTKADGLAVGRASR 340
Cdd:cd06447 242 AEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRPSG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 341 IAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSLENLSAD------FPMKNANHIVWATGGSM 414
Cdd:cd06447 322 LVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKryvrlgYRMENATHIVWATGGSM 401
|
...
gi 951374585 415 VPK 417
Cdd:cd06447 402 VPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
6-424 |
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: 527.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 6 LIEKYPEVKTMQELKPFFWRNP----DYGKKADLSIGIADVFDAEARFHRFAPYFEVAFPETVATHGILESPLIDLPYMK 81
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPgttsLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 82 ARLNKSFTNEIEGGLYLKADNYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEDNYAVLASKKYHDLFAKYGIAVGST 161
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 162 GNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYDLFLGY 241
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 242 SVAALRLQAQLKSQGIKVDKDHPLFVYLPAGVGGSPSGVTFGLKKVLGENAHAIFAEPTHIPSVTLGMVTGLNDKISVYD 321
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 322 IGIDGTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFT---------IMDQSLE 392
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAgpvrvcaseVSYRYMH 400
|
410 420 430
....*....|....*....|....*....|..
gi 951374585 393 NLSADfPMKNANHIVWATGGSMVPKEDMDRYL 424
Cdd:TIGR02035 401 GFSAE-QLRNATHLVWATGGGMVPEEEMNAYL 431
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
72-412 |
3.19e-41 |
|
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: 146.51 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 72 SPLIDLPYMKARLNksftneieGGLYLKADNYLPiSGSIKSRGGIYEVLKFAEKVAIqeggliyednyavlaskkyhdlf 151
Cdd:cd00640 1 TPLVRLKRLSKLGG--------ANIYLKLEFLNP-TGSFKDRGALNLILLAEEEGKL----------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 152 AKYGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDD 231
Cdd:cd00640 49 PKGVIIESTGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 232 EGSYDLFLGYSVAALRLQAQLksqgikvDKDHPLFVYLPAGVGGSPSGVTFGLKKvLGENAHAIFAEPthipsvtlgmvt 311
Cdd:cd00640 129 FDNPANIAGQGTIGLEILEQL-------GGQKPDAVVVPVGGGGNIAGIARALKE-LLPNVKVIGVEP------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 312 glndkisvydigidgttkadglavgrasriagknmrtlllGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSL 391
Cdd:cd00640 189 ----------------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA 228
|
330 340
....*....|....*....|.
gi 951374585 392 ENLsadfpMKNANHIVWATGG 412
Cdd:cd00640 229 KKL-----GKGKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
66-384 |
1.42e-38 |
|
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: 140.91 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 66 THGILESPLIDLPYMKARLNksftneieGGLYLKADNYLPiSGSIKSRGGIYEVLKFAEKvaiqeggliyednyavlask 145
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELG--------VDVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 146 kyhdlFAKYGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPM 225
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 226 TYFIDDEGSYDLFLGYSVAALRLQAQLksqGIKVDkdhplFVYLPAGVGGSPSGVTFGLKKvLGENAHAIFAEPTHIPSV 305
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQL---GGDPD-----AVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 306 TLGMVTGLNDKISVYDigidgtTKADGLAVGR-ASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAGF 384
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
37-426 |
3.74e-20 |
|
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: 90.87 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 37 IGIADVFDAEARFHRFAPyfevafpetvathgilESPLIDLPYMKARLNksftneieGGLYLKADNYLPIsGSIKSRGGI 116
Cdd:COG1171 6 PTLADIEAAAARIAGVVR----------------RTPLLRSPTLSERLG--------AEVYLKLENLQPT-GSFKLRGAY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 117 YEVLKFAEKVAiqeggliyednyavlaskkyhdlfaKYGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLR 196
Cdd:COG1171 61 NALASLSEEER-------------------------ARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 197 SFGVNVVEYNDNFTHAITEARKSAAADPMTyFI---DDEgsyDLFLGYSVAALRLQAQLKsqgikvDKDHplfVYLPAGV 273
Cdd:COG1171 116 AYGAEVVLHGDTYDDAEAAAAELAEEEGAT-FVhpfDDP---DVIAGQGTIALEILEQLP------DLDA---VFVPVGG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 274 GGSPSGVTFGLkKVLGENAHAIFAEPTHIPSVTLGMVTGlndKISVYDigiDGTTKADGLAVGRASRIAGKNMRTLLLGT 353
Cdd:COG1171 183 GGLIAGVAAAL-KALSPDIRVIGVEPEGAAAMYRSLAAG---EPVTLP---GVDTIADGLAVGRPGELTFEILRDLVDDI 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951374585 354 ATFKDEDMMKDVVRLYETEKIGLEPSAAAGFTIMDQSLENLsadfpmKNANHIVWATGGSMvpkeDMDRYLEI 426
Cdd:COG1171 256 VTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERL------KGKRVVVVLSGGNI----DPDRLAEI 318
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
67-384 |
1.06e-17 |
|
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: 83.31 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 67 HGILESPLIDLPYMKARLNksftNEIegglYLKADNyLPISGSIKSRGGIYEVLKFAEKvaiqeggliyEDNYAVLASkk 146
Cdd:cd01562 13 PVVRRTPLLTSPTLSELLG----AEV----YLKCEN-LQKTGSFKIRGAYNKLLSLSEE----------ERAKGVVAA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 147 yhdlfakygiavgSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMT 226
Cdd:cd01562 72 -------------SAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 227 yFI---DDEgsyDLFLGYSVAALRLQAQLKsqgiKVDkdhplFVYLPAGVGGSPSGVTFGLKKvLGENAHAIFAEPTHIP 303
Cdd:cd01562 139 -FIhpfDDP---DVIAGQGTIGLEILEQVP----DLD-----AVFVPVGGGGLIAGIATAVKA-LSPNTKVIGVEPEGAP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 304 SVTLGMVTGlndKISVYDIGidgTTKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAG 383
Cdd:cd01562 205 AMAQSLAAG---KPVTLPEV---DTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALA 278
|
.
gi 951374585 384 F 384
Cdd:cd01562 279 L 279
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
73-384 |
5.13e-12 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 66.00 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 73 PLIDLpymkARLNKSFTNEIegglYLKADNYLPiSGSIKSRGGIYEVLKFAEKVAIQEGGLIYEdnyavlaskkyhdlfa 152
Cdd:cd01561 4 PLVRL----NRLSPGTGAEI----YAKLEFFNP-GGSVKDRIALYMIEDAEKRGLLKPGTTIIE---------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 153 kygiavGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVV----EYNDNFTHAITEARKSAAADPMTYF 228
Cdd:cd01561 59 ------PTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVIltpeAEADGMKGAIAKARELAAETPNAFW 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 229 IDDEGSYDLFLG-YSVAALRLQAQLKSqgiKVDkdhplfvYLPAGVG--GSPSGVTFGLKKVlGENAHAIFAEPthipsv 305
Cdd:cd01561 133 LNQFENPANPEAhYETTAPEIWEQLDG---KVD-------AFVAGVGtgGTITGVARYLKEK-NPNVRIVGVDP------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 306 tLGMVTGLNDKISVYDI-GIdgttkadglavgRASRIaGKNM-RTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAAAG 383
Cdd:cd01561 196 -VGSVLFSGGPPGPHKIeGI------------GAGFI-PENLdRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAA 261
|
.
gi 951374585 384 F 384
Cdd:cd01561 262 V 262
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
96-227 |
1.76e-07 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 52.77 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 96 LYLKADNyLPISGSIKSRGGIYEVLKFAEKVAiqeggliyednyavlaskkyhdlfaKYGIAVGSTGNLGLSIGIVAQRL 175
Cdd:PRK06815 37 VYLKCEH-LQHTGSFKFRGASNKLRLLNEAQR-------------------------QQGVITASSGNHGQGVALAAKLA 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 951374585 176 GFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTY 227
Cdd:PRK06815 91 GIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVY 142
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
73-224 |
6.50e-07 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 51.02 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 73 PLIdlpymkaRLNkSFTNEIEGGLYLKADnYLPISGSIKSRGGIYEVLKFAEKVAIQEGGLIYEdnyavlaskkyhdlfa 152
Cdd:PRK10717 15 PLI-------RLN-RASEATGCEILGKAE-FLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVE---------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 153 kygiavGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVE-----YND--NFTH-AITEARKSAAADP 224
Cdd:PRK10717 70 ------GTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLvpaapYANpnNYVKgAGRLAEELVASEP 143
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
156-384 |
2.00e-06 |
|
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: 49.81 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 156 IAVGSTGNLGLSIGIVAQRLGFRTSVHMSAD-ASQWKKDKLRSFGVNVVEYNDNFTHAITEArKSAAADPMTYFiddEGS 234
Cdd:COG0498 116 IVCASSGNGSAALAAYAARAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLV-KELAADEGLYA---VNS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 235 YDLF--LGYSVAALRLQAQLKSQgikvdkdhPLFVYLPAGVGGSPSGVTFGLK--KVLGENAHA---IFAEPTHIPSVtl 307
Cdd:COG0498 192 INPArlEGQKTYAFEIAEQLGRV--------PDWVVVPTGNGGNILAGYKAFKelKELGLIDRLprlIAVQATGCNPI-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 308 gmVTGLNDKISVYDIgIDGTTKADGLAVGRASriagkNMRTLLL------GTATF-KDEDMMKDVVRLYETEKIGLEPSA 380
Cdd:COG0498 262 --LTAFETGRDEYEP-ERPETIAPSMDIGNPS-----NGERALFalresgGTAVAvSDEEILEAIRLLARREGIFVEPAT 333
|
....
gi 951374585 381 AAGF 384
Cdd:COG0498 334 AVAV 337
|
|
| PLN02970 |
PLN02970 |
serine racemase |
152-383 |
9.57e-06 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 47.37 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 152 AKYGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVeyndnFTHAITEARKSAAA----DPMTY 227
Cdd:PLN02970 74 AEKGVVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIIT-----WCEPTVESREAVAArvqqETGAV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 228 FIDDEGSYDLFLGYSVAALRLQAQLksQGIKVdkdhplfVYLPAGVGGSPSGVTFGLKKvLGENAHAIFAEPThipsvtl 307
Cdd:PLN02970 149 LIHPYNDGRVISGQGTIALEFLEQV--PELDV-------IIVPISGGGLISGIALAAKA-IKPSIKIIAAEPK------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 308 gmvtGLND----KISVYDIGIDGT-TKADGLavgRASriAGKN----MRTLLLGTATFKDEDMMKDVVRLYETEKIGLEP 378
Cdd:PLN02970 212 ----GADDaaqsKAAGEIITLPVTnTIADGL---RAS--LGDLtwpvVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEP 282
|
....*
gi 951374585 379 SAAAG 383
Cdd:PLN02970 283 SGAIG 287
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
94-384 |
2.30e-05 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 46.10 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 94 GGLYLKADnYLPISGSIKSRGGIYEVLKFAEKVAiqeggliyednyavlaskkyhdlfakyGIAVGSTGNLGLSIGIVAQ 173
Cdd:PRK08246 37 APVWLKLE-HLQHTGSFKARGAFNRLLAAPVPAA---------------------------GVVAASGGNAGLAVAYAAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 174 RLGFRTSVHMSADASQWKKDKLRSFGVNVV----EYNDNFTHAITEARKSAAAdpMTYFIDDEgsyDLFLGYSVAALRLQ 249
Cdd:PRK08246 89 ALGVPATVFVPETAPPAKVARLRALGAEVVvvgaEYADALEAAQAFAAETGAL--LCHAYDQP---EVLAGAGTLGLEIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 250 AQLKsqgiKVDKdhplfVYLPAGVGGSPSGVT---FGLKKVLGenahaifAEPTHIPSVTLGMVTGlndkiSVYDIGIDG 326
Cdd:PRK08246 164 EQAP----GVDT-----VLVAVGGGGLIAGIAawfEGRARVVA-------VEPEGAPTLHAALAAG-----EPVDVPVSG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951374585 327 TTkADGLAVGRASRIA-----GKNMRTLLLGtatfkDEDMMKDVVRLYETEKIGLEPSAAAGF 384
Cdd:PRK08246 223 IA-ADSLGARRVGEIAfalarAHVVTSVLVS-----DEAIIAARRALWEELRLAVEPGAATAL 279
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
155-381 |
2.33e-05 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 46.45 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 155 GIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTyFIDDEGS 234
Cdd:PLN02550 159 GVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRT-FIPPFDH 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 235 YDLFLGYSVAALRLQAQLKSqgikvdkdhPLF-VYLPAGVGGSPSGVTFGLKKVLGEnAHAIFAEPTHIPSVTLGMVTGl 313
Cdd:PLN02550 238 PDVIAGQGTVGMEIVRQHQG---------PLHaIFVPVGGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHHG- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951374585 314 nDKISVYDIGIdgttKADGLAVGRASRIAGKNMRTLLLGTATFKDEDMMKDVVRLYETEKIGLEPSAA 381
Cdd:PLN02550 307 -ERVMLDQVGG----FADGVAVKEVGEETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGA 369
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
155-288 |
4.99e-05 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 45.08 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 155 GIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAAdpMTYFIDDEGS 234
Cdd:PRK06381 65 GITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKE--NGIYDANPGS 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 951374585 235 ----YDLfLGYSVAALRLQAQLksqgikvdKDHPLFVYLPAGVGGSPSGVTFGLKKVL 288
Cdd:PRK06381 143 vnsvVDI-EAYSAIAYEIYEAL--------GDVPDAVAVPVGNGTTLAGIYHGFRRLY 191
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
131-335 |
6.52e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 41.52 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 131 GGLIYEDNYavlasKKYHDLFAkyGIAVGSTGNLGLSIGIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFT 210
Cdd:PRK06110 55 GGLVYFDRL-----ARRGPRVR--GVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 211 HAITEARKSAAADPMTYFiddeGSY--DLFLGYSVAALRLQAQLKsqgikvDKDhplFVYLPAGVGgspSGV--TFGLKK 286
Cdd:PRK06110 128 AAREEAARLAAERGLHMV----PSFhpDLVRGVATYALELFRAVP------DLD---VVYVPIGMG---SGIcgAIAARD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 951374585 287 VLGENAHAIFAEPTHIPSVTLGMVTGLNDKISVydigidGTTKADGLAV 335
Cdd:PRK06110 192 ALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPV------ATTLADGMAC 234
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
89-290 |
1.89e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 40.19 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 89 TNEIEGGLYLKADnYLPISGSIKSRGGIYEVLKFAEKvAIQEggliyednyavlaskkyhdlfakygIAVGSTGNLGLSI 168
Cdd:PRK08329 67 TVKRSIKVYFKLD-YLQPTGSFKDRGTYVTVAKLKEE-GINE-------------------------VVIDSSGNAALSL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951374585 169 GIVAQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTYFIDDEGSYdlFL-GYSVAALR 247
Cdd:PRK08329 120 ALYSLSEGIKVHVFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPY--FLeGTKTIAYE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 951374585 248 LQAQLKSqgikvdkdhPLFVYLPAGVGGSPSGVTFGLKKV--LGE 290
Cdd:PRK08329 198 IYEQIGV---------PDYAFVPVGSGTLFLGIWKGFKELheMGE 233
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
172-232 |
9.74e-03 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 38.20 E-value: 9.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951374585 172 AQRLGFRTSVHMSADASQWKKDKLRSFGVNVVEYNDNFTHAITEARKSAAADPMTyFI---DDE 232
Cdd:PRK09224 87 AARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLT-FIhpfDDP 149
|
|
| |
