|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
3-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 768.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 3 FEKIEIERWIQKYPLLDEITNLTPVVWLNSNINKMDQ-LSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQ 81
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEaLPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 82 LRKIPNMKNELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQ 161
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 162 FSIGVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDEN 241
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 242 SKHLFLGYSVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGE 321
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 322 KEKVSVQDFGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS 401
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 518243529 402 ---NYASNNNL--NVNQATHIVWATGGALVPEKDMEKFYEKGKSLM 442
Cdd:COG3048 401 agqAYLERHGLteKMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
6-441 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 713.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 6 IEIERWIQKYPLLDEITNLTPVVWLNSNINKMDQ-LSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRK 84
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEgLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 85 IPNMKNELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSI 164
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 165 GVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKH 244
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 245 LFLGYSVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEK 324
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 325 VSVQDFGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS-NY 403
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASvAY 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 518243529 404 ASNNNLN--VNQATHIVWATGGALVPEKDMEKFYEKGKSL 441
Cdd:PRK02991 401 LQRHGLSeqLKNATHLVWATGGSMVPEEEMEQYLAKGRAL 440
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
27-428 |
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: 619.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 27 VVWLNSNINKMDQLSTlPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRKIPNMKNELNHKYDAKITGDLYL 106
Cdd:cd06447 1 IFWKNPNYGKPAEALA-PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 107 KCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSIGVGSTGNLGLSIGIIGAKLGFN 186
Cdd:cd06447 80 KADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 187 VEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGYSVAAIRIKEQLAEESVQ 266
Cdd:cd06447 160 VTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 267 VDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQDFGIDNQTEGDGLAVGRP 346
Cdd:cd06447 240 VDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 347 SSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILASN---YASNNNLNVNQATHIVWATGG 423
Cdd:cd06447 320 SGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAegkRYVRLGYRMENATHIVWATGG 399
|
....*
gi 518243529 424 ALVPE 428
Cdd:cd06447 400 SMVPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
11-434 |
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: 573.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 11 WIQKYPLLDEITNLTPVVWLNSNI-NKMDQLSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRKIPNMK 89
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTtSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 90 NELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSIGVGST 169
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 170 GNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGY 249
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 250 SVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQD 329
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 330 FGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS----NYAS 405
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASevsyRYMH 400
|
410 420 430
....*....|....*....|....*....|
gi 518243529 406 N-NNLNVNQATHIVWATGGALVPEKDMEKF 434
Cdd:TIGR02035 401 GfSAEQLRNATHLVWATGGGMVPEEEMNAY 430
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
74-394 |
7.85e-40 |
|
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: 144.38 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 74 TGGIIESQLRKIPNMKNELNHkydakitgDLYLKCDNELPiAGSIKARGGVYEVLHYAEKlaieeglvaknddytvfssd 153
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGV--------DVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 154 kfkafFGQFSIGVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPM 233
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 234 GYFVDDENSKHLFLGYSVAAIRIKEQLAEEsvqVDAnhplfVYLPCGVGGSPGGINFGLKQIFGDnVHCFFVEPTHSPSV 313
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQLGGD---PDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 314 LIGLLTGEKEKVSVQDfgidnqTEGDGLAVGR-PSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGL 392
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
..
gi 518243529 393 LG 394
Cdd:pfam00291 273 AA 274
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
3-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 768.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 3 FEKIEIERWIQKYPLLDEITNLTPVVWLNSNINKMDQ-LSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQ 81
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEaLPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 82 LRKIPNMKNELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQ 161
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 162 FSIGVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDEN 241
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 242 SKHLFLGYSVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGE 321
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 322 KEKVSVQDFGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS 401
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLLGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 518243529 402 ---NYASNNNL--NVNQATHIVWATGGALVPEKDMEKFYEKGKSLM 442
Cdd:COG3048 401 agqAYLERHGLteKMANATHLVWATGGSMVPEEEMEAYLAKGKALL 446
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
6-441 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 713.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 6 IEIERWIQKYPLLDEITNLTPVVWLNSNINKMDQ-LSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRK 84
Cdd:PRK02991 1 ANINKLIAQYPLLKDLIALEETFWFNPNYTSLAEgLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 85 IPNMKNELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSI 164
Cdd:PRK02991 81 IPAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 165 GVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKH 244
Cdd:PRK02991 161 AVGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 245 LFLGYSVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEK 324
Cdd:PRK02991 241 LFLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 325 VSVQDFGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS-NY 403
Cdd:PRK02991 321 ISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASvAY 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 518243529 404 ASNNNLN--VNQATHIVWATGGALVPEKDMEKFYEKGKSL 441
Cdd:PRK02991 401 LQRHGLSeqLKNATHLVWATGGSMVPEEEMEQYLAKGRAL 440
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
27-428 |
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: 619.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 27 VVWLNSNINKMDQLSTlPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRKIPNMKNELNHKYDAKITGDLYL 106
Cdd:cd06447 1 IFWKNPNYGKPAEALA-PLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 107 KCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSIGVGSTGNLGLSIGIIGAKLGFN 186
Cdd:cd06447 80 KADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 187 VEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGYSVAAIRIKEQLAEESVQ 266
Cdd:cd06447 160 VTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 267 VDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQDFGIDNQTEGDGLAVGRP 346
Cdd:cd06447 240 VDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 347 SSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILASN---YASNNNLNVNQATHIVWATGG 423
Cdd:cd06447 320 SGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAegkRYVRLGYRMENATHIVWATGG 399
|
....*
gi 518243529 424 ALVPE 428
Cdd:cd06447 400 SMVPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
11-434 |
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: 573.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 11 WIQKYPLLDEITNLTPVVWLNSNI-NKMDQLSTLPVSKTDMEEATQLWQRFATYLAHEFPETQETGGIIESQLRKIPNMK 89
Cdd:TIGR02035 1 LIAQYPLIKDLIALKEVTWFNPGTtSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 90 NELNHKYDAKITGDLYLKCDNELPIAGSIKARGGVYEVLHYAEKLAIEEGLVAKNDDYTVFSSDKFKAFFGQFSIGVGST 169
Cdd:TIGR02035 81 KRLEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 170 GNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGY 249
Cdd:TIGR02035 161 GNLGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 250 SVAAIRIKEQLAEESVQVDANHPLFVYLPCGVGGSPGGINFGLKQIFGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQD 329
Cdd:TIGR02035 241 AVAASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 330 FGIDNQTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGPGRILAS----NYAS 405
Cdd:TIGR02035 321 IGIDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASevsyRYMH 400
|
410 420 430
....*....|....*....|....*....|
gi 518243529 406 N-NNLNVNQATHIVWATGGALVPEKDMEKF 434
Cdd:TIGR02035 401 GfSAEQLRNATHLVWATGGGMVPEEEMNAY 430
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
74-394 |
7.85e-40 |
|
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: 144.38 E-value: 7.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 74 TGGIIESQLRKIPNMKNELNHkydakitgDLYLKCDNELPiAGSIKARGGVYEVLHYAEKlaieeglvaknddytvfssd 153
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGV--------DVYLKLESLNP-TGSFKDRGALNLLLRLKEG-------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 154 kfkafFGQFSIGVGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPM 233
Cdd:pfam00291 53 -----EGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 234 GYFVDDENSKHLFLGYSVAAIRIKEQLAEEsvqVDAnhplfVYLPCGVGGSPGGINFGLKQIFGDnVHCFFVEPTHSPSV 313
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQLGGD---PDA-----VVVPVGGGGLIAGIARGLKELGPD-VRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 314 LIGLLTGEKEKVSVQDfgidnqTEGDGLAVGR-PSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGL 392
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
..
gi 518243529 393 LG 394
Cdd:pfam00291 273 AA 274
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
102-423 |
8.76e-37 |
|
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: 134.95 E-value: 8.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 102 GDLYLKCDNELPiAGSIKARGGVYEVLHYAEKLAIEEGLVAknddytvfssdkfkaffgqfsigVGSTGNLGLSIGIIGA 181
Cdd:cd00640 15 ANIYLKLEFLNP-TGSFKDRGALNLILLAEEEGKLPKGVII-----------------------ESTGGNTGIALAAAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 182 KLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGYSVAAIRIKEQLA 261
Cdd:cd00640 71 RLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 262 EEsvqvdanHPLFVYLPCGVGGSPGGINFGLKQIFGdNVHCFFVEPthspsvliglltgekekvsvqdfgidnqtegdgl 341
Cdd:cd00640 151 GQ-------KPDAVVVPVGGGGNIAGIARALKELLP-NVKVIGVEP---------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 342 avgrpssfassiseklvsGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLGpgrilASNYASNNNLNvnqATHIVWAT 421
Cdd:cd00640 189 ------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAA-----ALKLAKKLGKG---KTVVVILT 242
|
..
gi 518243529 422 GG 423
Cdd:cd00640 243 GG 244
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
98-392 |
6.12e-18 |
|
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: 84.32 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 98 AKITG-DLYLKCDNELPIaGSIKARGGVYEVLHYAEKLAiEEGLVAknddytvfssdkfkAffgqfsigvgSTGNLGLSI 176
Cdd:COG1171 34 SERLGaEVYLKLENLQPT-GSFKLRGAYNALASLSEEER-ARGVVA--------------A----------SAGNHAQGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 177 GIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQ------KTIIDPmgyFvDDEnskHLFLGYS 250
Cdd:COG1171 88 AYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAElaeeegATFVHP---F-DDP---DVIAGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 251 VAAIRIKEQLAEesvqVDAnhplfVYLPCGVGGSPGGINFGLKQIfGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQDf 330
Cdd:COG1171 161 TIALEILEQLPD----LDA-----VFVPVGGGGLIAGVAAALKAL-SPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVD- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518243529 331 gidnqTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGL 392
Cdd:COG1171 230 -----TIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL 286
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
93-392 |
1.16e-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: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 93 NHKYDAKITGDLYLKCDNeLPIAGSIKARGgvyeVLHYAEKLAIEE---GLVAknddytvfssdkfkaffgqfsigvGST 169
Cdd:cd01562 23 SPTLSELLGAEVYLKCEN-LQKTGSFKIRG----AYNKLLSLSEEErakGVVA------------------------ASA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 170 GNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQktIIDPMGY-FVDDENSKHLFLG 248
Cdd:cd01562 74 GNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARE--LAEEEGLtFIHPFDDPDVIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 249 YSVAAIRIKEQLAEesvqVDAnhplfVYLPCGVGGSPGGINFGLKQIfGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQ 328
Cdd:cd01562 152 QGTIGLEILEQVPD----LDA-----VFVPVGGGGLIAGIATAVKAL-SPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEV 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518243529 329 DfgidnqTEGDGLAVGRPSSFASSISEKLVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGL 392
Cdd:cd01562 222 D------TIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALAL 279
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
91-394 |
5.95e-11 |
|
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: 62.92 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 91 ELNHKYDAKItGDLYLKCDNELPiAGSIKARGGVYEVLHyaeklAIEEGLVAKNDdyTVFSSdkfkaffgqfsigvgSTG 170
Cdd:cd01561 7 RLNRLSPGTG-AEIYAKLEFFNP-GGSVKDRIALYMIED-----AEKRGLLKPGT--TIIEP---------------TSG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 171 NLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATVH----EFKGDFSEAIYVGRQKTIIDPMGYFVD----DENS 242
Cdd:cd01561 63 NTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVIltpeAEADGMKGAIAKARELAAETPNAFWLNqfenPANP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 243 K-HlflgYSVAAIRIKEQLAEEsvqVDAnhplFVylpCGVG--GSPGGINFGLKQiFGDNVHCFFVEPTHSPsvligLLT 319
Cdd:cd01561 143 EaH----YETTAPEIWEQLDGK---VDA----FV---AGVGtgGTITGVARYLKE-KNPNVRIVGVDPVGSV-----LFS 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518243529 320 GEKEKVSvqdfgidnQTEGDGlavgrpSSFASSISEK-LVSGIYTLEDDDLFKLLAILVDSEGIHLEPSAASGLLG 394
Cdd:cd01561 203 GGPPGPH--------KIEGIG------AGFIPENLDRsLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAA 264
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
102-390 |
3.62e-10 |
|
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: 61.07 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 102 GDLYLKCDNELPiAGSIKARGgVYEVLHYAEKLAIEEglvaknddytvfssdkfkaffgqfsIGVGSTGNLGLSIGIIGA 181
Cdd:cd01563 38 KNLYVKDEGLNP-TGSFKDRG-MTVAVSKAKELGVKA-------------------------VACASTGNTSASLAAYAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 182 KLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEAIYVGRQKTIIDPmGYFVddeNSKH-LFL-GYSVAAIRIKEQ 259
Cdd:cd01563 91 RAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENW-IYLS---NSLNpYRLeGQKTIAFEIAEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 260 LAEESvqvdanhPLFVYLPCGVGGSPGGINFGLKQIF-----GDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQDFgidn 334
Cdd:cd01563 167 LGWEV-------PDYVVVPVGNGGNITAIWKGFKELKelgliDRLPRMVGVQAEGAAPIVRAFKEGKDDIEPVENP---- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 518243529 335 QTEGDGLAVGRPSSFASSISEKLVSGIYTLE--DDDLFKLLAILVDSEGIHLEP-SAAS 390
Cdd:cd01563 236 ETIATAIRIGNPASGPKALRAVRESGGTAVAvsDEEILEAQKLLARTEGIFVEPaSAAS 294
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
98-344 |
2.77e-08 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 55.08 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 98 AKITGDLYLKCDNeLPIAGSIKARGGVYEVLHYAEKlAIEEGLVAknddytvfssdkfkaffgqfsigvGSTGNLGLSIG 177
Cdd:PRK06815 31 QHTGCEVYLKCEH-LQHTGSFKFRGASNKLRLLNEA-QRQQGVIT------------------------ASSGNHGQGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 178 IIGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGDFSEA-IYVGRQ-----KTIIDPmgYfvddeNSKHLFLGYSV 251
Cdd:PRK06815 85 LAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAeLAARRAaeqqgKVYISP--Y-----NDPQVIAGQGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 252 AAIRIKEQLAeesvQVDAnhplfVYLPCGVGGSPGGINFGLKQIfGDNVHCFFVEPTHSPSVLIGLLTGEKEKVSVQDfg 331
Cdd:PRK06815 158 IGMELVEQQP----DLDA-----VFVAVGGGGLISGIATYLKTL-SPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQP-- 225
|
250
....*....|...
gi 518243529 332 idnqTEGDGLAVG 344
Cdd:PRK06815 226 ----TLSDGTAGG 234
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
99-296 |
5.04e-07 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 51.37 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 99 KITGDLYLKCDNELPiAGSIKARGgVYEVLHYAEKLAIEEglvaknddytvfssdkfkaffgqfsIGVGSTGNLGLSIGI 178
Cdd:PRK08329 69 KRSIKVYFKLDYLQP-TGSFKDRG-TYVTVAKLKEEGINE-------------------------VVIDSSGNAALSLAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 179 IGAKLGFNVEVYMSADAKQWKKELLREKGATVHEFKGD----FSEAIYVGRQKTI------IDPmgYFVDdenskhlflG 248
Cdd:PRK08329 122 YSLSEGIKVHVFVSYNASKEKISLLSRLGAELHFVEGDrmevHEEAVKFSKRNNIpyvshwLNP--YFLE---------G 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518243529 249 YSVAAIRIKEQLAeesvqvdanHPLFVYLPCGVGGSPGGINFGLKQIF 296
Cdd:PRK08329 191 TKTIAYEIYEQIG---------VPDYAFVPVGSGTLFLGIWKGFKELH 229
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
164-392 |
3.25e-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: 49.04 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 164 IGVGSTGNLGLSIGIIGAKLGFNVEVYMSAD--AKQWKKELLREkGATVHEFKGDFSEAIYVGRQktIIDPMGYFvdDEN 241
Cdd:COG0498 116 IVCASSGNGSAALAAYAARAGIEVFVFVPEGkvSPGQLAQMLTY-GAHVIAVDGNFDDAQRLVKE--LAADEGLY--AVN 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 242 SKHLF--LGYSVAAIRIKEQLAEEsvqvdanhPLFVYLPCGVGGSPGGINFGLKQIFGDNVHC-----FFVEPTHSPSVL 314
Cdd:COG0498 191 SINPArlEGQKTYAFEIAEQLGRV--------PDWVVVPTGNGGNILAGYKAFKELKELGLIDrlprlIAVQATGCNPIL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 315 IGLLTGEKEKVSVQDfgidnQTEGDGLAVGRPSSFassisEKLV-----SG--IYTLEDDDLFKLLAILVDSEGIHLEPS 387
Cdd:COG0498 263 TAFETGRDEYEPERP-----ETIAPSMDIGNPSNG-----ERALfalreSGgtAVAVSDEEILEAIRLLARREGIFVEPA 332
|
....*
gi 518243529 388 AASGL 392
Cdd:COG0498 333 TAVAV 337
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
105-392 |
6.89e-05 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 44.60 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 105 YLKCDNELPiAGSIKARGgvyeVLHYAEKLAIEeglvAKNDDYTVFSSdkfkaffgqfsigvgSTGNLGLSIGIIGAKLG 184
Cdd:cd06448 19 FLKLENLQP-SGSFKIRG----IGHLCQKSAKQ----GLNECVHVVCS---------------SGGNAGLAAAYAARKLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 185 FNVEVYMSADAKQWKKELLREKGATVHEF-KGDFSEAIYVGRQKTIIDPMGYFVDDENSKHLFLGYSVAAIRIKEQLaEE 263
Cdd:cd06448 75 VPCTIVVPESTKPRVVEKLRDEGATVVVHgKVWWEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQL-QS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 264 SVQVDAnhplfvyLPCGVGGspG----GINFGLKQIFGDNVHCFFVEP--THS--PSVLIGLLTGEKEKVSVqdfgidnq 335
Cdd:cd06448 154 QEKVDA-------IVCSVGG--GgllnGIVQGLERNGWGDIPVVAVETegAHSlnASLKAGKLVTLPKITSV-------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 518243529 336 teGDGLAVGRPSSFASSISEKlvSGIYTLEDDDLFKLLAIL--VDSEGIHLEPSAASGL 392
Cdd:cd06448 217 --ATSLGAKTVSSQALEYAQE--HNIKSEVVSDRDAVQACLrfADDERILVEPACGAAL 271
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
78-210 |
4.18e-03 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 39.17 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518243529 78 IESQLRKIPNMKNELnhkyDAKITGDLYLKCDNeLPIAGSIKARGGVYEVLHYAEKlaiEEGLVAknddytvfssdkfka 157
Cdd:PRK08246 17 IAPHIRRTPVLEADG----AGFGPAPVWLKLEH-LQHTGSFKARGAFNRLLAAPVP---AAGVVA--------------- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 518243529 158 ffgqfsigvGSTGNLGLSIGIIGAKLGFNVEVYMSADAKQWKKELLREKGATV 210
Cdd:PRK08246 74 ---------ASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEV 117
|
|
| |
