|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 854.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 1 MENYDVETLKVNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESP 80
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 81 LIRIPNMKKQLEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSK 160
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 161 YSIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDEN 240
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 241 SHDLFLGYSVAASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGL 320
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 321 HDQISVQEIGIDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKL-HQ 399
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLlGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 947239738 400 QGMNYLNDHNLTGKIIKGTHIVWGTGGSMVPDNIKKDYYDKGI 442
Cdd:COG3048 401 AGQAYLERHGLTEKMANATHLVWATGGSMVPEEEMEAYLAKGK 443
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
5-441 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 814.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 5 DVETLKVNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRI 84
Cdd:PRK02991 2 NINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 85 PNMKKQLEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIV 164
Cdd:PRK02991 82 PAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 165 VGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDL 244
Cdd:PRK02991 162 VGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 245 FLGYSVAASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQI 324
Cdd:PRK02991 242 FLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 325 SVQEIGIDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQGmNY 404
Cdd:PRK02991 322 SVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASV-AY 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 947239738 405 LNDHNLTGKIIKGTHIVWGTGGSMVPDNIKKDYYDKG 441
Cdd:PRK02991 401 LQRHGLSEQLKNATHLVWATGGSMVPEEEMEQYLAKG 437
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
25-431 |
0e+00 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 700.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 25 LFWINPNLEEFESGItkSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRIPNMKKQLEQEYKQTIQAQLL 104
Cdd:cd06447 1 IFWKNPNYGKPAEAL--APLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 105 LKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIVVGSTGNLGLSIGIMSAKLGF 184
Cdd:cd06447 79 LKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 185 QVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDLFLGYSVAASRLSKQLMELNI 264
Cdd:cd06447 159 KVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 265 TVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQISVQEIGIDNKTDADGLAVGR 344
Cdd:cd06447 239 KVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 345 ASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQgMNYLNDHNLTGKIIKGTHIVWGT 424
Cdd:cd06447 319 PSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSE-AEGKRYVRLGYRMENATHIVWAT 397
|
....*..
gi 947239738 425 GGSMVPD 431
Cdd:cd06447 398 GGSMVPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
11-431 |
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: 663.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 11 VNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRIPNMKKQ 90
Cdd:TIGR02035 3 AQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQKR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 91 LEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIVVGSTGN 170
Cdd:TIGR02035 83 LEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGSTGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 171 LGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDLFLGYSV 250
Cdd:TIGR02035 163 LGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGYAV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 251 AASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQISVQEIG 330
Cdd:TIGR02035 243 AASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQDIG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 331 IDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQGMNYLNDHNL 410
Cdd:TIGR02035 323 IDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASEVSYRYMHGF 402
|
410 420
....*....|....*....|..
gi 947239738 411 TGKIIKG-THIVWGTGGSMVPD 431
Cdd:TIGR02035 403 SAEQLRNaTHLVWATGGGMVPE 424
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
73-401 |
2.56e-31 |
|
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: 121.65 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 73 SNGIIESPLIRIPNMKKQLeqeykqtiQAQLLLKCDSHLPiSGSIKARGGIYEVLKYAEKLAFEHgllsldddysildsh 152
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKEL--------GVDVYLKLESLNP-TGSFKDRGALNLLLRLKEGEGGKT--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 153 ifrqffskysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPT 232
Cdd:pfam00291 58 ----------VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 233 CHFVDDENSHDLFLGYSVAASRLSKQlmeLNITVDenhplFVYLPCGVGGGPGGVAFGLKLMFqDHVHCFFAEPTHSPCM 312
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQ---LGGDPD-----AVVVPVGGGGLIAGIARGLKELG-PDVRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 313 VVGLMTGLHDQISVQEigidnkTDADGLAVGR-ASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGM 391
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
330
....*....|
gi 947239738 392 IGpVKLHQQG 401
Cdd:pfam00291 273 AA-LKLALAG 281
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DsdA |
COG3048 |
D-serine dehydratase [Amino acid transport and metabolism]; |
1-442 |
0e+00 |
|
D-serine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 442282 Cd Length: 446 Bit Score: 854.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 1 MENYDVETLKVNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESP 80
Cdd:COG3048 1 MAGKTMAQLIADFPLLEDLIALEEVLWFNPNYTPAAEALPDVGLTAADVADAEARLQRFAPYLAKAFPETAASGGIIESP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 81 LIRIPNMKKQLEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSK 160
Cdd:COG3048 81 LVPIPAMQKALEERYGQPIPGRLLLKCDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLKEEDDYSKLASDEFRAFFSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 161 YSIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDEN 240
Cdd:COG3048 161 YSIAVGSTGNLGLSIGIMSAALGFQVTVHMSADAKQWKKDLLRSKGVTVVEYEGDYSVAVEQGRKQAEADPNCHFVDDEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 241 SHDLFLGYSVAASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGL 320
Cdd:COG3048 241 SRDLFLGYAVAALRLKKQLAEAGIVVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLATGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 321 HDQISVQEIGIDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKL-HQ 399
Cdd:COG3048 321 HDKISVQDIGLDNRTAADGLAVGRASGFVGRAMERLLSGVYTVEDDELYRLLALLADTEGIRLEPSALAGMPGPLRLlGS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 947239738 400 QGMNYLNDHNLTGKIIKGTHIVWGTGGSMVPDNIKKDYYDKGI 442
Cdd:COG3048 401 AGQAYLERHGLTEKMANATHLVWATGGSMVPEEEMEAYLAKGK 443
|
|
| PRK02991 |
PRK02991 |
D-serine dehydratase; Provisional |
5-441 |
0e+00 |
|
D-serine dehydratase; Provisional
Pssm-ID: 235096 Cd Length: 441 Bit Score: 814.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 5 DVETLKVNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRI 84
Cdd:PRK02991 2 NINKLIAQYPLLKDLIALEETFWFNPNYTSLAEGLPYVGLTEADVQDAEARLKRFAPYLAKAFPETAATGGIIESPLVAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 85 PNMKKQLEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIV 164
Cdd:PRK02991 82 PAMQKALEKEYGQPISGRLLLKKDSHLPISGSIKARGGIYEVLKHAEKLALEAGLLTLDDDYSKLASPEFRQFFSQYSIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 165 VGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDL 244
Cdd:PRK02991 162 VGSTGNLGLSIGIMSAALGFKVTVHMSADARQWKKDKLRSHGVTVVEYEGDYGVAVEEGRKAAESDPNCYFIDDENSRTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 245 FLGYSVAASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQI 324
Cdd:PRK02991 242 FLGYAVAGLRLKAQLAEQGIVVDADHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGLMTGLHDQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 325 SVQEIGIDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQGmNY 404
Cdd:PRK02991 322 SVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGVYTVSDETLYRLLGLLADTEGIRLEPSALAGMAGPVRVCASV-AY 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 947239738 405 LNDHNLTGKIIKGTHIVWGTGGSMVPDNIKKDYYDKG 441
Cdd:PRK02991 401 LQRHGLSEQLKNATHLVWATGGSMVPEEEMEQYLAKG 437
|
|
| D-Ser-dehyd |
cd06447 |
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
25-431 |
0e+00 |
|
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.
Pssm-ID: 107208 Cd Length: 404 Bit Score: 700.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 25 LFWINPNLEEFESGItkSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRIPNMKKQLEQEYKQTIQAQLL 104
Cdd:cd06447 1 IFWKNPNYGKPAEAL--APLSREDIFDAEARLKRFAPYIAKVFPETAASHGIIESPLLPIPRMKQALEKLYHQPIKGRLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 105 LKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIVVGSTGNLGLSIGIMSAKLGF 184
Cdd:cd06447 79 LKADSHLPISGSIKARGGIYEVLKHAEKLALEHGLLTLEDDYSKLASEKFRKLFSQYSIAVGSTGNLGLSIGIMAAALGF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 185 QVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDLFLGYSVAASRLSKQLMELNI 264
Cdd:cd06447 159 KVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVEEGRKQAAADPMCYFVDDENSRDLFLGYAVAASRLKAQLAELGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 265 TVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQISVQEIGIDNKTDADGLAVGR 344
Cdd:cd06447 239 KVDAEHPLFVYLPCGVGGAPGGVAFGLKLIFGDNVHCFFAEPTHSPCMLLGMATGLHDKISVQDIGIDNRTAADGLAVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 345 ASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQgMNYLNDHNLTGKIIKGTHIVWGT 424
Cdd:cd06447 319 PSGLVGKLMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSE-AEGKRYVRLGYRMENATHIVWAT 397
|
....*..
gi 947239738 425 GGSMVPD 431
Cdd:cd06447 398 GGSMVPE 404
|
|
| D_Ser_am_lyase |
TIGR02035 |
D-serine ammonia-lyase; This family consists of D-serine ammonia-lyase (EC 4.3.1.18), a ... |
11-431 |
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: 663.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 11 VNYPLLNHLISLEELFWINPNLEEFESGITKSPVTLEDVRDAEERLKRFAPYIANVFPETKESNGIIESPLIRIPNMKKQ 90
Cdd:TIGR02035 3 AQYPLIKDLIALKEVTWFNPGTTSLAEGLPYVGLTAQDVADAEARLQRFAPYIAKVFPETAATGGIIESPLVEIPAMQKR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 91 LEQEYKQTIQAQLLLKCDSHLPISGSIKARGGIYEVLKYAEKLAFEHGLLSLDDDYSILDSHIFRQFFSKYSIVVGSTGN 170
Cdd:TIGR02035 83 LEKEYQQPIPGRLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSILAEPEFKQFFSRYSIAVGSTGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 171 LGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDDENSHDLFLGYSV 250
Cdd:TIGR02035 163 LGLSIGIISAALGFQVTVHMSADARQWKKDKLRSHGVTVVEYESDYGVAVEEGRKAAQSDPNCYFIDDENSRTLFLGYAV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 251 AASRLSKQLMELNITVDENHPLFVYLPCGVGGGPGGVAFGLKLMFQDHVHCFFAEPTHSPCMVVGLMTGLHDQISVQEIG 330
Cdd:TIGR02035 243 AASRLKAQFDQQGIIVDAEHPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVYTGLHEQISVQDIG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 331 IDNKTDADGLAVGRASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLHQQGMNYLNDHNL 410
Cdd:TIGR02035 323 IDNLTAADGLAVGRPSGFVGRAMERLLDGFYTVDDQTLYDLLGWLAQSEGIRLEPSALAGMAGPVRVCASEVSYRYMHGF 402
|
410 420
....*....|....*....|..
gi 947239738 411 TGKIIKG-THIVWGTGGSMVPD 431
Cdd:TIGR02035 403 SAEQLRNaTHLVWATGGGMVPE 424
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
79-426 |
4.11e-33 |
|
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: 124.93 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 79 SPLIRIPNMKKQLEqeykqtiqAQLLLKCDSHLPiSGSIKARGGIYEVLKYAEKLAFEHGLlsldddysildshifrqff 158
Cdd:cd00640 1 TPLVRLKRLSKLGG--------ANIYLKLEFLNP-TGSFKDRGALNLILLAEEEGKLPKGV------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 159 skysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPTCHFVDD 238
Cdd:cd00640 53 ----IIESTGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 239 ENSHDLFLGYSVAASRLSKQLmelnitvDENHPLFVYLPCGVGGGPGGVAFGLKlMFQDHVHCFFAEPthspcmvvglmt 318
Cdd:cd00640 129 FDNPANIAGQGTIGLEILEQL-------GGQKPDAVVVPVGGGGNIAGIARALK-ELLPNVKVIGVEP------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 319 glhdqisvqeigidnktdadglavgrasrfvgkviepflsGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGMIGPVKLH 398
Cdd:cd00640 189 ----------------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA 228
|
330 340
....*....|....*....|....*...
gi 947239738 399 QQGMNylndhnltgkiiKGTHIVWGTGG 426
Cdd:cd00640 229 KKLGK------------GKTVVVILTGG 244
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
73-401 |
2.56e-31 |
|
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: 121.65 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 73 SNGIIESPLIRIPNMKKQLeqeykqtiQAQLLLKCDSHLPiSGSIKARGGIYEVLKYAEKLAFEHgllsldddysildsh 152
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKEL--------GVDVYLKLESLNP-TGSFKDRGALNLLLRLKEGEGGKT--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 153 ifrqffskysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEEGRKQAAADPT 232
Cdd:pfam00291 58 ----------VVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 233 CHFVDDENSHDLFLGYSVAASRLSKQlmeLNITVDenhplFVYLPCGVGGGPGGVAFGLKLMFqDHVHCFFAEPTHSPCM 312
Cdd:pfam00291 128 AYYINQYDNPLNIEGYGTIGLEILEQ---LGGDPD-----AVVVPVGGGGLIAGIARGLKELG-PDVRVIGVEPEGAPAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 313 VVGLMTGLHDQISVQEigidnkTDADGLAVGR-ASRFVGKVIEPFLSGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGM 391
Cdd:pfam00291 199 ARSLAAGRPVPVPVAD------TIADGLGVGDePGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAAL 272
|
330
....*....|
gi 947239738 392 IGpVKLHQQG 401
Cdd:pfam00291 273 AA-LKLALAG 281
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
39-391 |
4.94e-11 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 63.52 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 39 ITKSPVTLEDVRDAEERLKRFapyianvfpetkesngIIESPLIRIPNMKKQLeqeykqtiQAQLLLKCDSHLPIsGSIK 118
Cdd:COG1171 1 MTALMPTLADIEAAAARIAGV----------------VRRTPLLRSPTLSERL--------GAEVYLKLENLQPT-GSFK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 119 ARGGIYEVLKYAEKLAfEHGllsldddysildshifrqffskysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWK 198
Cdd:COG1171 56 LRGAYNALASLSEEER-ARG------------------------VVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 199 KDLLRSKNVTVIEYEADYSKAVEEGRkQAAADPTCHFVDDENSHDLFLGYSVAAsrlskqlMELnitVDENHPL-FVYLP 277
Cdd:COG1171 111 VAATRAYGAEVVLHGDTYDDAEAAAA-ELAEEEGATFVHPFDDPDVIAGQGTIA-------LEI---LEQLPDLdAVFVP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 278 CGVGGGPGGVAFGLKLMFQDhVHCFFAEPTHSPCMVVGLMTGlhDQISVQEIGidnkTDADGLAVGRASRFVGKVIEPFL 357
Cdd:COG1171 180 VGGGGLIAGVAAALKALSPD-IRVIGVEPEGAAAMYRSLAAG--EPVTLPGVD----TIADGLAVGRPGELTFEILRDLV 252
|
330 340 350
....*....|....*....|....*....|....
gi 947239738 358 SGSYTVSDEHLYRLLKQLVDTENVQLEPSALAGM 391
Cdd:COG1171 253 DDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL 286
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
46-391 |
1.69e-10 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 61.73 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 46 LEDVRDAEERLKRFapyianvfpetkesngIIESPLIRIPNmkkqLEQEYKqtiqAQLLLKCDsHLPISGSIKARGGIYE 125
Cdd:cd01562 1 LEDILAAAARIKPV----------------VRRTPLLTSPT----LSELLG----AEVYLKCE-NLQKTGSFKIRGAYNK 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 126 VLKY-AEKLAfeHGllsldddysildshifrqffskysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRS 204
Cdd:cd01562 56 LLSLsEEERA--KG------------------------VVAASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 205 KNVTVIEYEADYSKAVEEGRKQAAADpTCHFV---DDEnshDLFLGYSVAAsrlskqlMELNITVDENHPLFVylPCGVG 281
Cdd:cd01562 110 YGAEVVLYGEDFDEAEAKARELAEEE-GLTFIhpfDDP---DVIAGQGTIG-------LEILEQVPDLDAVFV--PVGGG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 282 GGPGGVAFGLKLmFQDHVHCFFAEPTHSPCMVVGLMTGlhdqiSVQEIGIDNkTDADGLAVGRASRFVGKVIEPFLSGSY 361
Cdd:cd01562 177 GLIAGIATAVKA-LSPNTKVIGVEPEGAPAMAQSLAAG-----KPVTLPEVD-TIADGLAVKRPGELTFEIIRKLVDDVV 249
|
330 340 350
....*....|....*....|....*....|...
gi 947239738 362 TVSDEHLYRLLKQLVDTENVQLEPS---ALAGM 391
Cdd:cd01562 250 TVSEDEIAAAMLLLFEREKLVAEPAgalALAAL 282
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
46-228 |
3.90e-07 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 51.62 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 46 LEDVRDAEERLKrfaPYIAnvfpetkesngiiESPLIRIPNMKKQLEqeykqtiqAQLLLKCDsHLPISGSIKARGGIYE 125
Cdd:PRK06815 4 FDAILEAHQRLR---PQVR-------------VTPLEHSPLLSQHTG--------CEVYLKCE-HLQHTGSFKFRGASNK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 126 VLkyaeklafehgllsldddysILDSHIFRQffskySIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSK 205
Cdd:PRK06815 59 LR--------------------LLNEAQRQQ-----GVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRAL 113
|
170 180
....*....|....*....|...
gi 947239738 206 NVTVIEYEADYSKAVEEGRKQAA 228
Cdd:PRK06815 114 GAEVRLYGGDALNAELAARRAAE 136
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
43-229 |
1.26e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 43.79 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 43 PVTLEDVRDAEERLkrfAPYIANVfpetkesngiiesPLiripnmkkqLEQEYKQTIQAQLLLKCDsHLPISGSIKARGG 122
Cdd:PRK08246 4 MITRSDVRAAAQRI---APHIRRT-------------PV---------LEADGAGFGPAPVWLKLE-HLQHTGSFKARGA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 123 IYEVLKYAEKlafEHGllsldddysildshifrqffskysIVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLL 202
Cdd:PRK08246 58 FNRLLAAPVP---AAG------------------------VVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARL 110
|
170 180
....*....|....*....|....*..
gi 947239738 203 RSKNVTVIEYEADYSKAVEEGRKQAAA 229
Cdd:PRK08246 111 RALGAEVVVVGAEYADALEAAQAFAAE 137
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
163-222 |
6.31e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 38.65 E-value: 6.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239738 163 IVVGSTGNLGLSIGIMSAKLGFQVTVHMSADAKQWKKDLLRSKNVTVIEYEADYSKAVEE 222
Cdd:PRK08329 107 VVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEE 166
|
|
| |
