|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
1-325 |
0e+00 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 593.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 1 MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVH 80
Cdd:PRK14045 1 MHPKVDALLSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 81 SNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGAS 160
Cdd:PRK14045 81 SNHAFVTGLAAKKLGLDAVLVLRGKEELKGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAEELKGEGRKPYIIPPGGAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 161 PIGTLGYVRAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAEL 237
Cdd:PRK14045 161 PVGTLGYVRAVGEIATQVKklgVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 238 LGVKVEV-RPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFH 316
Cdd:PRK14045 241 LGVKVKVqEPELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELGEKILFIHTGGISGTFH 320
|
....*....
gi 499186629 317 YGDKLLSLL 325
Cdd:PRK14045 321 YGDKMLSLL 329
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
15-321 |
4.65e-169 |
|
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).
Pssm-ID: 273533 [Multi-domain] Cd Length: 318 Bit Score: 472.37 E-value: 4.65e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 15 VELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKL 94
Cdd:TIGR01275 1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 95 GLDAILVLR-------GKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGY 167
Cdd:TIGR01275 81 GLHCVLLLRnpigttaENYLLNGNLLLDDLFGAETRIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 168 VRAVGEIATQ--SEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKV-EV 244
Cdd:TIGR01275 161 VEAALEIAQQleSEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVsAV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499186629 245 RPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEK-ILFIHTGGISGTFHYGDKL 321
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDKpILFIHTGGIPGLFAYHDHL 318
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
22-310 |
7.18e-138 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 392.94 E-value: 7.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 22 TPIQYLPNISREIG--ADVYIKRDDLT-GLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDA 98
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 99 ILVLRGKE-------ELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGA-SPIGTLGYVRA 170
Cdd:cd06449 81 VLVQENWVpysdavyDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 171 VGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLI--KEAAELLGVKVEVR 245
Cdd:cd06449 161 VLEIAQQEEelgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAqaKLAEEGLEVKEEDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499186629 246 PELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGE--LGEKILFIHTGG 310
Cdd:cd06449 241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEfkEGSKVLFIHLGG 307
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
11-319 |
3.62e-135 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 386.46 E-value: 3.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 11 KFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLA 90
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 91 AKKLGLDAILVLRGKE--ELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYV 168
Cdd:COG2515 81 AAKLGLKCVLVLRGEEptPLNGNLLLDRLLGAELHFVSRGEYRDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGALGYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 169 RAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVR 245
Cdd:COG2515 161 EAAAELAAQLAelgVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGLVSRAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499186629 246 PEL-YDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGEL--GEKILFIHTGGISGTFHYGD 319
Cdd:COG2515 241 IELdDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFppGSRVLFIHTGGLPGLFGYAE 317
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
15-309 |
8.12e-44 |
|
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: 152.08 E-value: 8.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 15 VELIPWETPIQYLPNISREIGADVYIKRDDLTGLGigGNKIRKLEYLLGDALS-KGADVVITVGAvhSNHAFVTGLAAKK 93
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTG--SFKDRGALNLLLRLKEgEGGKTVVEASS--GNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 94 LGLDAILVLRGKEElKGNYLLDKIMGIETRVYDAkdSFELmkyAEEIAEELKREGRKPYVIPPGGaSPIGTLGYVRAVGE 173
Cdd:pfam00291 77 LGLKVTIVVPEDAP-PGKLLLMRALGAEVVLVGG--DYDE---AVAAARELAAEGPGAYYINQYD-NPLNIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 174 IATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI------AVGRFGEVMTSKLDNLIKEAAELLGVKVEVRP- 246
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGVGDEPGAl 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499186629 247 --ELYDYSFGE-YGKITGEVAQIIRKVGTREGIILDPvYTGKAFYGLvDLARKGELGEK--ILFIHTG 309
Cdd:pfam00291 230 alDLLDEYVGEvVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGdrVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
1-325 |
0e+00 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 593.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 1 MHPKIFALLAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVH 80
Cdd:PRK14045 1 MHPKVDALLSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 81 SNHAFVTGLAAKKLGLDAILVLRGKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGAS 160
Cdd:PRK14045 81 SNHAFVTGLAAKKLGLDAVLVLRGKEELKGNYLLDKIMGIETRVYEAKDSFELMKYAEEVAEELKGEGRKPYIIPPGGAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 161 PIGTLGYVRAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAEL 237
Cdd:PRK14045 161 PVGTLGYVRAVGEIATQVKklgVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 238 LGVKVEV-RPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEKILFIHTGGISGTFH 316
Cdd:PRK14045 241 LGVKVKVqEPELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELGEKILFIHTGGISGTFH 320
|
....*....
gi 499186629 317 YGDKLLSLL 325
Cdd:PRK14045 321 YGDKMLSLL 329
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
15-321 |
4.65e-169 |
|
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).
Pssm-ID: 273533 [Multi-domain] Cd Length: 318 Bit Score: 472.37 E-value: 4.65e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 15 VELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKL 94
Cdd:TIGR01275 1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 95 GLDAILVLR-------GKEELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGY 167
Cdd:TIGR01275 81 GLHCVLLLRnpigttaENYLLNGNLLLDDLFGAETRIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 168 VRAVGEIATQ--SEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKV-EV 244
Cdd:TIGR01275 161 VEAALEIAQQleSEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVsAV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499186629 245 RPELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGELGEK-ILFIHTGGISGTFHYGDKL 321
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDKpILFIHTGGIPGLFAYHDHL 318
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
22-310 |
7.18e-138 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 392.94 E-value: 7.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 22 TPIQYLPNISREIG--ADVYIKRDDLT-GLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLAAKKLGLDA 98
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 99 ILVLRGKE-------ELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGA-SPIGTLGYVRA 170
Cdd:cd06449 81 VLVQENWVpysdavyDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 171 VGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLI--KEAAELLGVKVEVR 245
Cdd:cd06449 161 VLEIAQQEEelgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAqaKLAEEGLEVKEEDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499186629 246 PELYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGE--LGEKILFIHTGG 310
Cdd:cd06449 241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEfkEGSKVLFIHLGG 307
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
11-319 |
3.62e-135 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 386.46 E-value: 3.62e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 11 KFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTGLA 90
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 91 AKKLGLDAILVLRGKE--ELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYV 168
Cdd:COG2515 81 AAKLGLKCVLVLRGEEptPLNGNLLLDRLLGAELHFVSRGEYRDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGALGYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 169 RAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELLGVKVEVR 245
Cdd:COG2515 161 EAAAELAAQLAelgVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGLVSRAD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499186629 246 PEL-YDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGEL--GEKILFIHTGGISGTFHYGD 319
Cdd:COG2515 241 IELdDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFppGSRVLFIHTGGLPGLFGYAE 317
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
9-321 |
1.56e-131 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 377.63 E-value: 1.56e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 9 LAKFPRVELIPWETPIQYLPNISREIGADVYIKRDDLTGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAFVTG 88
Cdd:PRK03910 3 LARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 89 LAAKKLGLDAILVLRGKEELK-------GNYLLDKIMGIETRVYDAKDsfELMKYAEEIAEELKREGRKPYVIPPGGASP 161
Cdd:PRK03910 83 AAAAKLGLKCVLLLENPVPTEaenylanGNVLLDDLFGAEIHVVPAGT--DMDAQLEELAEELRAQGRRPYVIPVGGSNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 162 IGTLGYVRAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNLIKEAAELL 238
Cdd:PRK03910 161 LGALGYVACALEIAQQLAeggVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 239 GVKVEVRPE---LYDYSFGE-YGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGEL--GEKILFIHTGGIS 312
Cdd:PRK03910 241 GLPTEIPRAdirLWDDYVGPgYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFkkGGNVLFIHTGGAP 320
|
....*....
gi 499186629 313 GTFHYGDKL 321
Cdd:PRK03910 321 ALFAYADAF 329
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
9-310 |
1.40e-63 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 204.50 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 9 LAKFPRVELIPWETPIQYLPNISREIG--ADVYIKRDDL-TGLGIGGNKIRKLEYLLGDALSKGADVVITVGAVHSNHAF 85
Cdd:PRK12390 3 LQKFPRYPLTFGPTPIHPLKRLSAHLGgkVELYAKREDCnSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 86 VTGLAAKKLGLDAILVlrgKE----------ELKGNYLLDKIMGIETRVYDAKDSFELMKYAEEIAEELKREGRKPYVIp 155
Cdd:PRK12390 83 QVAAVAAHLGMKCVLV---QEnwvnyedavyDRVGNILLSRIMGADVRLVPDGFDIGIRKSWEDALEDVRAAGGKPYAI- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 156 PGGAS--PIGTLGYVRAVGEIATQSE---VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAVGRFGEVMTSKLDNL 230
Cdd:PRK12390 159 PAGASdhPLGGLGFVGFAEEVRAQEAelgFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 231 IKEAAELLGVKVEVRPE----LYDYSFGEYGKITGEVAQIIRKVGTREGIILDPVYTGKAFYGLVDLARKGEL--GEKIL 304
Cdd:PRK12390 239 ARNTAELVELGRDITEDdvvlDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFpeGSKVL 318
|
....*.
gi 499186629 305 FIHTGG 310
Cdd:PRK12390 319 YAHLGG 324
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
15-309 |
8.12e-44 |
|
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: 152.08 E-value: 8.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 15 VELIPWETPIQYLPNISREIGADVYIKRDDLTGLGigGNKIRKLEYLLGDALS-KGADVVITVGAvhSNHAFVTGLAAKK 93
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTG--SFKDRGALNLLLRLKEgEGGKTVVEASS--GNHGRALAAAAAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 94 LGLDAILVLRGKEElKGNYLLDKIMGIETRVYDAkdSFELmkyAEEIAEELKREGRKPYVIPPGGaSPIGTLGYVRAVGE 173
Cdd:pfam00291 77 LGLKVTIVVPEDAP-PGKLLLMRALGAEVVLVGG--DYDE---AVAAARELAAEGPGAYYINQYD-NPLNIEGYGTIGLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 174 IATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI------AVGRFGEVMTSKLDNLIKEAAELLGVKVEVRP- 246
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGVGDEPGAl 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499186629 247 --ELYDYSFGE-YGKITGEVAQIIRKVGTREGIILDPvYTGKAFYGLvDLARKGELGEK--ILFIHTG 309
Cdd:pfam00291 230 alDLLDEYVGEvVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGdrVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
22-310 |
3.34e-34 |
|
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: 125.32 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 22 TPIQYLPNISREIGADVYIKRDDLTGlgIGGNKIRKLEYLLGDALSKGADVVITVGAVHS-NHAFVTGLAAKKLGLDAIL 100
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNP--TGSFKDRGALNLILLAEEEGKLPKGVIIESTGgNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 101 VLrGKEELKGNYLLDKIMGIETRVYDAKdsfelMKYAEEIAEELKREGRKPYVIPPGgASPIGTLGYVRAVGEIATQS-E 179
Cdd:cd00640 79 VM-PEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQF-DNPANIAGQGTIGLEILEQLgG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 180 VKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGiavgrfgevmtskldnlikeaaellgvkveVRPELYDYSfgeygki 259
Cdd:cd00640 152 QKPDAVVVPVGGGGNIAGIARALKELLPNVKVIG------------------------------VEPEVVTVS------- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499186629 260 TGEVAQIIRKVGTREGIILDPVyTGKAFYGLVDLARKGELGEKILFIHTGG 310
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPS-SAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
14-214 |
1.98e-12 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 67.51 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 14 RVELIPWETPIQYLPNISREIGADVYIKRDDLTglGIGGNKIR----KLEYLLGDALSKGadvVITVGAvhSNHAFVTGL 89
Cdd:PRK12483 30 RVYDVARETPLQRAPNLSARLGNQVLLKREDLQ--PVFSFKIRgaynKMARLPAEQLARG---VITASA--GNHAQGVAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 90 AAKKLGLDAILVL-RGKEELKgnylLDKIMGIETRVYDAKDSF-ELMKYAEEIAEELKREGRKPYVIPPGGASPiGTLGY 167
Cdd:PRK12483 103 AAARLGVKAVIVMpRTTPQLK----VDGVRAHGGEVVLHGESFpDALAHALKLAEEEGLTFVPPFDDPDVIAGQ-GTVAM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499186629 168 vravgEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI 214
Cdd:PRK12483 178 -----EILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGV 219
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
22-306 |
1.08e-10 |
|
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: 61.38 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 22 TPIQYLPNISREIGADVYIKrddLTGLGIGGN-KIRKLEYLLGDALSKGA----DVVI--TVGavhsNhafvTGLA---- 90
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAK---LEFFNPGGSvKDRIALYMIEDAEKRGLlkpgTTIIepTSG----N----TGIGlamv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 91 AKKLGLDAILVLrgkeelkgnyllDKIMGIETR----------VYDAKDSFELMKYAEEIAEELKREGRKpYVIPPGGAS 160
Cdd:cd01561 72 AAAKGYRFIIVM------------PETMSEEKRkllralgaevILTPEAEADGMKGAIAKARELAAETPN-AFWLNQFEN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 161 PIGTLGYVRAVG-EIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIR-----PVGIAVGRFGEVMTSKLDnlikea 234
Cdd:cd01561 139 PANPEAHYETTApEIWEQLDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRivgvdPVGSVLFSGGPPGPHKIE------ 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499186629 235 aellGVKVEVRPELYDYSFG-EYGKITGEVA-QIIRKVGTREGIILDPVyTGKAFYGLVDLARKGELGEKILFI 306
Cdd:cd01561 213 ----GIGAGFIPENLDRSLIdEVVRVSDEEAfAMARRLAREEGLLVGGS-SGAAVAAALKLAKRLGPGKTIVTI 281
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
21-214 |
2.14e-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: 60.58 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDLTglGIGGNKIR----KLEYLLGDALSKGadvVITVGAvhSNHAFVTGLAAKKLGL 96
Cdd:cd01562 17 RTPLLTSPTLSELLGAEVYLKCENLQ--KTGSFKIRgaynKLLSLSEEERAKG---VVAASA--GNHAQGVAYAAKLLGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 97 DAILVL-RGKEELKgnylLDKI--MGIETRVYDAkDSFELMKYAEEIAEElkrEGRK-------PYVIppGGAspiGTLG 166
Cdd:cd01562 90 PATIVMpETAPAAK----VDATraYGAEVVLYGE-DFDEAEAKARELAEE---EGLTfihpfddPDVI--AGQ---GTIG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499186629 167 YvravgEIATQSEvKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI 214
Cdd:cd01562 157 L-----EILEQVP-DLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGV 198
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
21-214 |
1.04e-09 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 59.38 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDLTGlgIGGNKIR----KLEYLLGDALSKGadvVITVGAvhSNHAFVTGLAAKKLGL 96
Cdd:PRK09224 20 ETPLEKAPKLSARLGNQVLLKREDLQP--VFSFKLRgaynKMAQLTEEQLARG---VITASA--GNHAQGVALSAARLGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 97 DAILVL-RGKEELKgnylLDKIMGIETRVYDAKDSF-ELMKYAEEIAEElkrEGR-------KPYVIppGGAspiGTLGY 167
Cdd:PRK09224 93 KAVIVMpVTTPDIK----VDAVRAFGGEVVLHGDSFdEAYAHAIELAEE---EGLtfihpfdDPDVI--AGQ---GTIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499186629 168 vravgEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI 214
Cdd:PRK09224 161 -----EILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGV 202
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
21-214 |
1.41e-09 |
|
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: 58.12 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDL--TG----LGiGGNKIRKLEyllGDALSKGadvVITvgavHS--NHAFVTGLAAK 92
Cdd:COG1171 24 RTPLLRSPTLSERLGAEVYLKLENLqpTGsfklRG-AYNALASLS---EEERARG---VVA----ASagNHAQGVAYAAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 93 KLGLDAILVL-RGKEELKgnylLDKI--MGIETRVYDakDSF-ELMKYAEEIAEElkrEGRkpYVIPPGGASPI----GT 164
Cdd:COG1171 93 LLGIPATIVMpETAPAVK----VAATraYGAEVVLHG--DTYdDAEAAAAELAEE---EGA--TFVHPFDDPDViagqGT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499186629 165 LGYvravgEIATQSEvKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI 214
Cdd:COG1171 162 IAL-----EILEQLP-DLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGV 205
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
21-279 |
4.61e-09 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 56.62 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDLTglGIGGNKIR----KLEYLLGDALSKGadvVITvgAVHSNHAFVTGLAAKKLGL 96
Cdd:PRK06815 20 VTPLEHSPLLSQHTGCEVYLKCEHLQ--HTGSFKFRgasnKLRLLNEAQRQQG---VIT--ASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 97 DA-ILVLRGKEELKgnylLDKI--MGIETRVYDAkDSFELMKYAEEIAEElkrEGrKPYVIP---PGGASPIGTLGYvra 170
Cdd:PRK06815 93 PVtVYAPEQASAIK----LDAIraLGAEVRLYGG-DALNAELAARRAAEQ---QG-KVYISPyndPQVIAGQGTIGM--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 171 vgEIATQSEvKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGIAvGRFGEVMTSKLdnlikEAAELlgVKVEVRPELYD 250
Cdd:PRK06815 161 --ELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCW-PANSPSLYTSL-----EAGEI--VEVAEQPTLSD 229
|
250 260 270
....*....|....*....|....*....|...
gi 499186629 251 YSFG--EYGKITGEVAQ--IIRKVGTREGIILD 279
Cdd:PRK06815 230 GTAGgvEPGAITFPLCQqlIDQKVLVSEEEIKE 262
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
21-214 |
2.53e-08 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 55.31 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDLTglGIGGNKIR----KLEYLLGDALSKGadvVITVGAvhSNHAFVTGLAAKKLGL 96
Cdd:PLN02550 109 ESPLQLAKKLSERLGVKVLLKREDLQ--PVFSFKLRgaynMMAKLPKEQLDKG---VICSSA--GNHAQGVALSAQRLGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 97 DAILVLR-GKEELKGNYlLDKIMGIETRVYDAKDsfELMKYAEEIAEElkrEGRKpyVIPPGGASPI----GTLGYvrav 171
Cdd:PLN02550 182 DAVIAMPvTTPEIKWQS-VERLGATVVLVGDSYD--EAQAYAKQRALE---EGRT--FIPPFDHPDViagqGTVGM---- 249
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499186629 172 gEIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIRPVGI 214
Cdd:PLN02550 250 -EIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGV 291
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
116-212 |
7.04e-05 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 44.08 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 116 KIMGIETRVYDA---KDSFELMKYAEEIAEELKREGRKPYVIPPGGASPIGTLGYVRAVG-EIATQSEVKFDSIVVAAGS 191
Cdd:PRK10717 107 RALGAELVLVPAapyANPNNYVKGAGRLAEELVASEPNGAIWANQFDNPANREAHYETTGpEIWEQTDGKVDGFVCAVGT 186
|
90 100
....*....|....*....|.
gi 499186629 192 GGTLAGLSLGLSILNEDIRPV 212
Cdd:PRK10717 187 GGTLAGVSRYLKETNPKVKIV 207
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
21-199 |
3.28e-04 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 42.10 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 21 ETPIQYLPNISREIGADVYIKRDDLTGL---GIGG--NKIRKLEyllGDALSKGadvviTVGAVHSNHAFVTGLAAKKLG 95
Cdd:PRK08639 25 ETPLQRNDYLSEKYGANVYLKREDLQPVrsyKLRGayNAISQLS---DEELAAG-----VVCASAGNHAQGVAYACRHLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499186629 96 LDAILVL--------RGKEELKGNYLLDKIMGIETrvYDakDSF-ELMKYAEEiaeelkrEGRkpYVIPPGGASPI---- 162
Cdd:PRK08639 97 IPGVIFMpvttpqqkIDQVRFFGGEFVEIVLVGDT--FD--DSAaAAQEYAEE-------TGA--TFIPPFDDPDViagq 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 499186629 163 GTLGYvravgEIATQ--SEVKFDSIVVAAGSGGTLAGLS 199
Cdd:PRK08639 164 GTVAV-----EILEQleKEGSPDYVFVPVGGGGLISGVT 197
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
173-210 |
5.96e-03 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 38.05 E-value: 5.96e-03
10 20 30
....*....|....*....|....*....|....*...
gi 499186629 173 EIATQSEVKFDSIVVAAGSGGTLAGLSLGLSILNEDIR 210
Cdd:PLN02356 242 EIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIK 279
|
|
| |
