|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
6-330 |
3.75e-172 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 480.87 E-value: 3.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 6 LNRFERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTA 85
Cdd:PRK03910 3 LARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 86 ALAAKMGLACVALLENPIDTQEQNYLHNGNRLLLDLFGTRVEHVDNLEEPDLLLMAKADRLRATGKTPYVIPIGGSNALG 165
Cdd:PRK03910 83 AAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNALG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 166 TLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGV 245
Cdd:PRK03910 163 ALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELLGL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 246 -NVPENLDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGGAPAL 324
Cdd:PRK03910 243 pTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAPAL 322
|
....*.
gi 333115865 325 FAYQSL 330
Cdd:PRK03910 323 FAYADA 328
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
8-329 |
1.74e-136 |
|
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: 389.92 E-value: 1.74e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 8 RFERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAAL 87
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 88 AAKMGLACVALLENPIDTQeqnylHNGNRLLLDLFGTRVEHVDNLEEPDL--LLMAKADRLRATGKTPYVIPIGGSNALG 165
Cdd:COG2515 81 AAKLGLKCVLVLRGEEPTP-----LNGNLLLDRLLGAELHFVSRGEYRDRdeAMEAVAAELRARGGKPYVIPEGGSNPLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 166 TLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGV 245
Cdd:COG2515 156 ALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 246 NVPENldIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGGAPALF 325
Cdd:COG2515 236 VSRAD--IELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLF 313
|
....
gi 333115865 326 AYQS 329
Cdd:COG2515 314 GYAE 317
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
12-327 |
7.93e-132 |
|
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: 378.38 E-value: 7.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 12 LELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAALAAKM 91
Cdd:TIGR01275 1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 92 GLACVALLENPIDTQEQNYLHNGNRLLLDLFGT--RVEHVDNLEEPDLLLMAKADRLRATGKTPYVIPIGGSNALGTLGY 169
Cdd:TIGR01275 81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAetRIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 170 VKAGLEFAEQV-TAKGLDSgtLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGVNVP 248
Cdd:TIGR01275 161 VEAALEIAQQLeSEVKFDS--IVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVS 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333115865 249 EnlDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEgKPIVFLHTGGAPALFAY 327
Cdd:TIGR01275 239 A--VIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGD-KPILFIHTGGIPGLFAY 314
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
19-320 |
1.14e-114 |
|
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: 334.39 E-value: 1.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVG--RDIYVKRDDLT-LFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAALAAKMGLAC 95
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 96 VALLENPIDTQEQNYLHNGNRLLLDLFGTRVEHVDNLEEPDLLLMAK--ADRLRATGKTPYVIPIGGS-NALGTLGYVKA 172
Cdd:cd06449 81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEeaAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 173 GLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGVNVPENlD 252
Cdd:cd06449 161 VLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEE-D 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333115865 253 IELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGG 320
Cdd:cd06449 240 VVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
19-319 |
1.73e-48 |
|
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: 164.41 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVGRDIYVKRDDLTlfALGGNKARKLEYLgCDALAQHADTLITAGAIQSNHVRQTAALAAKMGLACVAL 98
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLN--PTGSFKDRGALNL-LLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 99 LenPIDTqeqnylHNGNRLLLDLFGTRVEHVD-NLEEPdlllMAKADRLRATGKTPYVIPiGGSNALGTLGYVKAGLEFA 177
Cdd:pfam00291 85 V--PEDA------PPGKLLLMRALGAEVVLVGgDYDEA----VAAARELAAEGPGAYYIN-QYDNPLNIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 178 EQVtakGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGI------TVSRPADLQRPKVMGLVQRTAELLGV-NVPEN 250
Cdd:pfam00291 152 EQL---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGVgDEPGA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333115865 251 LDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPvYTGKAFAGlLDGVQKGAFEEGKPIVFLHTG 319
Cdd:pfam00291 229 LALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAA-LKLALAGELKGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
6-330 |
3.75e-172 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 480.87 E-value: 3.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 6 LNRFERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTA 85
Cdd:PRK03910 3 LARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 86 ALAAKMGLACVALLENPIDTQEQNYLHNGNRLLLDLFGTRVEHVDNLEEPDLLLMAKADRLRATGKTPYVIPIGGSNALG 165
Cdd:PRK03910 83 AAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNALG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 166 TLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGV 245
Cdd:PRK03910 163 ALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELLGL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 246 -NVPENLDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGGAPAL 324
Cdd:PRK03910 243 pTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAPAL 322
|
....*.
gi 333115865 325 FAYQSL 330
Cdd:PRK03910 323 FAYADA 328
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
8-329 |
1.74e-136 |
|
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: 389.92 E-value: 1.74e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 8 RFERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAAL 87
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 88 AAKMGLACVALLENPIDTQeqnylHNGNRLLLDLFGTRVEHVDNLEEPDL--LLMAKADRLRATGKTPYVIPIGGSNALG 165
Cdd:COG2515 81 AAKLGLKCVLVLRGEEPTP-----LNGNLLLDRLLGAELHFVSRGEYRDRdeAMEAVAAELRARGGKPYVIPEGGSNPLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 166 TLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGV 245
Cdd:COG2515 156 ALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 246 NVPENldIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGGAPALF 325
Cdd:COG2515 236 VSRAD--IELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLF 313
|
....
gi 333115865 326 AYQS 329
Cdd:COG2515 314 GYAE 317
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
12-327 |
7.93e-132 |
|
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: 378.38 E-value: 7.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 12 LELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAALAAKM 91
Cdd:TIGR01275 1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 92 GLACVALLENPIDTQEQNYLHNGNRLLLDLFGT--RVEHVDNLEEPDLLLMAKADRLRATGKTPYVIPIGGSNALGTLGY 169
Cdd:TIGR01275 81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAetRIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 170 VKAGLEFAEQV-TAKGLDSgtLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGVNVP 248
Cdd:TIGR01275 161 VEAALEIAQQLeSEVKFDS--IVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVS 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333115865 249 EnlDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEgKPIVFLHTGGAPALFAY 327
Cdd:TIGR01275 239 A--VIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGD-KPILFIHTGGIPGLFAY 314
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
19-320 |
1.14e-114 |
|
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: 334.39 E-value: 1.14e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVG--RDIYVKRDDLT-LFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTAALAAKMGLAC 95
Cdd:cd06449 1 TPIQYLPRLSEHLGgkVEIYAKRDDCNsGLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 96 VALLENPIDTQEQNYLHNGNRLLLDLFGTRVEHVDNLEEPDLLLMAK--ADRLRATGKTPYVIPIGGS-NALGTLGYVKA 172
Cdd:cd06449 81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEeaAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 173 GLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAELLGVNVPENlD 252
Cdd:cd06449 161 VLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEE-D 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333115865 253 IELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVFLHTGG 320
Cdd:cd06449 240 VVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
6-327 |
1.66e-87 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 265.98 E-value: 1.66e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 6 LNRFERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHVRQTA 85
Cdd:PRK14045 9 LSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 86 ALAAKMGLACVALLENPIDTQeqnylhnGNRLLLDLFG--TRVEHVDNLEEpdLLLMAK--ADRLRATGKTPYVIPIGGS 161
Cdd:PRK14045 89 LAAKKLGLDAVLVLRGKEELK-------GNYLLDKIMGieTRVYEAKDSFE--LMKYAEevAEELKGEGRKPYIIPPGGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 162 NALGTLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQRTAE 241
Cdd:PRK14045 160 SPVGTLGYVRAVGEIATQVKKLGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 242 LLGVNVpENLDIELWDDYYGpRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGafEEGKPIVFLHTGGA 321
Cdd:PRK14045 240 LLGVKV-KVQEPELYDYSFG-EYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKG--ELGEKILFIHTGGI 315
|
....*.
gi 333115865 322 PALFAY 327
Cdd:PRK14045 316 SGTFHY 321
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
5-330 |
1.20e-85 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 261.50 E-value: 1.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 5 ALNRFERLELVPHATPLQHLLRLSHHVGR--DIYVKRDDL-TLFALGGNKARKLEYLGCDALAQHADTLITAGAIQSNHV 81
Cdd:PRK12390 2 NLQKFPRYPLTFGPTPIHPLKRLSAHLGGkvELYAKREDCnSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 82 RQTAALAAKMGLACVALLENPIDTQEQNYLHNGNRLLLDLFGTRVEHVD---NLEEPDLLLMAKADrLRATGKTPYVIPI 158
Cdd:PRK12390 82 RQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPdgfDIGIRKSWEDALED-VRAAGGKPYAIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 159 GGS-NALGTLGYVKAGLEFAEQVTAKGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVMGLVQ 237
Cdd:PRK12390 161 GASdHPLGGLGFVGFAEEVRAQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 238 RTAEL--LGVNVPENlDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPVYTGKAFAGLLDGVQKGAFEEGKPIVF 315
Cdd:PRK12390 241 NTAELveLGRDITED-DVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLY 319
|
330
....*....|....*
gi 333115865 316 LHTGGAPALFAYQSL 330
Cdd:PRK12390 320 AHLGGVPALNAYSFL 334
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
19-319 |
1.73e-48 |
|
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: 164.41 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVGRDIYVKRDDLTlfALGGNKARKLEYLgCDALAQHADTLITAGAIQSNHVRQTAALAAKMGLACVAL 98
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLN--PTGSFKDRGALNL-LLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 99 LenPIDTqeqnylHNGNRLLLDLFGTRVEHVD-NLEEPdlllMAKADRLRATGKTPYVIPiGGSNALGTLGYVKAGLEFA 177
Cdd:pfam00291 85 V--PEDA------PPGKLLLMRALGAEVVLVGgDYDEA----VAAARELAAEGPGAYYIN-QYDNPLNIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 178 EQVtakGLDSGTLVLASGSGATHAGLALALAHVLPEWRVLGI------TVSRPADLQRPKVMGLVQRTAELLGV-NVPEN 250
Cdd:pfam00291 152 EQL---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGVgDEPGA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333115865 251 LDIELWDDYYGPRYGEPNTGTLDAIRLLASSQGLLLDPvYTGKAFAGlLDGVQKGAFEEGKPIVFLHTG 319
Cdd:pfam00291 229 LALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAA-LKLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
19-320 |
1.26e-26 |
|
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: 105.29 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVGRDIYVKRDDLTlfALGGNKARKLEYLGCDALAQ---HADTLITAGAiqSNHVRQTAALAAKMGLAC 95
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLN--PTGSFKDRGALNLILLAEEEgklPKGVIIESTG--GNTGIALAAAAARLGLKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 96 VALLenPIDTQEqnylhnGNRLLLDLFGTRVEHVD-NLEEpdllLMAKADRLRATGKTPYVIPiGGSNALGTLGYVKAGL 174
Cdd:cd00640 77 TIVM--PEGASP------EKVAQMRALGAEVVLVPgDFDD----AIALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 175 EFAEQVTAKGLDsgTLVLASGSGATHAGLALALAHVLPEWRVLGItvsrpadlqrpkvmglvqrtaellgvnvpENLDIE 254
Cdd:cd00640 144 EILEQLGGQKPD--AVVVPVGGGGNIAGIARALKELLPNVKVIGV-----------------------------EPEVVT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333115865 255 LWDDyygprygepntGTLDAIRLLASSQGLLLDPVyTGKAFAGLLDGVQKGafEEGKPIVFLHTGG 320
Cdd:cd00640 193 VSDE-----------EALEAIRLLAREEGILVEPS-SAAALAAALKLAKKL--GKGKTVVVILTGG 244
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
10-320 |
1.83e-05 |
|
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: 45.56 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 10 ERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLTL---FALGG--NKARKLEYlgcdalAQHADTLITAGAiqSNHVrQT 84
Cdd:cd01562 9 ARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKtgsFKIRGayNKLLSLSE------EERAKGVVAASA--GNHA-QG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 85 AALAAKM-GLACVALLenPIDTQEQ---NYLHNGnrllldlfGTRVEHVDNLEEpdllLMAKADRL-RATGKTpYVIP-- 157
Cdd:cd01562 80 VAYAAKLlGIPATIVM--PETAPAAkvdATRAYG--------AEVVLYGEDFDE----AEAKARELaEEEGLT-FIHPfd 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 158 ----IGGsnaLGTLgyvkaGLEFAEQVtaKGLDsgTLVLASGSGATHAGLALALAHVLPEWRVLGITVSRPADLQRPKVM 233
Cdd:cd01562 145 dpdvIAG---QGTI-----GLEILEQV--PDLD--AVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 234 GLVQRTAELL----GVNVP----ENLDI--ELWDDYYGPRYGEpntgTLDAIRLLASSQGLLLDPvyTGK-AFAGLLdgv 302
Cdd:cd01562 213 GKPVTLPEVDtiadGLAVKrpgeLTFEIirKLVDDVVTVSEDE----IAAAMLLLFEREKLVAEP--AGAlALAALL--- 283
|
330
....*....|....*...
gi 333115865 303 QKGAFEEGKPIVFLHTGG 320
Cdd:cd01562 284 SGKLDLKGKKVVVVLSGG 301
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
19-316 |
4.68e-04 |
|
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: 41.35 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVGRDIYVKrddLTLFALGGN-KARKLEYLGCDALAQ----HADTLI--TAG----AIqsnhvrqtAAL 87
Cdd:cd01561 3 TPLVRLNRLSPGTGAEIYAK---LEFFNPGGSvKDRIALYMIEDAEKRgllkPGTTIIepTSGntgiGL--------AMV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 88 AAKMGLACVALLenPiDTQEQnylhnGNRLLLDLFGTRVEHVDNLEEPDLL-LMAKADRLRATGKTpYVIPIGGSNALGT 166
Cdd:cd01561 72 AAAKGYRFIIVM--P-ETMSE-----EKRKLLRALGAEVILTPEAEADGMKgAIAKARELAAETPN-AFWLNQFENPANP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 167 LGYVKA-GLEFAEQvTAKGLDsgTLVLASGSGATHAGLALALAHVLPEWRVLG------ITVSRPADLQRpKVMGlvqrt 239
Cdd:cd01561 143 EAHYETtAPEIWEQ-LDGKVD--AFVAGVGTGGTITGVARYLKEKNPNVRIVGvdpvgsVLFSGGPPGPH-KIEG----- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 240 aelLGVN-VPENLDIELWDDYYGprygepnTGTLDAI---RLLASSQGLLLDPVyTGKAFAGLLDgVQKgAFEEGKPIVF 315
Cdd:cd01561 214 ---IGAGfIPENLDRSLIDEVVR-------VSDEEAFamaRRLAREEGLLVGGS-SGAAVAAALK-LAK-RLGPGKTIVT 280
|
.
gi 333115865 316 L 316
Cdd:cd01561 281 I 281
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
19-319 |
2.00e-03 |
|
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: 39.80 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHVGRDIYVKRddltlfaLGGN-----KARKLEYLGCDALAQHADTLITA--GaiqsNHVRQTAALAAKM 91
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKE-------EGHNptgsfKDRAMQVAVSLALERGAKTIVCAssG----NGSAALAAYAARA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 92 GLACVALLenPidtqeQNYLHNGNRLLLDLFGTRVEHVD-NLEepDLLLMAKAdrlrATGKTPYViPIGGSNALGTLGYV 170
Cdd:COG0498 136 GIEVFVFV--P-----EGKVSPGQLAQMLTYGAHVIAVDgNFD--DAQRLVKE----LAADEGLY-AVNSINPARLEGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 171 KAGLEFAEQVTAKGlDsgTLVLASGSGathaGLALALAHVLPEWRVLGITVSRPadlqrpKVMG--------LVQRTAEL 242
Cdd:COG0498 202 TYAFEIAEQLGRVP-D--WVVVPTGNG----GNILAGYKAFKELKELGLIDRLP------RLIAvqatgcnpILTAFETG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 243 LGVNVPEN-------LDIELwddyygPRYGE----------------PNTGTLDAIRLLASSQGLLLDPvYTGKAFAGLL 299
Cdd:COG0498 269 RDEYEPERpetiapsMDIGN------PSNGEralfalresggtavavSDEEILEAIRLLARREGIFVEP-ATAVAVAGLR 341
|
330 340
....*....|....*....|
gi 333115865 300 DGVQKGAFEEGKPIVFLHTG 319
Cdd:COG0498 342 KLREEGEIDPDEPVVVLSTG 361
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
10-43 |
3.88e-03 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 38.63 E-value: 3.88e-03
10 20 30
....*....|....*....|....*....|....
gi 333115865 10 ERLELVPHATPLQHLLRLSHHVGRDIYVKRDDLT 43
Cdd:PRK08639 17 KRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQ 50
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
19-96 |
4.28e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 38.69 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333115865 19 TPLQHLLRLSHHV-GRDIYVKRDDLTlfALGgnkARKLEY-LGCDALAQH-------ADTlitaGAIQsnHVRQTAALAA 89
Cdd:PRK13028 63 TPLYHAKRLSEELgGAQIYLKREDLN--HTG---AHKINNcLGQALLAKRmgkkrliAET----GAGQ--HGVATATAAA 131
|
....*..
gi 333115865 90 KMGLACV 96
Cdd:PRK13028 132 LFGLECE 138
|
|
| |
