|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
1-331 |
0e+00 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 572.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 1 MNLAKFPRKKYTESYTPIEKLNNFSEVLGgPTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCR 80
Cdd:PRK03910 1 MNLARFPRLELAGLPTPLEPLPRLSAALG-PDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 81 LTLAAAVKEKMKCILVLEEGL-EPEEKPDFNGNYFLYHLLGAEnVIVVPNGADLMEEMHKVAKEVSEKGNTPYVIPVGGS 159
Cdd:PRK03910 80 QTAAAAAKLGLKCVLLLENPVpTEAENYLANGNVLLDDLFGAE-IHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 160 NPTGAMGYIACAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSA 239
Cdd:PRK03910 159 NALGALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 240 HVGIPNSISREAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGG 319
Cdd:PRK03910 239 LLGLPTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGG 318
|
330
....*....|..
gi 764649295 320 SPALYANTSLFA 331
Cdd:PRK03910 319 APALFAYADAFA 330
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
5-325 |
5.33e-155 |
|
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: 436.92 E-value: 5.33e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 5 KFPRKKYTESYTPIEKLNNFSEVLGgPTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLA 84
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALG-VELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 85 AAVKEKMKCILVLEEglepEEKPDFNGNYFLYHLLGAEnVIVVPNGA--DLMEEMHKVAKEVSEKGNTPYVIPVGGSNPT 162
Cdd:COG2515 80 AAAKLGLKCVLVLRG----EEPTPLNGNLLLDRLLGAE-LHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 163 GAMGYIACAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVG 242
Cdd:COG2515 155 GALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 243 IpnsISREAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGGSPA 322
Cdd:COG2515 235 L---VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPG 311
|
...
gi 764649295 323 LYA 325
Cdd:COG2515 312 LFG 314
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
16-325 |
1.15e-108 |
|
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: 319.45 E-value: 1.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGpTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLAAAVKEKMKCIL 95
Cdd:TIGR01275 8 TPIQYLPRLSDYLGR-EIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLHCVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 96 VLEEG-LEPEEKPDFNGNYFLYHLLGAENVIVVPNG-ADLMEEMHKVAKEVSEKGNTPYVIPVGGSNPTGAMGYIACAQE 173
Cdd:TIGR01275 87 LLRNPiGTTAENYLLNGNLLLDDLFGAETRIESCEEyTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGYVEAALE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 174 ImAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVGIPNSISREAVt 253
Cdd:TIGR01275 167 I-AQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAVIPLW- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764649295 254 cfDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNkEDNILFVHSGGSPALYA 325
Cdd:TIGR01275 245 --DDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFG-DKPILFIHTGGIPGLFA 313
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
16-319 |
3.23e-105 |
|
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: 310.12 E-value: 3.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGPT-IYFKRDDLLGLTA-GGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLAAAVKEKMKC 93
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVeIYAKRDDCNSGLAfGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 94 ILVLEEGLE-PEEKPDFNGNYFLYHLLGAEnVIVVPNGAD--LMEEMHKVAKEVSEKGNTPYVIPVGGS-NPTGAMGYIA 169
Cdd:cd06449 81 VLVQENWVPySDAVYDRVGNILLSRIMGAD-VRLVSAGFDigIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 170 CAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVGIpnSISR 249
Cdd:cd06449 160 FVLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGL--EVKE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 250 EAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGG 319
Cdd:cd06449 238 EDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
16-318 |
2.51e-55 |
|
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: 182.13 E-value: 2.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGPtIYFKRDDLLGLtaGGNKTRKLEFLVADA-QAKGADTLITAGGiqSNHCRLTLAAAVKEKMKCI 94
Cdd:pfam00291 8 TPLVRLPRLSKELGVD-VYLKLESLNPT--GSFKDRGALNLLLRLkEGEGGKTVVEASS--GNHGRALAAAAARLGLKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 95 LVLEEGLEPEekpdfngNYFLYHLLGAEnVIVVPNGADlmeEMHKVAKEVSEKGNTPYVIPVGGsNPTGAMGYIACAQEI 174
Cdd:pfam00291 83 IVVPEDAPPG-------KLLLMRALGAE-VVLVGGDYD---EAVAAARELAAEGPGAYYINQYD-NPLNIEGYGTIGLEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 175 MAQsfeQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGIN------VSRGKAEQEEKVAKLVDETSAHVGIPNSIS 248
Cdd:pfam00291 151 LEQ---LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEpegapaLARSLAAGRPVPVPVADTIADGLGVGDEPG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 249 REAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPvYTGKAVAGLiDLIRKGKFNKEDNILFVHSG 318
Cdd:pfam00291 228 ALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
1-331 |
0e+00 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 572.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 1 MNLAKFPRKKYTESYTPIEKLNNFSEVLGgPTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCR 80
Cdd:PRK03910 1 MNLARFPRLELAGLPTPLEPLPRLSAALG-PDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 81 LTLAAAVKEKMKCILVLEEGL-EPEEKPDFNGNYFLYHLLGAEnVIVVPNGADLMEEMHKVAKEVSEKGNTPYVIPVGGS 159
Cdd:PRK03910 80 QTAAAAAKLGLKCVLLLENPVpTEAENYLANGNVLLDDLFGAE-IHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 160 NPTGAMGYIACAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSA 239
Cdd:PRK03910 159 NALGALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 240 HVGIPNSISREAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGG 319
Cdd:PRK03910 239 LLGLPTEIPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGG 318
|
330
....*....|..
gi 764649295 320 SPALYANTSLFA 331
Cdd:PRK03910 319 APALFAYADAFA 330
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
5-325 |
5.33e-155 |
|
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: 436.92 E-value: 5.33e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 5 KFPRKKYTESYTPIEKLNNFSEVLGgPTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLA 84
Cdd:COG2515 1 RFPRLPLAFLPTPLQPLPRLSAALG-VELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 85 AAVKEKMKCILVLEEglepEEKPDFNGNYFLYHLLGAEnVIVVPNGA--DLMEEMHKVAKEVSEKGNTPYVIPVGGSNPT 162
Cdd:COG2515 80 AAAKLGLKCVLVLRG----EEPTPLNGNLLLDRLLGAE-LHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 163 GAMGYIACAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVG 242
Cdd:COG2515 155 GALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 243 IpnsISREAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGGSPA 322
Cdd:COG2515 235 L---VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPG 311
|
...
gi 764649295 323 LYA 325
Cdd:COG2515 312 LFG 314
|
|
| ACC_deam_rel |
TIGR01275 |
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ... |
16-325 |
1.15e-108 |
|
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: 319.45 E-value: 1.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGpTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLAAAVKEKMKCIL 95
Cdd:TIGR01275 8 TPIQYLPRLSDYLGR-EIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKLGLHCVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 96 VLEEG-LEPEEKPDFNGNYFLYHLLGAENVIVVPNG-ADLMEEMHKVAKEVSEKGNTPYVIPVGGSNPTGAMGYIACAQE 173
Cdd:TIGR01275 87 LLRNPiGTTAENYLLNGNLLLDDLFGAETRIESCEEyTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGYVEAALE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 174 ImAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVGIPNSISREAVt 253
Cdd:TIGR01275 167 I-AQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAVIPLW- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764649295 254 cfDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNkEDNILFVHSGGSPALYA 325
Cdd:TIGR01275 245 --DDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFG-DKPILFIHTGGIPGLFA 313
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
16-319 |
3.23e-105 |
|
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: 310.12 E-value: 3.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGPT-IYFKRDDLLGLTA-GGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLTLAAAVKEKMKC 93
Cdd:cd06449 1 TPIQYLPRLSEHLGGKVeIYAKRDDCNSGLAfGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 94 ILVLEEGLE-PEEKPDFNGNYFLYHLLGAEnVIVVPNGAD--LMEEMHKVAKEVSEKGNTPYVIPVGGS-NPTGAMGYIA 169
Cdd:cd06449 81 VLVQENWVPySDAVYDRVGNILLSRIMGAD-VRLVSAGFDigIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 170 CAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHVGIpnSISR 249
Cdd:cd06449 160 FVLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGL--EVKE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 250 EAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDNILFVHSGG 319
Cdd:cd06449 238 EDVVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
1-330 |
5.39e-96 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 287.70 E-value: 5.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 1 MNLAKFPRKKYTESYTPIEKLNNFSEVLGGPT-IYFKRDDL-LGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNH 78
Cdd:PRK12390 1 MNLQKFPRYPLTFGPTPIHPLKRLSAHLGGKVeLYAKREDCnSGLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 79 CRLTLAAAVKEKMKCILVlEEGLEPEEKP--DFNGNYFLYHLLGAEnVIVVPNGAD--LMEEMHKVAKEVSEKGNTPYVI 154
Cdd:PRK12390 81 TRQVAAVAAHLGMKCVLV-QENWVNYEDAvyDRVGNILLSRIMGAD-VRLVPDGFDigIRKSWEDALEDVRAAGGKPYAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 155 PVGGS-NPTGAMGYIACAQEIMAQSFEQGIDFSS-VVC-VSGSAgmHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVA 231
Cdd:PRK12390 159 PAGASdHPLGGLGFVGFAEEVRAQEAELGFKFDYiVVCsVTGST--QAGMVVGFAADGRARRVIGIDASAKPEQTRAQVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 232 KLVDETSAHVGIPNSISREAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNKEDN 311
Cdd:PRK12390 237 RIARNTAELVELGRDITEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSK 316
|
330
....*....|....*....
gi 764649295 312 ILFVHSGGSPALYANTSLF 330
Cdd:PRK12390 317 VLYAHLGGVPALNAYSFLF 335
|
|
| PRK14045 |
PRK14045 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
3-324 |
4.50e-75 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 172537 [Multi-domain] Cd Length: 329 Bit Score: 234.01 E-value: 4.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 3 LAKFPRKKYTESYTPIEKLNNFSEVLGGpTIYFKRDDLLGLTAGGNKTRKLEFLVADAQAKGADTLITAGGIQSNHCRLT 82
Cdd:PRK14045 9 LSKFPRVELIPWETPIQYLPNISRELGA-DVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 83 LAAAVKEKMKCILVLEEglepeeKPDFNGNYFLYHLLGAEN-VIVVPNGADLMEEMHKVAKEVSEKGNTPYVIPVGGSNP 161
Cdd:PRK14045 88 GLAAKKLGLDAVLVLRG------KEELKGNYLLDKIMGIETrVYEAKDSFELMKYAEEVAEELKGEGRKPYIIPPGGASP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 162 TGAMGYIACAQEIMAQSFEQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVSRGKAEQEEKVAKLVDETSAHV 241
Cdd:PRK14045 162 VGTLGYVRAVGEIATQVKKLGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKELL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 242 GIPNSISREAVtcFDEYVGPgYALPTPEMVEAVQLLAKTEGILLDPVYTGKAVAGLIDLIRKGKFNkeDNILFVHSGGSP 321
Cdd:PRK14045 242 GVKVKVQEPEL--YDYSFGE-YGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELG--EKILFIHTGGIS 316
|
...
gi 764649295 322 ALY 324
Cdd:PRK14045 317 GTF 319
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
16-318 |
2.51e-55 |
|
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: 182.13 E-value: 2.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGGPtIYFKRDDLLGLtaGGNKTRKLEFLVADA-QAKGADTLITAGGiqSNHCRLTLAAAVKEKMKCI 94
Cdd:pfam00291 8 TPLVRLPRLSKELGVD-VYLKLESLNPT--GSFKDRGALNLLLRLkEGEGGKTVVEASS--GNHGRALAAAAARLGLKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 95 LVLEEGLEPEekpdfngNYFLYHLLGAEnVIVVPNGADlmeEMHKVAKEVSEKGNTPYVIPVGGsNPTGAMGYIACAQEI 174
Cdd:pfam00291 83 IVVPEDAPPG-------KLLLMRALGAE-VVLVGGDYD---EAVAAARELAAEGPGAYYINQYD-NPLNIEGYGTIGLEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 175 MAQsfeQGIDFSSVVCVSGSAGMHAGLITGFSGTQSKIPVIGIN------VSRGKAEQEEKVAKLVDETSAHVGIPNSIS 248
Cdd:pfam00291 151 LEQ---LGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEpegapaLARSLAAGRPVPVPVADTIADGLGVGDEPG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 249 REAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPvYTGKAVAGLiDLIRKGKFNKEDNILFVHSG 318
Cdd:pfam00291 228 ALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
16-319 |
5.41e-32 |
|
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: 119.54 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEvLGGPTIYFKRDDLLglTAGGNKTRKLEFLVADAQAKG---ADTLITAGGiqSNHCRLTLAAAVKEKMK 92
Cdd:cd00640 1 TPLVRLKRLSK-LGGANIYLKLEFLN--PTGSFKDRGALNLILLAEEEGklpKGVIIESTG--GNTGIALAAAAARLGLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 93 CILVLEEGLEPEekpdfngNYFLYHLLGAEnVIVVPNGadlMEEMHKVAKEVSEKGNTPYVIPvGGSNPTGAMGYIACAQ 172
Cdd:cd00640 76 CTIVMPEGASPE-------KVAQMRALGAE-VVLVPGD---FDDAIALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 173 EIMAQSFEQGIDFssVVCVSGSAGMHAGLITGFSGTQSKIPVIGINVsrgkaeqeekvaklvdetsahvgipnsisrEAV 252
Cdd:cd00640 144 EILEQLGGQKPDA--VVVPVGGGGNIAGIARALKELLPNVKVIGVEP------------------------------EVV 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764649295 253 TCFDEyvgpgyalptpEMVEAVQLLAKTEGILLDPVyTGKAVAGLIDLIRKGkfNKEDNILFVHSGG 319
Cdd:cd00640 192 TVSDE-----------EALEAIRLLAREEGILVEPS-SAAALAAALKLAKKL--GKGKTVVVILTGG 244
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
13-310 |
4.88e-10 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 59.91 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 13 ESYTPIEKLNNFSEVLGGPTIYFKrDDLLGLTaGGNKTRKLEFLVADAQAKGADTLITA-GGIQSNhcrlTLAA-AVKEK 90
Cdd:cd01563 20 EGNTPLVRAPRLGERLGGKNLYVK-DEGLNPT-GSFKDRGMTVAVSKAKELGVKAVACAsTGNTSA----SLAAyAARAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 91 MKCILVLEEGLEPEEKPDFNGNyflyhllGAEnVIVVPNGADlmeEMHKVAKEVSEKgNTPYVIPVggSNPTGAMGYIAC 170
Cdd:cd01563 94 IKCVVFLPAGKALGKLAQALAY-------GAT-VLAVEGNFD---DALRLVRELAEE-NWIYLSNS--LNPYRLEGQKTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 171 AQEIMAQSfeqGIDFSSVVCV-SGSAGMHAGLITGF-----SGTQSKIP-------------VIGINVSRGKAEQEEKVa 231
Cdd:cd01563 160 AFEIAEQL---GWEVPDYVVVpVGNGGNITAIWKGFkelkeLGLIDRLPrmvgvqaegaapiVRAFKEGKDDIEPVENP- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 232 klvdETSAH-VGIPNSIS-REAVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPVyTGKAVAGLIDLIRKGKFNKE 309
Cdd:cd01563 236 ----ETIATaIRIGNPASgPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPA-SAASLAGLKKLREEGIIDKG 310
|
.
gi 764649295 310 D 310
Cdd:cd01563 311 E 311
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
16-315 |
2.57e-07 |
|
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: 51.36 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 16 TPIEKLNNFSEVLGgPTIYFKrddLLGLTAGGN-KTRKLEFLVADAQAKGA----DTLI--TAG--GIQsnhcrLTLAAA 86
Cdd:cd01561 3 TPLVRLNRLSPGTG-AEIYAK---LEFFNPGGSvKDRIALYMIEDAEKRGLlkpgTTIIepTSGntGIG-----LAMVAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 87 VKeKMKCILVLEEGLEPEEKPdfngnyfLYHLLGAENVIVVPNGADLMEEMHKVAKEVSEkgNTP-YVIPVGGSNPTGAM 165
Cdd:cd01561 74 AK-GYRFIIVMPETMSEEKRK-------LLRALGAEVILTPEAEADGMKGAIAKARELAA--ETPnAFWLNQFENPANPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 166 GYIAC-AQEIMAQsFEQGIDFssVVCVSGSAGMHAG-----------------------LITGFSGTQSKIPVIGINvsr 221
Cdd:cd01561 144 AHYETtAPEIWEQ-LDGKVDA--FVAGVGTGGTITGvarylkeknpnvrivgvdpvgsvLFSGGPPGPHKIEGIGAG--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 222 gkaeqeeKVAKLVDETSAHvgipnsisrEAVTCFDEyvgpgyalptpEMVEAVQLLAKTEGILLDPVyTGKAVAGLIDLI 301
Cdd:cd01561 218 -------FIPENLDRSLID---------EVVRVSDE-----------EAFAMARRLAREEGLLVGGS-SGAAVAAALKLA 269
|
330
....*....|....
gi 764649295 302 RKGKfnKEDNILFV 315
Cdd:cd01561 270 KRLG--PGKTIVTI 281
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
13-313 |
2.17e-06 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 49.04 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 13 ESYTPIEKLNNFSEVLGgPTIYFKRDdllgltaGGNKT-----RKLEFLVADAQAKGADTLITA--GgiqsnhcrlTLAA 85
Cdd:COG0498 64 EGGTPLVKAPRLADELG-KNLYVKEE-------GHNPTgsfkdRAMQVAVSLALERGAKTIVCAssG---------NGSA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 86 AV-----KEKMKCILVLEEGLEPEEKpdfngnyflyhLL-----GAENVIVVPNGADLMeemhKVAKEVSEKGNtpyVIP 155
Cdd:COG0498 127 ALaayaaRAGIEVFVFVPEGKVSPGQ-----------LAqmltyGAHVIAVDGNFDDAQ----RLVKELAADEG---LYA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 156 VGGSNPTGAMGYIACAQEIMAQsFEQGIDfssVVCVSGSAGmhaGLITGF---------SGTQSKIP-VIGI------NV 219
Cdd:COG0498 189 VNSINPARLEGQKTYAFEIAEQ-LGRVPD---WVVVPTGNG---GNILAGykafkelkeLGLIDRLPrLIAVqatgcnPI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764649295 220 SRGKAEQEEKVAKLVDETSAHV-GIPNSISRE-AVTCFDEYVGPGYALPTPEMVEAVQLLAKTEGILLDPvYTGKAVAGL 297
Cdd:COG0498 262 LTAFETGRDEYEPERPETIAPSmDIGNPSNGErALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEP-ATAVAVAGL 340
|
330
....*....|....*.
gi 764649295 298 IDLIRKGKFNKEDNIL 313
Cdd:COG0498 341 RKLREEGEIDPDEPVV 356
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
8-41 |
8.71e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 37.54 E-value: 8.71e-03
10 20 30
....*....|....*....|....*....|....
gi 764649295 8 RKKYTESYTPIEKLNNFSEVLGGPTIYFKRDDLL 41
Cdd:PRK13028 55 LKHYVGRPTPLYHAKRLSEELGGAQIYLKREDLN 88
|
|
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