|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
19-410 |
1.23e-46 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 164.54 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 19 RLRRETPAWGS-YAHFAHGSASLPPQVLYEALDSWLE---AERRWGVQRAAEHFAEPLLAVRDSVARVLGT-QPRHIALL 93
Cdd:COG0520 4 AIRADFPVLGKpLVYLDNAATGQKPRPVIDAIRDYYEpynANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 94 DCASRAWSVAFAAALAAHPRIRAISSFDEYGSNSLCLLAARQQRGLELRLIDARGDAAQLLQRLDEQLHDlapgQTPLLS 173
Cdd:COG0520 84 RGTTEAINLVAYGLGRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTP----RTKLVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 174 LSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALERL-- 251
Cdd:COG0520 160 VTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKRELLEALpp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 252 ALPDGldvGGAQWSDAFALQARDDARRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLRERIAQQL-----YRRL 326
Cdd:COG0520 239 FLGGG---GMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLaaipgVRIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 327 GWTPLEqgpHASALMTYAAPELSGEQWLKRLHARGVNASyIGPQYARWALREQALPGVLRLTPHYLTDDGEIERLGEALE 406
Cdd:COG0520 316 GPADPE---DRSGIVSFNVDGVHPHDVAALLDDEGIAVR-AGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....
gi 15596010 407 DCLR 410
Cdd:COG0520 392 KLAE 395
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
41-405 |
2.03e-28 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 114.87 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 41 PPQVLYEALD--SWLEAERRWGVQRAAEHFAEPLLAVRDSVARVLGTQ-PRHIALLDCASRAWS-VAFAAALAAHPRIRA 116
Cdd:cd06453 12 PQPVIDAIVDyyRHYNANVHRGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINlVAYGLGRANKPGDEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 117 ISSFDEYGSNSLCLLAARQQRGLELRLIDARGDAAQLLQRLDEQLHDlapgQTPLLSLSAVPTGHGAATALEGVAERIRA 196
Cdd:cd06453 92 VTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKEIGEIAHE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 197 HDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKWLrGPKGLGVLYLGERALERLaLPDGLDVGGAQWSDAFALQARDDA 276
Cdd:cd06453 168 AGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKML-GPTGIGVLYGKEELLEEM-PPYGGGGEMIEEVSFEETTYADLP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 277 RRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLRERIAQQLyRRLGW-TPLEQGPHASALMTYAAPELSGEQWLK 355
Cdd:cd06453 246 HKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERL-SEIPGvRVYGDAEDRAGVVSFNLEGIHPHDVAT 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15596010 356 RLHARGVNASyIGPQYARWALREQALPGVLRLTPHYLTDDGEIERLGEAL 405
Cdd:cd06453 325 ILDQYGIAVR-AGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
36-401 |
5.44e-21 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 93.47 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 36 GSASLPPQVLYEALD---SWLEAERRwGVQRAAEHFAEPLLAVRDSVARVLGTQPRH-IALLDCASRAWS-VAFAAALAA 110
Cdd:pfam00266 7 ATTQKPQEVLDAIQEyytDYNGNVHR-GVHTLGKEATQAYEEAREKVAEFINAPSNDeIIFTSGTTEAINlVALSLGRSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 111 HPRIRAISSFDEYGSNSLCLLAARQQRGLELRLI--DARGdaaqlLQRLDEQLHDLAPgQTPLLSLSAVPTGHGAATALE 188
Cdd:pfam00266 86 KPGDEIVITEMEHHANLVPWQELAKRTGARVRVLplDEDG-----LLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 189 GVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALERLA--LPDG-----LDVGG 261
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPplLGGGgmietVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 262 AQWSDAfalqarddARRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLreriAQQLYRRLGWTPLEQ--GPHA-S 338
Cdd:pfam00266 239 STFADA--------PWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHEL----AQYLYERLLSLPGIRlyGPERrA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596010 339 ALMTYAAPELSGEQWLKRLHARGVnASYIGPQYARWALREQALPGVLRLTPHYLTDDGEIERL 401
Cdd:pfam00266 307 SIISFNFKGVHPHDVATLLDESGI-AVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
76-263 |
9.90e-10 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 59.67 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 76 RDSVARVLGTQPRHIALLDCASRA--WSVAFAAALAAHPRIRAISSFDEYGsnslCLLA---ARQQRGLELRLI--DARG 148
Cdd:PLN02651 49 RAQVAALIGADPKEIIFTSGATESnnLAIKGVMHFYKDKKKHVITTQTEHK----CVLDscrHLQQEGFEVTYLpvKSDG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 149 --DAAQLLQRLDEQlhdlapgqTPLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVF 226
Cdd:PLN02651 125 lvDLDELAAAIRPD--------TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSI 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596010 227 PPRKwLRGPKGLGVLYLGERALERLalpDGLDVGGAQ 263
Cdd:PLN02651 197 SGHK-IYGPKGVGALYVRRRPRVRL---EPLMSGGGQ 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
19-410 |
1.23e-46 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 164.54 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 19 RLRRETPAWGS-YAHFAHGSASLPPQVLYEALDSWLE---AERRWGVQRAAEHFAEPLLAVRDSVARVLGT-QPRHIALL 93
Cdd:COG0520 4 AIRADFPVLGKpLVYLDNAATGQKPRPVIDAIRDYYEpynANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 94 DCASRAWSVAFAAALAAHPRIRAISSFDEYGSNSLCLLAARQQRGLELRLIDARGDAAQLLQRLDEQLHDlapgQTPLLS 173
Cdd:COG0520 84 RGTTEAINLVAYGLGRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTP----RTKLVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 174 LSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALERL-- 251
Cdd:COG0520 160 VTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKRELLEALpp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 252 ALPDGldvGGAQWSDAFALQARDDARRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLRERIAQQL-----YRRL 326
Cdd:COG0520 239 FLGGG---GMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLaaipgVRIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 327 GWTPLEqgpHASALMTYAAPELSGEQWLKRLHARGVNASyIGPQYARWALREQALPGVLRLTPHYLTDDGEIERLGEALE 406
Cdd:COG0520 316 GPADPE---DRSGIVSFNVDGVHPHDVAALLDDEGIAVR-AGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALK 391
|
....
gi 15596010 407 DCLR 410
Cdd:COG0520 392 KLAE 395
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
41-405 |
2.03e-28 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 114.87 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 41 PPQVLYEALD--SWLEAERRWGVQRAAEHFAEPLLAVRDSVARVLGTQ-PRHIALLDCASRAWS-VAFAAALAAHPRIRA 116
Cdd:cd06453 12 PQPVIDAIVDyyRHYNANVHRGVHELSARATDAYEAAREKVARFINAPsPDEIIFTRNTTEAINlVAYGLGRANKPGDEI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 117 ISSFDEYGSNSLCLLAARQQRGLELRLIDARGDAAQLLQRLDEQLHDlapgQTPLLSLSAVPTGHGAATALEGVAERIRA 196
Cdd:cd06453 92 VTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKEIGEIAHE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 197 HDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKWLrGPKGLGVLYLGERALERLaLPDGLDVGGAQWSDAFALQARDDA 276
Cdd:cd06453 168 AGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKML-GPTGIGVLYGKEELLEEM-PPYGGGGEMIEEVSFEETTYADLP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 277 RRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLRERIAQQLyRRLGW-TPLEQGPHASALMTYAAPELSGEQWLK 355
Cdd:cd06453 246 HKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERL-SEIPGvRVYGDAEDRAGVVSFNLEGIHPHDVAT 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15596010 356 RLHARGVNASyIGPQYARWALREQALPGVLRLTPHYLTDDGEIERLGEAL 405
Cdd:cd06453 325 ILDQYGIAVR-AGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
36-401 |
5.44e-21 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 93.47 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 36 GSASLPPQVLYEALD---SWLEAERRwGVQRAAEHFAEPLLAVRDSVARVLGTQPRH-IALLDCASRAWS-VAFAAALAA 110
Cdd:pfam00266 7 ATTQKPQEVLDAIQEyytDYNGNVHR-GVHTLGKEATQAYEEAREKVAEFINAPSNDeIIFTSGTTEAINlVALSLGRSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 111 HPRIRAISSFDEYGSNSLCLLAARQQRGLELRLI--DARGdaaqlLQRLDEQLHDLAPgQTPLLSLSAVPTGHGAATALE 188
Cdd:pfam00266 86 KPGDEIVITEMEHHANLVPWQELAKRTGARVRVLplDEDG-----LLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 189 GVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALERLA--LPDG-----LDVGG 261
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPplLGGGgmietVSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 262 AQWSDAfalqarddARRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQLreriAQQLYRRLGWTPLEQ--GPHA-S 338
Cdd:pfam00266 239 STFADA--------PWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHEL----AQYLYERLLSLPGIRlyGPERrA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596010 339 ALMTYAAPELSGEQWLKRLHARGVnASYIGPQYARWALREQALPGVLRLTPHYLTDDGEIERL 401
Cdd:pfam00266 307 SIISFNFKGVHPHDVATLLDESGI-AVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
76-263 |
9.90e-10 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 59.67 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 76 RDSVARVLGTQPRHIALLDCASRA--WSVAFAAALAAHPRIRAISSFDEYGsnslCLLA---ARQQRGLELRLI--DARG 148
Cdd:PLN02651 49 RAQVAALIGADPKEIIFTSGATESnnLAIKGVMHFYKDKKKHVITTQTEHK----CVLDscrHLQQEGFEVTYLpvKSDG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 149 --DAAQLLQRLDEQlhdlapgqTPLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVF 226
Cdd:PLN02651 125 lvDLDELAAAIRPD--------TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSI 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 15596010 227 PPRKwLRGPKGLGVLYLGERALERLalpDGLDVGGAQ 263
Cdd:PLN02651 197 SGHK-IYGPKGVGALYVRRRPRVRL---EPLMSGGGQ 229
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
135-330 |
3.45e-08 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 55.14 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 135 QQRGLELRLIDARGDaaqllQRLD-EQLHDLAPGQTPLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLP 213
Cdd:PLN02855 144 QKTGAVLKFVGLTPD-----EVLDvEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 214 LAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALErlALPDGLDvGGAQWSDAFALQA--RDDARRFECSEFNPGLRLA 291
Cdd:PLN02855 219 VDVQTLGADFLVASSHK-MCGPTGIGFLWGKSDLLE--SMPPFLG-GGEMISDVFLDHStyAPPPSRFEAGTPAIGEAIG 294
|
170 180 190
....*....|....*....|....*....|....*....
gi 15596010 292 LKASCDYLLQTDVRRIarrnRQLRERIAQQLYRRLGWTP 330
Cdd:PLN02855 295 LGAAIDYLSEIGMDRI----HEYEVELGTYLYEKLSSVP 329
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
135-322 |
5.93e-08 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 54.37 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 135 QQRGLELRLI----DARGDAAQLLQRLDEQlhdlapgqTPLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVG 210
Cdd:PRK09295 135 ARVGAELRVIplnpDGTLQLETLPALFDER--------TRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVM 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 211 QLPLAVEATGCDVLVFPPRKwLRGPKGLGVLYLGERALERLALPDGldvGGAQWSDAFALQARDDAR---RFECSEFNPG 287
Cdd:PRK09295 207 HHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEALLQEMPPWEG---GGSMIATVSLTEGTTWAKapwRFEAGTPNTG 282
|
170 180 190
....*....|....*....|....*....|....*
gi 15596010 288 LRLALKASCDYLLQTDVRRIARRNRQLRERIAQQL 322
Cdd:PRK09295 283 GIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQL 317
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
187-252 |
2.53e-05 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 45.85 E-value: 2.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596010 187 LEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKWLRGPKGLGVLYLGERALERLA 252
Cdd:COG0075 144 LEEIGALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIE 209
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
137-251 |
2.55e-05 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 46.13 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 137 RGLELRLIDARGDAAQLLQRLDEQLHDLAPGqtpLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAV 216
Cdd:cd06451 96 YGADVDVVEKPWGEAVSPEEIAEALEQHDIK---AVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRM 172
|
90 100 110
....*....|....*....|....*....|....*
gi 15596010 217 EATGCDVLVFPPRKWLRGPKGLGVLYLGERALERL 251
Cdd:cd06451 173 DEWGVDVAYTGSQKALGAPPGLGPIAFSERALERI 207
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
141-242 |
4.58e-04 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 40.83 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 141 LRLIDARGDAAQLLQRLDEQLHDLAPGQTPLLSLSAVPTGHGA-ATALEGVAERIRAHDGLFFLDASHAVGQLPLAVE-- 217
Cdd:cd01494 64 AKPVPVPVDDAGYGGLDVAILEELKAKPNVALIVITPNTTSGGvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVli 143
|
90 100
....*....|....*....|....*.
gi 15596010 218 -ATGCDVLVFPPRKWLRGPkGLGVLY 242
Cdd:cd01494 144 pEGGADVVTFSLHKNLGGE-GGGVVI 168
|
|
| PRK03080 |
PRK03080 |
phosphoserine transaminase; |
166-252 |
4.89e-04 |
|
phosphoserine transaminase;
Pssm-ID: 235103 Cd Length: 378 Bit Score: 42.10 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 166 PGQTPLLSlsAVPTGHGAATALEG--------VAERIRA-HDGLFFLDASHAVGQLPLAVEATgcDVLVFPPRKWLRGPK 236
Cdd:PRK03080 125 YGSLPDLS--AVDFDRDVVFTWNGtttgvrvpVARWIGAdREGLTICDATSAAFALPLDWSKL--DVYTFSWQKVLGGEG 200
|
90
....*....|....*.
gi 15596010 237 GLGVLYLGERALERLA 252
Cdd:PRK03080 201 GHGMAILSPRAVERLE 216
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
159-327 |
3.24e-03 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 39.64 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 159 EQLHDLAPGQTPLLSLSAVPTGHGAATALEGVAERIRAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKwLRGPKGL 238
Cdd:PRK10874 151 DLLPELITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHK-LYGPTGI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596010 239 GVLYLGERALERLALPDGldvGGAQWS----DAFALQARddARRFECSEFNPGLRLALKASCDYLLQTDVRRIARRNRQL 314
Cdd:PRK10874 230 GVLYGKSELLEAMSPWQG---GGKMLTevsfDGFTPQSA--PWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSL 304
|
170
....*....|...
gi 15596010 315 RERIAQQLYRRLG 327
Cdd:PRK10874 305 ATLAEDALAKLPG 317
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
195-251 |
4.24e-03 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 38.97 E-value: 4.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596010 195 RAHDGLFFLDASHAVGQLPLAVEATGCDVLVFPPRKWLRGPKGLGVLYLGERALERL 251
Cdd:PLN02409 166 AQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEAS 222
|
|
| |
