|
Name |
Accession |
Description |
Interval |
E-value |
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
54-350 |
3.36e-62 |
|
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: 203.40 E-value: 3.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALNIVTSSYGGWFGQWLQRGGASVKDIVAEPGLPIETEAVAKALDAGPHIDVLALVHAESASGSLNPLPEIL 133
Cdd:COG0075 69 NLVSPGDKVLVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 134 ALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRdSILSLADQKSWV 213
Cdd:COG0075 149 ALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPS-YYLDLKLWLKYW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 214 DggRRGLPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAKASNLVTAVPVPKALAPAA 293
Cdd:COG0075 228 E--KGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAA 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 294 -LIAAAGQLGVELTEGVGTAPARLMRLNHTGP--RAAFQTVLSnvvAYGAALRQAGHPSD 350
Cdd:COG0075 306 lRKRLKERYGIEIAGGLGPLKGKIFRIGHMGYvnPEDVLRTLA---ALEEALRELGVPVE 362
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
54-323 |
7.61e-43 |
|
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: 152.44 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALNIVTSSYGGWFGQWLQRGGASVKDIVAEPGLPIETEAVAKALDaGPHIDVLALVHAESASGSLNPLPEIL 133
Cdd:cd06451 69 NLLEPGDKVLVGVNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALE-QHDIKAVTLTHNETSTGVLNPLEGIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 134 ALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRDSILSLADQ-KSW 212
Cdd:cd06451 148 ALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGFYFDLLLLlKYW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 213 VDGGrrGLPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAKASNLVTAVPVPK-ALAP 291
Cdd:cd06451 228 GEGY--SYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEgVDGD 305
|
250 260 270
....*....|....*....|....*....|..
gi 655335246 292 AALIAAAGQLGVELTEGVGTAPARLMRLNHTG 323
Cdd:cd06451 306 EVVRRLMKRYNIEIAGGLGPTAGKVFRIGHMG 337
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
58-286 |
1.01e-22 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 98.29 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 58 PGLRalnIVTSSYGGWFGQW---LQRGGASVKDIVAEPGLPIETEAVAKAL--DAGPHIDVLALVHAESASGSLNPLPEI 132
Cdd:PLN02409 83 PGDK---VVSFRIGQFSLLWidqMQRLNFDVDVVESPWGQGADLDILKSKLrqDTNHKIKAVCVVHNETSTGVTNDLAGV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 133 LAL--ARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRdsilSLADQK 210
Cdd:PLN02409 160 RKLldCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPR----VFFDWA 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655335246 211 SWVDGGRRG--LPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAK-ASNLVTAVPVP 286
Cdd:PLN02409 236 DYLKFYKLGtyWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEwRSDTVTAVVVP 314
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
61-258 |
1.60e-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: 94.24 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 61 RALNIVTSSYGGWFGQ-----------------WL---QRGGASVKDIVAEPGLPIETEAVAKALDAGPhiDVLALVHAE 120
Cdd:pfam00266 72 EAINLVALSLGRSLKPgdeivitemehhanlvpWQelaKRTGARVRVLPLDEDGLLDLDELEKLITPKT--KLVAITHVS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 121 SASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALgGPAGVSALSVSGRA---WHLILRDG 197
Cdd:pfam00266 150 NVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY-GPTGIGVLYGRRDLlekMPPLLGGG 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655335246 198 APRDSIlSLaDQKSWVDGGRRGLPGTPAPLEFFALEKALDRIEAEGLENVVAR-HALAASAT 258
Cdd:pfam00266 229 GMIETV-SL-QESTFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHeHELAQYLY 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
54-350 |
3.36e-62 |
|
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: 203.40 E-value: 3.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALNIVTSSYGGWFGQWLQRGGASVKDIVAEPGLPIETEAVAKALDAGPHIDVLALVHAESASGSLNPLPEIL 133
Cdd:COG0075 69 NLVSPGDKVLVLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 134 ALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRdSILSLADQKSWV 213
Cdd:COG0075 149 ALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPS-YYLDLKLWLKYW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 214 DggRRGLPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAKASNLVTAVPVPKALAPAA 293
Cdd:COG0075 228 E--KGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAA 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 294 -LIAAAGQLGVELTEGVGTAPARLMRLNHTGP--RAAFQTVLSnvvAYGAALRQAGHPSD 350
Cdd:COG0075 306 lRKRLKERYGIEIAGGLGPLKGKIFRIGHMGYvnPEDVLRTLA---ALEEALRELGVPVE 362
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
54-323 |
7.61e-43 |
|
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: 152.44 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALNIVTSSYGGWFGQWLQRGGASVKDIVAEPGLPIETEAVAKALDaGPHIDVLALVHAESASGSLNPLPEIL 133
Cdd:cd06451 69 NLLEPGDKVLVGVNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALE-QHDIKAVTLTHNETSTGVLNPLEGIG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 134 ALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRDSILSLADQ-KSW 212
Cdd:cd06451 148 ALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGFYFDLLLLlKYW 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 213 VDGGrrGLPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAKASNLVTAVPVPK-ALAP 291
Cdd:cd06451 228 GEGY--SYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEgVDGD 305
|
250 260 270
....*....|....*....|....*....|..
gi 655335246 292 AALIAAAGQLGVELTEGVGTAPARLMRLNHTG 323
Cdd:cd06451 306 EVVRRLMKRYNIEIAGGLGPTAGKVFRIGHMG 337
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
58-286 |
1.01e-22 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 98.29 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 58 PGLRalnIVTSSYGGWFGQW---LQRGGASVKDIVAEPGLPIETEAVAKAL--DAGPHIDVLALVHAESASGSLNPLPEI 132
Cdd:PLN02409 83 PGDK---VVSFRIGQFSLLWidqMQRLNFDVDVVESPWGQGADLDILKSKLrqDTNHKIKAVCVVHNETSTGVTNDLAGV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 133 LAL--ARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILRDGAPRdsilSLADQK 210
Cdd:PLN02409 160 RKLldCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPR----VFFDWA 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655335246 211 SWVDGGRRG--LPGTPAPLEFFALEKALDRIEAEGLENVVARHALAASATRAGLAALGAPAWVPAAK-ASNLVTAVPVP 286
Cdd:PLN02409 236 DYLKFYKLGtyWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEwRSDTVTAVVVP 314
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
61-258 |
1.60e-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: 94.24 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 61 RALNIVTSSYGGWFGQ-----------------WL---QRGGASVKDIVAEPGLPIETEAVAKALDAGPhiDVLALVHAE 120
Cdd:pfam00266 72 EAINLVALSLGRSLKPgdeivitemehhanlvpWQelaKRTGARVRVLPLDEDGLLDLDELEKLITPKT--KLVAITHVS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 121 SASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALgGPAGVSALSVSGRA---WHLILRDG 197
Cdd:pfam00266 150 NVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY-GPTGIGVLYGRRDLlekMPPLLGGG 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655335246 198 APRDSIlSLaDQKSWVDGGRRGLPGTPAPLEFFALEKALDRIEAEGLENVVAR-HALAASAT 258
Cdd:pfam00266 229 GMIETV-SL-QESTFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHeHELAQYLY 288
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
62-258 |
6.37e-20 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 90.20 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 62 ALNIVTSSYGGW----------------FGQWLQ---RGGASVKDIVAEPGLPIETEAVAKALDagPHIDVLALVHAESA 122
Cdd:COG0520 89 AINLVAYGLGRLkpgdeilitemehhsnIVPWQElaeRTGAEVRVIPLDEDGELDLEALEALLT--PRTKLVAVTHVSNV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 123 SGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKaLGGPAGVSALSVSgRAWhliLRDGAPR-- 200
Cdd:COG0520 167 TGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGK-REL---LEALPPFlg 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655335246 201 --DSILSLADQKS-WVDGGRRGLPGTPAPLEFFALEKALDRIEAEGLENVVAR-HALAASAT 258
Cdd:COG0520 242 ggGMIEWVSFDGTtYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEAReRELTAYAL 303
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
95-252 |
5.48e-14 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 72.25 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 95 PIETEAVAKALDAGPHIDVLALVHAESASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKAL 174
Cdd:PRK13479 116 PPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 175 GGpagvsalsVSGRAWHLILRD------GAPRDSILSLADQksWV----DGGRRGLPGTPAPLeffALEKALDRIEAEGl 244
Cdd:PRK13479 196 EG--------VPGFGFVIARRSeleackGNSRSLSLDLYDQ--WAymekTGQWRFTPPTHVVA---AFYQALLELEEEG- 261
|
....*...
gi 655335246 245 eNVVARHA 252
Cdd:PRK13479 262 -GVPARGA 268
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
62-259 |
8.77e-13 |
|
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: 68.65 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 62 ALNIVTSSYGGWFGQ-----------------WLQ---RGGASVKDIVAEPGLPIETEAVAKALDagPHIDVLALVHAES 121
Cdd:cd06453 73 AINLVAYGLGRANKPgdeivtsvmehhsnivpWQQlaeRTGAKLKVVPVDDDGQLDLEALEKLLT--ERTKLVAVTHVSN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 122 ASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKALgGPAGVSALSVSgraWHLILR------ 195
Cdd:cd06453 151 VLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKML-GPTGIGVLYGK---EELLEEmppygg 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655335246 196 DGaprDSILSLADQKS-WVDGGRRGLPGTPAPLEFFALEKALDRIEAEGLENVVAR-HALAASATR 259
Cdd:cd06453 227 GG---EMIEEVSFEETtYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHeHELTAYALE 289
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
77-227 |
5.01e-11 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 63.13 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 77 WLQRGGASVKDI-VAEPGLpIETEAVAKALDagPHIDVLALVHAESASGSLNPLPEILALARARGVVTVVDAVASVGGHR 155
Cdd:PLN02651 107 HLQQEGFEVTYLpVKSDGL-VDLDELAAAIR--PDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIP 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655335246 156 LDVDDLGIDIAVIGPQKaLGGPAGVSALSVSGRAwhlilrdGAPRDSILSLADQkswvDGGRRGlpGT-PAPL 227
Cdd:PLN02651 184 VDVDDLGVDLMSISGHK-IYGPKGVGALYVRRRP-------RVRLEPLMSGGGQ----ERGRRS--GTeNTPL 242
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
76-183 |
2.75e-10 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 61.22 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 76 QWLQRGGASVKDI-VAEPGLpIETEAVAKALDAGPhidvlALV---HAESASGSLNPLPEILALARARGVVTVVDAVASV 151
Cdd:COG1104 108 RFLEKEGFEVTYLpVDEDGR-VDLEALEAALRPDT-----ALVsvmHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAV 181
|
90 100 110
....*....|....*....|....*....|..
gi 655335246 152 GGHRLDVDDLGIDIAVIGPQKaLGGPAGVSAL 183
Cdd:COG1104 182 GKIPVDVKELGVDLLSLSAHK-IYGPKGVGAL 212
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
79-247 |
4.55e-10 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 60.54 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 79 QRGGASVKDIVAEPGLPIETEAVAKALDagPHIDVLALVHAESASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDV 158
Cdd:PRK09295 135 ARVGAELRVIPLNPDGTLQLETLPALFD--ERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 159 DDLGIDIAVIGPQKaLGGPAGVSALSVSGRawhlILRDGAPRD------SILSLADQKSWVDGGRRGLPGTPAPLEFFAL 232
Cdd:PRK09295 213 QALDCDFYVFSGHK-LYGPTGIGILYVKEA----LLQEMPPWEgggsmiATVSLTEGTTWAKAPWRFEAGTPNTGGIIGL 287
|
170
....*....|....*
gi 655335246 233 EKALDRIEAEGLENV 247
Cdd:PRK09295 288 GAALDYVSALGLNNI 302
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
54-179 |
6.13e-08 |
|
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: 52.00 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALnIVTSSYGGWFGQWLQRGGASVKDIVA-EPGLPIETEAVAKALDAGPHIDVLALVHAESASGSLNPLPEI 132
Cdd:cd01494 36 ALLGPGDEVI-VDANGHGSRYWVAAELAGAKPVPVPVdDAGYGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEI 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 655335246 133 LALARARGVVTVVDAVASVGG---HRLDVDDLGIDIAVIGPQKALGGPAG 179
Cdd:cd01494 115 RKIAKEYGILLLVDAASAGGAspaPGVLIPEGGADVVTFSLHKNLGGEGG 164
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
76-191 |
6.64e-07 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 50.88 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 76 QWLQRGGASVKDI-VAEPGLpIETEAVAKALDagPHIDVLALVHAESASGSLNPLPEILALARARGVVTVVDAVASVGGH 154
Cdd:PRK02948 106 QSLESQGYTVTEIpVDKSGL-IRLVDLERAIT--PDTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKL 182
|
90 100 110
....*....|....*....|....*....|....*...
gi 655335246 155 RLDVDDLGIDIAVIGPQKaLGGPAGVSALSVS-GRAWH 191
Cdd:PRK02948 183 PIDVFEMGIDSLSVSAHK-IYGPKGVGAVYINpQVRWK 219
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
79-247 |
1.72e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 49.36 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 79 QRGGASVKDIVAEPGLPIETEAVaKALdAGPHIDVLALVHAESASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDV 158
Cdd:PLN02855 144 QKTGAVLKFVGLTPDEVLDVEQL-KEL-LSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDV 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 159 DDLGIDIAVIGPQKaLGGPAGVSALsvSGRawHLILRDGAP--------RDSILslaDQKSWVDGGRRGLPGTPAPLEFF 230
Cdd:PLN02855 222 QTLGADFLVASSHK-MCGPTGIGFL--WGK--SDLLESMPPflgggemiSDVFL---DHSTYAPPPSRFEAGTPAIGEAI 293
|
170
....*....|....*..
gi 655335246 231 ALEKALDRIEAEGLENV 247
Cdd:PLN02855 294 GLGAAIDYLSEIGMDRI 310
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
118-186 |
1.25e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 46.86 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655335246 118 HAESASGSLNPLPEILALARARGVVTVVDAVASVGGHRLDVDDLGIDIAVIGPQKaLGGPAGVSALSVS 186
Cdd:PRK14012 152 HVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK-IYGPKGIGALYVR 219
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
54-195 |
2.36e-03 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 39.49 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655335246 54 SLARPGLRALnIVTSSYGG---WFGQWLQRGGASVKdiVAEPGlpiETEAVAKALDAGPhidvlALVHAESASgslNPL- 129
Cdd:cd00614 74 ALLKAGDHVV-ASDDLYGGtyrLFERLLPKLGIEVT--FVDPD---DPEALEAAIKPET-----KLVYVESPT---NPTl 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655335246 130 -----PEILALARARGVVTVVDA-VASVGGHR-LdvdDLGIDIAVIGPQKALGGPAGVSALSVSGRAWHLILR 195
Cdd:cd00614 140 kvvdiEAIAELAHEHGALLVVDNtFATPYLQRpL---ELGADIVVHSATKYIGGHSDVIAGVVVGSGEALIQR 209
|
|
| |
