|
Name |
Accession |
Description |
Interval |
E-value |
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
4-360 |
2.14e-119 |
|
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: 350.16 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 4 TYLFSPGPVMVTDKVRNSLLHYDICHRGNEFMDLFKDTQQKINKLYNATSNyySLIVSGSGTSVNECVLSSIFDKEDAVL 83
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND--VVILTGSGTGAMEAALANLVSPGDKVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 84 LVSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIF 163
Cdd:COG0075 79 VLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 164 FVDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENQCKNVYLNLYKHYKVAKsSSQTPNTPN 243
Cdd:COG0075 159 IVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWE-KGQTPYTPP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 244 VTLIFALNEALTEFLED--DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVNEFILGLERESGYV 321
Cdd:COG0075 238 VSLLYALREALDLILEEglENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIE 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 497587946 322 VYPGKGKfLDANIFQVANMGEIYPEDCYKFLDILKSKLE 360
Cdd:COG0075 318 IAGGLGP-LKGKIFRIGHMGYVNPEDVLRTLAALEEALR 355
|
|
| PhnW-AepZ |
TIGR03301 |
2-aminoethylphosphonate aminotransferase; This family includes a number of ... |
5-356 |
3.73e-82 |
|
2-aminoethylphosphonate aminotransferase; This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.
Pssm-ID: 274512 [Multi-domain] Cd Length: 355 Bit Score: 254.22 E-value: 3.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVMVTDKVRNSLLHyDICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLL 84
Cdd:TIGR03301 1 ILLTPGPLSTSATVRDAMLV-DWCHWDSEFNDVTDQVRDRLLALAGGDDNHTCVLLQGSGTFAVEATIGSLVPRDGKLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 85 VSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFF 164
Cdd:TIGR03301 80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALAADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 165 VDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENqCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEELDVDALIASANKCLEGVPGFGFVIARRDLLEASAGN-ARSLYLDLYDQWAYMEKTGKWRFTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED---DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEIN-----VNEFIlgleR 316
Cdd:TIGR03301 239 HTVYAFAQALEELEAEggvPARIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDDPDfdfddFYQEL----K 314
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497587946 317 ESGYVVYPGKGKflDANIFQVANMGEIYPEDCYKFLDILK 356
Cdd:TIGR03301 315 ERGFVIYPGKLT--LADTFRIGTIGEIDAADIERLLEAIK 352
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
6-356 |
3.66e-71 |
|
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: 226.02 E-value: 3.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 6 LFSPGPVMVTDKVRNSLLHYDICHRGNEFMDLFKDTQQKINKLYNaTSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLLV 85
Cdd:cd06451 2 LLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQ-TENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 86 SNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKyIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFFV 165
Cdd:cd06451 81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAE-ALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 166 DAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQ-NIKENQCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:cd06451 160 DAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALErIKKKTKPKGFYFDLLLLLKYWGEGYSYPHTPPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED--DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVNEFILGLERESGYVV 322
Cdd:cd06451 240 NLLYALREALDLILEEglENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDEVVRRLMKRYNIEI 319
|
330 340 350
....*....|....*....|....*....|....
gi 497587946 323 YPGKGKFLDaNIFQVANMGEIYPEDCYKFLDILK 356
Cdd:cd06451 320 AGGLGPTAG-KVFRIGHMGEATREDVLGVLSALE 352
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
5-364 |
9.53e-53 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 178.57 E-value: 9.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVMVTDKVRNSLLHyDICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLL 84
Cdd:PRK13479 7 LLLTPGPLTTSRTVREAMLR-DWGSWDDDFNALTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPRDGKVLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 85 VSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFF 164
Cdd:PRK13479 86 PDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKRHGKRLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 165 VDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENqCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:PRK13479 166 VDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGN-SRSLSLDLYDQWAYMEKTGQWRFTPPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED---DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVN--EFILGLeRESG 319
Cdd:PRK13479 245 HVVAAFYQALLELEEEggvPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDfkEFYERL-KEQG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497587946 320 YVVYPgkGKFLDANIFQVANMGEIYPEDCYKFLDILKSKLEIKKV 364
Cdd:PRK13479 324 FVIYP--GKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYWMGI 366
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-300 |
8.87e-24 |
|
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: 100.78 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVM----VTDKVRNSLLHYD------ICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNeCVLSS 74
Cdd:pfam00266 2 YLDSAATTQkpqeVLDAIQEYYTDYNgnvhrgVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAIN-LVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 75 I---FDKEDAVLLV-----SNGVFGERLEEiLSTYNVKTYKPNFEWAeyPDLDILEKYIIENSdiKVIAMVFHETSSGMI 146
Cdd:pfam00266 81 LgrsLKPGDEIVITemehhANLVPWQELAK-RTGARVRVLPLDEDGL--LDLDELEKLITPKT--KLVAITHVSNVTGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 147 NPVPELGKLAKKYNKIFFVDAISASAGEYIDVEEFNIDIITGVGGKALGAfPGSAYLCAKESILQNIKENQ-----CKNV 221
Cdd:pfam00266 156 QPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGP-TGIGVLYGRRDLLEKMPPLLggggmIETV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 222 YLNLYKHYKvaksssqTPN-----TPNVTLIFALNEALtEFLE--DDSKIERY-KECSAILRNGMEELGLTFLLPDKYMS 293
Cdd:pfam00266 235 SLQESTFAD-------APWkfeagTPNIAGIIGLGAAL-EYLSeiGLEAIEKHeHELAQYLYERLLSLPGIRLYGPERRA 306
|
....*..
gi 497587946 294 NTVTSVF 300
Cdd:pfam00266 307 SIISFNF 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
4-360 |
2.14e-119 |
|
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: 350.16 E-value: 2.14e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 4 TYLFSPGPVMVTDKVRNSLLHYDICHRGNEFMDLFKDTQQKINKLYNATSNyySLIVSGSGTSVNECVLSSIFDKEDAVL 83
Cdd:COG0075 1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND--VVILTGSGTGAMEAALANLVSPGDKVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 84 LVSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIF 163
Cdd:COG0075 79 VLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 164 FVDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENQCKNVYLNLYKHYKVAKsSSQTPNTPN 243
Cdd:COG0075 159 IVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWE-KGQTPYTPP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 244 VTLIFALNEALTEFLED--DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVNEFILGLERESGYV 321
Cdd:COG0075 238 VSLLYALREALDLILEEglENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIE 317
|
330 340 350
....*....|....*....|....*....|....*....
gi 497587946 322 VYPGKGKfLDANIFQVANMGEIYPEDCYKFLDILKSKLE 360
Cdd:COG0075 318 IAGGLGP-LKGKIFRIGHMGYVNPEDVLRTLAALEEALR 355
|
|
| PhnW-AepZ |
TIGR03301 |
2-aminoethylphosphonate aminotransferase; This family includes a number of ... |
5-356 |
3.73e-82 |
|
2-aminoethylphosphonate aminotransferase; This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.
Pssm-ID: 274512 [Multi-domain] Cd Length: 355 Bit Score: 254.22 E-value: 3.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVMVTDKVRNSLLHyDICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLL 84
Cdd:TIGR03301 1 ILLTPGPLSTSATVRDAMLV-DWCHWDSEFNDVTDQVRDRLLALAGGDDNHTCVLLQGSGTFAVEATIGSLVPRDGKLLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 85 VSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFF 164
Cdd:TIGR03301 80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALAADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 165 VDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENqCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEELDVDALIASANKCLEGVPGFGFVIARRDLLEASAGN-ARSLYLDLYDQWAYMEKTGKWRFTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED---DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEIN-----VNEFIlgleR 316
Cdd:TIGR03301 239 HTVYAFAQALEELEAEggvPARIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDDPDfdfddFYQEL----K 314
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497587946 317 ESGYVVYPGKGKflDANIFQVANMGEIYPEDCYKFLDILK 356
Cdd:TIGR03301 315 ERGFVIYPGKLT--LADTFRIGTIGEIDAADIERLLEAIK 352
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
6-356 |
3.66e-71 |
|
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: 226.02 E-value: 3.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 6 LFSPGPVMVTDKVRNSLLHYDICHRGNEFMDLFKDTQQKINKLYNaTSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLLV 85
Cdd:cd06451 2 LLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQ-TENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 86 SNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKyIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFFV 165
Cdd:cd06451 81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAE-ALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 166 DAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQ-NIKENQCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:cd06451 160 DAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALErIKKKTKPKGFYFDLLLLLKYWGEGYSYPHTPPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED--DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVNEFILGLERESGYVV 322
Cdd:cd06451 240 NLLYALREALDLILEEglENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDEVVRRLMKRYNIEI 319
|
330 340 350
....*....|....*....|....*....|....
gi 497587946 323 YPGKGKFLDaNIFQVANMGEIYPEDCYKFLDILK 356
Cdd:cd06451 320 AGGLGPTAG-KVFRIGHMGEATREDVLGVLSALE 352
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
5-364 |
9.53e-53 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 178.57 E-value: 9.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVMVTDKVRNSLLHyDICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNECVLSSIFDKEDAVLL 84
Cdd:PRK13479 7 LLLTPGPLTTSRTVREAMLR-DWGSWDDDFNALTASVRAKLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPRDGKVLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 85 VSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFF 164
Cdd:PRK13479 86 PDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRITHVALVHCETTTGILNPLDEIAAVAKRHGKRLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 165 VDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENqCKNVYLNLYKHYKVAKSSSQTPNTPNV 244
Cdd:PRK13479 166 VDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGN-SRSLSLDLYDQWAYMEKTGQWRFTPPT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 245 TLIFALNEALTEFLED---DSKIERYKECSAILRNGMEELGLTFLLPDKYMSNTVTSVFLPKEINVN--EFILGLeRESG 319
Cdd:PRK13479 245 HVVAAFYQALLELEEEggvPARGARYANNQRTLVAGMRALGFEPLLDAEIQSPIIVTFHAPADPAYDfkEFYERL-KEQG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497587946 320 YVVYPgkGKFLDANIFQVANMGEIYPEDCYKFLDILKSKLEIKKV 364
Cdd:PRK13479 324 FVIYP--GKLTQVDTFRIGCIGDVDAADIRRLVAAIAEALYWMGI 366
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
5-311 |
1.87e-33 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 127.95 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVMVTDKVRNSLLHYDICHRGNEFMDLFKDTQQKINKLYNATSNYySLIVSGSGTSVNECVLSSIFDKEDAVLL 84
Cdd:PLN02409 11 HLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGT-PFIFPTTGTGAWESALTNTLSPGDKVVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 85 VSNGVFGERLEEILSTYNVKTYKPNFEWAEYPDLDILEKYIIENSD--IKVIAMVFHETSSGMINPVPELGKLAKKYNK- 161
Cdd:PLN02409 90 FRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNhkIKAVCVVHNETSTGVTNDLAGVRKLLDCAQHp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 162 -IFFVDAISASAGEYIDVEEFNIDIITGVGGKALGAFPGSAYLCAKESILQNIKENQCKNVYLNLYKHYKVAKSSSQTPN 240
Cdd:PLN02409 170 aLLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKFYKLGTYWPY 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497587946 241 TPNVTLIFALNEALTEFLED--DSKIERYKECSAILRNGMEELGLT-FLLPDKYMSNTVTSVFLPKEINVNEFI 311
Cdd:PLN02409 250 TPSIQLLYGLRAALDLIFEEglENVIARHARLGEATRLAVEAWGLKlCTKKPEWRSDTVTAVVVPEGIDSAEIV 323
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
5-300 |
8.87e-24 |
|
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: 100.78 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 5 YLFSPGPVM----VTDKVRNSLLHYD------ICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNeCVLSS 74
Cdd:pfam00266 2 YLDSAATTQkpqeVLDAIQEYYTDYNgnvhrgVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAIN-LVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 75 I---FDKEDAVLLV-----SNGVFGERLEEiLSTYNVKTYKPNFEWAeyPDLDILEKYIIENSdiKVIAMVFHETSSGMI 146
Cdd:pfam00266 81 LgrsLKPGDEIVITemehhANLVPWQELAK-RTGARVRVLPLDEDGL--LDLDELEKLITPKT--KLVAITHVSNVTGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 147 NPVPELGKLAKKYNKIFFVDAISASAGEYIDVEEFNIDIITGVGGKALGAfPGSAYLCAKESILQNIKENQ-----CKNV 221
Cdd:pfam00266 156 QPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGP-TGIGVLYGRRDLLEKMPPLLggggmIETV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 222 YLNLYKHYKvaksssqTPN-----TPNVTLIFALNEALtEFLE--DDSKIERY-KECSAILRNGMEELGLTFLLPDKYMS 293
Cdd:pfam00266 235 SLQESTFAD-------APWkfeagTPNIAGIIGLGAAL-EYLSeiGLEAIEKHeHELAQYLYERLLSLPGIRLYGPERRA 306
|
....*..
gi 497587946 294 NTVTSVF 300
Cdd:pfam00266 307 SIISFNF 313
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
52-201 |
4.09e-13 |
|
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: 66.64 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 52 TSNYYSLIVSgSGTSVNECVLSSIFDKEDAVLLVSNGVFgerleeilSTYNVKTYKPNFEWAEYPDLD----ILEKYIIE 127
Cdd:cd01494 15 PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHG--------SRYWVAAELAGAKPVPVPVDDagygGLDVAILE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 128 NSDIK--VIAMVFH--ETSSGMINPVPELGKLAKKYNKIFFVD---AISASAGEYIDVEEFNIDIITGVGGKALGAFPGS 200
Cdd:cd01494 86 ELKAKpnVALIVITpnTTSGGVLVPLKEIRKIAKEYGILLLVDaasAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGG 165
|
.
gi 497587946 201 A 201
Cdd:cd01494 166 V 166
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
59-284 |
9.69e-11 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 62.19 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 59 IVSGSGTSVNECVLSSIFDKEDAVLLVS-------NGVfgerleeILSTYNVKTYKPNfewaeypDLDILEKYIIENSDI 131
Cdd:cd06454 65 LVFSSGYAANDGVLSTLAGKGDLIISDSlnhasiiDGI-------RLSGAKKRIFKHN-------DMEDLEKLLREARRP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 132 KVIAMVFHET--S-SGMINPVPELGKLAKKYNKIFFVDAiSASAGEYID----VEEFN-----IDIITGVGGKALGAFPG 199
Cdd:cd06454 131 YGKKLIVTEGvySmDGDIAPLPELVDLAKKYGAILFVDE-AHSVGVYGPhgrgVEEFGgltddVDIIMGTLGKAFGAVGG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 200 saYLCAKESILQNIKENQCKNVYlnlykhykvakSSSQTPntpnvTLIFALNEALTEFLEDDSKIERYKECSAILRNGME 279
Cdd:cd06454 210 --YIAGSKELIDYLRSYARGFIF-----------STSLPP-----AVAAAALAALEVLQGGPERRERLQENVRYLRRGLK 271
|
....*
gi 497587946 280 ELGLT 284
Cdd:cd06454 272 ELGFP 276
|
|
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
35-284 |
1.88e-07 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 52.51 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 35 MDLFKDTQQKINKLYN--ATsnyyslIVSGSGTSVNECVLSSIFDKEDAVLlvS---------NGVfgeRLeeilSTYNV 103
Cdd:PRK06939 86 QDLHKELEEKLAKFLGteDA------ILYSSCFDANGGLFETLLGKEDAII--SdalnhasiiDGV---RL----CKAKR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 104 KTYKPNfewaeypDLDILEKYIIENSD----IKVIAM--VFheTSSGMINPVPELGKLAKKYNKIFFVDAISAS------ 171
Cdd:PRK06939 151 YRYANN-------DMADLEAQLKEAKEagarHKLIATdgVF--SMDGDIAPLPEICDLADKYDALVMVDDSHAVgfvgen 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 172 -AG--EYIDVEEfNIDIITGVGGKALGAFPGsAYLCAKESILQNIKenQCKNVYLNlykhykvakSSSQTPNTPNVTLif 248
Cdd:PRK06939 222 gRGtvEHFGVMD-RVDIITGTLGKALGGASG-GYTAGRKEVIDWLR--QRSRPYLF---------SNSLAPAIVAASI-- 286
|
250 260 270
....*....|....*....|....*....|....*.
gi 497587946 249 alnEALTEFLEDDSKIERYKECSAILRNGMEELGLT 284
Cdd:PRK06939 287 ---KVLELLEESDELRDRLWENARYFREGMTAAGFT 319
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
116-214 |
2.37e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 52.06 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 116 PDLDILEKYIieNSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFFVDAiSASAGEY-IDVEEFNIDIITGVGGKAL 194
Cdd:COG0520 142 LDLEALEALL--TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDG-AQSVPHLpVDVQALGCDFYAFSGHKLY 218
|
90 100
....*....|....*....|
gi 497587946 195 GAFpGSAYLCAKESILQNIK 214
Cdd:COG0520 219 GPT-GIGVLYGKRELLEALP 237
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
59-286 |
6.91e-07 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 50.82 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 59 IVSGSGTSVNECVLSSIFDKEDAVLL-------VSNGVfgerleeILSTYNVKTYKPNfewaeypDLDILEKYIIENSD- 130
Cdd:COG0156 101 LLFSSGYAANLGVISALAGRGDLIFSdelnhasIIDGA-------RLSGAKVVRFRHN-------DMDDLERLLKKARAa 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 131 -IKVIAM--VFhetssGM---INPVPELGKLAKKYNKIFFVD---AIS------ASAGEYIDVEEfNIDIITGVGGKALG 195
Cdd:COG0156 167 rRKLIVTdgVF-----SMdgdIAPLPEIVELAEKYGALLYVDdahGTGvlgetgRGLVEHFGLED-RVDIIMGTLSKALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 196 AFpGsAYLCAKESILQnikenqcknvYLnlyKHYkvAK----SSSQTPntpnvTLIFALNEALTEFLEDDSKIERYKECS 271
Cdd:COG0156 241 SS-G-GFVAGSKELID----------YL---RNR--ARpfifSTALPP-----AVAAAALAALEILREEPELRERLWENI 298
|
250
....*....|....*
gi 497587946 272 AILRNGMEELGLTFL 286
Cdd:COG0156 299 AYFREGLKELGFDLG 313
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
117-226 |
1.15e-06 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 50.11 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 117 DLDILEKYIIENSdikVIAMVFHETSS-GMINPVPELGKLAKKYNKIFFVDAISASAGEYIDVEEFNIDIITG-----VG 190
Cdd:PRK02948 127 RLVDLERAITPDT---VLASIQHANSEiGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVsahkiYG 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497587946 191 GKALGA------------FPGS-----------------AYLCAKESILQNIKENQCKNVYLNLY 226
Cdd:PRK02948 204 PKGVGAvyinpqvrwkpvFPGTthekgfrpgtvnvpgiaAFLTAAENILKNMQEESLRFKELRSY 268
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
117-282 |
1.59e-06 |
|
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: 49.39 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 117 DLDILEKYIieNSDIKVIAMVFHETSSGMINPVPELGKLAKKYNKIFFVDAiSASAGEY-IDVEEFNIDIITGVGGKALG 195
Cdd:cd06453 128 DLEALEKLL--TERTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDG-AQSAGHMpVDVQDLGCDFLAFSGHKMLG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 196 AfPGSAYLCAKESILQN----------IKEnqcknvylnlykhykVAKSSSQ---TPN-----TPNVTLIFALNEALtEF 257
Cdd:cd06453 205 P-TGIGVLYGKEELLEEmppyggggemIEE---------------VSFEETTyadLPHkfeagTPNIAGAIGLGAAI-DY 267
|
170 180
....*....|....*....|....*....
gi 497587946 258 LED---DsKIERY-KECSAILRNGMEELG 282
Cdd:cd06453 268 LEKigmE-AIAAHeHELTAYALERLSEIP 295
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
117-195 |
1.78e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 46.47 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 117 DLDILEKYIIENSDIKVIAMVFHETssGMINPVPELGKLAKKYNKIFFVDAiSASAGEY-IDVEEFNIDIITGVGGKALG 195
Cdd:PRK14012 133 DLEKLEAAMRDDTILVSIMHVNNEI--GVIQDIAAIGEICRERGIIFHVDA-AQSVGKVpIDLSKLKVDLMSFSAHKIYG 209
|
|
| SerC |
COG1932 |
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ... |
2-254 |
1.31e-04 |
|
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 441535 Cd Length: 358 Bit Score: 43.52 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 2 KKTYLFSPGPVM----VTDKVRNSLLHYD--------ICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNE 69
Cdd:COG1932 1 MRVYNFSAGPAKlpeeVLEQAQAELLDWNgsgmsvmeMSHRSKPFKAIVEEAEADLRELLGIPDGYEVLFLQGGATAQFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 70 CV---LSSIFDKEDAvllVSNGVFGE-------RLEEIL----STYNVKTYKPNFEwaeypDLDIlekyiieNSDIKVIA 135
Cdd:COG1932 81 MVpmnLLRGGKKADY---LVTGEWSKkaikeakKYGEVNvvasSEDDNFGYIPKPE-----EWQL-------SPDADYVH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 136 MVFHETSSG-MINPVPELGklakkyNKIFFVDAISASAGEYIDVEEFniDIITGVGGKALGafPGSAYLC-AKESILQNI 213
Cdd:COG1932 146 YTSNETITGvEFHELPDVG------DVPLVADMSSDILSRPVDVSKF--GLIYAGAQKNIG--PAGLTVViVRPDLLGRA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 497587946 214 KEnqckNV--YLNlykhYKVAKSSSQTPNTPNVTLIFALNEAL 254
Cdd:COG1932 216 ER----AIpsMLD----YKTHADNDSMYNTPPTFAIYLAGLVL 250
|
|
| PRK05355 |
PRK05355 |
3-phosphoserine/phosphohydroxythreonine transaminase; |
1-55 |
2.75e-04 |
|
3-phosphoserine/phosphohydroxythreonine transaminase;
Pssm-ID: 235428 Cd Length: 360 Bit Score: 42.39 E-value: 2.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497587946 1 MKKTYLFSPGPVM----VTDKVRNSLLHYD--------ICHRGNEFMDLFKDTQQKINKLYNATSNY 55
Cdd:PRK05355 1 MMRVYNFSAGPAMlpeeVLEQAQQELLDWNgsgmsvmeISHRSKEFEAVAEEAEADLRELLNIPDNY 67
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
117-192 |
7.11e-04 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 41.18 E-value: 7.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497587946 117 DLDILEKYIIENSDIKVIAMVFHETssGMINPVPELGKLAKKYNKIFFVDAISASAGEYIDVEEFNIDIITGVGGK 192
Cdd:PLN02651 127 DLDELAAAIRPDTALVSVMAVNNEI--GVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK 200
|
|
| PLN02624 |
PLN02624 |
ornithine-delta-aminotransferase |
78-211 |
1.55e-03 |
|
ornithine-delta-aminotransferase
Pssm-ID: 215335 [Multi-domain] Cd Length: 474 Bit Score: 40.15 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 78 KEDAVLLVSNGVFGERLEEILS-------TYNVKTYKPNFEWAEYPDLDILEKYIIENSDiKVIAMVFH--ETSSGMINP 148
Cdd:PLN02624 164 KNEAIIVSCCGCFHGRTLAAISmscdneaTRGFGPLLPGHLKVDFGDLDALEKIFEEDGD-RIAAFLFEpiQGEAGVVIP 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497587946 149 ----VPELGKLAKKYNKIFFVDAISASAGEY-----IDVEEFNIDIItgVGGKALGA--FPGSAYLCAKESILQ 211
Cdd:PLN02624 243 pdgyLKAVRELCSKHNVLMIADEIQTGLARTgkmlaCDWEEVRPDVV--ILGKALGGgvIPVSAVLADKDVMLC 314
|
|
| PLN02452 |
PLN02452 |
phosphoserine transaminase |
2-260 |
1.55e-03 |
|
phosphoserine transaminase
Pssm-ID: 178071 Cd Length: 365 Bit Score: 40.06 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 2 KKTYLFSPGPVM----VTDKVRNSLLHY--------DICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGTSVNE 69
Cdd:PLN02452 6 GRVFNFSAGPATlpanVLAKAQAELYNWegsgmsvmEMSHRGKEFLSIIQKAEADLRELLDIPDNYEVLFLQGGASTQFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 70 CVLSSIFDKEDAVLLVSNGVFGERLEEILSTY---NVKTYKPNFEWAEYPDLDILEKyiieNSDIKVIAMVFHETSSGMi 146
Cdd:PLN02452 86 AIPLNLCKPGDKADFVVTGSWSKKAAKEAKKYcktNVIASGKDEKYTKIPSVSEWEL----TPDAKFVHICANETIHGV- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497587946 147 npvpELGKLAKKYNKIFFVDAISASAGEYIDVEEFNidIITGVGGKALGAfPGSAYLCAKESILQNikENQCKNVYLNly 226
Cdd:PLN02452 161 ----EFKDYPDVGNVPLVADMSSNFLSKPVDVSKYG--VIYAGAQKNVGP-SGVTIVIIRKDLIGN--ARPITPGMLD-- 229
|
250 260 270
....*....|....*....|....*....|....
gi 497587946 227 khYKVAKSSSQTPNTPNVTLIFALNEALTEFLED 260
Cdd:PLN02452 230 --YKIHAENDSLYNTPPCFGIYMCGLVFEDLLAQ 261
|
|
| PSAT_like |
cd00611 |
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ... |
7-65 |
1.89e-03 |
|
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.
Pssm-ID: 99736 [Multi-domain] Cd Length: 355 Bit Score: 39.97 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497587946 7 FSPGPVM----VTDKVRNSLLHY--------DICHRGNEFMDLFKDTQQKINKLYNATSNYYSLIVSGSGT 65
Cdd:cd00611 3 FSAGPAAlpeeVLEQAQKELLDFnglgmsvmEMSHRSKDFEAIVNEAESDLRELLNIPDNYKVLFLQGGAT 73
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