|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
137-511 |
9.06e-171 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 489.24 E-value: 9.06e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 137 PHQLlegMEGFNLELSDQPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVF 215
Cdd:pfam00282 1 PGYL---KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPAC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 216 VLMEQLTLKKMREIIGWPNG----DGDALFSPGGAISNMYSVMVARYKYFPEVKTKGMSAAP-----RLVLFTSEHSHYS 286
Cdd:pfam00282 78 TELENVVMNWLGEMLGLPAEflgqEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 287 IKKAGAVLGFGkenVILLKTDERGRVIPADLEAKVIDAKQKGYVPLFVNATAGTTVYGAFDPINDIADICEKYNLWLHVD 366
Cdd:pfam00282 158 IEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 367 GAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVPLQCSAILVREKGILQGCNSMCAGYLFQPDKqydvTYDTGDKAI 446
Cdd:pfam00282 235 AAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35903113 447 QCGRHVDIFKFWLMWKAKGTIGFEQHIDRCLELSEYLYNKIKNREGYEMVFEgqPQHTNVCFWYI 511
Cdd:pfam00282 311 PLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAE--VGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
180-583 |
1.31e-154 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 447.04 E-value: 1.31e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 180 FFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIIGWPNGDGDALFSPGGAISNMYSVMVARYK 259
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 260 YFPEVKTKGMSAAPRLVLFTSEHSHYSIKKAGAVLGfgkENVILLKTDERGRVIPADLEAKVIDAKQKGYVPLFVNATAG 339
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 340 TTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVPLQCSAILVRekgilqg 419
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 420 cnsmcagylfqpdkqydvtydtgdkaiqcgrhvdIFKFWLMWKAKGTIGFEQHIDRCLELSEYLYNKIKNREGYEMVfeG 499
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELL--G 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 500 QPQHTNVCFWYIPPSlrgmpngderreKLHRVAPKIKAMMMECGTTMVGYQPQGDKvNFFRMVVSNHAVTKSDIDFLIDE 579
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 35903113 580 IERL 583
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
145-586 |
9.76e-134 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 398.05 E-value: 9.76e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 145 EGFNLELSDQPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTL 223
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 224 KKMREIIGWPNGdGDALFSPGGAISNMYSVMVARYKYFPE-VKTKGMSAAPRLVLFTSEHSHYSIKKAGAVLGFGKENVI 302
Cdd:COG0076 114 RWLADLLGLPEG-AGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 303 LLKTDERGRVIPADLEAKVIDAKQKGYVPLFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHRHK 382
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 383 LSGIERANSVTWNPHKMMGVPLQCSAILVREKGILQGCNSMCAGYLFQPDkqyDVTYDTGDKAIQCGRHVDIFKFWLMWK 462
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 463 AKGTIGFEQHIDRCLELSEYLYNKIKNREGYEMVfeGQPQHTNVCFWYIPPslrGMPNGDERREKLHRvapkikaMMMEC 542
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKPA---GLDEEDALNYALRD-------RLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 35903113 543 GTTMVGYQPQGDKVNfFRMVVSNHAVTKSDIDFLIDEIERLGQD 586
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
153-555 |
4.83e-39 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 150.63 E-value: 4.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 153 DQPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIIG 231
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 232 WPN-----GDGDALFSPGGAISNMYSVMVARYKYFPEVktkGMSAAPRLVLFTSEHSHYSIKKAGAVLGFGKENVILLKT 306
Cdd:PLN02590 185 LPDhflstGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 307 DERGR--VIPADLEAKVIDAKQKGYVPLFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHRHKLS 384
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 385 GIERANSVTWNPHKMMGVPLQCSAILVREKGILQGCNSMCAGYLFQPDKQYDVTYDTGDKAIQCGRHVDIFKFWLMWKAK 464
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 465 GTIGFEQHIDRCLELSEYLYNKIKNREGYEMVfeGQPQHTNVCFWYIPpslrgmPNGDErrEKLHRVAPKIKAMMMECGT 544
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVV--TTRYFSLVCFRLAP------VDGDE--DQCNERNRELLAAVNSTGK 491
|
410
....*....|.
gi 35903113 545 TMVGYQPQGDK 555
Cdd:PLN02590 492 IFISHTALSGK 502
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
153-514 |
8.92e-36 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 140.43 E-value: 8.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 153 DQPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIIG 231
Cdd:PLN02880 57 NQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 232 WPN-----GDGDALFSPGGAISNMYSVMVARYKYfpeVKTKGMSAAPRLVLFTSEHSHYSIKKAGAVLGFGKENVILLKT 306
Cdd:PLN02880 137 LPEqflstGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 307 DERGR--VIPADLEAKVIDAKQKGYVPLFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHRHKLS 384
Cdd:PLN02880 214 DSSTNyaLAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYID 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 385 GIERANSVTWNPHKMMGVPLQCSAILVREKGILQGCNSMCAGYLFQPDKQYDVTYDTGDKAIQCGRHVDIFKFWLMWKAK 464
Cdd:PLN02880 294 GVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLY 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 35903113 465 GTIGFEQHIDRCLELSEYLYNKIKNREGYEMVfeGQPQHTNVCFWYIPPS 514
Cdd:PLN02880 374 GVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVPPK 421
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
244-491 |
2.70e-23 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 102.04 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 244 GGAISNMYSVMVARyKYFPEVktkgmsaaprlVLFTSEHSHYSIKKAGAVLGFgKENVIllKTDERGRVIPADLEAKVID 323
Cdd:PRK02769 92 GGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRI-KSRVI--TSLPNGEIDYDDLISKIKE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 324 AKQKGYVplfVNATAGTTVYGAFDPINDIADICEKYNL---WLHVDGAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMM 400
Cdd:PRK02769 157 NKNQPPI---IFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 401 GVPLQCSAILVREKGIlqgcnsmcagylfqpDKQY-DVTY-DTGDKAIQCGR--HVDIfkfwLMWKA---KGTIGFEQHI 473
Cdd:PRK02769 234 GSPMPCGIVLAKKKYV---------------ERISvDVDYiGSRDQTISGSRngHTAL----LLWAAirsLGSKGLRQRV 294
|
250
....*....|....*...
gi 35903113 474 DRCLELSEYLYNKIKNRE 491
Cdd:PRK02769 295 QHCLDMAQYAVDRLQANG 312
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
245-488 |
9.99e-15 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 76.02 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 245 GAISNMYSVMVARYKYfpevktkgmsaaPRLVLFTSEHSHYSIKKAGAVLGFGKENVillKTDERGRVIPADLEAKVIDA 324
Cdd:PLN03032 94 GTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKV---PTLPSGEIDYDDLERALAKN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 325 KQKgyvPLFVNATAGTTVYGAFDPINDIADICEKYN-----LWLHVDGAWGGGLLMSRKHRHKLSGIERANSVTWNPHKM 399
Cdd:PLN03032 159 RDK---PAILNVNIGTTVKGAVDDLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 400 MGVPLQCSAILVREKGIlqgcNSMcagylfqpdkQYDVTY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTIGFEQHIDRC 476
Cdd:PLN03032 236 LGCPMPCGVALTRKKHV----KAL----------SQNVEYlNSRDATIMGSRngHAPLY-LWYTLRRKGYRGIKRDVQHC 300
|
250
....*....|..
gi 35903113 477 LELSEYLYNKIK 488
Cdd:PLN03032 301 MRNAHYLKDRLT 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
245-489 |
1.01e-13 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 73.70 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 245 GAISNMYSVMVARyKYFPEVktkgmsaaprlVLFTSEHSHYSIKKAGAVLGFGKENVillKTDERGRVIPADLEAKVIDA 324
Cdd:PLN02263 161 GTEGNLHGILVGR-EVFPDG-----------ILYASRESHYSVFKAARMYRMECVKV---DTLVSGEIDCADFKAKLLAN 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 325 KQKgyvPLFVNATAGTTVYGAFDPINDIADICEKY-----NLWLHVDGAWGGGLLMSRKHRHKLSGIERANSVTWNPHKM 399
Cdd:PLN02263 226 KDK---PAIINVNIGTTVKGAVDDLDLVIKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 400 MGVPLQCSAILVREKGIlqgcNSMCAgylfqpdkqyDVTY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTIGFEQHIDRC 476
Cdd:PLN02263 303 VGCPMPCGVQITRMEHI----NVLSS----------NVEYlASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKC 367
|
250
....*....|...
gi 35903113 477 LELSEYLYNKIKN 489
Cdd:PLN02263 368 LRNAHYLKDRLRE 380
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
233-412 |
4.12e-09 |
|
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: 55.85 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 233 PNGDGDALFSPGGAISNMYSVMVARykyfpevktkgmsaAPRLVLFTSEHSHYSIKKAGAVLGFGKENVILLKTDERGRV 312
Cdd:cd01494 14 QPGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 313 IPADLEakviDAKQKGYVPLFVnATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHrhkLSGIERANSV 392
Cdd:cd01494 80 DVAILE----ELKAKPNVALIV-ITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVV 151
|
170 180
....*....|....*....|
gi 35903113 393 TWNPHKMMGVPlQCSAILVR 412
Cdd:cd01494 152 TFSLHKNLGGE-GGGVVIVK 170
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
217-508 |
2.27e-05 |
|
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: 46.86 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 217 LMEQlTLKKMREIIGWPNGDgDALFSPGGAISNMysvMVArYKYFPEVKTKGmsaapRLVLFTSEHsHYSIKKAGAVLGF 296
Cdd:pfam00266 44 AYEE-AREKVAEFINAPSND-EIIFTSGTTEAIN---LVA-LSLGRSLKPGD-----EIVITEMEH-HANLVPWQELAKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 297 GKENVILLKTDERGRVIPADLEaKVIDAKQKgyvplFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGgglLMS 376
Cdd:pfam00266 112 TGARVRVLPLDEDGLLDLDELE-KLITPKTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 377 RKHRHKLSGIERANSVTwnpHKMMGvPLQCSAILVREKGI-----LQGCNSMcagyLFQPDKQYDVTYDTGDK------- 444
Cdd:pfam00266 183 RPIDVQKLGVDFLAFSG---HKLYG-PTGIGVLYGRRDLLekmppLLGGGGM----IETVSLQESTFADAPWKfeagtpn 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35903113 445 ---AIQCGRHVDifkfWLMwkakgTIGFEQHIDRCLELSEYLYNKIKNREGYEmVFEGQPQHTNVCF 508
Cdd:pfam00266 255 iagIIGLGAALE----YLS-----EIGLEAIEKHEHELAQYLYERLLSLPGIR-LYGPERRASIISF 311
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
225-369 |
4.62e-04 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 42.75 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 225 KMREIIGwpngDGDALFSPGGAISNM--YSVMVARYkyfPEVktkgmsaaprlvlFTSEHSHYSIKKAGA--VLGFGKen 300
Cdd:COG2008 43 RVAELFG----KEAALFVPSGTMANQlaLRAHTRPG---DEV-------------ICHETAHIYVDEGGApeALSGVK-- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35903113 301 VILLkTDERGRVIPADLEAkVIDAKQKGYVPLFV----NATAGTTVYgAFDPINDIADICEKYNLWLHVDGAW 369
Cdd:COG2008 101 LLPV-PGEDGKLTPEDLEA-AIRPGDVHFPQPGLvsleNTTEGGTVY-PLEELRAIAAVAREHGLPLHLDGAR 170
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
235-368 |
8.21e-04 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 41.93 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 235 GDGDALFSPGGAISNMYSVMVarykyfpevktkgmSAAPRLVLFTSEHSHYSIKKAGAVLGFGKENVILLKTdERGRVIP 314
Cdd:cd06502 46 GKEAALFVPSGTAANQLALAA--------------HTQPGGSVICHETAHIYTDEAGAPEFLSGVKLLPVPG-ENGKLTP 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 35903113 315 ADLEAKVIDAKQKGYVPLFV----NATAGTTVYgAFDPINDIADICEKYNLWLHVDGA 368
Cdd:cd06502 111 EDLEAAIRPRDDIHFPPPSLvsleNTTEGGTVY-PLDELKAISALAKENGLPLHLDGA 167
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
341-413 |
1.21e-03 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 41.08 E-value: 1.21e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35903113 341 TVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMS---RKHRHKLSGIERANSVtwnpHKMMGVPLQCSAILVRE 413
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
266-368 |
3.30e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 40.12 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 266 TKGMSAA--------PRL----VLFTSEHSHYS--------IKKAGAVlgfgkenVILLKTDERGRVIPADLEAKvIDAK 325
Cdd:COG0520 83 TRGTTEAinlvayglGRLkpgdEILITEMEHHSnivpwqelAERTGAE-------VRVIPLDEDGELDLEALEAL-LTPR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 35903113 326 QKgyvplFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGA 368
Cdd:COG0520 155 TK-----LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA 192
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
280-368 |
3.36e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 39.89 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35903113 280 SEHSHYSIKKAGAVLGFGKENVILLKTDERGRVIPADLEAKVIDAKQKGY--VPLFV----NATAGTTVYgAFDPINDIA 353
Cdd:pfam01212 77 GEPAHIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVGADIFppTGLISlentHNSAGGQVV-SLENLREIA 155
|
90
....*....|....*
gi 35903113 354 DICEKYNLWLHVDGA 368
Cdd:pfam01212 156 ALAREHGIPVHLDGA 170
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
314-374 |
6.45e-03 |
|
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: 39.08 E-value: 6.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35903113 314 PADLEAKVIDAKQKgYVPLFVnATAGttVY---GAFDPINDIADICEKYNLWLHVDGAWGGGLL 374
Cdd:cd06454 117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
|