|
Name |
Accession |
Description |
Interval |
E-value |
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
1-341 |
5.63e-117 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 341.28 E-value: 5.63e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 1 MISFENDYLEGAHEKVLQRIFDTNLIQASgYGDDQFSKQAAEEIKSAIKcpEATVRFLLGGTQTNQVVINSILEPYEGVI 80
Cdd:COG2008 2 MIDFRSDTVTGPHPEMLEAMAAANVGDDV-YGEDPTVNRLEERVAELFG--KEAALFVPSGTMANQLALRAHTRPGDEVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 81 SADTGHVAVHEGGAIEF-SGHKVLTVPSHEGKIRPKEVNAYLDTfyndfKREHMVFPGMVYISHPTEYGTLYSKKELKNL 159
Cdd:COG2008 79 CHETAHIYVDEGGAPEAlSGVKLLPVPGEDGKLTPEDLEAAIRP-----GDVHFPQPGLVSLENTTEGGTVYPLEELRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 160 ADVCKEHNVPLFMDGARLGYGLMSDQSDLTfeDIAKYCDIFYIGGTKIGALCGEAIVFTKNNEPKHFTTRIKQHGALLAK 239
Cdd:COG2008 154 AAVAREHGLPLHLDGARLFNAAAALGVSLA--EITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 240 GRLVGVQFLELFTNNlyLDISRHAINMANKMKKGFLEK-GYQLYFDSPTNQQFFVLSEEKIKELKQK-VKFAIWEKYddn 317
Cdd:COG2008 232 AGFLAAQGLAALEDD--LERLAEDHAMARRLAEGLAALpGVRVPEPVETNIVFVILPDELAERLREKgVLFYPWGPG--- 306
|
330 340
....*....|....*....|....
gi 1081105957 318 hrVVRFATSWATTEENVDKLLGLI 341
Cdd:COG2008 307 --AVRLVTHWDTTEEDVDAFLAAL 328
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
4-341 |
2.99e-78 |
|
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: 243.01 E-value: 2.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 4 FENDYLEGAHEKVLQRIFDTNLIQAsGYGDDQFSKQAAEEIKSAIKcpEATVRFLLGGTQTNQVVINSILEPYEGVISAD 83
Cdd:cd06502 2 FRSDTVTGPTPEMLEAMAAANVGDD-VYGEDPTTAKLEARAAELFG--KEAALFVPSGTAANQLALAAHTQPGGSVICHE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 84 TGHVAVHEGGAIEF-SGHKVLTVPSHEGKIRPKEVNAYLdTFYNDfkrEHMVFPGMVYISHPTEYGTLYSKKELKNLADV 162
Cdd:cd06502 79 TAHIYTDEAGAPEFlSGVKLLPVPGENGKLTPEDLEAAI-RPRDD---IHFPPPSLVSLENTTEGGTVYPLDELKAISAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 163 CKEHNVPLFMDGARLGYGLMSdqSDLTFEDIAKYCDIFYIGGTKIGALCGEAIVFTKNNEPKHFTTRIKQHGALLAKGRL 242
Cdd:cd06502 155 AKENGLPLHLDGARLANAAAA--LGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 243 VGVQFLELFTNNLYLDISRHAINMANKMKKGFLEKGYQ---------LYFDSPTNQQFFVLSEEKIKELKQKVKFaiwek 313
Cdd:cd06502 233 LAAAGLAALENDLWLRRLRHDHEMARRLAEALEELGGLesevqtnivLLDPVEANAVFVELSKEAIERRGEGVLF----- 307
|
330 340
....*....|....*....|....*...
gi 1081105957 314 YDDNHRVVRFATSWATTEENVDKLLGLI 341
Cdd:cd06502 308 YAWGEGGVRFVTHWDTTEEDVDELLSAL 335
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
52-245 |
7.93e-22 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 93.43 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 52 EATVRFLLG---------GTQTNQVVINSILEPYEGVISADTGHVAVHE-GGAIEFSGHKVLTVPS-HEGKIRPKEVNAY 120
Cdd:pfam01212 38 EDRVAELFGkeaalfvpsGTAANQLALMAHCQRGDEVICGEPAHIHFDEtGGHAELGGVQPRPLDGdEAGNMDLEDLEAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 121 LDtfynDFKREHMVFPGMVY--ISHPTEYGTLYSKKELKNLADVCKEHNVPLFMDGARLGYGlmSDQSDLTFEDIAKYCD 198
Cdd:pfam01212 118 IR----EVGADIFPPTGLISleNTHNSAGGQVVSLENLREIAALAREHGIPVHLDGARFANA--AVALGVIVKEITSYAD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1081105957 199 IFYIGGTKiGALCG-EAIVFTKnnePKHFTTRIKQHGALLAKGRLVGV 245
Cdd:pfam01212 192 SVTMCLSK-GLGAPvGSVLAGS---DDFIAKAIRQRKYLGGGLRQAGV 235
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
5-341 |
6.62e-09 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 56.54 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 5 ENDYLEGAHEKVLQRIFDTNLIQA-SGYGD----DQFSKQAAEEIKSAIKC---PEATVRFLLGGTQTNQVVINSILEPY 76
Cdd:pfam00155 8 SNEYLGDTLPAVAKAEKDALAGGTrNLYGPtdghPELREALAKFLGRSPVLkldREAAVVFGSGAGANIEALIFLLANPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 77 EGVISADTGHVAVHEGgaIEFSGHKVLTVPSHEGkirpkevnaylDTFYNDFkrEHMVF-----PGMVYI---SHPTeyG 148
Cdd:pfam00155 88 DAILVPAPTYASYIRI--ARLAGGEVVRYPLYDS-----------NDFHLDF--DALEAalkekPKVVLHtspHNPT--G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 149 TLYSKKELKNLADVCKEHNVPLFMDGAR--LGYGLMSDQSDLTFedIAKYCDIFYIG---------GTKIGALCGEAIV- 216
Cdd:pfam00155 151 TVATLEELEKLLDLAKEHNILLLVDEAYagFVFGSPDAVATRAL--LAEGPNLLVVGsfskafglaGWRVGYILGNAAVi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 217 --FTKNNEPKHFTTrikqHGALLAKGRLVGVQFLELFTNnlylDISRHAINMANKMKKGFLEKGYQlYFDSPTNqqFFV- 293
Cdd:pfam00155 229 sqLRKLARPFYSST----HLQAAAAAALSDPLLVASELE----EMRQRIKERRDYLRDGLQAAGLS-VLPSQAG--FFLl 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1081105957 294 --LSEEKIKELKQKVKfaiwekydDNHRVVRFA------TSW------ATTEENVDKLLGLI 341
Cdd:pfam00155 298 tgLDPETAKELAQVLL--------EEVGVYVTPgsspgvPGWlritvaGGTEEELEELLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
5-212 |
3.90e-07 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 51.19 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 5 ENDYlEGAHEKVLQRIFDTNLIQASGYGDDQFSKQAAEEI------KSAIKCPEATVRFLLGGTQTNQVVINSILEPYEG 78
Cdd:cd00609 7 EPDF-PPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIaewlgrRGGVDVPPEEIVVTNGAQEALSLLLRALLNPGDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 79 VISADTGHVAVHEggAIEFSGHKVLTVPSHEGKIRPkevnayLDTFYNDFKREHMvfPGMVYISH---PTeyGTLYSKKE 155
Cdd:cd00609 86 VLVPDPTYPGYEA--AARLAGAEVVPVPLDEEGGFL------LDLELLEAAKTPK--TKLLYLNNpnnPT--GAVLSEEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 156 LKNLADVCKEHNVPLFMDGArlgYG-LMSDQSDLTFEDIAKYCD-IFYIGG-TKIGALCG 212
Cdd:cd00609 154 LEELAELAKKHGILIISDEA---YAeLVYDGEPPPALALLDAYErVIVLRSfSKTFGLPG 210
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
53-175 |
8.84e-06 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 47.00 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 53 ATVRFLLGGTQTNQVVINSILEPYEGVIsAD-----TGHVAVHEGGAIefsghkVLTVPSHEGKIRPKEVNAYLDTFyND 127
Cdd:cd06452 60 DEARVTPGAREGKFAVMHSLCEKGDWVV-VDglahyTSYVAAERAGLN------VREVPNTGHPEYHITPEGYAEVI-EE 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1081105957 128 FKREHMVFPGMVYISHPT-EYGTLYskkELKNLADVCKEHNVPLFMDGA 175
Cdd:cd06452 132 VKDEFGKPPALALLTHVDgNYGNLH---DAKKIAKVCHEYGVPLLLNGA 177
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
55-215 |
9.05e-06 |
|
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: 45.45 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 55 VRFLLGGTQTNQVVINSILEPYEGVISADTGHVAvHEGGAIEFSGHKVLTVPSHEGKirpkevnAYLDTFYNDFKREHMV 134
Cdd:cd01494 20 AVFVPSGTGANEAALLALLGPGDEVIVDANGHGS-RYWVAAELAGAKPVPVPVDDAG-------YGGLDVAILEELKAKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 135 FPGMVYISHP-TEYGTLYSkkeLKNLADVCKEHNVPLFMDGARLGYGlMSDQSDLTFEDiakYCDIFYIGGTKigALCGE 213
Cdd:cd01494 92 NVALIVITPNtTSGGVLVP---LKEIRKIAKEYGILLLVDAASAGGA-SPAPGVLIPEG---GADVVTFSLHK--NLGGE 162
|
..
gi 1081105957 214 AI 215
Cdd:cd01494 163 GG 164
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
31-214 |
2.46e-05 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 45.52 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 31 YGDDQfSKQAAEEIKSAIKCPEATVrFLLGGTQTNQVVINSILEPYEGVISADTGHVAVHEGGaiefsGHKVLtvpsheG 110
Cdd:PRK10534 30 YGDDP-TVNALQDYAAELSGKEAAL-FLPTGTQANLVALLSHCERGEEYIVGQAAHNYLYEAG-----GAAVL------G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 111 KIRPKEVNAY------LDTFYNDFKREHMVFPGMVYIS-HPTEYGTLYSKKELKNLADVCKEHNVPLFMDGARLGYGLMS 183
Cdd:PRK10534 97 SIQPQPIDAAadgtlpLDKVAAKIKPDDIHFARTRLLSlENTHNGKVLPREYLKQAWEFTRERNLALHVDGARIFNAVVA 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1081105957 184 DQSDLtfEDIAKYCDIFYIG-----GTKIGA-LCGEA 214
Cdd:PRK10534 177 YGCEL--KEITQYCDSFTIClskglGTPVGSlLVGNR 211
|
|
| tnaA |
PRK13238 |
tryptophanase; |
152-212 |
9.72e-05 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 44.04 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 152 SKKELKNLADVCKEHNVPLFMDGARL------------GYGlmsdqsDLTFEDIAK----YCDIFYIGGTK-----IGAL 210
Cdd:PRK13238 196 SMANLRAVYEIAKKYGIPVVIDAARFaenayfikqrepGYK------DKSIKEIARemfsYADGLTMSAKKdamvnIGGL 269
|
..
gi 1081105957 211 CG 212
Cdd:PRK13238 270 LC 271
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
52-338 |
2.66e-04 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 42.37 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 52 EATVrFLLGGTQTNQVvinSIL----EPYEGVISADTGHVAVHEGGAIEFSG--HKVLTVPSHEGKIRPKEVNAYLDTfy 125
Cdd:PLN02721 56 EAAL-FVPSGTMGNLI---SVLvhcdVRGSEVILGDNSHIHLYENGGISTLGgvHPRTVKNNEDGTMDLDAIEAAIRP-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 126 ndfkREHMVFPGMVYI----SHPTEYGTLYSKKELKNLADVCKEHNVPLFMDGAR-------LGYGLmsdqsdltfEDIA 194
Cdd:PLN02721 130 ----KGDDHFPTTRLIclenTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGARifnasvaLGVPV---------HRLV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 195 KYCDIFYIGGTK-IGALCGEAIVFTKNNEPKHFTTR------IKQHGALLAKGrLVGVQflelftNN---LYLDiSRHAI 264
Cdd:PLN02721 197 KAADSVSVCLSKgLGAPVGSVIVGSKSFIRKAKRLRktlgggMRQVGVLAAAA-LVALQ------ENvpkLEDD-HKKAK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 265 NMANKMKKgflEKGYQLYFDSP-TNQQFFVLSEEKIKELKQKVKfaIWEKY-----DDNHRVVRFATSWATTEENVDKLL 338
Cdd:PLN02721 269 LLAEGLNQ---IKGLRVNVAAVeTNIVYFDITDGSRITAEKLCK--SLEEHgvllmPGNSSRIRVVTHHQISDSDVQYTL 343
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
142-173 |
3.46e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 42.03 E-value: 3.46e-04
10 20 30
....*....|....*....|....*....|..
gi 1081105957 142 SHPTeyGTLYSKKELKNLADVCKEHNVPLFMD 173
Cdd:PRK05764 174 SNPT--GAVYSPEELEAIADVAVEHDIWVLSD 203
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
38-175 |
1.73e-03 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 40.02 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 38 KQAAEEIKSAIKCPEATVRFLLGGTQTNQVVINSILEPYEG----VISADTGHVAVHEG-GAIEFSGHKVLTVPSH-EGK 111
Cdd:PLN02651 46 EKARAQVAALIGADPKEIIFTSGATESNNLAIKGVMHFYKDkkkhVITTQTEHKCVLDScRHLQQEGFEVTYLPVKsDGL 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1081105957 112 IRPKEVNAYL--DTfyndfkrehmvfpGMVYISHPT-EYGTLyskKELKNLADVCKEHNVPLFMDGA 175
Cdd:PLN02651 126 VDLDELAAAIrpDT-------------ALVSVMAVNnEIGVI---QPVEEIGELCREKKVLFHTDAA 176
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
142-242 |
2.74e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 39.45 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 142 SHPTeyGTLYSKKELKNLADVCKEHNVPLFMDGA--RLGYGLMSDQSDLTFEDIAKYCDI-------FYIGGTKIGALCg 212
Cdd:PRK07568 172 GNPT--GVVYTKEELEMLAEIAKKHDLFLISDEVyrEFVYDGLKYTSALSLEGLEDRVIIidsvskrYSACGARIGCLI- 248
|
90 100 110
....*....|....*....|....*....|
gi 1081105957 213 eaivfTKNNEpkhfttrIKQHGALLAKGRL 242
Cdd:PRK07568 249 -----SKNKE-------LIAAAMKLCQARL 266
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
42-217 |
2.81e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 39.35 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 42 EEIKSAI----KCPEATVRFLLGGTQTNQVVINSILEPYEGVISADTGHVAVhEGGAIEFSGHkVLTVPSHEG----KIR 113
Cdd:PRK06225 69 PELRELIlkdlGLDDDEALITAGATESLYLVMRAFLSPGDNAVTPDPGYLII-DNFASRFGAE-VIEVPIYSEecnyKLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 114 PKEVNAYLDtfyndfKREHMVFpgMVYISHPteYGTLYSKKELKNLADVCKEHNVPLFMDgarLGYGLMSDQSDLTFE-- 191
Cdd:PRK06225 147 PELVKENMD------ENTRLIY--LIDPLNP--LGSSYTEEEIKEFAEIARDNDAFLLHD---CTYRDFAREHTLAAEya 213
|
170 180 190
....*....|....*....|....*....|.
gi 1081105957 192 -----DIAKYCDIFYIGGTKIGALCGEAIVF 217
Cdd:PRK06225 214 pehtvTSYSFSKIFGMAGLRIGAVVATPDLI 244
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
144-206 |
3.38e-03 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 38.96 E-value: 3.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1081105957 144 PTeyGTLYSKKELKNLADVCKEHNVPlfmdgarlgygLMSDQ--SDLTFEDiAKYCDIFYIGGTK 206
Cdd:COG0436 175 PT--GAVYSREELEALAELAREHDLL-----------VISDEiyEELVYDG-AEHVSILSLPGLK 225
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
55-175 |
3.61e-03 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 38.76 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081105957 55 VRFLLGGTQTNQVVINSILEPYEGVIsAD-----TGHVAVheggaiEFSGHKVLTVPS---HEGKIRPKevnAYLDTFyN 126
Cdd:PRK09331 81 ARVTHGAREGKFAVMHSLCKKGDYVV-LDglahyTSYVAA------ERAGLNVREVPKtgyPEYKITPE---AYAEKI-E 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1081105957 127 DFKREHMVFPGMVYISHPT-EYGTLYskkELKNLADVCKEHNVPLFMDGA 175
Cdd:PRK09331 150 EVKEETGKPPALALLTHVDgNYGNLA---DAKKVAKVAHEYGIPFLLNGA 196
|
|
| avtA |
PRK09440 |
valine--pyruvate transaminase; Provisional |
137-180 |
3.91e-03 |
|
valine--pyruvate transaminase; Provisional
Pssm-ID: 236517 Cd Length: 416 Bit Score: 38.68 E-value: 3.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1081105957 137 GMVYISHPTE-YGTLYSKKELKNLADVCKEHNVPLFMDGArlgYG 180
Cdd:PRK09440 181 GAICVSRPTNpTGNVLTDEELEKLDALARQHNIPLLIDNA---YG 222
|
|
| |
