|
Name |
Accession |
Description |
Interval |
E-value |
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
4-337 |
4.45e-160 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 450.67 E-value: 4.45e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 4 LDLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGED 83
Cdd:COG2008 3 IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRPGDEVICHET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 84 CHIIMHETGAPAVIAGVQLRPIKSENGFMSLDDIQSKIRGENIHFPDTSLICVENAHSCGRVISLKHMEKIYNISRQHNI 163
Cdd:COG2008 83 AHIYVDEGGAPEALSGVKLLPVPGEDGKLTPEDLEAAIRPGDVHFPQPGLVSLENTTEGGTVYPLEELRAIAAVAREHGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 164 PIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAPGLVA 243
Cdd:COG2008 163 PLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAGFLAAQGLAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 244 LKEMIPQLKKDYENALLLGKELSKIPNIKVnLDDININMVFFSIENidydevDIINKFYSKGIKINGTEDGKFRFATHYW 323
Cdd:COG2008 243 LEDDLERLAEDHAMARRLAEGLAALPGVRV-PEPVETNIVFVILPD------ELAERLREKGVLFYPWGPGAVRLVTHWD 315
|
330
....*....|....
gi 1564166837 324 IKEEDISYIIETMK 337
Cdd:COG2008 316 TTEEDVDAFLAALA 329
|
|
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
4-336 |
2.72e-141 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 403.36 E-value: 2.72e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 4 LDLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGED 83
Cdd:NF041359 5 IDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEEYIVGDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 84 CHIIMHETGAPAVIAGVQLRPIKSE-NGFMSLDDIQSKIRGENIHFPDTSLICVENAHS--CGRVISLKHMEKIYNISRQ 160
Cdd:NF041359 85 AHIYLYEAGGAAVLGGIHPQPVPNQpDGSLDLDQVRAAIRPDDEHFPRTRLICLENTHNrcGGKVLPLEYLAAVRDLAHE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 161 HNIPIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAPG 240
Cdd:NF041359 165 HGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLAAAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 241 LVALKEMIPQLKKDYENALLLGKELSKIPNIKVNLDDININMVFFSIENIDYDEVDIINKFYSKGIKINGTEDGKFRFAT 320
Cdd:NF041359 245 IVALEEMVERLADDHANAQRLAEGLAALPGVAIQTEPVQTNMVFFSLHEPELDAQALLAFLKERGILLSDVGERRLRAVT 324
|
330
....*....|....*.
gi 1564166837 321 HYWIKEEDISYIIETM 336
Cdd:NF041359 325 HYGITRADIDQAIDAI 340
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
5-287 |
2.23e-140 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 398.90 E-value: 2.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 5 DLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDC 84
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 85 HIIMHETGAPAVIAGVQLRPIKSEN-GFMSLDDIQSKIRGENIH-FPDTSLICVENAH--SCGRVISLKHMEKIYNISRQ 160
Cdd:pfam01212 81 HIHFDETGGHAELGGVQPRPLDGDEaGNMDLEDLEAAIREVGADiFPPTGLISLENTHnsAGGQVVSLENLREIAALARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 161 HNIPIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAPG 240
Cdd:pfam01212 161 HGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1564166837 241 LVALKEMIPQLKKDYENALLLGKELSKIPNIKVNLDDININMVFFSI 287
Cdd:pfam01212 241 LRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAA 287
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
5-337 |
1.12e-129 |
|
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: 373.98 E-value: 1.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 5 DLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDC 84
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 85 HIIMHETGAPAVIAGVQLRPIKSENGFMSLDDIQSKIRGEN-IHFPDTSLICVENAHSCGRVISLKHMEKIYNISRQHNI 163
Cdd:cd06502 81 HIYTDEAGAPEFLSGVKLLPVPGENGKLTPEDLEAAIRPRDdIHFPPPSLVSLENTTEGGTVYPLDELKAISALAKENGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 164 PIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAPGLVA 243
Cdd:cd06502 161 PLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAGLAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 244 LKE--MIPQLKKDYENALLLGKELSKIPnIKVNLDDININMVFFSIEN---IDYDEVDIINKfySKGIKINGTEDGKFRF 318
Cdd:cd06502 241 LENdlWLRRLRHDHEMARRLAEALEELG-GLESEVQTNIVLLDPVEANavfVELSKEAIERR--GEGVLFYAWGEGGVRF 317
|
330
....*....|....*....
gi 1564166837 319 ATHYWIKEEDISYIIETMK 337
Cdd:cd06502 318 VTHWDTTEEDVDELLSALK 336
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
5-341 |
1.28e-127 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 369.40 E-value: 1.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 5 DLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCK-RGDEVILGED 83
Cdd:PLN02721 9 DLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDvRGSEVILGDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 84 CHIIMHETGAPAVIAGVQLRPIK-SENGFMSLDDIQSKIRG-ENIHFPDTSLICVENAH-SCG-RVISLKHMEKIYNISR 159
Cdd:PLN02721 89 SHIHLYENGGISTLGGVHPRTVKnNEDGTMDLDAIEAAIRPkGDDHFPTTRLICLENTHaNCGgRCLSVEYTDKVGELAK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 160 QHNIPIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAP 239
Cdd:PLN02721 169 RHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMRQVGVLAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 240 GLVALKEMIPQLKKDYENALLLGKELSKIPNIKVNLDDININMVFFSI-ENIDYDEVDIINKFYSKGIKINGTEDGKFRF 318
Cdd:PLN02721 249 ALVALQENVPKLEDDHKKAKLLAEGLNQIKGLRVNVAAVETNIVYFDItDGSRITAEKLCKSLEEHGVLLMPGNSSRIRV 328
|
330 340
....*....|....*....|...
gi 1564166837 319 ATHYWIKEEDISYIIETMKISLQ 341
Cdd:PLN02721 329 VTHHQISDSDVQYTLSCFQQAAL 351
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
4-287 |
1.14e-105 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 312.85 E-value: 1.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 4 LDLRSDTVTKPTENMRKAMFKANVGDDVYGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGED 83
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVGQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 84 CHIIMHETGAPAVIAGVQLRPIKS-ENGFMSLDDIQSKIRGENIHFPDTSLICVENAHScGRVISLKHMEKIYNISRQHN 162
Cdd:PRK10534 82 AHNYLYEAGGAAVLGSIQPQPIDAaADGTLPLDKVAAKIKPDDIHFARTRLLSLENTHN-GKVLPREYLKQAWEFTRERN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 163 IPIHLDGARLFNAAAYLDVGVKDITKYCDSVMFSISKGLCAPVGSILAGSKDFIKKARKKRKLMGGGLRQAGVLAAPGLV 242
Cdd:PRK10534 161 LALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILAAAGLY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1564166837 243 ALKEMIPQLKKDYENALLLGKELSKipnIKVNLDDININMVFFSI 287
Cdd:PRK10534 241 ALKHNVARLQEDHDNAAWLAEQLRE---AGADVMRQDTNMLFVRV 282
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
38-211 |
1.06e-17 |
|
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: 79.35 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 38 VNELEEYAANL--VGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDCHIimHETGAPAVIAGVQLRPIKSENGFMSLD 115
Cdd:cd01494 2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHG--SRYWVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 116 DIQSKIRGENIHFPdtSLICVE-NAHSCGRVISLKhmeKIYNISRQHNIPIHLDGARLFNAAAYLDVGVKDItkYCDSVM 194
Cdd:cd01494 80 DVAILEELKAKPNV--ALIVITpNTTSGGVLVPLK---EIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG--GADVVT 152
|
170
....*....|....*..
gi 1564166837 195 FSISKGLCAPVGSILAG 211
Cdd:cd01494 153 FSLHKNLGGEGGGVVIV 169
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
18-274 |
2.15e-09 |
|
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: 58.12 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 18 MRKAMFKANVGDDVYGDDPTVNELEEYAANLVGK--------ETALFVPSGVFGNQLSLFTHCKRGDEVILGE---DCHI 86
Cdd:cd00609 18 EALAAAALRAGLLGYYPDPGLPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDptyPGYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 87 IMhetgapAVIAGVQLRPI--KSENGFM-SLDDIQSKIRgenihfPDTSLICVENAHS-CGRVISLKHMEKIYNISRQHN 162
Cdd:cd00609 98 AA------ARLAGAEVVPVplDEEGGFLlDLELLEAAKT------PKTKLLYLNNPNNpTGAVLSEEELEELAELAKKHG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 163 IPIHLDGA--------RLFNAAAYLDVGVKDItkycdsVMFSISKGLCAP---VGSILAGSKDFIKKARKKRKLMGGGLR 231
Cdd:cd00609 166 ILIISDEAyaelvydgEPPPALALLDAYERVI------VLRSFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSGPS 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1564166837 232 QAGVLAA-----PGLVALKEMIPQLKkdyENALLLGKELSKIPNIKVN 274
Cdd:cd00609 240 TLSQAAAaaaldDGEEHLEELRERYR---RRRDALLEALKELGPLVVV 284
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
38-291 |
3.56e-09 |
|
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: 57.64 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 38 VNELEEYAANLVGKETA---LFVPSGVFGNQL---SLFTHCKRGDEVILGEDCHiimHETGAPAVIA----GVQLRPIKS 107
Cdd:pfam00266 45 YEEAREKVAEFINAPSNdeiIFTSGTTEAINLvalSLGRSLKPGDEIVITEMEH---HANLVPWQELakrtGARVRVLPL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 108 -ENGFMSLDDIQSKIRgenihfPDTSLIC---VENAHscGRVISLKHmekIYNISRQHNIPIHLDGARlfnAAAYLDVGV 183
Cdd:pfam00266 122 dEDGLLDLDELEKLIT------PKTKLVAithVSNVT--GTIQPVPE---IGKLAHQYGALVLVDAAQ---AIGHRPIDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 184 KDITkyCDSVMFSISKgLCAPVG-SILAGSKDFIKKArkkRKLMGGG------------------LRQAGVLAAPGLVAL 244
Cdd:pfam00266 188 QKLG--VDFLAFSGHK-LYGPTGiGVLYGRRDLLEKM---PPLLGGGgmietvslqestfadapwKFEAGTPNIAGIIGL 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1564166837 245 KEMIPQLKK-------DYENAL--LLGKELSKIPNIKVNLDDININMVFFSIENID 291
Cdd:pfam00266 262 GAALEYLSEigleaieKHEHELaqYLYERLLSLPGIRLYGPERRASIISFNFKGVH 317
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
73-337 |
1.97e-08 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 55.15 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 73 KRGDEVILGEDCH----IIMHETgapAVIAGVQLRPIKS-ENGFMSLDDIQSKIRgenihfPDTslicvenahscgRVIS 147
Cdd:COG0520 101 KPGDEILITEMEHhsniVPWQEL---AERTGAEVRVIPLdEDGELDLEALEALLT------PRT------------KLVA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 148 LKHM----------EKIYNISRQHNIPIHLDGARlfnAAAYLDVGVKDItkYCDSVMFSISKgLCAPVGS-ILAGSKDFI 216
Cdd:COG0520 160 VTHVsnvtgtvnpvKEIAALAHAHGALVLVDGAQ---SVPHLPVDVQAL--GCDFYAFSGHK-LYGPTGIgVLYGKRELL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 217 KKArkkRKLMGGG------------LRQ------AGVLAAPGLVALKEMI-------PQLKKDYENALL--LGKELSKIP 269
Cdd:COG0520 234 EAL---PPFLGGGgmiewvsfdgttYADlprrfeAGTPNIAGAIGLGAAIdyleaigMEAIEARERELTayALEGLAAIP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 270 NIKV---NLDDININMVFFSIENIDYDEV-DIINKfysKGI----------------KINGTedgkFRFATHYWIKEEDI 329
Cdd:COG0520 311 GVRIlgpADPEDRSGIVSFNVDGVHPHDVaALLDD---EGIavraghhcaqplmrrlGVPGT----VRASFHLYNTEEEI 383
|
....*...
gi 1564166837 330 SYIIETMK 337
Cdd:COG0520 384 DRLVEALK 391
|
|
| tnaA |
PRK13238 |
tryptophanase; |
3-210 |
4.08e-08 |
|
tryptophanase;
Pssm-ID: 237314 Cd Length: 460 Bit Score: 54.44 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 3 FLDLRSDTVTKP-TENMRKAMFkanVGDDVYGDDPTVNELEEYAANLVGKEtaLFVPsgvfgnqlslfTHCKRGDEVIL- 80
Cdd:PRK13238 47 FIDLLTDSGTGAmSDRQWAAMM---RGDEAYAGSRSYYRLEDAVKDIFGYP--YTIP-----------THQGRAAEQILf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 81 ---GEDCHII---MH--ETGAPAVIAGV--------QLRPIKSENGF---MSLDDIQSKIRG---ENIHFpdtSLICVEN 138
Cdd:PRK13238 111 pvlIKKGDVVpsnYHfdTTRAHIELNGAtavdlvidEALDTGSRHPFkgnFDLEKLEALIEEvgaENVPF---IVMTITN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 139 AHSCGRVISLKHMEKIYNISRQHNIPIHLDGARLF-NA-------AAYLDVGVKDITK----YCDSVMFSISKGLCAPVG 206
Cdd:PRK13238 188 NSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARFAeNAyfikqrePGYKDKSIKEIARemfsYADGLTMSAKKDAMVNIG 267
|
....
gi 1564166837 207 SILA 210
Cdd:PRK13238 268 GLLC 271
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
66-221 |
4.45e-07 |
|
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: 50.90 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 66 LSLFTHCKRGDEVILGE---DCHIIMhetgapAVIAGVQLRPI--KSENGF-MSLDDIQSKIRgenihfPDTSLICVENA 139
Cdd:COG0436 105 LALLALLNPGDEVLVPDpgyPSYRAA------VRLAGGKPVPVplDEENGFlPDPEALEAAIT------PRTKAIVLNSP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 140 HS-CGRVISLKHMEKIYNISRQHNIPI-------HL--DGARLFNAAAYldVGVKDITkycdSVMFSISKGLCAP---VG 206
Cdd:COG0436 173 NNpTGAVYSREELEALAELAREHDLLVisdeiyeELvyDGAEHVSILSL--PGLKDRT----IVINSFSKSYAMTgwrIG 246
|
170
....*....|....*
gi 1564166837 207 SIlAGSKDFIKKARK 221
Cdd:COG0436 247 YA-VGPPELIAALLK 260
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
14-168 |
4.02e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 48.07 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 14 PTENMRKAMFKANVGDDV--YGDDPTVNELEEYAANLVG--------KETALFVPSGVFGNQLSLFTHCK-RGDEVILGE 82
Cdd:pfam00155 15 TLPAVAKAEKDALAGGTRnlYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLAnPGDAILVPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 83 DCHIiMHETGApaVIAGVQLRPI---KSENGFMSLDDIQSKIRGEnihfpdTSLICVENAHS-CGRVISLKHMEKIYNIS 158
Cdd:pfam00155 95 PTYA-SYIRIA--RLAGGEVVRYplyDSNDFHLDFDALEAALKEK------PKVVLHTSPHNpTGTVATLEELEKLLDLA 165
|
170
....*....|
gi 1564166837 159 RQHNIPIHLD 168
Cdd:pfam00155 166 KEHNILLLVD 175
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
36-272 |
1.09e-05 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 46.84 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 36 PTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDC----HIIMHETgapAVIAGVQLRPIKSENgf 111
Cdd:pfam01053 47 PTRDVLEERIAALEGGAAALAFSSGMAAITAAILALLKAGDHIVATDDLyggtYRLFNKV---LPRFGIEVTFVDTSD-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 112 msLDDIQSKIRgenihfPDTSLICVENAHScgrvISLK--HMEKIYNISRQHNIPIHLDGArlFNAAAY---LDVGVkDI 186
Cdd:pfam01053 122 --PEDLEAAIK------PNTKAVYLETPTN----PLLKvvDIEAIAKLAKKHGILVVVDNT--FASPYLqrpLDLGA-DI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 187 -----TKYC----DSVMfsiskglcapvGSILAGSKDFIKKARKKRKLMGGGLR-QAGVLAAPGlvaLKEMIPQLKKDYE 256
Cdd:pfam01053 187 vvhsaTKYIgghsDVVG-----------GVIVVNGEELGKELYFLQNATGAVLSpFDAWLLLRG---LKTLGLRMEQHQE 252
|
250
....*....|....*.
gi 1564166837 257 NALLLGKELSKIPNIK 272
Cdd:pfam01053 253 NAQKVAEFLESHPKVE 268
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
7-274 |
1.74e-05 |
|
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: 46.04 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 7 RSDTVTKPTENMRKAMFKANVGDDVYG--DDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDC 84
Cdd:cd00614 9 QTSTFVFPSPAEAADLFALREGGYIYSriGNPTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 85 H---IIMHETGAPAViaGVQLRPIKSENgfmsLDDIQSKIRgenihfPDTSLICVEN-AHSCGRVISlkhMEKIYNISRQ 160
Cdd:cd00614 89 YggtYRLFERLLPKL--GIEVTFVDPDD----PEALEAAIK------PETKLVYVESpTNPTLKVVD---IEAIAELAHE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 161 HNIPIHLDgarlfN--AAAYL--------DVGVKDITKYC----DSVMfsiskglcapvGSILAGSKDFIKKARKKRKLM 226
Cdd:cd00614 154 HGALLVVD-----NtfATPYLqrplelgaDIVVHSATKYIgghsDVIA-----------GVVVGSGEALIQRLRFLRLAL 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1564166837 227 GGGLR-QAGVLAAPGlvaLKEMIPQLKKDYENALLLGKELSKIPNI-KVN 274
Cdd:cd00614 218 GTILSpFDAWLLLRG---LKTLPLRMERHSENALKVAEFLEKHPKVeRVY 264
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
15-337 |
2.30e-05 |
|
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: 45.84 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 15 TENMRKAMFKANVGDDV---------YGDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDCH 85
Cdd:cd06452 14 TPEARKALIEWGDGYSVcdfcrgrldEIEKPPIKDFHHDLAEFLGMDEARVTPGAREGKFAVMHSLCEKGDWVVVDGLAH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 86 iimHETGAPAVIAGVQLR--PIKSENGF-MSLDDIQSKIRGENIHFPDT-SLICVEnaHSCGRVISLKHMEKIYNISRQH 161
Cdd:cd06452 94 ---YTSYVAAERAGLNVRevPNTGHPEYhITPEGYAEVIEEVKDEFGKPpALALLT--HVDGNYGNLHDAKKIAKVCHEY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 162 NIPIHLDGARlfnAAAYLDVGVKDITkyCDSVMFSISKGL--CAPVGsILAGSKDFI--------KKARKKRKLMGGGLR 231
Cdd:cd06452 169 GVPLLLNGAY---TVGRMPVSGKELG--ADFIVGSGHKSMaaSAPIG-VLATTEEWAdivfrtsqMFKIKEVELLGCTLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 232 QAGVLaapGLVA----LKEMIPQLKKDYENALLLGKELSKIPNIKVnLDDI--NINMVFFsiENIDYDEVDIINK----F 301
Cdd:cd06452 243 GAPLV---TLMAsfphVKERVKRWDEEVEKARWFVAELEKIEGIKQ-LGEKpkNHDLMFF--ETPSFDEIAKKHKrrgyF 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1564166837 302 YSKGIK---INGTEDGK---FRFAThYWIKEEDISYIIETMK 337
Cdd:cd06452 317 LYSELKkrgIHGIKPGLtryFKLST-YGLTWEQVEYVVDAFK 357
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
85-274 |
3.26e-05 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 45.03 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 85 HIIMHETGAPAVIAG----------VQLRPIKSEnGFMSLDDIQSKIRgenihfPDTSLICVenAHSCGRVISLKHMEKI 154
Cdd:PLN02651 90 HVITTQTEHKCVLDScrhlqqegfeVTYLPVKSD-GLVDLDELAAAIR------PDTALVSV--MAVNNEIGVIQPVEEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 155 YNISRQHNIPIHLDGARlfnAAAYLDVGVKDItkycDSVMFSIS-------KGlcapVGSIlagskdFIKK---ARKKRK 224
Cdd:PLN02651 161 GELCREKKVLFHTDAAQ---AVGKIPVDVDDL----GVDLMSISghkiygpKG----VGAL------YVRRrprVRLEPL 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564166837 225 LMGGGL---RQAGVLAAP---GL-----VALKEM--IPQLKKDYENALLLGKElSKIPNIKVN 274
Cdd:PLN02651 224 MSGGGQergRRSGTENTPlvvGLgaaceLAMKEMdyDEKHMKALRERLLNGLR-AKLGGVRVN 285
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
33-337 |
3.71e-05 |
|
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: 44.86 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 33 GDDPTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHCKRGDEVILGEDCHIIMHE----TGAPAVIagvqlrpikse 108
Cdd:cd06454 43 GTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIIDgirlSGAKKRI----------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 109 ngFMSLD--DIQSKIRgENIHFPDTSLICVENAHS-CGrviSLKHMEKIYNISRQHNIPIHLD-----GARLFNAA--AY 178
Cdd:cd06454 112 --FKHNDmeDLEKLLR-EARRPYGKKLIVTEGVYSmDG---DIAPLPELVDLAKKYGAILFVDeahsvGVYGPHGRgvEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 179 LDVGVKDItkycDSVMFSISKGLcAPVGSILAGSKDFIKKarkkrklmgggLRQ----------------AGVLAApgLV 242
Cdd:cd06454 186 FGGLTDDV----DIIMGTLGKAF-GAVGGYIAGSKELIDY-----------LRSyargfifstslppavaAAALAA--LE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 243 ALKEMIPQLKKDYENALLLGKELSKIP-NIKVNLDDININMVFFSIENIdydeVDIINKFYSKGIKIN---------GTE 312
Cdd:cd06454 248 VLQGGPERRERLQENVRYLRRGLKELGfPVGGSPSHIIPPLIGDDPAKA----VAFSDALLERGIYVQairyptvprGTA 323
|
330 340
....*....|....*....|....*...
gi 1564166837 313 dgKFRF---ATHywiKEEDISYIIETMK 337
Cdd:cd06454 324 --RLRIslsAAH---TKEDIDRLLEALK 346
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
21-170 |
3.63e-04 |
|
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: 41.85 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 21 AMFKANVGDDVYGDD---PT--VNELEEYAANLVGKETALFVPSGV-FGNQLSLFTHCKRGDEVILGEDCHIIMHETgap 94
Cdd:cd00615 39 NLFKADVTELTGLDDlldPTgpIKEAQELAARAFGAKHTFFLVNGTsSSNKAVILAVCGPGDKILIDRNCHKSVING--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 95 AVIAGVQlrPIKSENGFMSLDDI-----QSKIRGENIHFPDTSLICVENAHSCGRVISLKhmeKIYNISRQHNIPIHLDG 169
Cdd:cd00615 116 LVLSGAV--PVYLKPERNPYYGIaggipPETFKKALIEHPDAKAAVITNPTYYGICYNLR---KIVEEAHHRGLPVLVDE 190
|
.
gi 1564166837 170 A 170
Cdd:cd00615 191 A 191
|
|
| Tnase_like |
cd00617 |
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ... |
133-210 |
7.82e-04 |
|
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.
Pssm-ID: 99741 Cd Length: 431 Bit Score: 41.19 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 133 LICVENAHSCGRVISLKHMEKIYNISRQHNIPIHLDGARLFNAA--------AYLDVGVKDITK----YCDSVMFSISKG 200
Cdd:cd00617 157 VLTITNNTAGGQPVSMANLREVRELAHKYGIPVVLDAARFAENAyfikereeGYRDKSIAEIARemfsYADGCTMSAKKD 236
|
90
....*....|
gi 1564166837 201 LCAPVGSILA 210
Cdd:cd00617 237 GLVNIGGFLA 246
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
63-223 |
9.10e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 40.69 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 63 GNQLSLFTHCKRGDEVIlgedchiIMHET-----GAPAVI-AGVQLRPIKSENGFM-SLDDIQSKIRgenihfPDTSLIC 135
Cdd:PRK07324 92 ANFLVLYALVEPGDHVI-------SVYPTyqqlyDIPESLgAEVDYWQLKEENGWLpDLDELRRLVR------PNTKLIC 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 136 VENAHS-CGRVISLKHMEKIYNISRQHNI---------PIHLDGarlfNAAAYLDVGVKDItkycdSVMfSISKGLCAP- 204
Cdd:PRK07324 159 INNANNpTGALMDRAYLEEIVEIARSVDAyvlsdevyrPLDEDG----STPSIADLYEKGI-----STN-SMSKTYSLPg 228
|
170 180
....*....|....*....|.
gi 1564166837 205 --VGSIlAGSKDFIKKARKKR 223
Cdd:PRK07324 229 irVGWI-AANEEVIDILRKYR 248
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
36-165 |
1.50e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 40.05 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 36 PTVNELEEYAANLVGKETALFVPSGVFGNQLSLFTHC-KRGDEVILgedchiimhetgaPA--------VIAGVQLRP-- 104
Cdd:COG0399 30 PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGiGPGDEVIT-------------PAftfvatanAILYVGATPvf 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1564166837 105 --IKSENGFMSLDDIQSKIRgenihfPDTSLICVenAHSCGRVIslkHMEKIYNISRQHNIPI 165
Cdd:COG0399 97 vdIDPDTYNIDPEALEAAIT------PRTKAIIP--VHLYGQPA---DMDAIMAIAKKHGLKV 148
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
81-206 |
8.42e-03 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 37.78 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1564166837 81 GEDCHIIMHETGApavIAGVQLRPIKS-ENGFMSLDDIQSKIRgENIHFPDTSLICVENAHSCGrVISLKHMEKIYNISR 159
Cdd:pfam00282 151 SDQAHSSIEKAAL---YGGVKLREIPSdDNGKMRGMDLEKAIE-EDKENGLIPFFVVATLGTTG-SGAFDDLQELGDICA 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1564166837 160 QHNIPIHLDGA---RLFNAAAY--LDVGVkditKYCDSVMFSISKGLCAPVG 206
Cdd:pfam00282 226 KHNLWLHVDAAyggSAFICPEFrhWLFGI----ERADSITFNPHKWMLVLLD 273
|
|
| |
