|
Name |
Accession |
Description |
Interval |
E-value |
| GntG_guanitoxin |
NF041359 |
GntG family PLP-dependent aldolase; |
34-375 |
2.75e-128 |
|
GntG family PLP-dependent aldolase;
Pssm-ID: 469251 [Multi-domain] Cd Length: 342 Bit Score: 372.16 E-value: 2.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 34 HTSIDLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIV 113
Cdd:NF041359 2 SEPIDLRSDTVTQPTPAMRQAMAEAEVGDDVYGEDPTVNRLEALAAELLGKEAALFVPSGTMGNLIALLSHCGRGEEYIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 114 GRYNHIHRWEQGNYAQFAGISATTLEVKPDGTMDLNDIEQAIRVKDCHMPASKLICIENTHNYTGGKALPIEWMRSVKQL 193
Cdd:NF041359 82 GDQAHIYLYEAGGAAVLGGIHPQPVPNQPDGSLDLDQVRAAIRPDDEHFPRTRLICLENTHNRCGGKVLPLEYLAAVRDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 194 AERRDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWRQSGILA 273
Cdd:NF041359 162 AHEHGLALHLDGARLFNAAVALGVDPADLVRPFDSVSVCLSKGLAAPVGSVLVGSREFIARARRLRKLLGGGMRQAGVLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 274 AAAHIALDHADATIRADHERAKTLARMINDATPEEFRTkvfaaEKDITNMVLVH-CQNGVTVQQLTDFFQKHDILAMTFD 352
Cdd:NF041359 242 AAGIVALEEMVERLADDHANAQRLAEGLAALPGVAIQT-----EPVQTNMVFFSlHEPELDAQALLAFLKERGILLSDVG 316
|
330 340
....*....|....*....|...
gi 193206524 353 ARRIRMVLNWNVSDENLETIVEV 375
Cdd:NF041359 317 ERRLRAVTHYGITRADIDQAIDA 339
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
37-381 |
2.42e-126 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 366.70 E-value: 2.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 37 IDLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRY 116
Cdd:COG2008 3 IDFRSDTVTGPHPEMLEAMAAANVGDDVYGEDPTVNRLEERVAELFGKEAALFVPSGTMANQLALRAHTRPGDEVICHET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 117 NHIHRWEQGNYAQFAGISATTLEVkPDGTMDLNDIEQAIRVKDCHMPASKLICIENTHNytGGKALPIEWMRSVKQLAER 196
Cdd:COG2008 83 AHIYVDEGGAPEALSGVKLLPVPG-EDGKLTPEDLEAAIRPGDVHFPQPGLVSLENTTE--GGTVYPLEELRAIAAVARE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 197 RDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWRQSGilaaaa 276
Cdd:COG2008 160 HGLPLHLDGARLFNAAAALGVSLAEITAGVDSVSFGLTKGLGAPGGAVLAGDPEFIEEARRWRKRLGGLMRQAG------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 277 hialdhadatI----------------RADHERAKTLARMINDATPEEFRTKVFaaekdiTNMVLVHCQNGvtvqqLTDF 340
Cdd:COG2008 234 ----------FlaaqglaaleddlerlAEDHAMARRLAEGLAALPGVRVPEPVE------TNIVFVILPDE-----LAER 292
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 193206524 341 FQKHDILAMTFDARRIRMVLNWNVSDENLETIVEVYKKFLK 381
Cdd:COG2008 293 LREKGVLFYPWGPGAVRLVTHWDTTEEDVDAFLAALAELLA 333
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
38-327 |
2.57e-125 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 362.69 E-value: 2.57e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 38 DLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRYN 117
Cdd:pfam01212 1 DLRSDTVTGPTPAMREAMAAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 118 HIHRWEQGNYAQFAGISATTLEVKPDGTMDLNDIEQAIR-VKDCHMPASKLICIENTHNYTGGKALPIEWMRSVKQLAER 196
Cdd:pfam01212 81 HIHFDETGGHAELGGVQPRPLDGDEAGNMDLEDLEAAIReVGADIFPPTGLISLENTHNSAGGQVVSLENLREIAALARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 197 RDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWRQSGILAAAA 276
Cdd:pfam01212 161 HGIPVHLDGARFANAAVALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQAGVLAAAG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 193206524 277 HIALDHADATIRADHERAKTLARMINDATPEEFRtkvfaaeKDITNMVLVH 327
Cdd:pfam01212 241 LRALEEGVARLARDHATARRLAEGLELLRLAIPR-------RVYTNTHMVY 284
|
|
| PLN02721 |
PLN02721 |
threonine aldolase |
30-383 |
3.78e-124 |
|
threonine aldolase
Pssm-ID: 178323 [Multi-domain] Cd Length: 353 Bit Score: 362.08 E-value: 3.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 30 SNKTHTSIDLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQ-RG 108
Cdd:PLN02721 1 GRMVSRVVDLRSDTVTKPTDAMRAAMANAEVDDDVLGYDPTALRLEEEMAKIFGKEAALFVPSGTMGNLISVLVHCDvRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 109 EEIIVGRYNHIHRWEQGNYAQFAGISATTLEVKPDGTMDLNDIEQAIRVK-DCHMPASKLICIENTHNYTGGKALPIEWM 187
Cdd:PLN02721 81 SEVILGDNSHIHLYENGGISTLGGVHPRTVKNNEDGTMDLDAIEAAIRPKgDDHFPTTRLICLENTHANCGGRCLSVEYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 188 RSVKQLAERRDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWR 267
Cdd:PLN02721 161 DKVGELAKRHGLKLHIDGARIFNASVALGVPVHRLVKAADSVSVCLSKGLGAPVGSVIVGSKSFIRKAKRLRKTLGGGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 268 QSGILAAAAHIALDHADATIRADHERAKTLARMINDATpeEFRTKVFAAEkdiTNMVLVHCQNG--VTVQQLTDFFQKHD 345
Cdd:PLN02721 241 QVGVLAAAALVALQENVPKLEDDHKKAKLLAEGLNQIK--GLRVNVAAVE---TNIVYFDITDGsrITAEKLCKSLEEHG 315
|
330 340 350
....*....|....*....|....*....|....*...
gi 193206524 346 ILAMTFDARRIRMVLNWNVSDENLETIVEVYKKFLKQL 383
Cdd:PLN02721 316 VLLMPGNSSRIRVVTHHQISDSDVQYTLSCFQQAALTL 353
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
38-379 |
6.79e-104 |
|
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: 310.03 E-value: 6.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 38 DLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRYN 117
Cdd:cd06502 1 DFRSDTVTGPTPEMLEAMAAANVGDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 118 HIHRWEQGNYAQFAGISATTLEvKPDGTMDLNDIEQAIRVK-DCHMPASKLICIENTHNYTGGKalPIEWMRSVKQLAER 196
Cdd:cd06502 81 HIYTDEAGAPEFLSGVKLLPVP-GENGKLTPEDLEAAIRPRdDIHFPPPSLVSLENTTEGGTVY--PLDELKAISALAKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 197 RDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWRQSGILAAAA 276
Cdd:cd06502 158 NGLPLHLDGARLANAAAALGVALKTYKSGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRKQAGGGMRQSGFLAAAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 277 HIALDHADATIRA--DHERAKTLArmindatpEEFRTKVFAAEKDITNMVLVH--CQNGVTVQ--QLTDFFQKHDILAMT 350
Cdd:cd06502 238 LAALENDLWLRRLrhDHEMARRLA--------EALEELGGLESEVQTNIVLLDpvEANAVFVElsKEAIERRGEGVLFYA 309
|
330 340
....*....|....*....|....*....
gi 193206524 351 FDARRIRMVLNWNVSDENLETIVEVYKKF 379
Cdd:cd06502 310 WGEGGVRFVTHWDTTEEDVDELLSALKAV 338
|
|
| PRK10534 |
PRK10534 |
L-threonine aldolase; Provisional |
37-382 |
1.14e-95 |
|
L-threonine aldolase; Provisional
Pssm-ID: 236710 [Multi-domain] Cd Length: 333 Bit Score: 288.97 E-value: 1.14e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 37 IDLRSDTVTVPSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRY 116
Cdd:PRK10534 2 IDLRSDTVTRPSRAMLEAMMAAPVGDDVYGDDPTVNALQDYAAELSGKEAALFLPTGTQANLVALLSHCERGEEYIVGQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 117 NHIHRWEQGNYAQFAGISATTLEVKPDGTMDLNDIEQAIRVKDCHMPASKLICIENTHNytgGKALPIEWMRSVKQLAER 196
Cdd:PRK10534 82 AHNYLYEAGGAAVLGSIQPQPIDAAADGTLPLDKVAAKIKPDDIHFARTRLLSLENTHN---GKVLPREYLKQAWEFTRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 197 RDLKVHMDGARIYNAAVASNCSVSKIASFADTVQMCFSKGLGAPVGSIVVGPKDFIDRARHSRKALGGGWRQSGILAAAA 276
Cdd:PRK10534 159 RNLALHVDGARIFNAVVAYGCELKEITQYCDSFTICLSKGLGTPVGSLLVGNRDYIKRARRWRKMTGGGMRQAGILAAAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 277 HIALDHADATIRADHERAKTLARMINDATPEEFRTKvfaaekdiTNMVLVHcQNGVTVQQLTDFFQKHDILAMTfdARRI 356
Cdd:PRK10534 239 LYALKHNVARLQEDHDNAAWLAEQLREAGADVMRQD--------TNMLFVR-VGEEQAAALGEYMRERNVLINA--SPIV 307
|
330 340
....*....|....*....|....*.
gi 193206524 357 RMVLNWNVSDENLETIVEVYKKFLKQ 382
Cdd:PRK10534 308 RLVTHLDVSREQLAEVVAHWRAFLAR 333
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
74-247 |
6.69e-16 |
|
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: 74.73 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 74 LEQRCAELF--GKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRYNHIhrweqGNYAQFAGI-SATTLEV-KPDGTMDLN 149
Cdd:cd01494 5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHG-----SRYWVAAELaGAKPVPVpVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 150 DIEQAIRVKdcHMPASKLICIENTHNYTGGKALPIEwmrsVKQLAERRDLKVHMDGARiynAAVASNCSVSKI-ASFADT 228
Cdd:cd01494 80 DVAILEELK--AKPNVALIVITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAAS---AGGASPAPGVLIpEGGADV 150
|
170
....*....|....*....
gi 193206524 229 VQMCFSKGLGAPVGSIVVG 247
Cdd:cd01494 151 VTFSLHKNLGGEGGGVVIV 169
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
45-256 |
2.21e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 52.31 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 45 TVPSVemRRAMAEAIVGDDV--YGEDTTTNRLEQRCAELFG--------KEAGLFVTSGTMGNL-LAIMAHCQRGEEIIV 113
Cdd:pfam00155 15 TLPAV--AKAEKDALAGGTRnlYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIeALIFLLANPGDAILV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 114 GRYNHihrweqGNYAQfaGISATTLEVKP-------DGTMDLNDIEQAIRvkdchmPASKLICIENTHNYTgGKALPIEW 186
Cdd:pfam00155 93 PAPTY------ASYIR--IARLAGGEVVRyplydsnDFHLDFDALEAALK------EKPKVVLHTSPHNPT-GTVATLEE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193206524 187 MRSVKQLAERRDLKVHMDgaRIYNAAVASNCSVSKIASFAD------TVQmCFSKGLGAP---VGsIVVGPKDFIDRAR 256
Cdd:pfam00155 158 LEKLLDLAKEHNILLLVD--EAYAGFVFGSPDAVATRALLAegpnllVVG-SFSKAFGLAgwrVG-YILGNAAVISQLR 232
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
89-206 |
9.47e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 50.52 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 89 FVTSGTMG-NLLA-IMAHCQRGEEIIVGRYNH---IHRWEQgnYAQFAGISATTLEVKPDGTMDLNDIEQAIRvkdchmP 163
Cdd:COG0520 82 FTRGTTEAiNLVAyGLGRLKPGDEILITEMEHhsnIVPWQE--LAERTGAEVRVIPLDEDGELDLEALEALLT------P 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 193206524 164 ASKLICIenTH--NYTGGKaLPIEWMrsvKQLAERRDLKVHMDGA 206
Cdd:COG0520 154 RTKLVAV--THvsNVTGTV-NPVKEI---AALAHAHGALVLVDGA 192
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
45-204 |
3.26e-06 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 48.57 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 45 TVP-SVEMRRAMAEAivGDDVYGED-------TTTNRLEQRCAELF-----GKEAGLFVTS-GTMGNLLAIM----AHCQ 106
Cdd:PRK02948 9 TTPmSKEALQTYQKA--ASQYFGNEsslhdigGTASSLLQVCRKTFaemigGEEQGIYFTSgGTESNYLAIQsllnALPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 107 RGEEIIVGRYNH--IHrweqgNYAQF---AGISATTLEVKPDGTMDLNDIEQAIRvkdchmPASKLICIENTHNYTGgka 181
Cdd:PRK02948 87 NKKHIITTPMEHasIH-----SYFQSlesQGYTVTEIPVDKSGLIRLVDLERAIT------PDTVLASIQHANSEIG--- 152
|
170 180
....*....|....*....|...
gi 193206524 182 lPIEWMRSVKQLAERRDLKVHMD 204
Cdd:PRK02948 153 -TIQPIAEIGALLKKYNVLFHSD 174
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
40-264 |
3.96e-06 |
|
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: 48.35 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 40 RSDTVTVPSVEMRRAMAEAIVGDDVYGEDT--TTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGR-- 115
Cdd:cd00614 9 QTSTFVFPSPAEAADLFALREGGYIYSRIGnpTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDdl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 116 YnhihrweQGNYAQFA------GISATTleVKPDgtmDLNDIEQAIRvkdchmPASKLICIENTHNYTgGKALPIEwmrS 189
Cdd:cd00614 89 Y-------GGTYRLFErllpklGIEVTF--VDPD---DPEALEAAIK------PETKLVYVESPTNPT-LKVVDIE---A 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 190 VKQLAERRDLKVHMD--------------GARIynaaVASncSVSK-IASFADTVqmcfskglgapVGSIVVGPKDFIDR 254
Cdd:cd00614 147 IAELAHEHGALLVVDntfatpylqrplelGADI----VVH--SATKyIGGHSDVI-----------AGVVVGSGEALIQR 209
|
250
....*....|
gi 193206524 255 ARHSRKALGG 264
Cdd:cd00614 210 LRFLRLALGT 219
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
74-256 |
1.49e-05 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 46.77 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 74 LEQRCAELFGKEAGLFVTSGTMGNLLAI--MAHCQRGEEIIVGRYNHIHRWEqgnyaqfaGISATTLEVKPDGTMDLNDI 151
Cdd:PRK13392 96 LERELADLHGKESALLFTSGYVSNDAALstLGKLLPGCVILSDALNHASMIE--------GIRRSGAEKQVFRHNDLADL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 152 EQAIRVKDCHMPasKLICIENTHNYTGGKAlPIEwmrSVKQLAERRDL-----KVHMDGarIYNAAVASNCSVSKIASFA 226
Cdd:PRK13392 168 EEQLASVDPDRP--KLIAFESVYSMDGDIA-PIE---AICDLADRYNAltyvdEVHAVG--LYGARGGGIAERDGLMDRI 239
|
170 180 190
....*....|....*....|....*....|
gi 193206524 227 DTVQMCFSKGLGApVGSIVVGPKDFIDRAR 256
Cdd:PRK13392 240 DMIQGTLAKAFGC-LGGYIAASADLIDFVR 268
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
66-257 |
1.99e-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: 46.01 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 66 GEDTTTNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRYNHIHRWEqgnyaqfaGISATTLEVKPDGT 145
Cdd:cd06454 43 GTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLAGKGDLIISDSLNHASIID--------GIRLSGAKKRIFKH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 146 MDLNDIEQAIRvKDCHMPASKLICIENTHNYTGGKAlPIewmRSVKQLAERRDLKVHMD--------GARiyNAAVASNC 217
Cdd:cd06454 115 NDMEDLEKLLR-EARRPYGKKLIVTEGVYSMDGDIA-PL---PELVDLAKKYGAILFVDeahsvgvyGPH--GRGVEEFG 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 193206524 218 SV-SKIasfaDTVQMCFSKGLGApVGSIVVGPKDFIDRARH 257
Cdd:cd06454 188 GLtDDV----DIIMGTLGKAFGA-VGGYIAGSKELIDYLRS 223
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
75-206 |
2.21e-05 |
|
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: 45.70 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 75 EQRCAELFGKEAGLFVTSGT-MGNLLAIMAHCQRGEEIIVGRYNH--IHrweqgNYAQFAGISATTLEVKPDGTMDLN-- 149
Cdd:cd00615 65 QELAARAFGAKHTFFLVNGTsSSNKAVILAVCGPGDKILIDRNCHksVI-----NGLVLSGAVPVYLKPERNPYYGIAgg 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 193206524 150 -DIEQAIRVKDCHMPASKLICIENThnYTGgkalPIEWMRSVKQLAERRDLKVHMDGA 206
Cdd:cd00615 140 iPPETFKKALIEHPDAKAAVITNPT--YYG----ICYNLRKIVEEAHHRGLPVLVDEA 191
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
45-206 |
3.49e-05 |
|
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: 45.59 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 45 TVPSVEMRRAMAEAI---VGDdvYGEDTTTNRLEQRC----AELFG--KEA-GLFVTSGTMGNLLAIMA--HCQRGEEII 112
Cdd:COG0076 78 TTPAALAADLLASALnqnMGD--WDTSPAATELEREVvrwlADLLGlpEGAgGVFTSGGTEANLLALLAarDRALARRVR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 113 VGRYNHIHRW-----EQGNY-----AQFAGI---SATTLEVKPDGTMDLNDIEQAIRvkDCHMPASKLICI----ENThn 175
Cdd:COG0076 156 AEGLPGAPRPrivvsEEAHSsvdkaARLLGLgrdALRKVPVDEDGRMDPDALEAAID--EDRAAGLNPIAVvataGTT-- 231
|
170 180 190
....*....|....*....|....*....|..
gi 193206524 176 YTGgkAL-PIEwmrSVKQLAERRDLKVHMDGA 206
Cdd:COG0076 232 NTG--AIdPLA---EIADIAREHGLWLHVDAA 258
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
62-206 |
7.34e-05 |
|
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: 44.50 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 62 DDVYGEDTTTNRLEQRC----AELFG----KEAGLFVTSGTMGNLLAIMAH-------CQRGEEIIVGRYN-----HIH- 120
Cdd:cd06450 27 DFTWDESPAATEMEAEVvnwlAKLFGlpseDADGVFTSGGSESNLLALLAArdrarkrLKAGGGRGIDKLVivcsdQAHv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 121 RWEQGnyAQFAGISATTLEVKPDGTMDLNDIEQAI--RVKDCHMPASkLICIENTHNYtgGKALPIEwmrSVKQLAERRD 198
Cdd:cd06450 107 SVEKA--AAYLDVKVRLVPVDEDGRMDPEALEAAIdeDKAEGLNPIM-VVATAGTTDT--GAIDPLE---EIADLAEKYD 178
|
....*...
gi 193206524 199 LKVHMDGA 206
Cdd:cd06450 179 LWLHVDAA 186
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
47-360 |
1.17e-04 |
|
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: 43.87 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 47 PSVEMRRAMAEAIVGDDVYGEDTTTNRLEQRCAELFGKEAGL-------FVTSG-TMGNLLAIMAHCQRGEEIIVGRYN- 117
Cdd:cd00609 14 PEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVdvppeeiVVTNGaQEALSLLLRALLNPGDEVLVPDPTy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 118 HIHRweqgNYAQFAGISATTLEVKPDGtMDLNDIEQAIRVKDchmPASKLICIENTHNYTGgKALPIEWMRSVKQLAERR 197
Cdd:cd00609 94 PGYE----AAARLAGAEVVPVPLDEEG-GFLLDLELLEAAKT---PKTKLLYLNNPNNPTG-AVLSEEELEELAELAKKH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 198 DLKVHMDGAriYNAAVASNCSVSKIASFADTVQMC----FSKGLGAP---VGSIVVGPKDFIDRARHSRKALGGGwrQSG 270
Cdd:cd00609 165 GILIISDEA--YAELVYDGEPPPALALLDAYERVIvlrsFSKTFGLPglrIGYLIAPPEELLERLKKLLPYTTSG--PST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 271 ILAAAAHIALDHADATIRADH----ERAKTLARMINDATPEEFRtkvfaaEKDITNMVLVHCQNGVTVQQLTDFFQKHDI 346
Cdd:cd00609 241 LSQAAAAAALDDGEEHLEELReryrRRRDALLEALKELGPLVVV------KPSGGFFLWLDLPEGDDEEFLERLLLEAGV 314
|
330 340
....*....|....*....|
gi 193206524 347 LAMTFDA------RRIRMVL 360
Cdd:cd00609 315 VVRPGSAfgeggeGFVRLSF 334
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
71-201 |
2.04e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 43.13 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 71 TNRLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHC-QRGEEIIVGRYNhihrweqgnyaqFAgisATTL----------- 138
Cdd:COG0399 32 VKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGiGPGDEVITPAFT------------FV---ATANailyvgatpvf 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193206524 139 -EVKPD-GTMDLNDIEQAIRvkdchmPASKLICIenTHNYtGgkaLPIEwMRSVKQLAERRDLKV 201
Cdd:COG0399 97 vDIDPDtYNIDPEALEAAIT------PRTKAIIP--VHLY-G---QPAD-MDAIMAIAKKHGLKV 148
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
73-118 |
2.71e-04 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 42.84 E-value: 2.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 193206524 73 RLEQRCAELFGKEAGLFVTSGTMGNLLAIMAHCQRGEEIIVGRYNH 118
Cdd:PRK05958 88 ALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNH 133
|
|
| Tnase_like |
cd00617 |
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ... |
144-234 |
1.34e-03 |
|
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: 40.42 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 144 GTMDLNDIEQAIrvKDCHMPASKLICIENTHNYTGGKALPIEWMRSVKQLAERRDLKVHMDGARIynaavASNCSVSKI- 222
Cdd:cd00617 134 GNIDVAKLEKLI--DEVGAENIPYIVLTITNNTAGGQPVSMANLREVRELAHKYGIPVVLDAARF-----AENAYFIKEr 206
|
90
....*....|....*...
gi 193206524 223 ------ASFADTVQMCFS 234
Cdd:cd00617 207 eegyrdKSIAEIAREMFS 224
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
75-118 |
2.00e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 40.18 E-value: 2.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 193206524 75 EQRCAELFGKEAGLFVTSGTMG-NLLAIMAHCQRGEEIIVGRYNH 118
Cdd:pfam01276 72 QKYAARVFGADKSYFVVNGTSGsNKTVGMAVCTPGDTILIDRNCH 116
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
76-265 |
2.22e-03 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 39.64 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 76 QRCAELFGKEAG--LFVTSGTMGNLLAI----MAHCQRGEEIIVGRYNHIHRWEQGNYAQFAGISATTLEVKPDGTMDLN 149
Cdd:PLN02651 50 AQVAALIGADPKeiIFTSGATESNNLAIkgvmHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 150 DIEQAIRvkdchmPASKLICIENTHNYTGGkalpIEWMRSVKQLAERRDLKVHMDGARiynaavasncSVSKIASFADT- 228
Cdd:PLN02651 130 ELAAAIR------PDTALVSVMAVNNEIGV----IQPVEEIGELCREKKVLFHTDAAQ----------AVGKIPVDVDDl 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 193206524 229 -VQMCFSKG--LGAP--VGSIVVGPkdfidRARHSRKAL--GGG 265
Cdd:PLN02651 190 gVDLMSISGhkIYGPkgVGALYVRR-----RPRVRLEPLmsGGG 228
|
|
| YnbB |
COG4100 |
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion ... |
62-255 |
2.73e-03 |
|
Cystathionine beta-lyase family protein involved in aluminum resistance [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 443276 Cd Length: 409 Bit Score: 39.70 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 62 DDVyGEDTttnrLEQRCAELFGKEAGL----FVtSGT-------MGNL------LAIMahcqrG------EEIIVGRYNh 118
Cdd:COG4100 55 DDI-GRDT----LERVYADVFGAEDALvrpqIV-SGThaialalFGVLrpgdelLSIT-----GkpydtlEEVIGIRGE- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193206524 119 ihrwEQGNYAQFaGISATTLEVKPDGTMDLNDIEQAIRvkdchmPASKLICIENTHNYTGGKALPI----EWMRSVKqlA 194
Cdd:COG4100 123 ----GQGSLKEF-GISYRQVPLTEDGKIDLEAIKKAIN------EKTKMVLIQRSRGYSWRPSLTIeeigEIIKFVK--S 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193206524 195 ERRDLKVHMDgariynaavasNCsvskIASFADTVQ--------MCFS--KGLG---APVGSIVVGPKDFIDRA 255
Cdd:COG4100 190 INPDVICFVD-----------NC----YGEFVETREptevgadlMAGSliKNPGgglAPTGGYIAGRKDLVELA 248
|
|
| |
