|
Name |
Accession |
Description |
Interval |
E-value |
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
222-638 |
1.46e-127 |
|
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: 381.40 E-value: 1.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 222 PLNPVFDTTTVAKTIAIFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLH 301
Cdd:COG0436 2 KLSSRLARLPPSPIREVSALAAELKAAGEDVIDLGIGEPDFPTPDHIREAAIEALDDGVTGYTPSAGIPELREAIAAYYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 302 CTKGVSYDPaTEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTL 381
Cdd:COG0436 82 RRYGVDLDP-DEILVTNGAKEALALALLALLNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENGFLPDPEALEAAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 382 TanPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQD-EGVServcknFAMIPGMYERTI 460
Cdd:COG0436 161 T--PRTKAIVLNSPNNPTGAVYSREELEALAELARE---HDLLVISDEIYEELVYDGaEHVS------ILSLPGLKDRTI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 461 LINGFSKAYAMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEkgEVRiakdlHELDLKRQYV 540
Cdd:COG0436 230 VINSFSKSYAMTGWRIGYAVGPPELIAALLKLQSNLTSCAPTPAQYAAAAALEGPQDYVE--EMR-----AEYRRRRDLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 541 VKRLREMpKMRFAYPTSSFYIFMDLAlyfegktayspdktEVLHNVDDFCDYLIRTTGVAVGPGSDMGEPLG--IRISYA 618
Cdd:COG0436 303 VEGLNEI-GLSVVKPEGAFYLFADVP--------------ELGLDSEEFAERLLEEAGVAVVPGSAFGPAGEgyVRISYA 367
|
410 420
....*....|....*....|
gi 2064415124 619 GPMDTMVRAMDGLELALKSL 638
Cdd:COG0436 368 TSEERLEEALERLARFLERY 387
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
235-639 |
3.10e-123 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 370.61 E-value: 3.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 235 TIAIFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPAtEI 314
Cdd:PRK05764 16 TLAVTAKAKELKAQGRDVISLGAGEPDFDTPEHIKEAAIEALDDGKTKYTPAAGIPELREAIAAKLKRDNGLDYDPS-QV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 315 QICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCN 394
Cdd:PRK05764 95 IVTTGAKQALYNAFMALLDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENGFKLTVEQLEAAIT--PKTKALILNS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 395 PSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVSERVcknfAMIPGMYERTILINGFSKAYAMTGL 474
Cdd:PRK05764 173 PSNPTGAVYSPEELEAIADVAVE---HDIWVLSDEIYEKLVYDGAEFTSIA----SLSPELRDRTITVNGFSKAYAMTGW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 475 RIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEkgEVRiakdlHELDLKRQYVVKRLREMPKMRFAY 554
Cdd:PRK05764 246 RLGYAAGPKELIKAMSKLQSHSTSNPTSIAQYAAVAALNGPQDEVE--EMR-----QAFEERRDLMVDGLNEIPGLECPK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 555 PTSSFYIFMDLALYFEGKTAyspdktevlhNVDDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVRAMDGLELA 634
Cdd:PRK05764 319 PEGAFYVFPNVSKLLGKSIT----------DSLEFAEALLEEAGVAVVPGIAFGAPGYVRLSYATSLEDLEEGLERIERF 388
|
....*
gi 2064415124 635 LKSLT 639
Cdd:PRK05764 389 LESLK 393
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
253-632 |
3.98e-85 |
|
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: 270.37 E-value: 3.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 253 YSLCVGEPDFPPPKSVLDAGVRALQN-GQTKYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSGAQQALYNVILAI 331
Cdd:cd00609 1 IDLSIGEPDFPPPPEVLEALAAAALRaGLLGYYPDPGLPELREAIAEWLGRRGGVDVPP-EEIVVTNGAQEALSLLLRAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 332 CCPGDKVILPSPYWGNYEGIITQvkAGLVPLHNSLEEDYLINPAELEKTLTANPETKIVILCNPSNPAGTLHSPEHLEKI 411
Cdd:cd00609 80 LNPGDEVLVPDPTYPGYEAAARL--AGAEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSEEELEEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 412 AAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPK-HFIEACQ 490
Cdd:cd00609 158 AELAKK---HGILIISDEAYAELVYDGEPPP------ALALLDAYERVIVLRSFSKTFGLPGLRIGYLIAPPeELLERLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 491 LMQGQTTSCANSVGQVMAIEAMKLELASIEkgEVRiakdlHELDLKRQYVVKRLREMPKMRFAYPTSSFYIFMDLalyfe 570
Cdd:cd00609 229 KLLPYTTSGPSTLSQAAAAAALDDGEEHLE--ELR-----ERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL----- 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064415124 571 gktaysPDKTEvlhnvDDFCDYLIRTTGVAVGPGSDMGEPL--GIRISYAGPMDTMVRAMDGLE 632
Cdd:cd00609 297 ------PEGDD-----EEFLERLLLEAGVVVRPGSAFGEGGegFVRLSFATPEEELEEALERLA 349
|
|
| PRK06107 |
PRK06107 |
aspartate transaminase; |
241-638 |
3.59e-79 |
|
aspartate transaminase;
Pssm-ID: 180403 Cd Length: 402 Bit Score: 256.59 E-value: 3.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 241 KTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPAtEIQICSGA 320
Cdd:PRK06107 24 RARELRAAGRSIVDLTVGEPDFDTPDHIKQAAVAAIERGETKYTLVNGTPALRKAIIAKLERRNGLHYADN-EITVGGGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 321 QQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAG 400
Cdd:PRK06107 103 KQAIFLALMATLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQGFKLTPEALEAAIT--PRTRWLILNAPSNPTG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 401 TLHSPEHLEKIAAVLRKpqFRHVVVISDEIYEQLVYQDEGVSERVcknfAMIPGMYERTILINGFSKAYAMTGLRIGYMA 480
Cdd:PRK06107 181 AVYSRAELRALADVLLR--HPHVLVLTDDIYDHIRFDDEPTPHLL----AAAPELRDRVLVTNGVSKTYAMTGWRIGYAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 481 GPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLElASIEKGEVRIAKdlheldLKRQYVVKRLREMPKMRFAYPTSSFY 560
Cdd:PRK06107 255 GPADLIAAINKLQSQSSSCPSSISQAAAAAALNGD-QSFVTESVAVYK------QRRDYALALLNAIPGLSCLVPDGAFY 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064415124 561 IFMDLALYFeGKTaySPDKTeVLHNVDDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVRAMDGLELALKSL 638
Cdd:PRK06107 328 LYVNCAGLI-GKT--TPEGK-VLETDQDVVLYLLDSAGVAVVQGTAYGLSPYFRLSIATSLETLEEACARIERAVAAL 401
|
|
| PRK07682 |
PRK07682 |
aminotransferase; |
245-628 |
1.64e-75 |
|
aminotransferase;
Pssm-ID: 181082 [Multi-domain] Cd Length: 378 Bit Score: 246.19 E-value: 1.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 245 LEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQAL 324
Cdd:PRK07682 15 LAANMEGVISLGVGEPDFVTPWNVREASIRSLEQGYTSYTANAGLLELRQEIAKYLKKRFAVSYDPNDEIIVTVGASQAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 325 YNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAGTLHS 404
Cdd:PRK07682 95 DVAMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENEFKVQPAQIEAAIT--AKTKAILLCSPNNPTGAVLN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 405 PEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKH 484
Cdd:PRK07682 173 KSELEEIAVIVEK---HDLIVLSDEIYAELTYDEAYTS------FASIKGMRERTILISGFSKGFAMTGWRLGFIAAPVY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 485 FIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEkgevRIAKDLHEldlKRQYVVKRLREMpKMRFAYPTSSFYIFMD 564
Cdd:PRK07682 244 FSEAMLKIHQYSMMCAPTMAQFAALEALRAGNDDVI----RMRDSYRK---RRNFFVTSFNEI-GLTCHVPGGAFYAFPS 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064415124 565 LAlyfegKTAYSPDKtevlhnvddFCDYLIRTTGVAVGPGSDMGEPlG---IRISYAGPMDTMVRAM 628
Cdd:PRK07682 316 IS-----STGLSSEE---------FAEQLLLEEKVAVVPGSVFGES-GegfIRCSYATSLEQLQEAM 367
|
|
| PRK07683 |
PRK07683 |
aminotransferase A; Validated |
233-637 |
3.05e-72 |
|
aminotransferase A; Validated
Pssm-ID: 236075 Cd Length: 387 Bit Score: 238.09 E-value: 3.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 233 AKTIAIFG--KTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDP 310
Cdd:PRK07683 9 VKDIQISGirQFSNMVQNYDNLISLTIGQPDFPTPSHVKEAAKRAITENYTSYTHNAGLLELRKAACNFVKDKYDLHYSP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 311 ATEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQvkAGLVPLH-NSLEEDYLINPAELEKTLTanPETKI 389
Cdd:PRK07683 89 ESEIIVTIGASEAIDIAFRTILEPGTEVILPAPIYPGYEPIIRL--CGAKPVFiDTRSTGFRLTAEALENAIT--EKTRC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 390 VILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTILINGFSKAY 469
Cdd:PRK07683 165 VVLPYPSNPTGVTLSKEELQDIADVLKD---KNIFVLSDEIYSELVYEQPHTS------IAHFPEMREKTIVINGLSKSH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 470 AMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMklelaSIEKGEVRIAKdlHELDLKRQYVVKRLREMpK 549
Cdd:PRK07683 236 SMTGWRIGFLFAPSYLAKHILKVHQYNVTCASSISQYAALEAL-----TAGKDDAKMMR--HQYKKRRDYVYNRLISM-G 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 550 MRFAYPTSSFYIFMDLALYfeGKTAYspdktevlhnvdDFCDYLIRTTGVAVGPG---SDMGEPLgIRISYAGPMDTMVR 626
Cdd:PRK07683 308 LDVEKPTGAFYLFPSIGHF--TMSSF------------DFALDLVEEAGLAVVPGsafSEYGEGY-VRLSYAYSIETLKE 372
|
410
....*....|.
gi 2064415124 627 AMDGLELALKS 637
Cdd:PRK07683 373 GLDRLEAFLQQ 383
|
|
| PRK07309 |
PRK07309 |
pyridoxal phosphate-dependent aminotransferase; |
255-632 |
4.01e-68 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235985 Cd Length: 391 Bit Score: 227.30 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 255 LCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNVILAICCP 334
Cdd:PRK07309 35 LTLGEPDFTTPDHVKEAAKRAIDANQSHYTGMAGLLELRQAAADFVKEKYNLDYAPENEILVTIGATEALSASLTAILEP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 335 GDKVILPSPYWGNYEGIITQVKAGLVPLHNSlEEDYLINPAELEKTLTANPET-KIVILCNPSNPAGTLHSPEHLEKIAA 413
Cdd:PRK07309 115 GDKVLLPAPAYPGYEPIVNLVGAEIVEIDTT-ENDFVLTPEMLEKAILEQGDKlKAVILNYPANPTGVTYSREQIKALAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 414 VLRKPQfrhVVVISDEIYEQLVYQDEG-VServcknfaMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKHFI-EACQL 491
Cdd:PRK07309 194 VLKKYD---IFVISDEVYSELTYTGEPhVS--------IAEYLPDQTILINGLSKSHAMTGWRIGLIFAPAEFTaQLIKS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 492 MQGQTTScANSVGQVMAIEAMKlelasiekgevrIAKDlHELDLKRQYVVKR---LREMPKMRF--AYPTSSFYIFmdla 566
Cdd:PRK07309 263 HQYLVTA-ATTMAQFAAVEALT------------NGKD-DALPMKKEYIKRRdyiIEKMTDLGFkiIKPDGAFYIF---- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064415124 567 lyfegktAYSPDKTEvlHNVDDFCDYLIRTTGVAVGPGSDMGePLG---IRISYAGPMDTMVRAMDGLE 632
Cdd:PRK07309 325 -------AKIPAGYN--QDSFKFLQDFARKKAVAFIPGAAFG-PYGegyVRLSYAASMETIKEAMKRLK 383
|
|
| PRK06348 |
PRK06348 |
pyridoxal phosphate-dependent aminotransferase; |
238-632 |
2.87e-56 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180537 Cd Length: 384 Bit Score: 195.32 E-value: 2.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQIC 317
Cdd:PRK06348 17 IMAEIATLAKKFPDIIDLSLGDPDLITDESIINAAFEDAKKGHTRYTDSGGDVELIEEIIKYYSKNYDLSFKR-NEIMAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 318 SGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSN 397
Cdd:PRK06348 96 VGACHGMYLALQSILDPGDEVIIHEPYFTPYKDQIEMVGGKPIILETYEEDGFQINVKKLEALIT--SKTKAIILNSPNN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 398 PAGTLHSPEHLEKIAAVLRKPQFrhvVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTILINGFSKAYAMTGLRIG 477
Cdd:PRK06348 174 PTGAVFSKETLEEIAKIAIEYDL---FIISDEVYDGFSFYEDFVP------MATLAGMPERTITFGSFSKDFAMTGWRIG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 478 YMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLElasiEKGEVRIAKDLHEldlKRQYVVKRLREMPKMRFAYPTS 557
Cdd:PRK06348 245 YVIAPDYIIETAKIINEGICFSAPTISQRAAIYALKHR----DTIVPLIKEEFQK---RLEYAYKRIESIPNLSLHPPKG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064415124 558 SFYIFMDLAlyfegKTAYSPdktevlhnvDDFCDYLIRTTGVAVGPGSDMGEpLG---IRISYAGPMDTMVRAMDGLE 632
Cdd:PRK06348 318 SIYAFINIK-----KTGLSS---------VEFCEKLLKEAHVLVIPGKAFGE-SGegyIRLACTVGIEVLEEAFNRIE 380
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
255-631 |
2.72e-55 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 191.75 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 255 LCVGEPDFPPPKSVLDAGVRALQNGQTK-YCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNVILAICC 333
Cdd:pfam00155 6 LGSNEYLGDTLPAVAKAEKDALAGGTRNlYGPTDGHPELREALAKFLGRSPVLKLDREAAVVFGSGAGANIEALIFLLAN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 334 PGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIAA 413
Cdd:pfam00155 86 PGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALK--EKPKVVLHTSPHNPTGTVATLEELEKLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 414 VLRKpqfRHVVVISDEIYEQLVYQDEGVSERVCknFAMipgMYERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQLMQ 493
Cdd:pfam00155 164 LAKE---HNILLLVDEAYAGFVFGSPDAVATRA--LLA---EGPNLLVVGSFSKAFGLAGWRVGYILGNAAVISQLRKLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 494 GQTTSCanSVGQVMAIEAMKLELASIEKGEVRIAKdLHELdlkRQYVVKRLREmpkMRFAYPTSS--FYIFMDLALYFEg 571
Cdd:pfam00155 236 RPFYSS--THLQAAAAAALSDPLLVASELEEMRQR-IKER---RDYLRDGLQA---AGLSVLPSQagFFLLTGLDPETA- 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064415124 572 ktayspdktevlhnvDDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAG-PMDTMVRAMDGL 631
Cdd:pfam00155 306 ---------------KELAQVLLEEVGVYVTPGSSPGVPGWLRITVAGgTEEELEELLEAI 351
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
246-636 |
4.31e-55 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 192.37 E-value: 4.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 246 EAEGKPVYSLCVGEPDFPPPKSVLDAgVRALQNGQTKYCDMRGMAELRELITKYLHcTKGVSYDPaTEIQICSGAQQALY 325
Cdd:PRK07568 26 KKRGIKVYHLNIGQPDIKTPEVFFEA-IKNYDEEVLAYSHSQGIPELREAFAKYYK-KWGIDVEP-DEILITNGGSEAIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 326 NVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDY-LINPAELEKTLTanPETKIVILCNPSNPAGTLHS 404
Cdd:PRK07568 103 FAMMAICDPGDEILVPEPFYANYNGFATSAGVKIVPVTTKIEEGFhLPSKEEIEKLIT--PKTKAILISNPGNPTGVVYT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 405 PEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDegvseRVCKNFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGP-K 483
Cdd:PRK07568 181 KEELEMLAEIAKK---HDLFLISDEVYREFVYDG-----LKYTSALSLEGLEDRVIIIDSVSKRYSACGARIGCLISKnK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 484 HFIEACqLMQGQTTSCANSVGQVMAIEAMKLELASIEkgEVRIakdlhELDLKRQYVVKRLREMPKMRFAYPTSSFYIFM 563
Cdd:PRK07568 253 ELIAAA-MKLCQARLSPPTLEQIGAAALLDTPESYFD--EVRE-----EYKKRRDILYEELNKIPGVVCEKPKGAFYIIA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 564 DLalyfegktaysPDKtevlhNVDDFCDYLIR-------TTGVAVGPGSDMGEPLG---IRISYAGPMDTMVRAMDGLEL 633
Cdd:PRK07568 325 KL-----------PVD-----DAEDFAKWLLTdfnyngeTVMVAPASGFYATPGLGkneIRIAYVLNEEDLKRAMEILKE 388
|
...
gi 2064415124 634 ALK 636
Cdd:PRK07568 389 ALE 391
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
233-638 |
1.19e-50 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 180.46 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 233 AKTIAIFGKTKQLEAegkpVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPaT 312
Cdd:PRK08361 20 SKIRELFERASKMEN----VISLGIGEPDFDTPKNIKEAAKRALDEGWTHYTPNAGIPELREAIAEYYKKFYGVDVDV-D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 313 EIQICSGAQQALYNVILAICCPGDKVILPSPYWGNY--EGIITQVKAGLVPLHNslEEDYLINPAELEKTLTANpeTKIV 390
Cdd:PRK08361 95 NVIVTAGAYEATYLAFESLLEEGDEVIIPDPAFVCYveDAKIAEAKPIRIPLRE--ENEFQPDPDELLELITKR--TRMI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 391 ILCNPSNPAGTLHSPEHLEKIAAVlrkPQFRHVVVISDEIYEQLVYQDegvservCKNFAMIPGMYERTILINGFSKAYA 470
Cdd:PRK08361 171 VINYPNNPTGATLDKEVAKAIADI---AEDYNIYILSDEPYEHFLYEG-------AKHYPMIKYAPDNTILANSFSKTFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 471 MTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEKGEVRiakdlHELDLKRQYVVKRLREMPKM 550
Cdd:PRK08361 241 MTGWRLGFVIAPEQVIKDMIKLHAYIIGNVASFVQIAGIEALRSKESWKAVEEMR-----KEYNERRKLVLKRLKEMPHI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 551 RFAYPTSSFYIFmdlalyfegktaysPDKTEVLHNVDDFCDYLIRTTGVAVGPGSDMGePLG---IRISYAGPMDTMVRA 627
Cdd:PRK08361 316 KVFEPKGAFYVF--------------ANIDETGMSSEDFAEWLLEKARVVVIPGTAFG-KAGegyIRISYATSKEKLIEA 380
|
410
....*....|.
gi 2064415124 628 MDGLELALKSL 638
Cdd:PRK08361 381 MERMEKALEEL 391
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
254-638 |
2.43e-50 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 179.50 E-value: 2.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 254 SLCVGEPDFPPPKSVLDAGVRALQN-GQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNVILAIC 332
Cdd:PRK05957 31 SLGQGVVSYPPPPEAIEALNNFLANpENHKYQAVQGIPPLLEAITQKLQQDNGIELNNEQAIVVTAGSNMAFMNAILAIT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 333 CPGDKVILPSPYWGNYEGIITQvkAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIA 412
Cdd:PRK05957 111 DPGDEIILNTPYYFNHEMAITM--AGCQPILVPTDDNYQLQPEAIEQAIT--PKTRAIVTISPNNPTGVVYPEALLRAVN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 413 AVLRKPQFRHvvvISDEIYEQLVYQDegvservCKNF--AMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQ 490
Cdd:PRK05957 187 QICAEHGIYH---ISDEAYEYFTYDG-------VKHFspGSIPGSGNHTISLYSLSKAYGFASWRIGYMVIPIHLLEAIK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 491 LMQGQTTSCANSVGQVMAIEAMKLelasiekGEVRIAKDLHELDLKRQYVVKRLREMPKMRF-AYPTSSFYIFMdlalyf 569
Cdd:PRK05957 257 KIQDTILICPPVVSQYAALGALQV-------GKSYCQQHLPEIAQVRQILLKSLGQLQDRCTlHPANGAFYCFL------ 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064415124 570 egktayspdktEVLHNVDDF--CDYLIRTTGVAVGPGSDMGEPLG--IRISY-AGPMDTMVRAMDGLELALKSL 638
Cdd:PRK05957 324 -----------KVNTDLNDFelVKQLIREYRVAVIPGTTFGMKNGcyLRIAYgALQKATAKEGIERLVQGLKTI 386
|
|
| PRK08363 |
PRK08363 |
alanine aminotransferase; Validated |
243-632 |
1.42e-47 |
|
alanine aminotransferase; Validated
Pssm-ID: 181402 Cd Length: 398 Bit Score: 172.30 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 243 KQLEAEGKPVYSLCVGEP---DFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSG 319
Cdd:PRK08363 23 RELEKKGIKVIRLNIGDPvkfDFQPPEHMKEAYCRAIKEGHNYYGPSEGLPELREAIVKREKRKNGVDITP-DDVRVTAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 320 AQQALYNVILAICCPGDKVILPSPYWGNYegiitqvkAGLVPLHNSL--------EEDYLINPAELEKTLTAnpETKIVI 391
Cdd:PRK08363 102 VTEALQLIFGALLDPGDEILIPGPSYPPY--------TGLVKFYGGVpveyrtieEEGWQPDIDDIRKKITE--KTKAIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 392 LCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknfamiPGMYER---TILINGFSKA 468
Cdd:PRK08363 172 VINPNNPTGALYEKKTLKEILDIAGE---HDLPVISDEIYDLMTYEGKHVS----------PGSLTKdvpVIVMNGLSKV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 469 YAMTGLRIGYMA--GPKHFIEACQ---LMQGQTTSCANSVGQVMAIEAMKLELASIEKGevriakdLHELDLKRQYVVKR 543
Cdd:PRK08363 239 YFATGWRLGYIYfvDPEGKLAEVReaiDKLARIRLCPNTPAQFAAIAGLTGPMDYLEEY-------MKKLKERRDYIYKR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 544 LREMPKMRFAYPTSSFYIFmdlalyfeGKTAYSPDKTEvlhnvDDFCDYLIRTTGVAVGPGSDMGEpLG---IRISYAGP 620
Cdd:PRK08363 312 LNEIPGISTTKPQGAFYIF--------PRIEEGPWKDD-----KEFVLDVLHEAHVLFVHGSGFGE-YGaghFRLVFLPP 377
|
410
....*....|..
gi 2064415124 621 MDTMVRAMDGLE 632
Cdd:PRK08363 378 VEILEEAMDRFE 389
|
|
| PRK08960 |
PRK08960 |
pyridoxal phosphate-dependent aminotransferase; |
236-637 |
5.29e-45 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181595 Cd Length: 387 Bit Score: 164.84 E-value: 5.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 236 IAIFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPAtEIQ 315
Cdd:PRK08960 18 MALLARANELEAAGHDVIHLEIGEPDFTTAEPIVAAGQAALAAGHTRYTAARGLPALREAIAGFYAQRYGVDVDPE-RIL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 316 ICSGAQQALYNVILAICCPGDKVILPSP-YWGN------YEGiitqvKAGLVPLHNslEEDYLINPAELEKTLtaNPETK 388
Cdd:PRK08960 97 VTPGGSGALLLASSLLVDPGKHWLLADPgYPCNrhflrlVEG-----AAQLVPVGP--DSRYQLTPALVERHW--NADTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 389 IVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVSerVCknfamipGMYERTILINGFSKA 468
Cdd:PRK08960 168 GALVASPANPTGTLLSRDELAALSQALRA---RGGHLVVDEIYHGLTYGVDAAS--VL-------EVDDDAFVLNSFSKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 469 YAMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLElaSIEKGEVRiakdLHELDLKRQYVVKRLREMP 548
Cdd:PRK08960 236 FGMTGWRLGWLVAPPAAVPELEKLAQNLYISASTPAQHAALACFEPE--TLAILEAR----RAEFARRRDFLLPALRELG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 549 KMRFAYPTSSFYIFMDLalyfegkTAYSPDKTEvlhnvddFCDYLIRTTGVAVGPGSDMGEPLG---IRISYAGPMDTMV 625
Cdd:PRK08960 310 FGIAVEPQGAFYLYADI-------SAFGGDAFA-------FCRHFLETEHVAFTPGLDFGRHQAgqhVRFAYTQSLPRLQ 375
|
410
....*....|..
gi 2064415124 626 RAMDGLELALKS 637
Cdd:PRK08960 376 EAVERIARGLRS 387
|
|
| PRK07337 |
PRK07337 |
pyridoxal phosphate-dependent aminotransferase; |
244-632 |
5.67e-45 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180937 Cd Length: 388 Bit Score: 164.85 E-value: 5.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 244 QLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPAtEIQICSGAQQA 323
Cdd:PRK07337 24 ALERAGRDIIHMGIGEPDFTAPEPVVEAAARALRRGVTQYTSALGLAPLREAIAAWYARRFGLDVAPE-RIVVTAGASAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 324 LYNVILAICCPGDKVILPSP-YWGNYEGIIT-QVKAGLVPlhNSLEEDYLINPAELEKTLtaNPETKIVILCNPSNPAGT 401
Cdd:PRK07337 103 LLLACLALVERGDEVLMPDPsYPCNRHFVAAaEGRPVLVP--SGPAERFQLTAADVEAAW--GERTRGVLLASPSNPTGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 402 LHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknfAMIPGmyERTILINGFSKAYAMTGLRIGYMAG 481
Cdd:PRK07337 179 SIAPDELRRIVEAVRA---RGGFTIVDEIYQGLSYDAAPVS-------ALSLG--DDVITINSFSKYFNMTGWRLGWLVV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 482 PKHFIEACQLMQGQTTSCANSVGQVMAIEAmkLELASIEKGEVRIAkdlhELDLKRQYVVKRLREM----PKMrfayPTS 557
Cdd:PRK07337 247 PEALVGTFEKLAQNLFICASALAQHAALAC--FEPDTLAIYERRRA----EFKRRRDFIVPALESLgfkvPVM----PDG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064415124 558 SFYIFMDLALYFEGKTAYSpdktevlhnvDDFCDYLIRTTGVAVGPGSDMGEPLG---IRISYAGPMDTMVRAMDGLE 632
Cdd:PRK07337 317 AFYVYADCRGVAHPAAGDS----------AALTQAMLHDAGVVLVPGRDFGPHAPrdyIRLSYATSMSRLEEAVARLG 384
|
|
| PLN00175 |
PLN00175 |
aminotransferase family protein; Provisional |
258-636 |
8.99e-42 |
|
aminotransferase family protein; Provisional
Pssm-ID: 215089 [Multi-domain] Cd Length: 413 Bit Score: 156.56 E-value: 8.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 258 GEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNVILAICCPGDK 337
Cdd:PLN00175 62 GFPNFDGPDFVKEAAIQAIRDGKNQYARGFGVPELNSAIAERFKKDTGLVVDPEKEVTVTSGCTEAIAATILGLINPGDE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 338 VILPSPYWGNYEGIITQVKAGL--VPLHnslEEDYLINPAELEKTLTANpeTKIVILCNPSNPAGTLHSPEHLEKIAAVL 415
Cdd:PLN00175 142 VILFAPFYDSYEATLSMAGAKIktVTLR---PPDFAVPEDELKAAFTSK--TRAILINTPHNPTGKMFTREELELIASLC 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 416 RKpqfRHVVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQLMQGQ 495
Cdd:PLN00175 217 KE---NDVLAFTDEVYDKLAFEGDHIS------MASLPGMYERTVTMNSLGKTFSLTGWKIGWAIAPPHLTWGVRQAHSF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 496 TTSCANSVGQVMAIEAMKlelasiekgevriAKDLHELDLKRQYVVKR---LREMPKMRF-AYPTSSFYIFMdlalyfeg 571
Cdd:PLN00175 288 LTFATATPMQWAAVAALR-------------APESYYEELKRDYSAKKdilVEGLKEVGFkVYPSSGTYFVM-------- 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064415124 572 ktaysPDKTEV-LHNVDDFCDYLIRTTGVAVGPGS------DMGEPLgIRISYAGPMDTMVRAMDGLELALK 636
Cdd:PLN00175 347 -----VDHTPFgFENDIAFCEYLIEEVGVAAIPPSvfylnpEDGKNL-VRFAFCKDEETLRAAVERMKTKLK 412
|
|
| PRK07777 |
PRK07777 |
putative succinyldiaminopimelate transaminase DapC; |
238-488 |
1.33e-41 |
|
putative succinyldiaminopimelate transaminase DapC;
Pssm-ID: 236095 [Multi-domain] Cd Length: 387 Bit Score: 155.20 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEAEGKPVySLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQIC 317
Cdd:PRK07777 13 IFAEMSALAVRTGAV-NLGQGFPDEDGPPEMLEAAQEAIAGGVNQYPPGPGIPELRAAIAAQRRRRYGLEYDPDTEVLVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 318 SGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQvkAGL----VPLHNSlEEDYLINPAELEKTLTanPETKIVILC 393
Cdd:PRK07777 92 VGATEAIAAAVLGLVEPGDEVLLIEPYYDSYAAVIAM--AGAhrvpVPLVPD-GRGFALDLDALRAAVT--PRTRALIVN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 394 NPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDegvseRVCKNFAMIPGMYERTILINGFSKAYAMTG 473
Cdd:PRK07777 167 SPHNPTGTVLTAAELAAIAELAVE---HDLLVITDEVYEHLVFDG-----ARHLPLATLPGMRERTVTISSAAKTFNVTG 238
|
250
....*....|....*
gi 2064415124 474 LRIGYMAGPKHFIEA 488
Cdd:PRK07777 239 WKIGWACGPAPLIAA 253
|
|
| PRK08912 |
PRK08912 |
aminotransferase; |
222-484 |
9.50e-41 |
|
aminotransferase;
Pssm-ID: 181580 Cd Length: 387 Bit Score: 152.82 E-value: 9.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 222 PLNPVFDTTTVAktiaIFGKTKQLEAEGKPVySLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELI-TKYL 300
Cdd:PRK08912 3 MGNPVFADLPTT----IFEVMSQLAREHGAI-NLGQGFPDDPGPEDVRRAAADALLDGSNQYPPMMGLPELRQAVaAHYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 301 HcTKGVSYDPATEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQvkAGLVPLHNSLEE-DYLINPAELEK 379
Cdd:PRK08912 78 R-FQGLDLDPETEVMVTSGATEALAAALLALVEPGDEVVLFQPLYDAYLPLIRR--AGGVPRLVRLEPpHWRLPRAALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 380 TLTanPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRkpqfRH-VVVISDEIYEQLVYqdEGVSERvckNFAMIPGMYER 458
Cdd:PRK08912 155 AFS--PRTKAVLLNNPLNPAGKVFPREELALLAEFCQ----RHdAVAICDEVWEHVVF--DGRRHI---PLMTLPGMRER 223
|
250 260
....*....|....*....|....*.
gi 2064415124 459 TILINGFSKAYAMTGLRIGYMAGPKH 484
Cdd:PRK08912 224 TVKIGSAGKIFSLTGWKVGFVCAAPP 249
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
252-636 |
8.70e-39 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 147.65 E-value: 8.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 252 VYSLCVGEPDFPPPKSVLDAGVRALQNGQT---KYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICsGAQQALyNVI 328
Cdd:PRK06836 35 VFDFSLGNPSVPPPAAVKEALRELAEEEDPglhGYMPNAGYPEVREAIAESLNRRFGTPLTADHIVMTC-GAAGAL-NVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 329 L-AICCPGDKVILPSPYWGNYEGIITQVKAGLVPLhNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEH 407
Cdd:PRK06836 113 LkAILNPGDEVIVFAPYFVEYRFYVDNHGGKLVVV-PTDTDTFQPDLDALEAAIT--PKTKAVIINSPNNPTGVVYSEET 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 408 LEKIAAVLRKPQFRH---VVVISDEIYEQLVYQDEGVservcknfAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKH 484
Cdd:PRK06836 190 LKALAALLEEKSKEYgrpIYLISDEPYREIVYDGAEV--------PYIFKYYDNSIVVYSFSKSLSLPGERIGYIAVNPE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 485 FIEACQLMQGQTTS-------CANSVGQVMaIEAMklelasiekgeVRIAKDLHELDLKRQYVVKRLREMpKMRFAYPTS 557
Cdd:PRK06836 262 MEDADDLVAALVFAnrilgfvNAPALMQRV-VAKC-----------LDATVDVSIYKRNRDLLYDGLTEL-GFECVKPQG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 558 SFYIFMDlalyfegktaySPDKtevlhnvDD--FCDYLIRTTGVAVgPGSDMGEPLGIRISYAGPMDTMVRAMDGLELAL 635
Cdd:PRK06836 329 AFYLFPK-----------SPEE-------DDvaFCEKAKKHNLLLV-PGSGFGCPGYFRLSYCVDTETIERSLPAFEKLA 389
|
.
gi 2064415124 636 K 636
Cdd:PRK06836 390 K 390
|
|
| PRK06108 |
PRK06108 |
pyridoxal phosphate-dependent aminotransferase; |
255-609 |
1.02e-38 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180404 Cd Length: 382 Bit Score: 147.01 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 255 LCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSyDPATEIQICSGAQQALYNVILAICCP 334
Cdd:PRK06108 29 LWFGESDLPTPDFIRDAAAAALADGETFYTHNLGIPELREALARYVSRLHGVA-TPPERIAVTSSGVQALMLAAQALVGP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 335 GDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEED-YLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIAA 413
Cdd:PRK06108 108 GDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGGGgWTLDLDRLLAAIT--PRTRALFINSPNNPTGWTASRDDLRAILA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 414 VLRkpqfRH-VVVISDEIYEQLVYQDEGVServcKNFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKhfieacQLM 492
Cdd:PRK06108 186 HCR----RHgLWIVADEVYERLYYAPGGRA----PSFLDIAEPDDRIIFVNSFSKNWAMTGWRLGWLVAPP------ALG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 493 QGQT------TSCANSVGQVMAIeamklelASIEKGEVRIAKDLHELDLKRQYVVKRLREMPKMRFAYPTSSFYIFMDLa 566
Cdd:PRK06108 252 QVLEklieynTSCVAQFVQRAAV-------AALDEGEDFVAELVARLRRSRDHLVDALRALPGVEVAKPDGAMYAFFRI- 323
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2064415124 567 lyfegktaysPDKTEVLHnvddFCDYLIRTTGVAVGPGSDMGE 609
Cdd:PRK06108 324 ----------PGVTDSLA----LAKRLVDEAGLGLAPGTAFGP 352
|
|
| PRK09082 |
PRK09082 |
methionine aminotransferase; Validated |
238-482 |
1.35e-38 |
|
methionine aminotransferase; Validated
Pssm-ID: 181642 [Multi-domain] Cd Length: 386 Bit Score: 146.98 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEAEGKPVySLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQIC 317
Cdd:PRK09082 19 IFTVMSALAAEHGAI-NLSQGFPDFDGPPYLVEALAYAMAAGHNQYPPMTGVAALREAIAAKTARLYGRQYDADSEITVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 318 SGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQvkAGLVPLHNSLE-EDYLINPAELEKTLTanPETKIVILCNPS 396
Cdd:PRK09082 98 AGATEALFAAILALVRPGDEVIVFDPSYDSYAPAIEL--AGGRAVRVALQpPDFRVDWQRFAAAIS--PRTRLIILNTPH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 397 NPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYqDEGVSERVCKnfamIPGMYERTILINGFSKAYAMTGLRI 476
Cdd:PRK09082 174 NPSGTVWSAADMRALWQLIAG---TDIYVLSDEVYEHIVF-DGAGHASVLR----HPELRERAFVVSSFGKTYHVTGWKV 245
|
....*.
gi 2064415124 477 GYMAGP 482
Cdd:PRK09082 246 GYCVAP 251
|
|
| PRK12414 |
PRK12414 |
putative aminotransferase; Provisional |
238-625 |
2.48e-37 |
|
putative aminotransferase; Provisional
Pssm-ID: 183514 Cd Length: 384 Bit Score: 143.39 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEAEGKPVySLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQIC 317
Cdd:PRK12414 18 IFTVIGQLAAQHDAL-NLSQGAPNFAPDPALVEGVARAMRDGHNQYAPMAGIAALREALAEKTERLYGARYDPASEVTVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 318 SGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLeEDYLINPAELEKTLTanPETKIVILCNPSN 397
Cdd:PRK12414 97 ASASEGLYAAISALVHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSP-EDFRVNWDEVAAAIT--PRTRMIIVNTPHN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 398 PAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLVYQDegvseRVCKNFAMIPGMYERTILINGFSKAYAMTGLRIG 477
Cdd:PRK12414 174 PSATVFSAADLARLAQLTRNTD---IVILSDEVYEHVVFDG-----ARHHSMARHRELAERSVIVSSFGKSYHVTGWRVG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 478 YMAGPKHFI-EACQLMQGQTTScANSVGQVMAIEAMklelasiekgevriAKDLHELDLKRQYVVKR---LREMPKMRFA 553
Cdd:PRK12414 246 YCLAPAELMdEIRKVHQFMVFS-ADTPMQHAFAEAL--------------AEPASYLGLGAFYQRKRdllARELAGSRFE 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064415124 554 YPTSSFYIFMdLALYfegktAYSPDKTEvlhnvDDFCDYLIRTTGVAVGP-------GSDMGEplgIRISYAGPMDTMV 625
Cdd:PRK12414 311 LLPSEGSFFM-LARF-----RHFSDESD-----SDFVLRLIRDARVATIPlsafytdGTDTGL---IRLSFSKDDATLV 375
|
|
| PheA2 |
COG0077 |
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ... |
6-208 |
2.08e-36 |
|
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439847 [Multi-domain] Cd Length: 274 Bit Score: 137.54 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 6 STRVAYQesaefaGAK----EAAAQMLSAvDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYSL 81
Cdd:COG0077 1 MMRIAYL------GPEgtfsHQAARKYFG-PDAELVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLESDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 82 AVVGE-----------------------------------------------------------SESPAKTS-------- 94
Cdd:COG0077 74 KIVGEvvlpihhcllarpgtklediktvyshpqalaqcreflrehlpgaelvpvsstaaaarlvAEEGDPGAaaiasela 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 95 -----------------GKQTRFWLVAKTPAEPSlkaAACKTSLAFAFAsgNAHGQLYRALGVFASRGLDLSKIESRpws 157
Cdd:COG0077 154 aelyglevlaeniednpNNTTRFLVLGREPAAPT---GADKTSLVFSLP--NRPGALYKALGVFATRGINLTKIESR--- 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2064415124 158 stdPSAGKA-DFIFYVDVKARQSDTDVLEAIASLRSACSYVRVLGCYASVDG 208
Cdd:COG0077 226 ---PIKGGLwEYVFFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL 274
|
|
| HisC |
COG0079 |
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ... |
243-616 |
8.48e-33 |
|
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid transport and metabolism]; Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439849 [Multi-domain] Cd Length: 341 Bit Score: 129.10 E-value: 8.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 243 KQLEAEGKPVYsLCVGE-PdFPPPKSVLDAgVRALQNGQTKYCDmRGMAELRELITKYLHCtkgvsydPATEIQICSGAQ 321
Cdd:COG0079 7 GPIEEPEDIIK-LSSNEnP-YGPPPKVLEA-IAAALDALNRYPD-PDATALREALAEYYGV-------PPEQVLVGNGSD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 322 QALYNVILAICCPGDKVILPSPYWGNYEgIITQVkAGLVPLHNSLEEDYLINPAELEKTLTanPETKIVILCNPSNPAGT 401
Cdd:COG0079 76 ELIQLLARAFLGPGDEVLVPEPTFSEYP-IAARA-AGAEVVEVPLDEDFSLDLDALLAAIT--ERTDLVFLCNPNNPTGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 402 LHSPEHLEKIAAVLRKpqfrHVVVISDEIYEQLVYQDEGVSERVcknfamipGMYERTILINGFSKAYAMTGLRIGYMAG 481
Cdd:COG0079 152 LLPREELEALLEALPA----DGLVVVDEAYAEFVPEEDSALPLL--------ARYPNLVVLRTFSKAYGLAGLRLGYAIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 482 PKHFIEACQLMQGQTTscANSVGQVMAIEAMKlELASIEKGEVRIAKDlheldlkRQYVVKRLREMpKMRFaYPTSSFYI 561
Cdd:COG0079 220 SPELIAALRRVRGPWN--VNSLAQAAALAALE-DRAYLEETRARLRAE-------RERLAAALRAL-GLTV-YPSQANFV 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2064415124 562 FMDLAlyfegktayspdktevlHNVDDFCDYLIRtTGVAVGPGSDMGEPLGIRIS 616
Cdd:COG0079 288 LVRVP-----------------EDAAELFEALLE-RGILVRDFSSFGLPDYLRIT 324
|
|
| MalY |
COG1168 |
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor ... |
261-635 |
7.49e-30 |
|
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor activities [Amino acid transport and metabolism, General function prediction only];
Pssm-ID: 440782 Cd Length: 387 Bit Score: 121.74 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 261 DFPPPKSVLDAGVRALQNGQTKYCDMRgmAELRELITKYLHCTKGVSYDPAtEIQICSGAQQALYNVILAICCPGDKVIL 340
Cdd:COG1168 40 DFATPPAVIEALKERVEHGVFGYTAPP--DEYYEAIIDWLKRRHGWEIDPE-WIVFTPGVVPGLALAIRAFTEPGDGVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 341 PSPYWGNYEGIITqvKAGLVPLHNSLEED---YLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRK 417
Cdd:COG1168 117 QTPVYPPFFKAIE--NNGRELVENPLILEdgrYRIDFDDLEAKLD--PGVKLLLLCNPHNPTGRVWTREELERLAELCER 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 418 pqfRHVVVISDEIYEQLVYQDEG-VServcknFAMIPGMY-ERTILINGFSKAYAMTGLRIGYMAGP-----KHFIEACQ 490
Cdd:COG1168 193 ---HDVLVISDEIHADLVLPGHKhTP------FASLSEEAaDRTITLTSPSKTFNLAGLKASYAIIPnpalrARFARALE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 491 LMQGQTTScansvgqVMAIEAMKlelASIEKGEvriakD-----LHELDLKRQYVVKRLRE-MPKMRFAYPTSSFYIFMD 564
Cdd:COG1168 264 GLGLPSPN-------VLGLVATE---AAYREGE-----EwldelLAYLRGNRDLLAEFLAEhLPGVKVTPPEATYLAWLD 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064415124 565 LalyfegkTAYSPDktevlhnVDDFCDYLIRTTGVAVGPGSDMGEPLG--IRISYAGPMDTMVRAMDGLELAL 635
Cdd:COG1168 329 C-------RALGLD-------DEELAEFLLEKAGVALSDGATFGEGGEgfVRLNFACPRAVLEEALERLAKAL 387
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
248-629 |
9.46e-30 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 121.68 E-value: 9.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 248 EGKPVYSLCVGEP----DFPPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYLHCTKGVSYDpATEIQICSGAQQ 322
Cdd:TIGR01265 29 PEKPVIPLSHGDPsvfgNLRTDPEAEEAVKDALRSGKfNGYAPSVGALAAREAVAEYLSSDLPGKLT-ADDVVLTSGCSQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 323 ALYNVILAICCPGDKVILPSPYWGNYEgiiTQVKA-GL-VPLHNSL-EEDYLINPAELEKTltANPETKIVILCNPSNPA 399
Cdd:TIGR01265 108 AIEICIEALANPGANILVPRPGFPLYD---TRAAFsGLeVRLYDLLpEKDWEIDLDGLESL--ADEKTVAIVVINPSNPC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 400 GTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDegvservCKNFAM------IPgmyerTILINGFSKAYAMTG 473
Cdd:TIGR01265 183 GSVFSRDHLQKIAEVAEK---LGIPIIADEIYGHMVFGD-------APFIPMasfasiVP-----VLSLGGISKRWVVPG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 474 LRIGYMAGPKHF-IEACQLMQGQTTSCANSVGQVMAI-EAMKlelASIEKGE----VRIAKDLHEldlKRQYVVKRLREM 547
Cdd:TIGR01265 248 WRLGWIIIHDPHgIFRDTVLQGLKNLLQRILGPATIVqGALP---DILENTPqeffDGKISVLKS---NAELCYEELKDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 548 PKMRFAYPTSSFYIFMDLALyfegkTAYSPDKTEVlhnvdDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVRA 627
Cdd:TIGR01265 322 PGLVCPKPEGAMYLMVKLEL-----ELFPEIKDDV-----DFCEKLAREESVICLPGSAFGLPNWVRITITVPESMLEEA 391
|
..
gi 2064415124 628 MD 629
Cdd:TIGR01265 392 CS 393
|
|
| PRK07681 |
PRK07681 |
LL-diaminopimelate aminotransferase; |
243-488 |
2.40e-28 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 181081 Cd Length: 399 Bit Score: 117.60 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 243 KQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQ 322
Cdd:PRK07681 25 KEKIAAGHKMIDLSIGNPDMPPADFVREEMVHTANQKESYGYTLSGIQEFHEAVTEYYNNTHNVILNADKEVLLLMGSQD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 323 ALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLIN----PAELEKtltanpETKIVILCNPSNP 398
Cdd:PRK07681 105 GLVHLPMVYANPGDIILVPDPGYTAYETGIQMAGATSYYMPLKKENDFLPDleliPEEIAD------KAKMMILNFPGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 399 AGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVY-QDEGVServcknFAMIPGMYERTILINGFSKAYAMTGLRIG 477
Cdd:PRK07681 179 VPAMAHEDFFKEVIAFAKK---HNIIVVHDFAYAEFYFdGNKPIS------FLSVPGAKEVGVEINSLSKSYSLAGSRIG 249
|
250
....*....|.
gi 2064415124 478 YMAGPKHFIEA 488
Cdd:PRK07681 250 YMIGNEEIVRA 260
|
|
| PLN02317 |
PLN02317 |
arogenate dehydratase |
4-204 |
3.07e-28 |
|
arogenate dehydratase
Pssm-ID: 215181 [Multi-domain] Cd Length: 382 Bit Score: 116.76 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 4 GTSTRVAYQesAEFAGAKEAAAqmLSAVDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYSLAV 83
Cdd:PLN02317 92 GSKLRVAYQ--GVPGAYSEAAA--RKAYPNCEAVPCEQFEAAFQAVELWLADRAVLPIENSLGGSIHRNYDLLLRHRLHI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 84 VGE---------------------------------------------------------------------SESPAKTS 94
Cdd:PLN02317 168 VGEvqlpvhhcllalpgvrkeelkrvishpqalaqcentltklgvvreavddtagaakmvaanglrdtaaiaSARAAELY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 95 GKQ-------------TRFWLVAKTPAEPSLKAAAcKTSLAFAFASGNahGQLYRALGVFASRGLDLSKIESRPWS---- 157
Cdd:PLN02317 248 GLDilaegiqddsdnvTRFLMLAREPIIPRTDRPF-KTSIVFSLEEGP--GVLFKALAVFALRDINLTKIESRPQRkrpl 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2064415124 158 -----STDPSAGKADFIFYVDVKARQSDTDVLEAIASLRSACSYVRVLGCYA 204
Cdd:PLN02317 325 rvvddSNSGTAKYFDYLFYVDFEASMADPRAQNALAHLQEFATFLRVLGSYP 376
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
288-638 |
1.59e-27 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 114.65 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 288 GMAELRELITK-YLHCtkgvsydPATEIQICSGAQQALYNVILAICCPGDKVI--LPSpYWGNY---EGIITQVKagLVP 361
Cdd:PRK07324 63 GSPEFKEAVASlYQNV-------KPENILQTNGATGANFLVLYALVEPGDHVIsvYPT-YQQLYdipESLGAEVD--YWQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 362 LHNslEEDYLINPAELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLvyqDEGv 441
Cdd:PRK07324 133 LKE--ENGWLPDLDELRRLVR--PNTKLICINNANNPTGALMDRAYLEEIVEIARSVD---AYVLSDEVYRPL---DED- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 442 servcKNFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEK 521
Cdd:PRK07324 202 -----GSTPSIADLYEKGISTNSMSKTYSLPGIRVGWIAANEEVIDILRKYRDYTMICAGVFDDMLASLALEHRDAILER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 522 GEvRIAKDlhELDLKRQYVVKRlremPKMRFAYPTSsfyifmdlalyfeGKTAYSpdKTEVLHNVDDFCDYLIRTTGVAV 601
Cdd:PRK07324 277 NR-KIVRT--NLAILDEWVAKE----PRVSYVKPKA-------------VSTSFV--KLDVDMPSEDFCLKLLKETGVLL 334
|
330 340 350
....*....|....*....|....*....|....*..
gi 2064415124 602 GPGSDMGEPLGIRISYAGPMDTMVRAMDGLELALKSL 638
Cdd:PRK07324 335 VPGNRFDLEGHVRIGYCCDTETLKKGLKKLSEFLREF 371
|
|
| PRK09276 |
PRK09276 |
LL-diaminopimelate aminotransferase; Provisional |
241-632 |
2.44e-27 |
|
LL-diaminopimelate aminotransferase; Provisional
Pssm-ID: 181749 Cd Length: 385 Bit Score: 114.24 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 241 KTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQT-KYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSG 319
Cdd:PRK09276 22 KKAEKIARGVDVISLGIGDPDLPTPDHIIEAMCKAVEDPENhQYPSYEGMLEFRKAVADWYKRRFGVELDPETEVISLIG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 320 AQQALYNVILAICCPGDKVILPSPYWGNYeGIITQVKAG---LVPLhnsLEE-DYLINpaelektLTANPE-----TKIV 390
Cdd:PRK09276 102 SKEGIAHIPLAFVNPGDVVLVPDPGYPVY-KIGTIFAGGepyFMPL---KEEnGFLPD-------LDAIPEdvakkAKLM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 391 ILCNPSNPAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLVYQDEGVservcKNFAMIPGMYERTILINGFSKAYA 470
Cdd:PRK09276 171 FINYPNNPTGAVADLEFFEEVVDFAKKYD---IIVCHDAAYSEIAYDGYKP-----PSFLEVPGAKDVGIEFHSLSKTYN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 471 MTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEKgEVRIAKDlheldlKRQYVVKRLREMpKM 550
Cdd:PRK09276 243 MTGWRIGFAVGNADLIAGLGKVKSNVDSGVFQAIQEAGIAALNGPQEVVEE-LRKIYQE------RRDILVEGLRKL-GL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 551 RFAYPTSSFYIFmdlALYFEGKTAYSpdktevlhnvddFCDYLIRTTGVAVGPGSDMGEPlG---IRISYAGPMDTMVRA 627
Cdd:PRK09276 315 EVEPPKATFYVW---APVPKGYTSAE------------FATLLLDKAGVVVTPGNGFGEY-GegyFRIALTVPDERIEEA 378
|
....*
gi 2064415124 628 MDGLE 632
Cdd:PRK09276 379 VERIK 383
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
244-638 |
8.48e-27 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 114.16 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 244 QLEAEGKPVYSLCVGEPD---FPPP--KSVLDAGVRALQNGQTKYCDMRGMAELRELITKYLHcTKGVSYDPAtEIQICS 318
Cdd:COG1167 100 RLLEAAPGVIDLGSGAPDpdlFPLAalRRALRRALRRLPPALLGYGDPQGLPELREAIARYLA-RRGVPASPD-QILITS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 319 GAQQALYNVILAICCPGDKVILPSP-YWGNYEgIITQvkAGL----VPLHnslEEDylINPAELEKTLTANPeTKiVILC 393
Cdd:COG1167 178 GAQQALDLALRALLRPGDTVAVESPtYPGALA-ALRA--AGLrlvpVPVD---EDG--LDLDALEAALRRHR-PR-AVYV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 394 NPS--NPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVservcknfAMIPGM--YERTILINGFSKAY 469
Cdd:COG1167 248 TPShqNPTGATMSLERRRALLELARR---HGVPIIEDDYDSELRYDGRPP--------PPLAALdaPGRVIYIGSFSKTL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 470 AmTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAmklelasIEKGEVR--IAKDLHELDLKRQYVVKRLREM 547
Cdd:COG1167 317 A-PGLRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEF-------LESGHYDrhLRRLRREYRARRDLLLAALARH 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 548 --PKMRFAYPTSSFYIFMDLalyfegktaysPDKTevlhNVDDFCDYLIRtTGVAVGPGSD--MGEPL--GIRISYAGP- 620
Cdd:COG1167 389 lpDGLRVTGPPGGLHLWLEL-----------PEGV----DAEALAAAALA-RGILVAPGSAfsADGPPrnGLRLGFGAPs 452
|
410
....*....|....*...
gi 2064415124 621 MDTMVRAMDGLELALKSL 638
Cdd:COG1167 453 EEELEEALRRLAELLREL 470
|
|
| PRK07550 |
PRK07550 |
aminotransferase; |
222-512 |
2.12e-26 |
|
aminotransferase;
Pssm-ID: 181026 [Multi-domain] Cd Length: 386 Bit Score: 111.59 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 222 PLNPVFDTTTVAKTIAIFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYL 300
Cdd:PRK07550 1 PLNPLIAALFPPPIPEVRAWLAGYDGADGPLIDLSQAVPGYPPPPELLRALAEAAADPAaHLYGPVEGLPELREAYAAHY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 301 HCTKGVSYDPAtEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYE------GIitqvKAGLVPLHNslEEDYLINP 374
Cdd:PRK07550 81 SRLYGAAISPE-QVHITSGCNQAFWAAMVTLAGAGDEVILPLPWYFNHKmwldmlGI----RPVYLPCDE--GPGLLPDP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 375 AELEKTLTanPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQlvYQDEGvsERVCKNFAMiPG 454
Cdd:PRK07550 154 AAAEALIT--PRTRAIALVTPNNPTGVVYPPELLHELYDLARR---HGIALILDETYRD--FDSGG--GAPHDLFAD-PD 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 455 MYERTILINGFSKAYAMTGLRIGYMAGPKHFIEacQLMQGQTTS--CANSVGQVMAIEAM 512
Cdd:PRK07550 224 WDDTLVHLYSFSKSYALTGHRVGAVVASPARIA--EIEKFMDTVaiCAPRIGQIAVAWGL 281
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
250-627 |
3.10e-26 |
|
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273529 [Multi-domain] Cd Length: 401 Bit Score: 111.41 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 250 KPVYSLCVGEP----DFPPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYLHCTKGVSydPATEIQICSGAQQAL 324
Cdd:TIGR01264 31 KPMIKLSIGDPtvfgNLPTDPEVMQAMKDSLDSGKyNGYAPTVGALSAREAIASYYHNPDGPI--EADDVVLCSGCSHAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 325 YNVILAICCPGDKVILPSPYWGNYEGIITQVKAGlVPLHNSL-EEDYLINPAELEKTLTANpeTKIVILCNPSNPAGTLH 403
Cdd:TIGR01264 109 EMCIAALANAGQNILVPRPGFPLYETLAESMGIE-VKLYNLLpDKSWEIDLKQLESLIDEK--TAALIVNNPSNPCGSVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 404 SPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDegvservCKNFAMIPGMYERTILI-NGFSKAYAMTGLRIGYMAGP 482
Cdd:TIGR01264 186 SRQHLEEILAVAER---QCLPIIADEIYGDMVFSG-------ATFEPLASLSSTVPILScGGLAKRWLVPGWRLGWIIIH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 483 KHF----------IEACQLMQGQTTSCANSVGQVMaieamkleLASIEKGEVRIAKDLHEldlKRQYVVKRLREMPKMRF 552
Cdd:TIGR01264 256 DRRgilrdirdglVKLSQRILGPCTIVQGALPSIL--------LRTPQEYFDGTLSVLES---NAMLCYGALAAVPGLRP 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064415124 553 AYPTSSFYIFMDLALyfegkTAYSPDKTEVlhnvdDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVRA 627
Cdd:TIGR01264 325 VMPSGAMYMMVGIEM-----EHFPEFKNDV-----EFTERLVAEQSVFCLPGSCFEYPGFFRVVLTVPVVMMEEA 389
|
|
| PRK06290 |
PRK06290 |
LL-diaminopimelate aminotransferase; |
241-608 |
1.47e-25 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 235772 Cd Length: 410 Bit Score: 109.36 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 241 KTKQLEAEGKPVYSLC---VGEPDFPPPKSVldagVRALQNGQTK-----YCDmRGMAELRELITKYLHCTKGV-SYDPA 311
Cdd:PRK06290 32 RAKRAAKEKHPDMELIdmgVGEPDEMADESV----VEVLCEEAKKpenrgYAD-NGIQEFKEAAARYMEKVFGVkDIDPV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 312 TEIQICSGAQQALYNVILAICCPGDKVILPSPywgNYE--GIITQVKAGLV---PLHNslEEDYL-----INPAELEKTl 381
Cdd:PRK06290 107 TEVIHSIGSKPALAMLPSCFINPGDVTLMTVP---GYPvtGTHTKYYGGEVynlPLLE--ENNFLpdldsIPKDIKEKA- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 382 tanpetKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEGVServcknFAMIPGMYERTIL 461
Cdd:PRK06290 181 ------KLLYLNYPNNPTGAVATKEFYEEVVDFAKE---NNIIVVQDAAYAALTFDGKPLS------FLSVPGAKEVGVE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 462 INGFSKAYAMTGLRIGYMAGPKHFIEACQLMQGQTTScansvGQVMAIEamKLELASIEKGEVrIAKDLHELDLKRQYVV 541
Cdd:PRK06290 246 IHSLSKAYNMTGWRLAFVVGNELIVKAFATVKDNNDS-----GQFIAIQ--KAGIYALDHPEI-TEKIREKYSRRLDKLV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064415124 542 KRLREM---PKMrfayPTSSFYifmdlaLYFEgktaySPDKTE---VLHNVDDFCDYLIRTTGVAVGPGSDMG 608
Cdd:PRK06290 318 KILNEVgfkAEM----PGGTFY------LYVK-----APKGTKsgiKFENAEEFSQYLIKEKLISTVPWDDAG 375
|
|
| PRK05942 |
PRK05942 |
aspartate aminotransferase; Provisional |
238-634 |
1.85e-25 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 180317 Cd Length: 394 Bit Score: 109.04 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEA----EGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTK-YCDMRGMAELRELITKYLHCTKGVSYDPAT 312
Cdd:PRK05942 19 VFARLDELKArareQGLDLIDLGMGNPDGAAPQPVIEAAIAALADPQNHgYPPFEGTASFRQAITDWYHRRYGVELDPDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 313 EIQICSGAQQALYNVILAICCPGDKVILPSP-YWGNYEGIITqVKAGLVPLHNSLEEDYLINpaelektLTANPE----- 386
Cdd:PRK05942 99 EALPLLGSKEGLTHLALAYVNPGDVVLVPSPaYPAHFRGPLI-AGAQIYPIILKPENDWLID-------LSSIPEevaqq 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 387 TKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLV---YQDEGVSErvcknfamIPGMYERTILIN 463
Cdd:PRK05942 171 AKILYFNYPSNPTTATAPREFFEEIVAFARKYE---IMLVHDLCYAELAfdgYQPTSLLE--------IPGAKDIGVEFH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 464 GFSKAYAMTGLRIGYMAGPKHFIeacqlmQGQTTSCAN------SVGQVMAIEAMKLELASIEKGEVRIAKdlheldlKR 537
Cdd:PRK05942 240 TLSKTYNMAGWRVGFVVGNRHII------QGLRTLKTNldygifSALQKAAETALQLPDSYLQQVQERYRT-------RR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 538 QYVVKRLREMpKMRFAYPTSSFYIFMdlalyfegktayspdKTEVLHNVDDFCDYLIRTTGVAVGPGSDMGEplG----I 613
Cdd:PRK05942 307 DFLIQGLGEL-GWNIPPTKATMYLWV---------------PCPVGMGSTDFALNVLQKTGVVVTPGNAFGE--GgegyV 368
|
410 420
....*....|....*....|.
gi 2064415124 614 RISYAGPMDTMVRAMDGLELA 634
Cdd:PRK05942 369 RISLIADCDRLGEALDRLKQA 389
|
|
| PRK08068 |
PRK08068 |
transaminase; Reviewed |
238-609 |
6.16e-25 |
|
transaminase; Reviewed
Pssm-ID: 181219 Cd Length: 389 Bit Score: 107.32 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 238 IFGKTKQLEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQT-KYCDMRGMAELRELITKYLHCTKGVSYDPATEIQI 316
Cdd:PRK08068 20 LVAKVNKKVAEGHDVINLGQGNPDQPTPEHIVEALQEAAENPANhKYSPFRGYPFLKEAAADFYKREYGVTLDPETEVAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 317 CSGAQQALYNVILAICCPGDKVILPSP----YWgnyEGI-ITQVKAGLVPLHNslEEDYLIN----PAELEKtltanpET 387
Cdd:PRK08068 100 LFGGKAGLVELPQCLMNPGDTILVPDPgypdYL---SGVaLARAQFETMPLIA--ENNFLPDytkiPEEVAE------KA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 388 KIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEG-VServcknFAMIPGMYERTILINGFS 466
Cdd:PRK08068 169 KLMYLNYPNNPTGAVATKAFFEETVAFAKK---HNIGVVHDFAYGAIGFDGQKpVS------FLQTPGAKDVGIELYTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 467 KAYAMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEKgevriAKDLHEldLKRQYVVKRLRE 546
Cdd:PRK08068 240 KTFNMAGWRVAFAVGNESVIEAINLLQDHLFVSLFGAIQDAAIEALLSDQSCVAE-----LVARYE--SRRNAFISACRE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064415124 547 MPKMRFAyPTSSFYIFMDLAlyfEGKTAYSpdktevlhnvddFCDYLIRTTGVAVGPGSDMGE 609
Cdd:PRK08068 313 IGWEVDA-PKGSFFAWMPVP---KGYTSEQ------------FADLLLEKAHVAVAPGNGFGE 359
|
|
| PRK11898 |
PRK11898 |
prephenate dehydratase; Provisional |
22-207 |
1.01e-24 |
|
prephenate dehydratase; Provisional
Pssm-ID: 237013 [Multi-domain] Cd Length: 283 Bit Score: 104.52 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 22 EAAAQMLSAVDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYS-LAVVGE-------------- 86
Cdd:PRK11898 16 AAALKFFPADGEAELVPYDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYLAHGSpLQIVAEivlpiaqhllvhpg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 87 --------------------------------------------SESPAKT-------------------------SGKQ 97
Cdd:PRK11898 96 haakirtvyshpqalaqcrkwlaehlpgaelepanstaaaaqyvAEHPDEPiaaiaselaaelygleilaediqdyPNNR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 98 TRFWLVAKTPAEPSLKAAACKTSLAFAFASgNAHGQLYRALGVFASRGLDLSKIESRPwssTDPSAGkaDFIFYVDVKAR 177
Cdd:PRK11898 176 TRFWLLGRKKPPPPLRTGGDKTSLVLTLPN-NLPGALYKALSEFAWRGINLTRIESRP---TKTGLG--TYFFFIDVEGH 249
|
250 260 270
....*....|....*....|....*....|
gi 2064415124 178 QSDTDVLEAIASLRSACSYVRVLGCYASVD 207
Cdd:PRK11898 250 IDDVLVAEALKELEALGEDVKVLGSYPVYW 279
|
|
| PRK03321 |
PRK03321 |
putative aminotransferase; Provisional |
249-510 |
8.48e-23 |
|
putative aminotransferase; Provisional
Pssm-ID: 179559 Cd Length: 352 Bit Score: 100.43 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 249 GKPV---YSLCVGEPDFPPPKSVLDAGVRALQnGQTKYCDMrGMAELRELITKYLhctkGVsydPATEIQICSG----AQ 321
Cdd:PRK03321 18 GKTVpgaIKLSSNETPFGPLPSVRAAIARAAA-GVNRYPDM-GAVELRAALAEHL----GV---PPEHVAVGCGsvalCQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 322 QalynVILAICCPGDKVILPspyWGNYEG--IITQVkAGLVPLHNSLEEDYLInpaELEKTLTA-NPETKIVILCNPSNP 398
Cdd:PRK03321 89 Q----LVQATAGPGDEVIFA---WRSFEAypILVQV-AGATPVQVPLTPDHTH---DLDAMAAAiTDRTRLIFVCNPNNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 399 AGTLHSPEHLEK-IAAVlrkPqfRHVVVISDEIYEQLVYQDEG------VSERvcKNFAMIpgmyeRTilingFSKAYAM 471
Cdd:PRK03321 158 TGTVVTPAELARfLDAV---P--ADVLVVLDEAYVEYVRDDDVpdglelVRDH--PNVVVL-----RT-----FSKAYGL 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 2064415124 472 TGLRIGYMAGPKHFIEAcqLMQGQTTSCANSVGQVMAIE 510
Cdd:PRK03321 221 AGLRVGYAVGHPEVIAA--LRKVAVPFSVNSLAQAAAIA 257
|
|
| PRK09265 |
PRK09265 |
aminotransferase AlaT; Validated |
243-511 |
2.51e-22 |
|
aminotransferase AlaT; Validated
Pssm-ID: 181738 Cd Length: 404 Bit Score: 99.89 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 243 KQLEAEGKPVYSLCVGEP---DFPPPKSVLDAGVRALQNGQtKYCDMRGMAELRELITKYlHCTKGVSYDPATEIQICSG 319
Cdd:PRK09265 26 KRLEEEGHKILKLNIGNPapfGFEAPDEILRDVIRNLPTAQ-GYSDSKGLFSARKAIMQY-YQQKGIPDVDVDDIYIGNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 320 -------AQQALYNvilaiccPGDKVILPSP-Y--WgnyegiiTQVK--AGLVPLHNSLEE--DYLINPAELEKTLTANp 385
Cdd:PRK09265 104 vselivmAMQALLN-------NGDEVLVPAPdYplW-------TAAVslSGGKPVHYLCDEeaGWFPDLDDIRSKITPR- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 386 eTKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDE------GVSERVCknfamipgmyerT 459
Cdd:PRK09265 169 -TKAIVIINPNNPTGAVYSKELLEEIVEIARQ---HNLIIFADEIYDKILYDGAvhisiaSLAPDLL------------C 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2064415124 460 ILINGFSKAYAMTGLRIGYMA--GPKH----FIEACQlMQGQTTSCANSVGQvMAIEA 511
Cdd:PRK09265 233 VTFNGLSKAYRVAGFRVGWMVlsGPKKhakgYIEGLD-MLASMRLCANVPAQ-HAIQT 288
|
|
| PRK08175 |
PRK08175 |
aminotransferase; Validated |
226-609 |
5.82e-22 |
|
aminotransferase; Validated
Pssm-ID: 181268 [Multi-domain] Cd Length: 395 Bit Score: 98.63 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 226 VFDTTTVAKTIAifgktkqlEAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQT-KYCDMRGMAELRELITKYLHCTK 304
Cdd:PRK08175 13 VFNITAELKMAA--------RRRGEDIIDFSMGNPDGPTPPHIVEKLCEVAQRPDThGYSTSRGIPRLRRAISRWYQDRY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 305 GVSYDPATEIQICSGAQQALYNVILAICCPGDKVILPSPYW--GNYEGIITQVKAGLVPLHNslEEDYLinpAELEKTLT 382
Cdd:PRK08175 85 DVDIDPESEAIVTIGSKEGLAHLMLATLDHGDTVLVPNPSYpiHIYGAVIAGAQVRSVPLVE--GVDFF---NELERAIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 383 AN-PETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLVYQDegvseRVCKNFAMIPGMYERTIL 461
Cdd:PRK08175 160 ESyPKPKMMILGFPSNPTAQCVELEFFEKVVALAKRYD---VLVVHDLAYADIVYDG-----WKAPSIMQVPGAKDVAVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 462 INGFSKAYAMTGLRIGYMAGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMklelasieKGEVRIAKDLHELDLKRQYV- 540
Cdd:PRK08175 232 FFTLSKSYNMAGWRIGFMVGNPELVSALARIKSYHDYGTFTPLQVAAIAAL--------EGDQQCVRDIAEQYKRRRDVl 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064415124 541 VKRLREMPKMrFAYPTSSFYIFmdlalyfegktAYSPDKTEVLHNVdDFCDYLIRTTGVAVGPGSDMGE 609
Cdd:PRK08175 304 VKGLHEAGWM-VEMPKASMYVW-----------AKIPEPYAAMGSL-EFAKKLLNEAKVCVSPGIGFGD 359
|
|
| ACT_CM-PDT |
cd04905 |
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ... |
118-203 |
1.21e-21 |
|
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153177 [Multi-domain] Cd Length: 80 Bit Score: 89.10 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 118 KTSLAFAfaSGNAHGQLYRALGVFASRGLDLSKIESRpwsstdPSAGKA-DFIFYVDVKARQSDTDVLEAIASLRSACSY 196
Cdd:cd04905 1 KTSIVFT--LPNKPGALYDVLGVFAERGINLTKIESR------PSKGGLwEYVFFIDFEGHIEDPNVAEALEELKRLTEF 72
|
....*..
gi 2064415124 197 VRVLGCY 203
Cdd:cd04905 73 VKVLGSY 79
|
|
| PRK06225 |
PRK06225 |
pyridoxal phosphate-dependent aminotransferase; |
263-543 |
2.00e-21 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235749 [Multi-domain] Cd Length: 380 Bit Score: 96.75 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 263 PPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYLhctkGVsydPATEIQICSGAQQALYNVILAICCPGDKVILP 341
Cdd:PRK06225 41 GPHEEVREAMIRCIEEGEyCKYPPPEGFPELRELILKDL----GL---DDDEALITAGATESLYLVMRAFLSPGDNAVTP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 342 SPYWGNYEGIITQVKAGL--VPLHNSlEEDYLINPAELEKTLTANpeTKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpq 419
Cdd:PRK06225 114 DPGYLIIDNFASRFGAEVieVPIYSE-ECNYKLTPELVKENMDEN--TRLIYLIDPLNPLGSSYTEEEIKEFAEIARD-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 420 fRHVVVISDEIYeqlvyqdegvservcKNFAmiPGMY-------ERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQLM 492
Cdd:PRK06225 189 -NDAFLLHDCTY---------------RDFA--REHTlaaeyapEHTVTSYSFSKIFGMAGLRIGAVVATPDLIEVVKSI 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2064415124 493 QGQTTScANSVGQVMAIEAMKLELASIEKgevriakdLHELDLKRQYVVKR 543
Cdd:PRK06225 251 VINDLG-TNVIAQEAAIAGLKVKDEWIDR--------IRRTTFKNQKLIKE 292
|
|
| PRK13355 |
PRK13355 |
bifunctional HTH-domain containing protein/aminotransferase; Provisional |
244-568 |
2.47e-21 |
|
bifunctional HTH-domain containing protein/aminotransferase; Provisional
Pssm-ID: 237361 [Multi-domain] Cd Length: 517 Bit Score: 97.88 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 244 QLEAEGKPVYSLCVGEP---DFPPPKSVLDAGVRALQNGqTKYCDMRGMAELRELITKYLHcTKGVSYDPATEIQICSGA 320
Cdd:PRK13355 140 RMEAAGTHILKLNIGNPapfGFRTPDEVVYDMAQQLTDT-EGYSDSKGLFSARKAIMQYAQ-LKGLPNVDVDDIYTGNGV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 321 QQALYNVILAICCPGDKVILPSPYWGNYEGIITQvkAGLVPLHNSLEEDYLINP--AELEKTLTANpeTKIVILCNPSNP 398
Cdd:PRK13355 218 SELINLSMSALLDDGDEVLIPSPDYPLWTACVNL--AGGTAVHYRCDEQSEWYPdiDDIRSKITSR--TKAIVIINPNNP 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 399 AGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLVYQD-EGVSerVCknfAMIPGMYerTILINGFSKAYAMTGLRIG 477
Cdd:PRK13355 294 TGALYPREVLQQIVDIAREHQ---LIIFSDEIYDRLVMDGlEHTS--IA---SLAPDLF--CVTFSGLSKSHMIAGYRIG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 478 YM--AGPKH----FIEACQlMQGQTTSCANSVGQVMAIEAM----KLELASIEKGEVriakdlHEldlKRQYVVKRLREM 547
Cdd:PRK13355 364 WMilSGNKRiakdYIEGLN-MLANMRLCSNVPAQSIVQTALgghqSVKDYLVPGGRV------YE---QRELVYNALNAI 433
|
330 340
....*....|....*....|...
gi 2064415124 548 PKMRFAYPTSSFYIF--MDLALY 568
Cdd:PRK13355 434 PGISAVKPKAAFYIFpkIDVKKF 456
|
|
| hisC |
TIGR01141 |
histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; ... |
262-565 |
3.79e-21 |
|
histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273467 Cd Length: 350 Bit Score: 95.41 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 262 FPPPKSVLDAGVRALQNGqTKYCDmRGMAELRELITKYLhctkGVSYDpateiQIC--SGAQQALYNVILAICCPGDKVI 339
Cdd:TIGR01141 32 FGPPEKAKEALRAELKKL-HRYPD-PDPAELKQALADYY----GVDPE-----QILlgNGSDEIIDLLIRAFLEPGDAVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 340 LPSPYWGNYEgIITQVKAGLVpLHNSLEEDYLINpaeLEKTLTAN-PETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKP 418
Cdd:TIGR01141 101 VPPPTYSMYE-ISAKIHGAEV-VKVPLDEDGQLD---LEDILVAIdDKPKLVFLCSPNNPTGNLFSRGDIEAVLERTPGD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 419 qfrhVVVISDEIYEQLVYQDEGVServcknfaMIPGmYERTILINGFSKAYAMTGLRIGYMAGPKHFIEAcqLMQGQTTS 498
Cdd:TIGR01141 176 ----ALVVVDEAYGEFSGEPSTLP--------LLAE-YPNLIVLRTLSKAFGLAGLRIGYAIANAEIIDA--LNKVRAPF 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064415124 499 CANSVGQVMAIEAMKlELASIEKgevRIAKDLHEldlkRQYVVKRLREMPKMRfAYPTSSFYIFMDL 565
Cdd:TIGR01141 241 NLSRLAQAAAIAALR-DDDFIEA---TVEEINAE----RERLYDGLKKLPGLE-VYPSDANFVLIRF 298
|
|
| PTZ00433 |
PTZ00433 |
tyrosine aminotransferase; Provisional |
249-629 |
7.49e-21 |
|
tyrosine aminotransferase; Provisional
Pssm-ID: 185613 Cd Length: 412 Bit Score: 95.24 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 249 GKPVYSLCVGEP----DFPPPKSVLDAGVRALQNGQTK-YCDMRGMAELRELITKYLHCTKGVSYDPATEIQ-----ICS 318
Cdd:PTZ00433 32 PKSIIKLSVGDPtldgNLLTPAIQTKALVEAVDSQECNgYPPTVGSPEAREAVATYWRNSFVHKESLKSTIKkdnvvLCS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 319 GAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLtaNPETKIVILCNPSNP 398
Cdd:PTZ00433 112 GVSHAILMALTALCDEGDNILVPAPGFPHYETVCKAYGIEMRFYNCRPEKDWEADLDEIRRLV--DDRTKALIMTNPSNP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 399 AGTLHSPEHlekIAAVLRKPQFRHVVVISDEIYEQLVYQDEGVSErVCKNFAMIPgmyeRTILiNGFSKAYAMTGLRIGY 478
Cdd:PTZ00433 190 CGSNFSRKH---VEDIIRLCEELRLPLISDEIYAGMVFNGATFTS-VADFDTTVP----RVIL-GGTAKNLVVPGWRLGW 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 479 MAGPKHFIEACQLMQG-----QTTSCANSVGQVMAIEAMklelasIEKGEVRIAKDLHELDLKRQYVVKRLREMPKMRFA 553
Cdd:PTZ00433 261 LLLVDPHGNGGDFLDGmkrlgMLVCGPCSVVQAALGEAL------LNTPQEHLEQIVAKLEEGAMVLYNHIGECIGLSPT 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064415124 554 YPTSSFYIFMDLALYFegktaYSPDKTEVlhnvdDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVRAMD 629
Cdd:PTZ00433 335 MPRGSMFLMSRLDLEK-----FRDIKSDV-----EFYEKLLEEENVQVLPGEIFHMPGFTRLTISRPVEVLREAVE 400
|
|
| PRK07366 |
PRK07366 |
LL-diaminopimelate aminotransferase; |
226-608 |
1.18e-20 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 180947 Cd Length: 388 Bit Score: 94.36 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 226 VFDTTTVAKTIAIfgktkqleAEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTK-YCDMRGMAELRELITKYLHCTK 304
Cdd:PRK07366 14 VFADMDRAKAQAR--------AAGKELIDLSLGSSDLPAPAHALEAIAQSLHDPSTHgYLLFHGTLDFREAAAQWYEQRF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 305 GVSYDPATEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTAn 384
Cdd:PRK07366 86 GLAVDPETEVLPLIGSQEGTAHLPLAVLNPGDFALLLDPGYPSHAGGVYLAGGQIYPMPLRAENDFLPVFADIPTEVLA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 385 pETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQfrhVVVISDEIYEQLVYQDEgvservcknfAMIPGMY----ERTI 460
Cdd:PRK07366 165 -QARLMVLSYPHNPTTAIAPLSFFQEAVAFCQQHD---LVLVHDFPYVDLVFDGE----------VEPPSILqadpEKSV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 461 LINGF--SKAYAMTGLRIGYMAGPKHFIEAcqLMQGQTTSCANSVGQVM--AIEAMKLELASIEKgEVRIAKDlheldlK 536
Cdd:PRK07366 231 SIEFFtlSKSYNMGGFRIGFAIGNAQLIQA--LRQVKAVVDFNQYRGILngAIAALTGPQATVQQ-TVQIFRQ------R 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064415124 537 RQYVVKRLREM----PKmrfayPTSSFYIFMDLALYFEGKTAyspdktevlhnvdDFCDYLIRTTGVAVGPGSDMG 608
Cdd:PRK07366 302 RDAFINALHQIgwpvPL-----PEATMYVWAKLPEPWQGNSV-------------EFCTQLVAQTGVAASPGSGFG 359
|
|
| PRK09148 |
PRK09148 |
LL-diaminopimelate aminotransferase; |
247-609 |
1.53e-19 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 181674 [Multi-domain] Cd Length: 405 Bit Score: 91.28 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 247 AEGKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQT-KYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALY 325
Cdd:PRK09148 27 AAGADIIDLGMGNPDLPTPQHIVDKLCETAQDPRThRYSASKGIPGLRRAQAAYYARRFGVKLNPDTQVVATLGSKEGFA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 326 NVILAICCPGDKVILPSP-YWGNYEGIITqvkAGLVPLHNSLEEDYLINPAeLEKTLTAN-PETKIVILCNPSNPAGTLH 403
Cdd:PRK09148 107 NMAQAITAPGDVILCPNPsYPIHAFGFIM---AGGVIRSVPAEPDEEFFPA-LERAVRHSiPKPIALIVNYPSNPTAYVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 404 SPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDEgvserVCKNFAMIPGMYERTILINGFSKAYAMTGLRIGYMAGPK 483
Cdd:PRK09148 183 DLDFYKDVVAFAKK---HDIIILSDLAYSEIYFDGN-----PPPSVLQVPGAKDVTVEFTSMSKTFSMAGWRMGFAVGNE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 484 HFIEACQLMQGQTTSCANSVGQVMAIEAMklelasieKGEVRIAKDLHELDLKRQYVVkrLREMPKMRFAYPTSSFYIFm 563
Cdd:PRK09148 255 RLIAALTRVKSYLDYGAFTPIQVAATAAL--------NGPQDCIAEMRELYKKRRDVL--VESFGRAGWDIPPPAASMF- 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2064415124 564 dlalyfegKTAYSPDKTEVLHNVdDFCDYLIRTTGVAVGPGSDMGE 609
Cdd:PRK09148 324 --------AWAPIPEAFRHLGSL-EFSKLLVEKADVAVAPGVGFGE 360
|
|
| ACT_AAAH-PDT-like |
cd04880 |
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ... |
123-201 |
1.07e-17 |
|
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153152 [Multi-domain] Cd Length: 75 Bit Score: 77.92 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 123 FAFASGNAHGQLYRALGVFASRGLDLSKIESRpwsstdPSAGKA-DFIFYVDVKARQSDTDVLEAIASLRSACSYVRVLG 201
Cdd:cd04880 2 LVFSLKNKPGALAKALKVFAERGINLTKIESR------PSRKGLwEYEFFVDFEGHIDDPDVKEALEELKRVTEDVKVLG 75
|
|
| PRK06207 |
PRK06207 |
pyridoxal phosphate-dependent aminotransferase; |
263-629 |
3.00e-17 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235742 Cd Length: 405 Bit Score: 84.43 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 263 PPPKS--VLDAGVRAlqNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNVILAICCPGDKVIL 340
Cdd:PRK06207 54 PTPGAfeLFSAGVER--GGVQAYTEYRGDADIRELLAARLAAFTGAPVDAADELIITPGTQGALFLAVAATVARGDKVAI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 341 PSP-YWGNYEgIITQVKAGLVPlhnsLEEDYL-------INPAELEKTLTANpeTKIVILCNPSNPAGTLHSPEHLEKIA 412
Cdd:PRK06207 132 VQPdYFANRK-LVEFFEGEMVP----VQLDYLsadkragLDLDQLEEAFKAG--VRVFLFSNPNNPAGVVYSAEEIAQIA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 413 AVLRKpqfRHVVVISDEIYEQLVYQDEGVSERVCKNFAMipgmyERTILINGFSKAYAMTGLRIGYMAGPKHFIEACQLM 492
Cdd:PRK06207 205 ALARR---YGATVIVDQLYSRLLYDGTSYTHLRALPIDP-----ENVITIMGPSKTESLSGYRLGVAFGSPAIIDRMEKL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 493 QGQTTSCANSVGQvmaieAMKLELASIEKG--EVRIAKdlHEldLKRQYVVKRLREMPKMRFAYPTSSFYIFMDLAlyfe 570
Cdd:PRK06207 277 QAIVSLRAAGYSQ-----AVLRTWFSEPDGwmKDRIAR--HQ--AIRDDLLRVLRGVEGVFVRAPQAGSYLFPRLP---- 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064415124 571 gKTAYSPdktevlhnvDDFCDYLIRTTGVAVGPGSDMGEPLG--IRISYAGPMDTMVRAMD 629
Cdd:PRK06207 344 -RLAVSL---------HDFVKILRLQAGVIVTPGTEFSPHTAdsIRLNFSQDHAAAVAAAE 394
|
|
| PLN00145 |
PLN00145 |
tyrosine/nicotianamine aminotransferase; Provisional |
249-637 |
7.47e-17 |
|
tyrosine/nicotianamine aminotransferase; Provisional
Pssm-ID: 215074 [Multi-domain] Cd Length: 430 Bit Score: 83.28 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 249 GKPVYSLCVGEPD----FPPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYLHCTkgVSYDPAT-EIQICSGAQQ 322
Cdd:PLN00145 51 PRPVLPLGHGDPSafpcFRTAPEAEDAVAAALRSGKyNSYSTCVGLLPARRAIAEYLSRD--LPYELSTdDIYLTAGCAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 323 ALYNVILAICCPGDKVILPSPYWGNYEGiiTQVKAGLVPLHNSL--EEDYLINPAELEKTLTANpeTKIVILCNPSNPAG 400
Cdd:PLN00145 129 AIEIIMSVLAQPGANILLPRPGYPLYEA--RAVFSGLEVRHFDLlpERGWEVDLEGVEALADEN--TVAMVIINPNNPCG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 401 TLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQDegvservcKNFamIP-GMYERT---ILINGFSKAYAMTGLRI 476
Cdd:PLN00145 205 SVYSYEHLAKIAETARK---LGILVIADEVYDHLTFGS--------KPF--VPmGVFGEVapvLTLGSISKRWVVPGWRL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 477 GYMA--GPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELASIEKgEVRIAKDLHELDLKRQYVVKRLREMPKMRFAY 554
Cdd:PLN00145 272 GWIAtcDPNGILKETKVVDSIRNYLNISTDPATFVQGAIPQIIANTK-EEFFTKTLGLLKETADICYEKIKEIKCITCPH 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 555 -PTSSFYIFMDLAL-YFEGktayspdktevLHNVDDFCDYLIRTTGVAVGPGSDMGEPLGIRISYAGPMDTMVramDGLE 632
Cdd:PLN00145 351 kPEGSMFVMVKLDLsCLSG-----------IKDDMDFCCKLAKEESVVVLPGSALGMKNWLRITFAIDPPSLE---DGLE 416
|
....*
gi 2064415124 633 lALKS 637
Cdd:PLN00145 417 -RLKS 420
|
|
| PRK09147 |
PRK09147 |
succinyldiaminopimelate transaminase; Provisional |
239-488 |
1.17e-15 |
|
succinyldiaminopimelate transaminase; Provisional
Pssm-ID: 236393 Cd Length: 396 Bit Score: 79.15 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 239 FGKTKQLEA-----EGKPVYSLCVGEPDFPPPKSVLDAGVRALQnGQTKYCDMRGMAELRELITKYLHCTKGV-SYDPAT 312
Cdd:PRK09147 13 FEKLRALFAgvtppADLPPISLSIGEPKHPTPAFIKDALAANLD-GLASYPTTAGLPALREAIAAWLERRYGLpALDPAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 313 EIQICSGAQQALYNVILAI---CCPGDKVILPSPYWGNYEGiiTQVKAGLVPLH-NSLEE-----DYLINPAELEKtlta 383
Cdd:PRK09147 92 QVLPVNGSREALFAFAQTVidrDGPGPLVVCPNPFYQIYEG--AALLAGAEPYFlNCDPAnnfapDFDAVPAEVWA---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 384 npETKIVILCNPSNPAGTLHSPEHLEKIAAVlrkpQFRHVVVI-SDEIYEQLvYQDE-----GVSErVCKnfAMIPGMYE 457
Cdd:PRK09147 166 --RTQLLFVCSPGNPTGAVLPLDDWKKLFAL----SDRYGFVIaSDECYSEI-YFDEaapplGLLE-AAA--ELGRDDFK 235
|
250 260 270
....*....|....*....|....*....|.
gi 2064415124 458 RTILINGFSKAYAMTGLRIGYMAGPKHFIEA 488
Cdd:PRK09147 236 RLVVFHSLSKRSNVPGLRSGFVAGDAALLKK 266
|
|
| PRK08636 |
PRK08636 |
LL-diaminopimelate aminotransferase; |
249-490 |
2.56e-15 |
|
LL-diaminopimelate aminotransferase;
Pssm-ID: 236316 Cd Length: 403 Bit Score: 78.21 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 249 GKPVYSLCVGEPDFPPPKSVLDAGVRALQNGQTK-YCDMRGMAELRELITKYLHCTKGVSYDPATEIQICSGAQQALYNV 327
Cdd:PRK08636 32 GEDIIDFSMGNPDGPTPQHIIDKLCESAQKPKTHgYSVSKGIYKLRLAICNWYKRKYNVDLDPETEVVATMGSKEGYVHL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 328 ILAICCPGDKVILPSPYW--GNYEGIITQVKAGLVPLHnsLEEDYLINPAE----LEKTL-TANPETKIVILCNPSNPAG 400
Cdd:PRK08636 112 VQAITNPGDVAIVPDPAYpiHSQAFILAGGNVHKMPLE--YNEDFELDEDQffenLEKALrESSPKPKYVVVNFPHNPTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 401 TLHSPEHLEKIAAVLRKPQFrhvVVISDEIYEQLVYqDEGVSERVCKnfamIPGMYERTILINGFSKAYAMTGLRIGYMA 480
Cdd:PRK08636 190 ATVEKSFYERLVALAKKERF---YIISDIAYADITF-DGYKTPSILE----VEGAKDVAVESYTLSKSYNMAGWRVGFVV 261
|
250
....*....|
gi 2064415124 481 GPKHFIEACQ 490
Cdd:PRK08636 262 GNKKLVGALK 271
|
|
| PBP2_Ct-PDT_like |
cd13631 |
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ... |
6-86 |
2.95e-14 |
|
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270349 [Multi-domain] Cd Length: 182 Bit Score: 71.29 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 6 STRVAYQesaefaGAK-----EAAAQMLSAVDgfEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYS 80
Cdd:cd13631 1 MKRVAYQ------GVPgayshLAARKYFGEDE--EVPCCKTFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEYD 72
|
....*.
gi 2064415124 81 LAVVGE 86
Cdd:cd13631 73 LYIVGE 78
|
|
| PRK05166 |
PRK05166 |
histidinol-phosphate transaminase; |
283-634 |
2.01e-13 |
|
histidinol-phosphate transaminase;
Pssm-ID: 179950 Cd Length: 371 Bit Score: 72.09 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 283 YCDMRGMAeLRELITkylhctkgVSYD-PATEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEgIITQV---KAG 358
Cdd:PRK05166 68 YPDPQGRA-LREAIA--------ARTGvPADRIILGNGSEDLIAVICRAVLRPGDRVVTLYPSFPLHE-DYPTMmgaRVE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 359 LVPLHNSLEedylINPAELEKTLTANPetKIVILCNPSNPAGTLHSPEHLEKIAAVLrKPQfrhVVVISDEIYEQLVYQD 438
Cdd:PRK05166 138 RVTVTPDLG----FDLDALCAAVARAP--RMLMFSNPSNPVGSWLTADQLARVLDAT-PPE---TLIVVDEAYAEYAAGD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 439 EGVSE-RVCKNFAMiPGMYERTilingFSKAYAMTGLRIGY-MAGPKhfiEACQLM-QGQTTSCANSVGQVMAIEAMkLE 515
Cdd:PRK05166 208 DYPSAlTLLKARGL-PWIVLRT-----FSKAYGLAGLRVGYgLVSDP---ELVGLLdRVRTPFNVNGAAQAAALAAL-DD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 516 LASIEKGevrIAKDLHEldlkRQYVVKRLREMpKMRFAYPTSSFyifmdlaLYFEGKTAYSPdktevlhnvddFCDYLIR 595
Cdd:PRK05166 278 EEHLAKG---VALALAE----RERLKKELAEM-GYRIAPSRANF-------LFFDARRPASA-----------VAEALLR 331
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2064415124 596 tTGVAVGPGSDMGEPLGIRISYAGPMDT--MVRAMDGLELA 634
Cdd:PRK05166 332 -QGVIVKPWKQPGFETFIRVSIGSPEENdhFVAALDKVLEA 371
|
|
| PLN00143 |
PLN00143 |
tyrosine/nicotianamine aminotransferase; Provisional |
234-618 |
3.74e-13 |
|
tyrosine/nicotianamine aminotransferase; Provisional
Pssm-ID: 165711 [Multi-domain] Cd Length: 409 Bit Score: 71.58 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 234 KTIAIFGKTKQLEAEGKPVYSLCVGEPD----FPPPKSVLDAGVRALQNGQ-TKYCDMRGMAELRELITKYLhcTKGVSY 308
Cdd:PLN00143 16 DDAVKFLKENFNEDDHRLAISFGFGDPScfecFRTTNIAEDAIVEAVRSAKfNSYAPTGGILPARRAIADYL--SNDLPY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 309 DPATE-IQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTltANPET 387
Cdd:PLN00143 94 QLSPDdVYLTLGCKHAAEIIIKVLARPEANILLPRPGFPDVETYAIFHHLEIRHFDLLPEKGWEVDLDAVEAI--ADENT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 388 KIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYqdeGVSERVCKNF--AMIPgmyerTILINGF 465
Cdd:PLN00143 172 IAMVIINPGNPCGSVYSYEHLNKIAETARK---LGILVIADEVYGHIVF---GSKPFVPMGLfaSIVP-----VITLGSI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 466 SKAYAMTGLRIGYM--AGPKHFIEACQLMQGQTTSCANSVGQVMAIEAMKLELasIEK-GEVRIAKDLHELDLKRQYVVK 542
Cdd:PLN00143 241 SKRWMIPGWGLGWLvtCDPSGLLQICEIADSIKKALNPAPFPPTFIQAAIPEI--LEKtTEDFFSKTINILRAALAFCYD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 543 RLREMPKMRFAY-PTSSFYIFMDLALyfegktayspdktEVLHNVDD---FCDYLIRTTGVAVGPGSDMGEPLGIRISYA 618
Cdd:PLN00143 319 KLKEIPCIMCPQkAEGAFFALVKLNL-------------LLLEDIEDdmeFCLKLAKEESLIILPGVTVGLKNWLRITFA 385
|
|
| PLN02656 |
PLN02656 |
tyrosine transaminase |
228-618 |
5.19e-13 |
|
tyrosine transaminase
Pssm-ID: 178262 [Multi-domain] Cd Length: 409 Bit Score: 71.11 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 228 DTTTVAKTIAIFGKTKQL------EAEGKPVYSLCVGEPD----FPPPKSVLDAGVRALQ-NGQTKYCDMRGMAELRELI 296
Cdd:PLN02656 3 NGADTTKTITIKGILSLLmesiddEENGKRVISLGMGDPTayscFHTTHVAQEAVVDALQsNKFNGYAPTVGLPQARRAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 297 TKYLhcTKGVSYDPATE-IQICSGAQQALyNVILAICC-PGDKVILPSPYWGNYEgiITQVKAGLVPLHNSL--EEDYLI 372
Cdd:PLN02656 83 AEYL--SRDLPYKLSLDdVFITSGCTQAI-DVALSMLArPGANILLPRPGFPIYE--LCAAFRHLEVRYVDLlpEKGWEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 373 NPAELEktLTANPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQFrhvVVISDEIYEQLVYqdegvservcKNFAMI 452
Cdd:PLN02656 158 DLDAVE--ALADQNTVALVIINPGNPCGNVYSYQHLKKIAETAEKLKI---LVIADEVYGHLAF----------GSNPFV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 453 P----GMYERTILINGFSKAYAMTGLRIGYMA---------GPKhFIEACQ----LMQGQTTSCANSVGQVMAieamkle 515
Cdd:PLN02656 223 PmgvfGSIVPVLTLGSLSKRWIVPGWRLGWFVttdpsgsfrDPK-IVERIKkyfdILGGPATFIQAAVPTILE------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 516 lasiEKGEVRIAKDLHELDLKRQYVVKRLREMPKMRFAY-PTSSFYIFMDLALYFegktayspdkTEVLHNVDDFCDYLI 594
Cdd:PLN02656 295 ----QTDESFFKKTINILKQSSDICCDRIKEIPCITCPHkPEGSMAVMVKLNLSL----------LEDISDDIDFCFKLA 360
|
410 420
....*....|....*....|....
gi 2064415124 595 RTTGVAVGPGSDMGEPLGIRISYA 618
Cdd:PLN02656 361 REESVIILPGTAVGLKNWLRITFA 384
|
|
| PRK08637 |
PRK08637 |
hypothetical protein; Provisional |
334-568 |
1.25e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181512 Cd Length: 388 Bit Score: 69.98 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 334 PGDKVILPSPYWGNYEGII-TQVKAGLVPlHNSLEEDYLINPAELEKTLTANPE-TKIVILCN-PSNPAGTLHSPEHLEK 410
Cdd:PRK08637 92 QGDTVLLPDHNWGNYKLTFnTRRGAEIVT-YPIFDEDGGFDTDALKEALQAAYNkGKVIVILNfPNNPTGYTPTEKEATA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 411 IAAVLRK--PQFRHVVVISDEIYEQLVYQDeGVSERVcknFAMIPGMYER--TILINGFSKAYAMTGLRIGYMAGPKHFI 486
Cdd:PRK08637 171 IVEAIKElaDAGTKVVAVVDDAYFGLFYED-SYKESL---FAALANLHSNilAVKLDGATKEEFVWGFRVGFITFGTKAG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 487 EACQLMQG----------QTTSCANSVGQVMAIEAMKLELASIEKGE-VRIAKdlheldlKRQYVVKRLREMPKMRFA-- 553
Cdd:PRK08637 247 SSQTVKEAlekkvkglirSNISNGPHPSQSAVLRALNSPEFDKEKQEkFQILK-------ERYEKTKEVLYDGKYDDAwq 319
|
250
....*....|....*.
gi 2064415124 554 -YPTSSFYiFMDLALY 568
Cdd:PRK08637 320 aYPFNSGY-FMCLKLK 334
|
|
| PRK08354 |
PRK08354 |
putative aminotransferase; Provisional |
313-488 |
1.64e-12 |
|
putative aminotransferase; Provisional
Pssm-ID: 169399 Cd Length: 311 Bit Score: 68.60 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 313 EIQICSGAQQALYnvILAI-CCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNsleedyliNPAELEKTLTANpetKIVI 391
Cdd:PRK08354 56 PIVITAGITEALY--LIGIlALRDRKVIIPRHTYGEYERVARFFAARIIKGPN--------DPEKLEELVERN---SVVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 392 LCNPSNPAGTLHSPEHLekiAAVLRKPQFRHVVVISDEIYEQLVYQDEGVServcknfamipgmYERTILINGFSKAYAM 471
Cdd:PRK08354 123 FCNPNNPDGKFYNFKEL---KPLLDAVEDRNALLILDEAFIDFVKKPESPE-------------GENIIKLRTFTKSYGL 186
|
170
....*....|....*..
gi 2064415124 472 TGLRIGYMAGpkhFIEA 488
Cdd:PRK08354 187 PGIRVGYVKG---FEEA 200
|
|
| PTZ00377 |
PTZ00377 |
alanine aminotransferase; Provisional |
283-628 |
3.01e-12 |
|
alanine aminotransferase; Provisional
Pssm-ID: 240391 [Multi-domain] Cd Length: 481 Bit Score: 69.22 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 283 YCDMRGMAELRELITKYLHCTKGVSYDPATeIQICSGAQQALYNVI-LAICCPGDKVILPSPYWGNYEGIITQVkaGLVP 361
Cdd:PTZ00377 111 YTDSAGYPFVRKAVAAFIERRDGVPKDPSD-IFLTDGASSGIKLLLqLLIGDPSDGVMIPIPQYPLYSAAITLL--GGKQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 362 LHNSLEED--YLINPAELEKTLT------ANPetKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQ 433
Cdd:PTZ00377 188 VPYYLDEEkgWSLDQEELEEAYEqavrngITP--RALVVINPGNPTGQVLTRDVMEEIIKFCYE---KGIVLMADEVYQE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 434 LVYQDEG--VSERvcKNFAMIPGMYERTILINGF---SKA-YAMTGLRIGYMAG---PKHFIEacQLMQGQTTS-CANSV 503
Cdd:PTZ00377 263 NIYDGEKpfISFR--KVLLELPAEYNTDVELVSFhstSKGiIGECGRRGGYFELtniPPEVRE--QIYKLASINlCSNVV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 504 GQVMaieaMKLELASIEKGEVRIAKDLHELD-----LKR--QYVVKRLREMPKMRFAYPTSSFYIFMDLAL---YFEG-- 571
Cdd:PTZ00377 339 GQLM----TGLMCNPPREGDASYPLYKRERDaiftsLKRraELLTDELNKIEGVSCQPVEGAMYAFPRIELpekAIQEak 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 572 KTAYSPDKTevlhnvddFCDYLIRTTGVAVGPGSDMGEPLG---IRISYAGPMDTMVRAM 628
Cdd:PTZ00377 415 ERGLAPDVL--------YCLELLESTGIVVVPGSGFGQKPGtyhFRITILPPEEQIEEMV 466
|
|
| PRK05839 |
PRK05839 |
succinyldiaminopimelate transaminase; |
248-481 |
7.04e-12 |
|
succinyldiaminopimelate transaminase;
Pssm-ID: 180281 Cd Length: 374 Bit Score: 67.41 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 248 EGKPVYSLCVGEPDFPPPKSVLDagvrALQNGQT---KYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSGAQQAL 324
Cdd:PRK05839 22 KEYKGLDLTIGEPQFETPKFIQD----ALKNNAHllnKYPKSAGEESLREAQRGFFKRRFKIELKE-NELIPTFGTREVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 325 YNV--ILAICCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDY--LINPAELEktltanpETKIVILCNPSNPAG 400
Cdd:PRK05839 97 FNFpqFVLFDKQNPTIAYPNPFYQIYEGAAIASRAKVLLMPLTKENDFtpSLNEKELQ-------EVDLVILNSPNNPTG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 401 TLHSpehLEKIAAVLRKPQFRHVVVISDEIYEQLvYQDEGVSERVCKNFAMIPGMYERTILINGFSKAYAMTGLRIGYMA 480
Cdd:PRK05839 170 RTLS---LEELIEWVKLALKHDFILINDECYSEI-YENTPPPSLLEASILVGNESFKNVLVINSISKRSSAPGLRSGFIA 245
|
.
gi 2064415124 481 G 481
Cdd:PRK05839 246 G 246
|
|
| PDT |
pfam00800 |
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ... |
9-86 |
7.59e-12 |
|
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein catalyzes the decarboxylation of prephenate to phenylpyruvate.
Pssm-ID: 425875 [Multi-domain] Cd Length: 181 Bit Score: 64.49 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 9 VAYQesaefaGAK----EAAAQMLSAVDgFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYSLAVV 84
Cdd:pfam00800 1 IAYL------GPPgtfsHQAALKYFGED-AELVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKSDLKIV 73
|
..
gi 2064415124 85 GE 86
Cdd:pfam00800 74 GE 75
|
|
| PLN03026 |
PLN03026 |
histidinol-phosphate aminotransferase; Provisional |
319-487 |
8.80e-12 |
|
histidinol-phosphate aminotransferase; Provisional
Pssm-ID: 178597 Cd Length: 380 Bit Score: 67.03 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 319 GAQQALYNVILAICCPGDKVILPSPYWGNYE--GIITQVKAGLVPLhnslEEDYLINPAELEKTLTaNPETKIVILCNPS 396
Cdd:PLN03026 111 GADELIDLLMRCVLDPGDKIIDCPPTFGMYVfdAAVNGAEVIKVPR----TPDFSLDVPRIVEAVE-THKPKLLFLTSPN 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 397 NPAGTLHSPEHLEKIaavLRKPqfrhVVVISDEIYEQLVYQDEGVSErVCKnfamipgmYERTILINGFSKAYAMTGLRI 476
Cdd:PLN03026 186 NPDGSIISDDDLLKI---LELP----ILVVLDEAYIEFSTQESRMKW-VKK--------YDNLIVLRTFSKRAGLAGLRV 249
|
170
....*....|.
gi 2064415124 477 GYMAGPKHFIE 487
Cdd:PLN03026 250 GYGAFPLSIIE 260
|
|
| PLN02187 |
PLN02187 |
rooty/superroot1 |
270-616 |
1.12e-11 |
|
rooty/superroot1
Pssm-ID: 215119 [Multi-domain] Cd Length: 462 Bit Score: 67.44 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 270 DAGVRALQNGQ-TKYCDMRGMAELRELITKYLHCTKGVSYDPAtEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNY 348
Cdd:PLN02187 90 DAVVDVLRSGKgNSYGPGAGILPARRAVADYMNRDLPHKLTPE-DIFLTAGCNQGIEIVFESLARPNANILLPRPGFPHY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 349 EGI-----ITQVKAGLVPlhnslEEDYLINPAELEKTLTANPETKIVIlcNPSNPAGTLHSPEHLEKIAAVLRKpqfRHV 423
Cdd:PLN02187 169 DARaaysgLEVRKFDLLP-----EKEWEIDLEGIEAIADENTVAMVVI--NPNNPCGNVYSHDHLKKVAETARK---LGI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 424 VVISDEIYEQLVYQDEGVSErVCKNFAMIPgmyerTILINGFSKAYAMTGLRIGYMA--GPKHFIEACQLMQGQTTSCAN 501
Cdd:PLN02187 239 MVISDEVYDRTIFGDNPFVS-MGKFASIVP-----VLTLAGISKGWVVPGWKIGWIAlnDPEGVFETTKVLQSIKQNLDV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 502 SVGQVMAIEAMKleLASIEKGEVR-IAKDLHELDLKRQYVVKRLREMPKMRF-AYPTSSFYIFMDLALyfegktayspdk 579
Cdd:PLN02187 313 TPDPATIIQAAL--PAILEKADKNfFAKKNKILKHNVDLVCDRLKDIPCVVCpKKPESCTYLLTKLEL------------ 378
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2064415124 580 tEVLHNVD---DFCDYLIRTTGVAVGPGSDMGEPLGIRIS 616
Cdd:PLN02187 379 -SLMDNIKddiDFCVKLAREENLVFLPGDALGLKNWMRIT 417
|
|
| PLN02368 |
PLN02368 |
alanine transaminase |
262-439 |
1.28e-10 |
|
alanine transaminase
Pssm-ID: 177996 [Multi-domain] Cd Length: 407 Bit Score: 63.67 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 262 FPPpksvlDAGVRA------LQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSGAQQALYNVILAIC-CP 334
Cdd:PLN02368 81 FPA-----DAIARAkhylslTSGGLGAYSDSRGLPGVRKEVAEFIERRDGYPSDP-ELIFLTDGASKGVMQILNAVIrGE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 335 GDKVILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTANPETKIV----ILCNPSNPAGTLHSPEHLEK 410
Cdd:PLN02368 155 KDGVLVPVPQYPLYSATISLLGGTLVPYYLEESENWGLDVNNLRQSVAQARSKGITvramVIINPGNPTGQCLSEANLRE 234
|
170 180
....*....|....*....|....*....
gi 2064415124 411 IaavLRKPQFRHVVVISDEIYEQLVYQDE 439
Cdd:PLN02368 235 I---LKFCYQERLVLLGDEVYQQNIYQDE 260
|
|
| PLN02376 |
PLN02376 |
1-aminocyclopropane-1-carboxylate synthase |
283-436 |
1.47e-10 |
|
1-aminocyclopropane-1-carboxylate synthase
Pssm-ID: 178004 [Multi-domain] Cd Length: 496 Bit Score: 63.95 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 283 YCDMRGMAELRELITKYLHCTKG--VSYDPAtEIQICSGAQQALYNVILAICCPGDKVILPSPYWGNYEGII---TQVKA 357
Cdd:PLN02376 90 FQDYHGLKKFRQAIAHFMGKARGgkVTFDPE-RVVMSGGATGANETIMFCLADPGDVFLIPSPYYAAFDRDLrwrTGVEI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 358 GLVPLHNSLEEDYLINPAE--LEKTLTANPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKPQFrHVVVisDEIYEQLV 435
Cdd:PLN02376 169 IPVPCSSSDNFKLTVDAADwaYKKAQESNKKVKGLILTNPSNPLGTMLDKDTLTNLVRFVTRKNI-HLVV--DEIYAATV 245
|
.
gi 2064415124 436 Y 436
Cdd:PLN02376 246 F 246
|
|
| PRK03317 |
PRK03317 |
histidinol-phosphate aminotransferase; Provisional |
255-491 |
4.33e-10 |
|
histidinol-phosphate aminotransferase; Provisional
Pssm-ID: 235115 Cd Length: 368 Bit Score: 61.80 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 255 LCVGEPDFPPPKSVLDA---GVRALQNGQTKYCDmRGMAELRELITKYLHCTKGVSYDPAtEIQICSGAQQALYNVILAI 331
Cdd:PRK03317 31 LNTNENPYPPSPALVADiaeAVAEAAAGLNRYPD-RDAVALRADLAAYLTAQTGVGLTVE-NVWAANGSNEILQQLLQAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 332 CCPGDKVILPSPYWGNYEGIITQVKAGLVPLHNslEEDYLINPaelEKTLTANPETK--IVILCNPSNPAGTLHSPEHLE 409
Cdd:PRK03317 109 GGPGRTALGFVPSYSMHPIIARGTHTEWVEGPR--AADFTLDV---DAAVAAIAEHRpdVVFLTSPNNPTGTALPLDDVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 410 KIAAVLRKpqfrhvVVISDEIYEQlvYQDEGVSERVcknfAMIPGmYERTILINGFSKAYAMTGLRIGYMAGPKHFIEAC 489
Cdd:PRK03317 184 AILDAAPG------IVVVDEAYAE--FRRSGTPSAL----TLLPE-YPRLVVSRTMSKAFAFAGGRLGYLAAAPAVVDAL 250
|
..
gi 2064415124 490 QL 491
Cdd:PRK03317 251 RL 252
|
|
| PLN02450 |
PLN02450 |
1-aminocyclopropane-1-carboxylate synthase |
285-477 |
9.93e-10 |
|
1-aminocyclopropane-1-carboxylate synthase
Pssm-ID: 178069 [Multi-domain] Cd Length: 468 Bit Score: 61.31 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 285 DMRGMAELRELITKYLHCTKG--VSYDPaTEIQICSGAQQAlyNVILAICC--PGDKVILPSPYwgnYEGIITQVK---- 356
Cdd:PLN02450 84 DYHGLPAFKNALAEFMSEIRGnkVTFDP-NKLVLTAGATSA--NETLMFCLaePGDAFLLPTPY---YPGFDRDLKwrtg 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 357 AGLVPLHNSLEEDYLINPAELEKT----LTANPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYE 432
Cdd:PLN02450 158 VEIVPIHCSSSNGFQITESALEEAyqqaQKLNLKVKGVLITNPSNPLGTTTTRTELNLLVDFITA---KNIHLISDEIYS 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2064415124 433 QLVYQDEG---VSERVCKNFAMIPGMYERTILINGFSKAYAMTGLRIG 477
Cdd:PLN02450 235 GTVFDSPGfvsVMEVLKDRKLENTDVSNRVHIVYSLSKDLGLPGFRVG 282
|
|
| PLN02607 |
PLN02607 |
1-aminocyclopropane-1-carboxylate synthase |
285-477 |
1.14e-09 |
|
1-aminocyclopropane-1-carboxylate synthase
Pssm-ID: 215327 [Multi-domain] Cd Length: 447 Bit Score: 61.06 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 285 DMRGMAELRELITKYLHCTKG--VSYDPaTEIQICSGAQQA--LYNVILAicCPGDKVILPSPYWGNYEGII---TQVKa 357
Cdd:PLN02607 93 DYHGLKSFRQAMASFMEQIRGgkARFDP-DRIVLTAGATAAneLLTFILA--DPGDALLVPTPYYPGFDRDLrwrTGVK- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 358 gLVPLHNSLEEDYLINPAELE----KTLTANPETKIVILCNPSNPAGTLHSPEHLEKIAA-VLRKpqfrHVVVISDEIYE 432
Cdd:PLN02607 169 -IVPIHCDSSNNFQVTPQALEaayqEAEAANIRVRGVLITNPSNPLGATVQRSVLEDILDfVVRK----NIHLVSDEIYS 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2064415124 433 -------QLVYQDEGVSERVCKNFAmipgmyERTILINGFSKAYAMTGLRIG 477
Cdd:PLN02607 244 gsvfsasEFVSVAEIVEARGYKGVA------ERVHIVYSLSKDLGLPGFRVG 289
|
|
| pheA |
PRK10622 |
bifunctional chorismate mutase/prephenate dehydratase; Provisional |
6-205 |
1.52e-09 |
|
bifunctional chorismate mutase/prephenate dehydratase; Provisional
Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 60.13 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 6 STRVAyqesaeFAGAKEA----AAQMLSA--VDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKY 79
Cdd:PRK10622 103 SARIA------FLGPKGSyshlAARQYAArhFEQFIESGCAKFADIFNQVETGQADYAVLPIENTSSGAINDVYDLLQHT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 80 SLAVVGE-----------------------------------------------SESPAKTSGK---------------- 96
Cdd:PRK10622 177 SLSIVGEmtlpidhcvlvsgttdlstietvyshpqpfqqcsqflnryphwkieyTESTAAAMEKvaqansphvaalgsea 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 97 --------------------QTRFWLVAKTPAEPSLKAAAcKTSLAFAfaSGNAHGQLYRALGVFASRGLDLSKIESRP- 155
Cdd:PRK10622 257 ggalyglqvlernlanqqqnITRFIVLARKAINVSDQVPA-KTTLLMA--TGQQAGALVEALLVLRNHNLIMTKLESRPi 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2064415124 156 ----WSStdpsagkadfIFYVDVKARQSDTDVLEAIASLRSACSYVRVLGCYAS 205
Cdd:PRK10622 334 hgnpWEE----------MFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPS 377
|
|
| PRK09275 |
PRK09275 |
bifunctional aspartate transaminase/aspartate 4-decarboxylase; |
334-480 |
1.63e-09 |
|
bifunctional aspartate transaminase/aspartate 4-decarboxylase;
Pssm-ID: 236444 Cd Length: 527 Bit Score: 60.65 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 334 PGDKVILPSPYWGNYEGI--ITQVKAGLVPLHNSLEEDYLINPAELEKTLtaNPETKIVILCNPSNPAGTLHSPEHLEKI 411
Cdd:PRK09275 189 AGDKIALMTPIFTPYLEIpeLPRYDLEVVHINADEENEWQYPDSELEKLR--DPSIKALFLVNPSNPPSVAMSDESLEKI 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064415124 412 AAVLRK--PQfrhVVVISDEIYEQLVyqDEGVSErvcknFAMIPgmyERTILINGFSKAYAMTGLRIGYMA 480
Cdd:PRK09275 267 ADIVNEkrPD---LMIITDDVYGTFV--DDFRSL-----FAVLP---YNTILVYSFSKYFGATGWRLGVIA 324
|
|
| PRK09105 |
PRK09105 |
pyridoxal phosphate-dependent aminotransferase; |
264-482 |
4.61e-09 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181651 Cd Length: 370 Bit Score: 58.52 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 264 PPKSVLDAGVRALQNGqTKYcDMRGMAELRELITKYLhctkGVsydPATEIQICSGAQQALYNVILAICCPGDKVILPSP 343
Cdd:PRK09105 57 PSPAARDAAARSAALS-GRY-DLELEDDLRTLFAAQE----GL---PADHVMAYAGSSEPLNYAVLAFTSPTAGLVTADP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 344 ywgNYEGIITQVKAGLVPLHN-SLEEDYLInpaELEKTLTANPETKIVILCNPSNPAGTLHSPEHLEKIAAvlRKPqfRH 422
Cdd:PRK09105 128 ---TYEAGWRAADAQGAPVAKvPLRADGAH---DVKAMLAADPNAGLIYICNPNNPTGTVTPRADIEWLLA--NKP--AG 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064415124 423 VVVISDEIYEQlvYQDE-GVSERVCKNfamipgmyERTILINGFSKAYAMTGLRIGYMAGP 482
Cdd:PRK09105 198 SVLLVDEAYIH--FSDApSVVDLVAQR--------KDLIVLRTFSKLYGMAGMRLGLAAAR 248
|
|
| PLN02231 |
PLN02231 |
alanine transaminase |
283-609 |
2.48e-08 |
|
alanine transaminase
Pssm-ID: 177876 [Multi-domain] Cd Length: 534 Bit Score: 56.87 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 283 YCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSGAQQALYNVI-LAICCPGDKVILPSPYWGNYEGIITQVKAGLVP 361
Cdd:PLN02231 164 YSHSQGIKGLRDAIAAGIEARDGFPADP-NDIFLTDGASPAVHMMMqLLIRSEKDGILCPIPQYPLYSASIALHGGTLVP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 362 LHNSLEEDYLINPAELEKTLTANPETKI----VILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDEIYEQLVYQ 437
Cdd:PLN02231 243 YYLDEATGWGLEISELKKQLEDARSKGItvraLVVINPGNPTGQVLAEENQRDIVEFCKQ---EGLVLLADEVYQENVYV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 438 DEGVSERVcKNFAMIPGMYERTILINGF---SKA-YAMTGLRIGYM--AGPKHFIEACQLMQGQTTSCANSVGQVMAIEA 511
Cdd:PLN02231 320 PDKKFHSF-KKVARSMGYGEKDISLVSFqsvSKGyYGECGKRGGYMevTGFTSDVREQIYKVASVNLCSNISGQILASLV 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 512 MKLELASIEKGEVRIA-KD--LHELDLKRQYVVKRLREMPKMRFAYPTSSFYIFMDLALYFEGKTAYSPDKTEVlhnvDD 588
Cdd:PLN02231 399 MSPPKPGDESYESYMAeKDgiLSSLARRAKTLEDALNSLEGVTCNKAEGAMYLFPRIHLPQKAIKAAEAAKTAP----DA 474
|
330 340
....*....|....*....|..
gi 2064415124 589 F-CDYLIRTTGVAVGPGSDMGE 609
Cdd:PLN02231 475 FyCKRLLNATGIVVVPGSGFGQ 496
|
|
| PRK06855 |
PRK06855 |
pyridoxal phosphate-dependent aminotransferase; |
275-479 |
2.27e-07 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180734 Cd Length: 433 Bit Score: 53.42 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 275 ALQNGQTKYCDMRGMAELRELITKYLHCTKGVSYDPaTEIQICSGAQQALYNVILAICcPGDKVILPSPYWGNY---EGi 351
Cdd:PRK06855 61 VMDDKSYGYCPTKGVLETREFLAELNNKRGGAQITP-DDIIFFNGLGDAIAKIYGLLR-REARVIGPSPAYSTHssaEA- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 352 itqVKAGLVPLHNSLEEDYLINP--AELEKTLTANPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVVISDE 429
Cdd:PRK06855 138 ---AHAGYPPVTYRLDPENNWYPdlDDLENKVKYNPSIAGILLINPDNPTGAVYPKEILREIVDIARE---YDLFIICDE 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2064415124 430 IYEQLVYQDEGvSERVCKNFAMIPGMYERtilinGFSKAYAMTGLRIGYM 479
Cdd:PRK06855 212 IYNNIVYNGKK-TVPLSEVIGDVPGIALK-----GISKELPWPGSRCGWI 255
|
|
| PBP2_PDT_like |
cd13532 |
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ... |
22-86 |
5.54e-07 |
|
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270250 [Multi-domain] Cd Length: 184 Bit Score: 50.22 E-value: 5.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064415124 22 EAAAQMLSAvDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYS-LAVVGE 86
Cdd:cd13532 15 HQAALQLFG-DSVELLPLPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLRDRPdVKIVGE 79
|
|
| PRK11899 |
PRK11899 |
prephenate dehydratase; Provisional |
8-203 |
1.31e-06 |
|
prephenate dehydratase; Provisional
Pssm-ID: 237014 [Multi-domain] Cd Length: 279 Bit Score: 50.27 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 8 RVAYQeSAEFAGAKEAAAQMLSavdGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYSLAVVGE- 86
Cdd:PRK11899 6 RIAFQ-GEPGANSHLACRDAFP---DMEPLPCATFEDAFEAVESGEADLAMIPIENSLAGRVADIHHLLPESGLHIVGEy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 87 --------------------------------------------------------SESPAKT----------------- 93
Cdd:PRK11899 82 flpirhqlmalpgatleeiktvhshphalgqcrkiiralglkpvvaadtagaarlvAERGDPSmaalasrlaaelygldi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 94 --------SGKQTRFWLVAKTPAEPSLKAAACKTSlaFAFASGNAHGQLYRALGVFASRGLDLSKIESR----PWSSTDp 161
Cdd:PRK11899 162 laeniedaDHNTTRFVVLSREADWAARGDGPIVTT--FVFRVRNIPAALYKALGGFATNGVNMTKLESYmvggSFTATQ- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2064415124 162 sagkadfiFYVDVKARQSDTDVLEAIASLRSACSYVRVLGCY 203
Cdd:PRK11899 239 --------FYADIEGHPEDRNVALALEELRFFSEEVRILGVY 272
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
316-413 |
4.07e-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: 47.38 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 316 ICSGAQQALYNVILAICCPGDKVILPSP-YWGNYEGIITQVKAGLVPLHNSLEEDYLINPAELEKTLTAnPETKIVILCN 394
Cdd:cd01494 22 FVPSGTGANEAALLALLGPGDEVIVDANgHGSRYWVAAELAGAKPVPVPVDDAGYGGLDVAILEELKAK-PNVALIVITP 100
|
90
....*....|....*....
gi 2064415124 395 PSNPAGTLHSPEHLEKIAA 413
Cdd:cd01494 101 NTTSGGVLVPLKEIRKIAK 119
|
|
| PBP2_Sa-PDT_like |
cd13633 |
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, ... |
22-86 |
7.32e-06 |
|
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, subgroup 4; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.
Pssm-ID: 270351 [Multi-domain] Cd Length: 184 Bit Score: 46.73 E-value: 7.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064415124 22 EAAAQMLSAVDGFEAASYASFEDAALAVKKQDVNFAVLPVETSTCGSCYETYDLLLKYS-LAVVGE 86
Cdd:cd13633 15 EEAALALFGGEEAELVPYPTIPDVIEAVAEGEVDYGVVPIENSIEGSVNLTLDLLAHEVdLPIQGE 80
|
|
| ACT_AAAH |
cd04904 |
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ... |
125-200 |
1.62e-05 |
|
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe; TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines; and TPH catalyses the hydroxylation of L-Trp to 5-hydroxytryptophan, the rate limiting step in the biosynthesis of 5-hydroxytryptamine (serotonin) and the first reaction in the synthesis of melatonin. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains (this CD) and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes are regulated in part by the phosphorylation of serine residues N-terminal of the ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153176 [Multi-domain] Cd Length: 74 Bit Score: 43.32 E-value: 1.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064415124 125 FASGNAHGQLYRALGVFASRGLDLSKIESRPwsstdPSAGKADFIFYVDVKARQSDTDvlEAIASLRSACSYVRVL 200
Cdd:cd04904 5 FSLKEEVGALARALKLFEEFGVNLTHIESRP-----SRRNGSEYEFFVDCEVDRGDLD--QLISSLRRVVADVNIL 73
|
|
| avtA |
PRK09440 |
valine--pyruvate transaminase; Provisional |
287-552 |
2.51e-05 |
|
valine--pyruvate transaminase; Provisional
Pssm-ID: 236517 Cd Length: 416 Bit Score: 47.16 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 287 RGMAELRELITKYLHCTKGVSYDPAtEIQICSGAQQALYNVILAICCPGD-----KVILP-SP-YWGnYEGIitqvkagl 359
Cdd:PRK09440 74 QGKDELIEALAALLNERYGWNISPQ-NIALTNGSQSAFFYLFNLFAGRRAdgslkKILFPlAPeYIG-YADA-------- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 360 vplhnSLEEDYLI-NPAELEK-------------TLTANPETKIVILCNPSNPAGTLHSPEHLEKIAAVLRKpqfRHVVV 425
Cdd:PRK09440 144 -----GLEEDLFVsYRPNIELlpegqfkyhvdfeHLHIDEDTGAICVSRPTNPTGNVLTDEELEKLDALARQ---HNIPL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 426 ISDEIY----EQLVYQDegvservcknfaMIPGMYERTILINGFSKAyAMTGLRIGYMAGPKHFIEACQLMQGQTTSCAN 501
Cdd:PRK09440 216 LIDNAYgppfPGIIFSE------------ATPLWNPNIILCMSLSKL-GLPGVRCGIVIADEEIIEALSNMNGIISLAPG 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2064415124 502 SVGQVMAIEAmklelasIEKGEVriaKDLHELDL------KRQYVVKRLRE-MPKMRF 552
Cdd:PRK09440 283 RLGPAIAAEM-------IESGDL---LRLSETVIrpfyrqKVQLAIALLRRyLPDEPC 330
|
|
| ACT_TH |
cd04930 |
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine ... |
102-200 |
1.40e-04 |
|
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH); ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH). TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines (dopamine, noradrenaline and adrenaline), functioning as hormones and neurotransmitters. The enzyme is not regulated by its amino acid substrate, but instead by phosphorylation at several serine residues located N-terminal of the ACT domain, and by feedback inhibition by catecholamines at the active site. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153202 [Multi-domain] Cd Length: 115 Bit Score: 41.61 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 102 LVAKTPAEPSlKAAACKTSLAFAFASGNAHGQLYRALGVFASRGLDLSKIESRPwsstdPSAGKADFIFYVDVKARQSDT 181
Cdd:cd04930 24 DLDSEVFEEK-EGKAVPQKATLLFSLKEGFSSLSRILKVFETFEAKIHHLESRP-----SRKEGGDLEVLVRCEVHRSDL 97
|
90
....*....|....*....
gi 2064415124 182 DVLeaIASLRSACSYVRVL 200
Cdd:cd04930 98 LQL--ISSLRQVAEDVRLT 114
|
|
| PLN02672 |
PLN02672 |
methionine S-methyltransferase |
296-480 |
7.29e-04 |
|
methionine S-methyltransferase
Pssm-ID: 215360 [Multi-domain] Cd Length: 1082 Bit Score: 42.84 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 296 ITKYLHCTKGVSYDPATEIqICSGAQQALYNViLAICCPGDK--VILPSPYWGNYEGIITQVKAGLVPLHNSLEEDYLIN 373
Cdd:PLN02672 739 ILQFIKSNYGFPTDSCTEF-VYGDTSLALFNK-LVLCCVQEGgtLCFPAGSNGTYVSAAKFLKANFRRIPTKSSDGFKLT 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 374 PAELEKTLTaNPETKIVILCNPS-NPAGTLHSPEHLEKIAAVLRKPQFRhvvVISDEIYEQLVYQDEGVSERVCKNFamI 452
Cdd:PLN02672 817 AKTLASTLE-TVKKPWVYISGPTiNPTGLLYSNSEIEEILSVCAKYGAR---VIIDTSFSGLEYDTSGWGGWDLKSI--L 890
|
170 180 190
....*....|....*....|....*....|...
gi 2064415124 453 PGMYERT-----ILINGFSKAYAMTGLRIGYMA 480
Cdd:PLN02672 891 SRLKSSNpsfavALLGGLSTELLSGGHEFGFLA 923
|
|
| PRK07908 |
PRK07908 |
threonine-phosphate decarboxylase; |
366-481 |
2.15e-03 |
|
threonine-phosphate decarboxylase;
Pssm-ID: 236128 Cd Length: 349 Bit Score: 40.76 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 366 LEEDYLINPAELektltanPE-TKIVILCNPSNPAGTLHSPEHLekiaAVLRKPQfRHVVVisDEiyeqlVYQDEGVSER 444
Cdd:PRK07908 125 LDPPFRLDPAAV-------PDdADLVVIGNPTNPTSVLHPAEQL----LALRRPG-RILVV--DE-----AFADAVPGEP 185
|
90 100 110
....*....|....*....|....*....|....*..
gi 2064415124 445 vcknFAMIPGMYERTILINGFSKAYAMTGLRIGYMAG 481
Cdd:PRK07908 186 ----ESLAGDDLPGVLVLRSLTKTWSLAGLRVGYALG 218
|
|
| PRK02610 |
PRK02610 |
histidinol-phosphate transaminase; |
291-481 |
2.49e-03 |
|
histidinol-phosphate transaminase;
Pssm-ID: 235053 Cd Length: 374 Bit Score: 40.47 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 291 ELRELITKYLHCTKGVSYDPATE-IQICSGAQQALYNVILAICCPGDKVIL-PSPYWGNYeGIITQVKAglVPLHN--SL 366
Cdd:PRK02610 70 ALKQAIAEYVNESAAGSSQITPAnISVGNGSDELIRSLLIATCLGGEGSILvAEPTFSMY-GILAQTLG--IPVVRvgRD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064415124 367 EEDYLINPAELEKTL--TANPETKIVILCNPSNPAGTLHSPEHLEKIAAVlrkPQfrHVVVISDEIYEQLvyqdegvser 444
Cdd:PRK02610 147 PETFEIDLAAAQSAIeqTQNPPVRVVFVVHPNSPTGNPLTAAELEWLRSL---PE--DILVVIDEAYFEF---------- 211
|
170 180 190
....*....|....*....|....*....|....*....
gi 2064415124 445 vcKNFAMIPGMYERT--ILINGFSKAYAMTGLRIGYMAG 481
Cdd:PRK02610 212 --SQTTLVGELAQHPnwVILRTFSKAFRLAAHRVGYAIG 248
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
129-191 |
3.76e-03 |
|
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5
Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 36.13 E-value: 3.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064415124 129 NAHGQLYRALGVFASRGLDLSKIESRpwsstdPSAGKADFIFYVDVKARQSDTDVLEAIASLR 191
Cdd:pfam01842 9 DRPGLLARVLGALADRGINITSIEQG------TSEDKGGIVFVVIVVDEEDLEEVLEALKKLE 65
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
129-187 |
5.57e-03 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 35.73 E-value: 5.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2064415124 129 NAHGQLYRALGVFASRGLDLSKIESRpwsstdPSAGKADFIFYVDVKARQSDTDVLEAI 187
Cdd:cd02116 7 DRPGLLAKVLSVLAEAGINITSIEQR------TSGDGGEADIFIVVDGDGDLEKLLEAL 59
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