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Conserved domains on  [gi|1805513901|ref|WP_162129955|]
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MULTISPECIES: aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [Pantoea]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15481 super family cl28326
transcriptional regulatory protein PtsJ; Provisional
 66-489 0e+00

transcriptional regulatory protein PtsJ; Provisional


The actual alignment was detected with superfamily member PRK15481:

Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 552.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  66 TASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQAEDVPEQEGPARQT 145
Cdd:PRK15481    6 TANEIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 146 HLIDVSGGNPEPSALPDVASLLQAVSLTPRSYGGSVINPGLEKAGREWFCPDAPGMFGLGLTHGAVDAIERLITGYLTAG 225
Cdd:PRK15481   86 PLHDLAGGNPDPQRLPDLSRYFARLSRTPRLYGDAPVSPELHAWAARWLRDDCPVAFEIDLTSGAIDAIERLLCAHLLPG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 226 EKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEAGAQVVIVTPRAHNPTGCSLNPQRASEIRAVLARFP 305
Cdd:PRK15481  166 DSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGARAVILTPRAHNPTGCSLSARRAAALRNLLARYP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 306 HVMVIVDDHFSLLSGSEYQNVIAAETRNWAIVRSVSKFFGPDLRLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEA 385
Cdd:PRK15481  246 QVLVIIDDHFALLSSSPYHSVIPQTTQRWALIRSVSKALGPDLRLAFVASDSATSARLRLRLNSGTQWVSHLLQDLVYAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 386 LASADVVRKVSEAATLYRDRRNALLAALRTRNVMALQEYDGLNVWLPLCHEPSGLIRLMEARGWLIRAGAGFYLTDPGHA 465
Cdd:PRK15481  326 LTDPEYQARLAQARLFYAQRRQKLARALQQYGIAIPSPGDGLNLWLPLDTDSQATALTLAKSGWLVREGEAFGVSAPSHG 405

                         410       420
                  ....*....|....*....|....
gi 1805513901 466 IRLTPGVLSDEQCDALAQDLTDAL 489
Cdd:PRK15481  406 LRITLSTLNDAEINRLAADLHQAL 429
 
Name Accession Description Interval E-value
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 66-489 0e+00

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 552.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  66 TASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQAEDVPEQEGPARQT 145
Cdd:PRK15481    6 TANEIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 146 HLIDVSGGNPEPSALPDVASLLQAVSLTPRSYGGSVINPGLEKAGREWFCPDAPGMFGLGLTHGAVDAIERLITGYLTAG 225
Cdd:PRK15481   86 PLHDLAGGNPDPQRLPDLSRYFARLSRTPRLYGDAPVSPELHAWAARWLRDDCPVAFEIDLTSGAIDAIERLLCAHLLPG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 226 EKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEAGAQVVIVTPRAHNPTGCSLNPQRASEIRAVLARFP 305
Cdd:PRK15481  166 DSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGARAVILTPRAHNPTGCSLSARRAAALRNLLARYP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 306 HVMVIVDDHFSLLSGSEYQNVIAAETRNWAIVRSVSKFFGPDLRLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEA 385
Cdd:PRK15481  246 QVLVIIDDHFALLSSSPYHSVIPQTTQRWALIRSVSKALGPDLRLAFVASDSATSARLRLRLNSGTQWVSHLLQDLVYAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 386 LASADVVRKVSEAATLYRDRRNALLAALRTRNVMALQEYDGLNVWLPLCHEPSGLIRLMEARGWLIRAGAGFYLTDPGHA 465
Cdd:PRK15481  326 LTDPEYQARLAQARLFYAQRRQKLARALQQYGIAIPSPGDGLNLWLPLDTDSQATALTLAKSGWLVREGEAFGVSAPSHG 405

                         410       420
                  ....*....|....*....|....
gi 1805513901 466 IRLTPGVLSDEQCDALAQDLTDAL 489
Cdd:PRK15481  406 LRITLSTLNDAEINRLAADLHQAL 429
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 70-491 1.42e-60

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: 205.83  E-value: 1.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  70 IFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGT--------------TISQAEDV 135
Cdd:COG1167    17 LADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTfvaarlpapapaprAAAAVAAP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 136 PEQEGPARQTHLIDVSGGNPEPSALP--DVASLLQAVSLTPR----SYGGSVINPGLEKAGREWfcpdapgMFGLGL--- 206
Cdd:COG1167    97 ALRRLLEAAPGVIDLGSGAPDPDLFPlaALRRALRRALRRLPpallGYGDPQGLPELREAIARY-------LARRGVpas 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 207 ------THGAVDAIERLITGYLTAGEKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEA-GAQVVIVTP 279
Cdd:COG1167   170 pdqiliTSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRhRPRAVYVTP 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 280 RAHNPTGCSLNPQRASEIRAVLARFpHVMVIVDDHFSLLSGSE-----------YQNVIAaetrnwaiVRSVSKFFGPDL 348
Cdd:COG1167   250 SHQNPTGATMSLERRRALLELARRH-GVPIIEDDYDSELRYDGrpppplaaldaPGRVIY--------IGSFSKTLAPGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 349 RLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEALASADVVRKVSEAATLYRDRRNALLAALRTR---NVMALQEYD 425
Cdd:COG1167   321 RLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHlpdGLRVTGPPG 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805513901 426 GLNVWLPLchePSG-----LIRLMEARGWLIRAGAGFYLTD-PGHAIRLTPGVLSDEQCDALAQDLTDALRE 491
Cdd:COG1167   401 GLHLWLEL---PEGvdaeaLAAAALARGILVAPGSAFSADGpPRNGLRLGFGAPSEEELEEALRRLAELLRE 469
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 148-469 2.23e-34

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: 132.47  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 148 IDVSGGNPEPSALPDVASLLQAVSLTPRS--YGGSVINPGLEKAGREWFcpdaPGMFGLG-------LTHGAVDAIERLI 218
Cdd:cd00609     1 IDLSIGEPDFPPPPEVLEALAAAALRAGLlgYYPDPGLPELREAIAEWL----GRRGGVDvppeeivVTNGAQEALSLLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 219 TGYLTAGEKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEA---GAQVVIVTPrAHNPTGCSLNPQRAS 295
Cdd:cd00609    77 RALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAktpKTKLLYLNN-PNNPTGAVLSEEELE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 296 EIrAVLARFPHVMVIVDDHFSLLSGSEYQNVIAA---ETRNWAIVRSVSKFFG-PDLRLALVACNPDTSERLSRRMASGT 371
Cdd:cd00609   156 EL-AELAKKHGILIISDEAYAELVYDGEPPPALAlldAYERVIVLRSFSKTFGlPGLRIGYLIAPPEELLERLKKLLPYT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 372 HW-VSHILQDMTEEALASADvvRKVSEAATLYRDRRNALLAALRTRNVMALQEYDG-LNVW--LPLCHEPSGLIRLMEAR 447
Cdd:cd00609   235 TSgPSTLSQAAAAAALDDGE--EHLEELRERYRRRRDALLEALKELGPLVVVKPSGgFFLWldLPEGDDEEFLERLLLEA 312

                         330       340
                  ....*....|....*....|..
gi 1805513901 448 GWLIRAGAGFYLTDPGHaIRLT 469
Cdd:cd00609   313 GVVVRPGSAFGEGGEGF-VRLS 333
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
145-483 1.25e-14

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 75.03  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 145 THLIDVSGGNPEPSALPDVASLLQAVSLTP--RSYGGSVINPGLEKA-----GREWFCPDAPGMfGLGLTHGAVDAIERL 217
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKDALAGGtrNLYGPTDGHPELREAlakflGRSPVLKLDREA-AVVFGSGAGANIEAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 218 ITGYLTAGEKIAVEEPCFLSSINAIRSLG--------YVPAGVPVDRDGLLpgplqETLEAGAQVVIVTpRAHNPTGCSL 289
Cdd:pfam00155  80 IFLLANPGDAILVPAPTYASYIRIARLAGgevvryplYDSNDFHLDFDALE-----AALKEKPKVVLHT-SPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 290 NPQrasEIRAVLARFP--HVMVIVDD---HFSLLSGSEYQNVIAAETR-NWAIVRSVSKFFG-PDLRLALVACNPDTSER 362
Cdd:pfam00155 154 TLE---ELEKLLDLAKehNILLLVDEayaGFVFGSPDAVATRALLAEGpNLLVVGSFSKAFGlAGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 363 LsRRMASGThWVSHILQDMTEEAL-ASADVVRKVSEAATLYRDRRNALLAALRTRNVMALQEYDGLNVWLPLCHE--PSG 439
Cdd:pfam00155 231 L-RKLARPF-YSSTHLQAAAAAALsDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPEtaKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1805513901 440 LIRLMEARGWLIRAGAGFYLtdPGHaIRLTPGVLSDEQCDALAQ 483
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGV--PGW-LRITVAGGTEEELEELLE 349
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
70-129 1.49e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 62.21  E-value: 1.49e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901   70 IFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTI 129
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
 
Name Accession Description Interval E-value
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 66-489 0e+00

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 552.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  66 TASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQAEDVPEQEGPARQT 145
Cdd:PRK15481    6 TANEIFDSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 146 HLIDVSGGNPEPSALPDVASLLQAVSLTPRSYGGSVINPGLEKAGREWFCPDAPGMFGLGLTHGAVDAIERLITGYLTAG 225
Cdd:PRK15481   86 PLHDLAGGNPDPQRLPDLSRYFARLSRTPRLYGDAPVSPELHAWAARWLRDDCPVAFEIDLTSGAIDAIERLLCAHLLPG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 226 EKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEAGAQVVIVTPRAHNPTGCSLNPQRASEIRAVLARFP 305
Cdd:PRK15481  166 DSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGARAVILTPRAHNPTGCSLSARRAAALRNLLARYP 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 306 HVMVIVDDHFSLLSGSEYQNVIAAETRNWAIVRSVSKFFGPDLRLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEA 385
Cdd:PRK15481  246 QVLVIIDDHFALLSSSPYHSVIPQTTQRWALIRSVSKALGPDLRLAFVASDSATSARLRLRLNSGTQWVSHLLQDLVYAC 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 386 LASADVVRKVSEAATLYRDRRNALLAALRTRNVMALQEYDGLNVWLPLCHEPSGLIRLMEARGWLIRAGAGFYLTDPGHA 465
Cdd:PRK15481  326 LTDPEYQARLAQARLFYAQRRQKLARALQQYGIAIPSPGDGLNLWLPLDTDSQATALTLAKSGWLVREGEAFGVSAPSHG 405

                         410       420
                  ....*....|....*....|....
gi 1805513901 466 IRLTPGVLSDEQCDALAQDLTDAL 489
Cdd:PRK15481  406 LRITLSTLNDAEINRLAADLHQAL 429
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 70-491 1.42e-60

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: 205.83  E-value: 1.42e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  70 IFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGT--------------TISQAEDV 135
Cdd:COG1167    17 LADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTfvaarlpapapaprAAAAVAAP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 136 PEQEGPARQTHLIDVSGGNPEPSALP--DVASLLQAVSLTPR----SYGGSVINPGLEKAGREWfcpdapgMFGLGL--- 206
Cdd:COG1167    97 ALRRLLEAAPGVIDLGSGAPDPDLFPlaALRRALRRALRRLPpallGYGDPQGLPELREAIARY-------LARRGVpas 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 207 ------THGAVDAIERLITGYLTAGEKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEA-GAQVVIVTP 279
Cdd:COG1167   170 pdqiliTSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRhRPRAVYVTP 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 280 RAHNPTGCSLNPQRASEIRAVLARFpHVMVIVDDHFSLLSGSE-----------YQNVIAaetrnwaiVRSVSKFFGPDL 348
Cdd:COG1167   250 SHQNPTGATMSLERRRALLELARRH-GVPIIEDDYDSELRYDGrpppplaaldaPGRVIY--------IGSFSKTLAPGL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 349 RLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEALASADVVRKVSEAATLYRDRRNALLAALRTR---NVMALQEYD 425
Cdd:COG1167   321 RLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHlpdGLRVTGPPG 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805513901 426 GLNVWLPLchePSG-----LIRLMEARGWLIRAGAGFYLTD-PGHAIRLTPGVLSDEQCDALAQDLTDALRE 491
Cdd:COG1167   401 GLHLWLEL---PEGvdaeaLAAAALARGILVAPGSAFSADGpPRNGLRLGFGAPSEEELEEALRRLAELLRE 469
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 148-469 2.23e-34

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: 132.47  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 148 IDVSGGNPEPSALPDVASLLQAVSLTPRS--YGGSVINPGLEKAGREWFcpdaPGMFGLG-------LTHGAVDAIERLI 218
Cdd:cd00609     1 IDLSIGEPDFPPPPEVLEALAAAALRAGLlgYYPDPGLPELREAIAEWL----GRRGGVDvppeeivVTNGAQEALSLLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 219 TGYLTAGEKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPGPLQETLEA---GAQVVIVTPrAHNPTGCSLNPQRAS 295
Cdd:cd00609    77 RALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAktpKTKLLYLNN-PNNPTGAVLSEEELE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 296 EIrAVLARFPHVMVIVDDHFSLLSGSEYQNVIAA---ETRNWAIVRSVSKFFG-PDLRLALVACNPDTSERLSRRMASGT 371
Cdd:cd00609   156 EL-AELAKKHGILIISDEAYAELVYDGEPPPALAlldAYERVIVLRSFSKTFGlPGLRIGYLIAPPEELLERLKKLLPYT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 372 HW-VSHILQDMTEEALASADvvRKVSEAATLYRDRRNALLAALRTRNVMALQEYDG-LNVW--LPLCHEPSGLIRLMEAR 447
Cdd:cd00609   235 TSgPSTLSQAAAAAALDDGE--EHLEELRERYRRRRDALLEALKELGPLVVVKPSGgFFLWldLPEGDDEEFLERLLLEA 312

                         330       340
                  ....*....|....*....|..
gi 1805513901 448 GWLIRAGAGFYLTDPGHaIRLT 469
Cdd:cd00609   313 GVVVRPGSAFGEGGEGF-VRLS 333
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 206-491 1.99e-22

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: 98.28  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 206 LTHGAVDAIERLITGYLTAGEKIAVEEPCFLSSINAIRSLGYVPAGVPVDRDGLLPgpLQETLEAGAQ----VVIVTPra 281
Cdd:COG0079    70 VGNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPLDEDFSLD--LDALLAAITErtdlVFLCNP-- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 282 HNPTGCSLNPqraSEIRAVLARFP-HVMVIVD--------DHFSLLSgseyqnvIAAETRNWAIVRSVSKFFG-PDLRLA 351
Cdd:COG0079   146 NNPTGTLLPR---EELEALLEALPaDGLVVVDeayaefvpEEDSALP-------LLARYPNLVVLRTFSKAYGlAGLRLG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 352 LVACNPDTSERLSRRMasgTHW-VSHILQDMTEEALASADVVRkvsEAATLYRDRRNALLAALRTrnvMALQEYDG-LN- 428
Cdd:COG0079   216 YAIASPELIAALRRVR---GPWnVNSLAQAAALAALEDRAYLE---ETRARLRAERERLAAALRA---LGLTVYPSqANf 286

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805513901 429 VWLPLCHEPSGLIRLMEARGWLIRAGAGFYLtdpGHAIRLTPGvlSDEQCDALAQdltdALRE 491
Cdd:COG0079   287 VLVRVPEDAAELFEALLERGILVRDFSSFGL---PDYLRITVG--TPEENDRLLA----ALKE 340
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
70-149 2.07e-16

DNA-binding transcriptional regulator YhcF, GntR family [Transcription];


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 75.22  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901  70 IFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTIsqAEDVPEQEGPARQTHLID 149
Cdd:COG1725    15 IADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFV--AEDARELLEERREEFLEE 92
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
145-483 1.25e-14

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 75.03  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 145 THLIDVSGGNPEPSALPDVASLLQAVSLTP--RSYGGSVINPGLEKA-----GREWFCPDAPGMfGLGLTHGAVDAIERL 217
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKDALAGGtrNLYGPTDGHPELREAlakflGRSPVLKLDREA-AVVFGSGAGANIEAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 218 ITGYLTAGEKIAVEEPCFLSSINAIRSLG--------YVPAGVPVDRDGLLpgplqETLEAGAQVVIVTpRAHNPTGCSL 289
Cdd:pfam00155  80 IFLLANPGDAILVPAPTYASYIRIARLAGgevvryplYDSNDFHLDFDALE-----AALKEKPKVVLHT-SPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 290 NPQrasEIRAVLARFP--HVMVIVDD---HFSLLSGSEYQNVIAAETR-NWAIVRSVSKFFG-PDLRLALVACNPDTSER 362
Cdd:pfam00155 154 TLE---ELEKLLDLAKehNILLLVDEayaGFVFGSPDAVATRALLAEGpNLLVVGSFSKAFGlAGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 363 LsRRMASGThWVSHILQDMTEEAL-ASADVVRKVSEAATLYRDRRNALLAALRTRNVMALQEYDGLNVWLPLCHE--PSG 439
Cdd:pfam00155 231 L-RKLARPF-YSSTHLQAAAAAALsDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPEtaKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1805513901 440 LIRLMEARGWLIRAGAGFYLtdPGHaIRLTPGVLSDEQCDALAQ 483
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGV--PGW-LRITVAGGTEEELEELLE 349
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 69-130 1.04e-13

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 65.93  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805513901  69 EIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTIS 130
Cdd:cd07377     5 QIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
70-129 1.49e-12

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 62.21  E-value: 1.49e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901   70 IFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTI 129
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 66-129 2.34e-12

Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 61.86  E-value: 2.34e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1805513901  66 TASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTI 129
Cdd:pfam00392   1 LYEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
56-134 6.26e-08

DNA-binding transcriptional regulator, FadR family [Transcription];


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 53.40  E-value: 6.26e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1805513901  56 RPVEAGTekmTASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQAED 134
Cdd:COG2186     1 KPIRRRS---LAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSP 76
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
 64-138 8.98e-07

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 50.15  E-value: 8.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1805513901  64 KMTASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTI-SQAEDVPEQ 138
Cdd:PRK10421    1 RRLSDEVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIrWRHETWSEQ 76
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
69-131 2.44e-06

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 48.70  E-value: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1805513901  69 EIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQ 131
Cdd:COG2188     9 QIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAE 71
PRK09764 PRK09764
GntR family transcriptional regulator;
69-118 7.20e-05

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 44.43  E-value: 7.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1805513901  69 EIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGI 118
Cdd:PRK09764    9 QIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQI 58
PRK03837 PRK03837
transcriptional regulator NanR; Provisional
 53-123 1.19e-03

transcriptional regulator NanR; Provisional


Pssm-ID: 235166 [Multi-domain]  Cd Length: 241  Bit Score: 40.39  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1805513901  53 QIRRPVEagtEKMTASEIFESVRQKVRTGQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAG-IAVTNG 123
Cdd:PRK03837    4 LRSRPIA---RKKLSEEVEERLEQMIRSGEFGPGDQLPSERELMAFFGVGRPAVREALQALKRKGlVQISHG 72
PRK06107 PRK06107
aspartate transaminase;
266-413 1.51e-03

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 40.87  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 266 ETLEAGaqvviVTPRAH--------NPTGCSLNPQRASEIRAVLARFPHVMVIVDD-----HFSLLSGSEYQNVIAAETR 332
Cdd:PRK06107  157 EALEAA-----ITPRTRwlilnapsNPTGAVYSRAELRALADVLLRHPHVLVLTDDiydhiRFDDEPTPHLLAAAPELRD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805513901 333 NWAIVRSVSKFFG-PDLRLALVACNPDTSERLSRRMASGTHWVSHILQDMTEEALASADvvRKVSEAATLYRDRRNALLA 411
Cdd:PRK06107  232 RVLVTNGVSKTYAmTGWRIGYAAGPADLIAAINKLQSQSSSCPSSISQAAAAAALNGDQ--SFVTESVAVYKQRRDYALA 309


                  ..
gi 1805513901 412 AL 413
Cdd:PRK06107  310 LL 311
pdhR PRK09464
pyruvate dehydrogenase complex transcriptional repressor PdhR;
81-118 5.05e-03

pyruvate dehydrogenase complex transcriptional repressor PdhR;


Pssm-ID: 181879 [Multi-domain]  Cd Length: 254  Bit Score: 38.85  E-value: 5.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1805513901  81 GQLHPGDALPPVREMAAQLSVHRNTVASAYKKLAAAGI 118
Cdd:PRK09464   26 GTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGL 63
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
67-131 9.84e-03

DNA-binding transcriptional regulator, GntR family [Transcription];


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 37.59  E-value: 9.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1805513901  67 ASEIFESVRQKVRTGQLHPGDALpPVREMAAQLSVHRNTVASAYKKLAAAGIAVTNGRYGTTISQ 131
Cdd:COG1802    13 AEQVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAP 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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