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Conserved domains on  [gi|1093454868|ref|WP_070832942|]
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MULTISPECIES: PLP-dependent aminotransferase family protein [Corynebacterium]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 11439382)

pyridoxal phosphate (PLP)-dependent aminotransferase family protein may catalyze the reversible exchange of an amino group from one molecule with a keto group from another molecule

CATH:  3.40.640.10
Gene Ontology:  GO:0030170
PubMed:  17109392
SCOP:  4000670

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-451 2.68e-108

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: 328.71  E-value: 2.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868   9 LVGELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGLVEVrvgvgvfvrhRQQ--------LPRADFS 78
Cdd:COG1167    17 LADALREAILSGrlPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIES----------RPGsgtfvaarLPAPAPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  79 WQVGALGPQPNTGRVLAatqraSTDEAISLHSGYPDESLLPTNLVRRALTRVSKSHDAY--RRAPVRGMAELRQWFASQL 156
Cdd:COG1167    87 PRAAAAVAAPALRRLLE-----AAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPAllGYGDPQGLPELREAIARYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 157 ----VRANERDVVIVPGTQSGLGAIFRA-ISPKELI-IESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRTSS 230
Cdd:COG1167   162 arrgVPASPDQILITSGAQQALDLALRAlLRPGDTVaVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 231 ARAFYGQPTFGNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFD-APDVPIAADDAEGHVIYLRSLTKVISPAVR 309
Cdd:COG1167   242 PRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDgRPPPPLAALDAPGRVIYIGSFSKTLAPGLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 310 VGAVIAKGPVLQRILAEVSAEALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSRYAPSVETPHVPQGG 389
Cdd:COG1167   322 LGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGLRVTGPPGG 401
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 390 LNLWCRLPDGTDPQEVAERCEGRGLIVAPGRDWFPSEEIGPYLRLNFAGPHPERFVDAAMIL 451
Cdd:COG1167   402 LHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRL 463
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-451 2.68e-108

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: 328.71  E-value: 2.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868   9 LVGELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGLVEVrvgvgvfvrhRQQ--------LPRADFS 78
Cdd:COG1167    17 LADALREAILSGrlPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIES----------RPGsgtfvaarLPAPAPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  79 WQVGALGPQPNTGRVLAatqraSTDEAISLHSGYPDESLLPTNLVRRALTRVSKSHDAY--RRAPVRGMAELRQWFASQL 156
Cdd:COG1167    87 PRAAAAVAAPALRRLLE-----AAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPAllGYGDPQGLPELREAIARYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 157 ----VRANERDVVIVPGTQSGLGAIFRA-ISPKELI-IESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRTSS 230
Cdd:COG1167   162 arrgVPASPDQILITSGAQQALDLALRAlLRPGDTVaVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 231 ARAFYGQPTFGNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFD-APDVPIAADDAEGHVIYLRSLTKVISPAVR 309
Cdd:COG1167   242 PRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDgRPPPPLAALDAPGRVIYIGSFSKTLAPGLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 310 VGAVIAKGPVLQRILAEVSAEALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSRYAPSVETPHVPQGG 389
Cdd:COG1167   322 LGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGLRVTGPPGG 401
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 390 LNLWCRLPDGTDPQEVAERCEGRGLIVAPGRDWFPSEEIGPYLRLNFAGPHPERFVDAAMIL 451
Cdd:COG1167   402 LHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRL 463
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
106-442 9.11e-58

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: 194.10  E-value: 9.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 106 ISLHSGYPDESLLPtnLVRRALTRVSKSHDAYRRAPVRGMAELRQWFASQL-----VRANERDVVIVPGTQSGLGAIFRA 180
Cdd:cd00609     1 IDLSIGEPDFPPPP--EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLgrrggVDVPPEEIVVTNGAQEALSLLLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 181 ISPK--ELIIESPSYWGAILAARQAGISLLPVESDDEGPIPES--LERLLRTSSARAFYgqptFGNPH---GKRWSTARR 253
Cdd:cd00609    79 LLNPgdEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDleLLEAAKTPKTKLLY----LNNPNnptGAVLSEEEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 254 KTIIEIIRAFNAFLIEDDwAH-DFAFD-APDVPIAADDAEGHVIYLRSLTKVIS-PAVRVGAVIA-KGPVLQRILAEVSA 329
Cdd:cd00609   155 EELAELAKKHGILIISDE-AYaELVYDgEPPPALALLDAYERVIVLRSFSKTFGlPGLRIGYLIApPEELLERLKKLLPY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 330 EALYTSGILQAVALDVVKQsaYATHLKNMQVALRQRRNDLLEALSRYAPsvETPHVPQGGLNLWCRLPDGTDPQEVAERC 409
Cdd:cd00609   234 TTSGPSTLSQAAAAAALDD--GEEHLEELRERYRRRRDALLEALKELGP--LVVVKPSGGFFLWLDLPEGDDEEFLERLL 309
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1093454868 410 EGRGLIVAPGRDWFPSEEigPYLRLNFAGPHPE 442
Cdd:cd00609   310 LEAGVVVRPGSAFGEGGE--GFVRLSFATPEEE 340
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
21-420 1.85e-20

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 93.19  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  21 KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGLVEVRVgvgvfvrHRQQLPRADFSwqVGAL-GPQPNTgrVLaatqr 99
Cdd:PRK15481   24 RPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQG-------RNGTVIRGSPS--PVALeGGDPGT--PL----- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 100 astdeaISLHSGYPDESLLPTnlVRRALTRVSKSHDAYRRAPV--RGMAELRQWFASQLVRANERDVvivpgTQSGLGAI 177
Cdd:PRK15481   88 ------HDLAGGNPDPQRLPD--LSRYFARLSRTPRLYGDAPVspELHAWAARWLRDDCPVAFEIDL-----TSGAIDAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 178 FRA-----ISPKELIIESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRtSSARAFYGQPTFGNPHGKRWSTAR 252
Cdd:PRK15481  155 ERLlcahlLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALA-QGARAVILTPRAHNPTGCSLSARR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 253 RKTIIEIIRAF-NAFLIEDDwaHdFAF--DAPDVPIAADDAeGHVIYLRSLTKVISPAVRVGAVIAKGPVLQRILAEVSA 329
Cdd:PRK15481  234 AAALRNLLARYpQVLVIIDD--H-FALlsSSPYHSVIPQTT-QRWALIRSVSKALGPDLRLAFVASDSATSARLRLRLNS 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 330 EALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSRYAPSVETPHvpqGGLNLWcrLPDGTDPQEVAERC 409
Cdd:PRK15481  310 GTQWVSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKLARALQQYGIAIPSPG---DGLNLW--LPLDTDSQATALTL 384
                         410
                  ....*....|.
gi 1093454868 410 EGRGLIVAPGR 420
Cdd:PRK15481  385 AKSGWLVREGE 395
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
12-55 4.55e-06

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 43.72  E-value: 4.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1093454868   12 ELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:smart00345   4 RLREDIVSGelRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGL 49
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
6-55 8.26e-05

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: 40.29  E-value: 8.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093454868   6 TSMLVGELETWIAQ--HKAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:pfam00392   2 YEQVYARLREDILSgrLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGL 53
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
12-55 1.78e-04

trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages and does not include the TreR from E. coli. [Regulatory functions, DNA interactions]


Pssm-ID: 274116 [Multi-domain]  Cd Length: 233  Bit Score: 42.74  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1093454868  12 ELETWI--AQHKAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:TIGR02404   8 DLEQKItkGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGY 53
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-451 2.68e-108

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: 328.71  E-value: 2.68e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868   9 LVGELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGLVEVrvgvgvfvrhRQQ--------LPRADFS 78
Cdd:COG1167    17 LADALREAILSGrlPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIES----------RPGsgtfvaarLPAPAPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  79 WQVGALGPQPNTGRVLAatqraSTDEAISLHSGYPDESLLPTNLVRRALTRVSKSHDAY--RRAPVRGMAELRQWFASQL 156
Cdd:COG1167    87 PRAAAAVAAPALRRLLE-----AAPGVIDLGSGAPDPDLFPLAALRRALRRALRRLPPAllGYGDPQGLPELREAIARYL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 157 ----VRANERDVVIVPGTQSGLGAIFRA-ISPKELI-IESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRTSS 230
Cdd:COG1167   162 arrgVPASPDQILITSGAQQALDLALRAlLRPGDTVaVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRRHR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 231 ARAFYGQPTFGNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFD-APDVPIAADDAEGHVIYLRSLTKVISPAVR 309
Cdd:COG1167   242 PRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDgRPPPPLAALDAPGRVIYIGSFSKTLAPGLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 310 VGAVIAKGPVLQRILAEVSAEALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSRYAPSVETPHVPQGG 389
Cdd:COG1167   322 LGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDGLRVTGPPGG 401
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 390 LNLWCRLPDGTDPQEVAERCEGRGLIVAPGRDWFPSEEIGPYLRLNFAGPHPERFVDAAMIL 451
Cdd:COG1167   402 LHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRL 463
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
106-442 9.11e-58

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: 194.10  E-value: 9.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 106 ISLHSGYPDESLLPtnLVRRALTRVSKSHDAYRRAPVRGMAELRQWFASQL-----VRANERDVVIVPGTQSGLGAIFRA 180
Cdd:cd00609     1 IDLSIGEPDFPPPP--EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLgrrggVDVPPEEIVVTNGAQEALSLLLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 181 ISPK--ELIIESPSYWGAILAARQAGISLLPVESDDEGPIPES--LERLLRTSSARAFYgqptFGNPH---GKRWSTARR 253
Cdd:cd00609    79 LLNPgdEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDleLLEAAKTPKTKLLY----LNNPNnptGAVLSEEEL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 254 KTIIEIIRAFNAFLIEDDwAH-DFAFD-APDVPIAADDAEGHVIYLRSLTKVIS-PAVRVGAVIA-KGPVLQRILAEVSA 329
Cdd:cd00609   155 EELAELAKKHGILIISDE-AYaELVYDgEPPPALALLDAYERVIVLRSFSKTFGlPGLRIGYLIApPEELLERLKKLLPY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 330 EALYTSGILQAVALDVVKQsaYATHLKNMQVALRQRRNDLLEALSRYAPsvETPHVPQGGLNLWCRLPDGTDPQEVAERC 409
Cdd:cd00609   234 TTSGPSTLSQAAAAAALDD--GEEHLEELRERYRRRRDALLEALKELGP--LVVVKPSGGFFLWLDLPEGDDEEFLERLL 309
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1093454868 410 EGRGLIVAPGRDWFPSEEigPYLRLNFAGPHPE 442
Cdd:cd00609   310 LEAGVVVRPGSAFGEGGE--GFVRLSFATPEEE 340
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
21-420 1.85e-20

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 93.19  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  21 KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGLVEVRVgvgvfvrHRQQLPRADFSwqVGAL-GPQPNTgrVLaatqr 99
Cdd:PRK15481   24 RPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQG-------RNGTVIRGSPS--PVALeGGDPGT--PL----- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 100 astdeaISLHSGYPDESLLPTnlVRRALTRVSKSHDAYRRAPV--RGMAELRQWFASQLVRANERDVvivpgTQSGLGAI 177
Cdd:PRK15481   88 ------HDLAGGNPDPQRLPD--LSRYFARLSRTPRLYGDAPVspELHAWAARWLRDDCPVAFEIDL-----TSGAIDAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 178 FRA-----ISPKELIIESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRtSSARAFYGQPTFGNPHGKRWSTAR 252
Cdd:PRK15481  155 ERLlcahlLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALA-QGARAVILTPRAHNPTGCSLSARR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 253 RKTIIEIIRAF-NAFLIEDDwaHdFAF--DAPDVPIAADDAeGHVIYLRSLTKVISPAVRVGAVIAKGPVLQRILAEVSA 329
Cdd:PRK15481  234 AAALRNLLARYpQVLVIIDD--H-FALlsSSPYHSVIPQTT-QRWALIRSVSKALGPDLRLAFVASDSATSARLRLRLNS 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 330 EALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSRYAPSVETPHvpqGGLNLWcrLPDGTDPQEVAERC 409
Cdd:PRK15481  310 GTQWVSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKLARALQQYGIAIPSPG---DGLNLW--LPLDTDSQATALTL 384
                         410
                  ....*....|.
gi 1093454868 410 EGRGLIVAPGR 420
Cdd:PRK15481  385 AKSGWLVREGE 395
PRK07681 PRK07681
LL-diaminopimelate aminotransferase;
96-455 8.47e-12

LL-diaminopimelate aminotransferase;


Pssm-ID: 181081  Cd Length: 399  Bit Score: 66.75  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  96 ATQRASTDEAISLHSGYPDesLLPTNLVRRALTRVSKSHDAYRRApVRGMAELRQWFAS------QLVRANERDVVIVPG 169
Cdd:PRK07681   25 KEKIAAGHKMIDLSIGNPD--MPPADFVREEMVHTANQKESYGYT-LSGIQEFHEAVTEyynnthNVILNADKEVLLLMG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 170 TQSGLGAIFRA-ISPKELI-IESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRTSSARA---FYGQPtfGNPH 244
Cdd:PRK07681  102 SQDGLVHLPMVyANPGDIIlVPDPGYTAYETGIQMAGATSYYMPLKKENDFLPDLELIPEEIADKAkmmILNFP--GNPV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 245 GKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFDAPD------VPIAADDAeghvIYLRSLTKVISPA-VRVGAVIAKG 317
Cdd:PRK07681  180 PAMAHEDFFKEVIAFAKKHNIIVVHDFAYAEFYFDGNKpisflsVPGAKEVG----VEINSLSKSYSLAgSRIGYMIGNE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 318 PVLqRILAEVSAEALYtsGI---LQAVALDVVKQSAyaTHLKNMQVALRQRRNDLLEALSRYAPSVETPhvpQGGLNLWC 394
Cdd:PRK07681  256 EIV-RALTQFKSNTDY--GVflpIQKAACAALRNGA--AFCEKNRGIYQERRDTLVDGFRTFGWNVDKP---AGSMFVWA 327
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 395 RLPDGTDPQEVA-ERCEGRGLIVAPGRDWfpseeigpylrlnfaGPHPERFVDAAMILDSVV 455
Cdd:PRK07681  328 EIPKGWTSLSFAyALMDRANVVVTPGHAF---------------GPHGEGFVRIALVQDEEV 374
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
125-447 1.95e-10

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: 62.07  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 125 RALTRVSKSHDAYRRAPVRGMAELRQwFASQLVRANERDVVIVPGTQSGLGAIFRAISP--KELIIESPSYWGAILAARQ 202
Cdd:COG0079    30 KVLEAIAAALDALNRYPDPDATALRE-ALAEYYGVPPEQVLVGNGSDELIQLLARAFLGpgDEVLVPEPTFSEYPIAARA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 203 AGISLLPVESDDEGPIPesLERLLRTSSARA---FYGQPTfgNPHGKRWStarRKTIIEIIRAF--NAFLIEDDwA-HDF 276
Cdd:COG0079   109 AGAEVVEVPLDEDFSLD--LDALLAAITERTdlvFLCNPN--NPTGTLLP---REELEALLEALpaDGLVVVDE-AyAEF 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 277 AFDAPDVpIAADDAEGHVIYLRSLTKVIS-PAVRVGAVIAKGPVLQRI-----------LAEVSAEAlytsgilqavALD 344
Cdd:COG0079   181 VPEEDSA-LPLLARYPNLVVLRTFSKAYGlAGLRLGYAIASPELIAALrrvrgpwnvnsLAQAAALA----------ALE 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 345 vvkqsaYATHLKNMQVALRQRRNDLLEALSR----YAPSVetphvpqgGLNLWCRLPDgtDPQEVAERCEGRGLIVapgR 420
Cdd:COG0079   250 ------DRAYLEETRARLRAERERLAAALRAlgltVYPSQ--------ANFVLVRVPE--DAAELFEALLERGILV---R 310
                         330       340
                  ....*....|....*....|....*....
gi 1093454868 421 DwFPSEEIGPYLRLNfAGPHPE--RFVDA 447
Cdd:COG0079   311 D-FSSFGLPDYLRIT-VGTPEEndRLLAA 337
avtA PRK09440
valine--pyruvate transaminase; Provisional
293-455 3.51e-10

valine--pyruvate transaminase; Provisional


Pssm-ID: 236517  Cd Length: 416  Bit Score: 61.79  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 293 HVIYLRSLTKVISPAVRVGAVIAKGPVLQRILAEVSAEALYTSGILQAVALDVVKQSAYATHLKN-MQVALRQRRNDLLE 371
Cdd:PRK09440  240 NIILCMSLSKLGLPGVRCGIVIADEEIIEALSNMNGIISLAPGRLGPAIAAEMIESGDLLRLSETvIRPFYRQKVQLAIA 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 372 ALSRYAPSVetP---HVPQGGLNLWCRLPD-GTDPQEVAERCEGRGLIVAPGRDWFP-SEEIGPY----LRLNFAgPHPE 442
Cdd:PRK09440  320 LLRRYLPDE--PcliHKPEGAIFLWLWFKDlPITTEELYQRLKARGVLVVPGHYFFPgLDEDWPHahqcIRMNYV-QDDE 396
                         170
                  ....*....|...
gi 1093454868 443 RFVDAAMILDSVV 455
Cdd:PRK09440  397 EIEKGIAILAEEV 409
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
123-347 1.97e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 59.00  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 123 VRRALTRVSKSHDAYRRAPVRGMAELRQWFASQLVRANErDVVIVPGTQSGLGAIFRAI-SPKELIIES-PSY-WGAILA 199
Cdd:PRK06225   46 VREAMIRCIEEGEYCKYPPPEGFPELRELILKDLGLDDD-EALITAGATESLYLVMRAFlSPGDNAVTPdPGYlIIDNFA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 200 ARQAG-ISLLPVESDDEG--PIPESLERLLRTSSARAFYGQPTfgNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDF 276
Cdd:PRK06225  125 SRFGAeVIEVPIYSEECNykLTPELVKENMDENTRLIYLIDPL--NPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDF 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 277 afdAPDVPIAADDAEGHVIYLRSLTKVISPA-VRVGAVIAKgPVLQRILAEVSAEALYTSGILQAVALDVVK 347
Cdd:PRK06225  203 ---AREHTLAAEYAPEHTVTSYSFSKIFGMAgLRIGAVVAT-PDLIEVVKSIVINDLGTNVIAQEAAIAGLK 270
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
9-55 2.25e-08

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: 50.52  E-value: 2.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1093454868   9 LVGELETWIA--QHKAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:cd07377     6 IADQLREAILsgELKPGDRLPSERELAEELGVSRTTVREALRELEAEGL 54
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
108-429 9.88e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 53.70  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 108 LHSGYPDeslLPT-NLVRRALTRVSKSHDAYrrAPVRGMAELRQWFASQLVRAN---ERDVVIVpgTQSGLGAIFRAISP 183
Cdd:PRK07568   35 LNIGQPD---IKTpEVFFEAIKNYDEEVLAY--SHSQGIPELREAFAKYYKKWGidvEPDEILI--TNGGSEAILFAMMA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 184 -----KELIIESPSYWGAILAARQAGISLLPVESD-DEG---PIPESLERLLrTSSARAF-YGQPtfGNPHGKRWSTARR 253
Cdd:PRK07568  108 icdpgDEILVPEPFYANYNGFATSAGVKIVPVTTKiEEGfhlPSKEEIEKLI-TPKTKAIlISNP--GNPTGVVYTKEEL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 254 KTIIEIIRAFNAFLIEDDWAHDFAFDAPDVPIAAD--DAEGHVIYLRSLTKVISP-AVRVGAVIAKGP-VLQRIL----- 324
Cdd:PRK07568  185 EMLAEIAKKHDLFLISDEVYREFVYDGLKYTSALSleGLEDRVIIIDSVSKRYSAcGARIGCLISKNKeLIAAAMklcqa 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 325 -------AEVSAEALYTSGilqavaldvvkqsayATHLKNMQVALRQRRNDLLEALSRYaPSVeTPHVPQGGLNLWCRLP 397
Cdd:PRK07568  265 rlspptlEQIGAAALLDTP---------------ESYFDEVREEYKKRRDILYEELNKI-PGV-VCEKPKGAFYIIAKLP 327
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1093454868 398 -DgtDPQEVAERC------EGRGLIVAPGRDWFPSEEIG 429
Cdd:PRK07568  328 vD--DAEDFAKWLltdfnyNGETVMVAPASGFYATPGLG 364
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
106-388 5.76e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 51.61  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 106 ISLHSG---YPdesllPTNLVRRALTRVSKSHDAYRRAPVRGMAELRQWFASQLVRAN------ERDVVIVPGTQSGLGA 176
Cdd:PRK05957   30 ISLGQGvvsYP-----PPPEAIEALNNFLANPENHKYQAVQGIPPLLEAITQKLQQDNgielnnEQAIVVTAGSNMAFMN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 177 IFRAI-SP-KELIIESPSYWGAILAARQAGISLLPVESDDE-GPIPESLERLLrTSSARAFYG-QPTfgNPHGKRWSTAR 252
Cdd:PRK05957  105 AILAItDPgDEIILNTPYYFNHEMAITMAGCQPILVPTDDNyQLQPEAIEQAI-TPKTRAIVTiSPN--NPTGVVYPEAL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 253 RKTIIEIIRAFNAFLIEDDWAHDFAFD-APDV-PIAADDAEGHVIYLRSLTKVISPAV-RVGAVIAKgPVLQRILAEVSA 329
Cdd:PRK05957  182 LRAVNQICAEHGIYHISDEAYEYFTYDgVKHFsPGSIPGSGNHTISLYSLSKAYGFASwRIGYMVIP-IHLLEAIKKIQD 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093454868 330 EALYTSGILQ---AVALDVVKQSAYATHLKnmqvALRQRRNDLLEALSRyAPSVETPHVPQG 388
Cdd:PRK05957  261 TILICPPVVSqyaALGALQVGKSYCQQHLP----EIAQVRQILLKSLGQ-LQDRCTLHPANG 317
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
12-55 4.55e-06

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 43.72  E-value: 4.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1093454868   12 ELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:smart00345   4 RLREDIVSGelRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGL 49
PRK08361 PRK08361
aspartate aminotransferase; Provisional
98-437 9.05e-06

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 47.56  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  98 QRASTDE-AISLHSGYPDESLlPTNLVRRALTRVSKSHDAYrrAPVRGMAELRQWFASQL-----VRANERDVVIVPGTQ 171
Cdd:PRK08361   27 ERASKMEnVISLGIGEPDFDT-PKNIKEAAKRALDEGWTHY--TPNAGIPELREAIAEYYkkfygVDVDVDNVIVTAGAY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 172 SGLGAIFRAI--SPKELIIESPSYWGAILAAR--QAGISLLPV-ESDDEGPIPESLERLLRTSSARAFYGQPTfgNPHGK 246
Cdd:PRK08361  104 EATYLAFESLleEGDEVIIPDPAFVCYVEDAKiaEAKPIRIPLrEENEFQPDPDELLELITKRTRMIVINYPN--NPTGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 247 RWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFDA----PDVPIAADDaeghVIYLRSLTKVIS-PAVRVGAVIAKGPVLQ 321
Cdd:PRK08361  182 TLDKEVAKAIADIAEDYNIYILSDEPYEHFLYEGakhyPMIKYAPDN----TILANSFSKTFAmTGWRLGFVIAPEQVIK 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 322 RILAEVSAEALYTSGILQAVALDVVKQSAYATHLKNMQVALRQRRNDLLEALSryapsvETPHV----PQGGLNLWCRLp 397
Cdd:PRK08361  258 DMIKLHAYIIGNVASFVQIAGIEALRSKESWKAVEEMRKEYNERRKLVLKRLK------EMPHIkvfePKGAFYVFANI- 330
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1093454868 398 DGTD--PQEVAE-RCEGRGLIVAPGRDWFPSEEigPYLRLNFA 437
Cdd:PRK08361  331 DETGmsSEDFAEwLLEKARVVVIPGTAFGKAGE--GYIRISYA 371
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
12-55 1.11e-05

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 46.39  E-value: 1.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1093454868  12 ELETWIAQH--KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:COG2188    13 ALRERIESGelPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGL 58
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
6-55 8.26e-05

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: 40.29  E-value: 8.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1093454868   6 TSMLVGELETWIAQ--HKAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:pfam00392   2 YEQVYARLREDILSgrLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGL 53
trehalos_R_Bsub TIGR02404
trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR ...
12-55 1.78e-04

trehalose operon repressor, B. subtilis-type; This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages and does not include the TreR from E. coli. [Regulatory functions, DNA interactions]


Pssm-ID: 274116 [Multi-domain]  Cd Length: 233  Bit Score: 42.74  E-value: 1.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1093454868  12 ELETWI--AQHKAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:TIGR02404   8 DLEQKItkGQYKEGDYLPSEHELMDQYGASRETVRKALNLLTERGY 53
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
95-315 7.43e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 41.63  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868  95 AATQRASTDEAISLHSGYPDeslLPTN--LVRRALTRVSKSHDAYRrAPVrGMAELRQwfasQLVRANERD--------- 163
Cdd:PRK06348   21 IATLAKKFPDIIDLSLGDPD---LITDesIINAAFEDAKKGHTRYT-DSG-GDVELIE----EIIKYYSKNydlsfkrne 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 164 VVIVPGTQSGLGAIFRAI--SPKELIIESP---SYWGAILAARQAGISLLPVESDDEGPIPESLERLLrTSSARAFYGQp 238
Cdd:PRK06348   92 IMATVGACHGMYLALQSIldPGDEVIIHEPyftPYKDQIEMVGGKPIILETYEEDGFQINVKKLEALI-TSKTKAIILN- 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093454868 239 TFGNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFDAPDVPIAA-DDAEGHVIYLRSLTKVIS-PAVRVGAVIA 315
Cdd:PRK06348  170 SPNNPTGAVFSKETLEEIAKIAIEYDLFIISDEVYDGFSFYEDFVPMATlAGMPERTITFGSFSKDFAmTGWRIGYVIA 248
PRK06425 PRK06425
histidinol-phosphate aminotransferase; Validated
164-314 1.04e-03

histidinol-phosphate aminotransferase; Validated


Pssm-ID: 102370  Cd Length: 332  Bit Score: 40.99  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 164 VVIVPGTQSGLGAIFRAISPKELIIESPSY--WGAILAARQAGISLLPVesddeGPIPESLERLLRTSSARAFYGQPTfg 241
Cdd:PRK06425   60 VLIGPGLTHFIYRLLSYINVGNIIIVEPNFneYKGYAFTHGIRISALPF-----NLINNNPEILNNYNFDLIFIVSPD-- 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1093454868 242 NPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFDAPDVPIAADDAEGHVIYLRSLTKVIS-PAVRVGAVI 314
Cdd:PRK06425  133 NPLGNLISRDSLLTISEICRKKGALLFIDEAFIDFVPNRAEEDVLLNRSYGNVIIGRSLTKILGiPSLRIGYIA 206
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
21-55 1.13e-03

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 38.62  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1093454868  21 KAGEKLPSSREITRSYSVSPVTVRNAIHELATRGL 55
Cdd:COG1725    29 KPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGL 63
PRK07908 PRK07908
threonine-phosphate decarboxylase;
287-447 3.64e-03

threonine-phosphate decarboxylase;


Pssm-ID: 236128  Cd Length: 349  Bit Score: 39.22  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 287 ADDAEGHVIYLRSLTKVISPA-VRVGAVIAKGPVLQRILAevsAEALYTSGILQAVALDVVKQSAYATHLKNMQVALRQR 365
Cdd:PRK07908  189 AGDDLPGVLVLRSLTKTWSLAgLRVGYALGAPDVLARLTR---GRAHWPVGTLQLEAIAACCAPRAVAEAAADAARLAAD 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 366 RNDLLEALSRYAPSVetpHVPQGGLNLWCRLPDGTdpqEVAERCEGRGLIVAPGrDWFPSeeIGP-YLRLNFAGP-HPER 443
Cdd:PRK07908  266 RAEMVAGLRAVGARV---VDPAAAPFVLVRVPDAE---LLRKRLRERGIAVRRG-DTFPG--LDPdYLRLAVRPRaEVPV 336

                  ....
gi 1093454868 444 FVDA 447
Cdd:PRK07908  337 LVQA 340
Asp_aminotransf pfam12897
Aspartate amino-transferase; These proteins catalyze the reversible transfer of an amino group ...
169-290 4.59e-03

Aspartate amino-transferase; These proteins catalyze the reversible transfer of an amino group from the amino acid substrate to an acceptor alpha-keto acid. They require pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze this reaction. Trans-amination reactions are of central importance in amino acid metabolism and in links to carbohydrate and fat metabolism. This class of amino-transferases acts as dimers in a head-to-tail configuration. It has been demonstrated that these proteins are aspartate amino-transferases from Bacteria (Jansen, R.S. et al. Nat Commun 11, 1960 (2020)).


Pssm-ID: 403948  Cd Length: 419  Bit Score: 39.08  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 169 GTQSGLGAIFRAISPKeLIIESPSYWGAILAARQAGISLLPVESDDEGPIPESLERLLRT-SSARAFYGQPTFGNPHGKR 247
Cdd:pfam12897 110 GVRDGEGPWVAQETVK-FLCPVPGYDRHFAILETLGIEMITVDLQDDGPDMDAVERLVAKdPSIKGIWFVPKYSNPTGET 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1093454868 248 WSTARRKTIIEIIRAfnaflieddwahdfafdAPDVPIAADDA 290
Cdd:pfam12897 189 ISEEVARRLAGMKTA-----------------APDFRIFWDNA 214
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
143-448 6.38e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 38.77  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 143 RGMAELRQWFASQLVR------ANERDVVivpgTQSGLGAIFRAI----SP-KELIIESPSYWGAILAARQAGISLLPVE 211
Cdd:PRK06108   61 LGIPELREALARYVSRlhgvatPPERIAV----TSSGVQALMLAAqalvGPgDEVVAVTPLWPNLVAAPKILGARVVCVP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 212 SDDEGPIPE-SLERLLR--TSSARA-FYGQPTfgNPHGKRWSTARRKTIIEIIRAFNAFLIEDDWAHDFAFDAPD-VPIA 286
Cdd:PRK06108  137 LDFGGGGWTlDLDRLLAaiTPRTRAlFINSPN--NPTGWTASRDDLRAILAHCRRHGLWIVADEVYERLYYAPGGrAPSF 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 287 ADDAE--GHVIYLRSLTKVIS-PAVRVGAVIAKgPVLQRILAEVsaeALY-TSGI---LQAVALDVVKQSAyaTHLKNMQ 359
Cdd:PRK06108  215 LDIAEpdDRIIFVNSFSKNWAmTGWRLGWLVAP-PALGQVLEKL---IEYnTSCVaqfVQRAAVAALDEGE--DFVAELV 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093454868 360 VALRQRRNDLLEALSRyAPSVETPhVPQGGLNLWCRLPDGTDPQEVAER-CEGRGLIVAPGRDWFPSEEIgpYLRLNFAG 438
Cdd:PRK06108  289 ARLRRSRDHLVDALRA-LPGVEVA-KPDGAMYAFFRIPGVTDSLALAKRlVDEAGLGLAPGTAFGPGGEG--FLRWCFAR 364
                         330
                  ....*....|
gi 1093454868 439 pHPERFVDAA 448
Cdd:PRK06108  365 -DPARLDEAV 373
 
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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