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Conserved domains on  [gi|516732207|ref|WP_018072262|]
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PLP-dependent aminotransferase family protein [Rhizobium ruizarguesonis]

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

 Zoom to residue level

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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 ...
9-463 2.47e-94

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: 293.27  E-value: 2.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207   9 SRGSGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGE 88
Cdd:COG1167    7 RDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  89 QIDPLTVSLGG-TRVHDAPANKIRFDT-TAAPDLGQGKVIAGILAEIGEQHFSEISSYS--------RnfpsnwfEAGRL 158
Cdd:COG1167   87 PRAAAAVAAPAlRRLLEAAPGVIDLGSgAPDPDLFPLAALRRALRRALRRLPPALLGYGdpqglpelR-------EAIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 159 WLARSGWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERLCQQ 238
Cdd:COG1167  160 YLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 239 QHPKIAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL--LASL-APDRTFLVNGLSKSVAAG 315
Cdd:COG1167  240 HRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPppLAALdAPGRVIYIGSFSKTLAPG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 316 VRGGWVACPPHFAQRIKVTHRMITGGLPFILAETCARLVESGTAHEIRKESVEELSRRVRLAREQLQ-----GFDFQSHP 390
Cdd:COG1167  320 LRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALArhlpdGLRVTGPP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516732207 391 HAPFLWLKLPEPWMSGTFKNAAFRDGVLVDDEDEFkaARGEKTYHRVRIGFSSPkTGQELVSGLMILRRLLEN 463
Cdd:COG1167  400 GGLHLWLELPEGVDAEALAAAALARGILVAPGSAF--SADGPPRNGLRLGFGAP-SEEELEEALRRLAELLRE 469
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-463 2.47e-94

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: 293.27  E-value: 2.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207   9 SRGSGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGE 88
Cdd:COG1167    7 RDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  89 QIDPLTVSLGG-TRVHDAPANKIRFDT-TAAPDLGQGKVIAGILAEIGEQHFSEISSYS--------RnfpsnwfEAGRL 158
Cdd:COG1167   87 PRAAAAVAAPAlRRLLEAAPGVIDLGSgAPDPDLFPLAALRRALRRALRRLPPALLGYGdpqglpelR-------EAIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 159 WLARSGWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERLCQQ 238
Cdd:COG1167  160 YLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 239 QHPKIAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL--LASL-APDRTFLVNGLSKSVAAG 315
Cdd:COG1167  240 HRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPppLAALdAPGRVIYIGSFSKTLAPG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 316 VRGGWVACPPHFAQRIKVTHRMITGGLPFILAETCARLVESGTAHEIRKESVEELSRRVRLAREQLQ-----GFDFQSHP 390
Cdd:COG1167  320 LRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALArhlpdGLRVTGPP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516732207 391 HAPFLWLKLPEPWMSGTFKNAAFRDGVLVDDEDEFkaARGEKTYHRVRIGFSSPkTGQELVSGLMILRRLLEN 463
Cdd:COG1167  400 GGLHLWLELPEGVDAEALAAAALARGILVAPGSAF--SADGPPRNGLRLGFGAP-SEEELEEALRRLAELLRE 469
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
159-459 2.30e-46

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: 164.44  E-value: 2.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 159 WLARS-GWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERL-- 235
Cdd:cd00609   48 WLGRRgGVDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLea 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 236 CQQQHPKIAFLMPtVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTP---LLASLAPDRTFLVNGLSKSV 312
Cdd:cd00609  128 AKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELVYDGEPppaLALLDAYERVIVLRSFSKTF 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 313 A-AGVRGGWVACPP-HFAQRIKVTHRMITGGLPFILAETCARLVESGTAHeiRKESVEELSRRVRLAREQLQGFDF---Q 387
Cdd:cd00609  207 GlPGLRIGYLIAPPeELLERLKKLLPYTTSGPSTLSQAAAAAALDDGEEH--LEELRERYRRRRDALLEALKELGPlvvV 284
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516732207 388 SHPHAPFLWLKLPEPWMSGTFKNAAFRDGVLVDDEDEFkaarGEKTYHRVRIGFSSPKtgQELVSGLMILRR 459
Cdd:cd00609  285 KPSGGFFLWLDLPEGDDEEFLERLLLEAGVVVRPGSAF----GEGGEGFVRLSFATPE--EELEEALERLAE 350
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
171-454 1.00e-15

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 78.12  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  171 NIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVE---SDELGVIPEDFERLCQQQHpkIAFLM 247
Cdd:pfam00155  65 AVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydSNDFHLDFDALEAALKEKP--KVVLH 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  248 PTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGM---SGDDTPLLASLAP-DRTFLVNGLSKS-VAAGVRGGWVA 322
Cdd:pfam00155 143 TSPHNPTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFvfgSPDAVATRALLAEgPNLLVVGSFSKAfGLAGWRVGYIL 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  323 CPPHFAQRIKVTHRmitgglPFILAETCARLVESGTAHEIR-----KESVEELSRRVRLAREQLQ--GFDFQSHPHAPFL 395
Cdd:pfam00155 223 GNAAVISQLRKLAR------PFYSSTHLQAAAAAALSDPLLvaselEEMRQRIKERRDYLRDGLQaaGLSVLPSQAGFFL 296
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516732207  396 WLKLPEPWMSGTFKNAAFRDGVLVDDEDEFKAARgektyhRVRIGFS--SPKTGQELVSGL 454
Cdd:pfam00155 297 LTGLDPETAKELAQVLLEEVGVYVTPGSSPGVPG------WLRITVAggTEEELEELLEAI 351
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
21-400 2.98e-13

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 71.23  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  21 DSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVlnRSETPPGEQidplTVSLGGT 100
Cdd:PRK15481  12 DSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVI--RGSPSPVAL----EGGDPGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 101 RVHD-APANKirfDTTAAPDLGQgkVIAGILAE---IGEQHFS-EISSYsrnfpsnwfeaGRLWLARSgwMPEAENIVPT 175
Cdd:PRK15481  86 PLHDlAGGNP---DPQRLPDLSR--YFARLSRTprlYGDAPVSpELHAW-----------AARWLRDD--CPVAFEIDLT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 176 LGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERLCQQQhPKIAFLMPTVHNPTV 255
Cdd:PRK15481 148 SGAIDAIERLLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQG-ARAVILTPRAHNPTG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 256 SIMPYERRVTIAAIARKH-GVWLIEDDLYGGMSGDD-TPLLASLAPdRTFLVNGLSKSVAAGVRGGWVACPPHFAQRIKV 333
Cdd:PRK15481 227 CSLSARRAAALRNLLARYpQVLVIIDDHFALLSSSPyHSVIPQTTQ-RWALIRSVSKALGPDLRLAFVASDSATSARLRL 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516732207 334 THRMITGGLPFILAE-TCARLVESGTAHEIRKESVEELSRRVRLARE-QLQGFDFQSHPHAPFLWLKLP 400
Cdd:PRK15481 306 RLNSGTQWVSHLLQDlVYACLTDPEYQARLAQARLFYAQRRQKLARAlQQYGIAIPSPGDGLNLWLPLD 374
C_P_lyase_phnF TIGR02325
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for ...
8-81 9.75e-11

phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond. [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]


Pssm-ID: 131378 [Multi-domain]  Cd Length: 238  Bit Score: 61.72  E-value: 9.75e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732207    8 ISRGSGP-VYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNR 81
Cdd:TIGR02325   1 IERTSGVaLWRQIADKIEQEIAAGHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGTFVAAR 75
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-78 1.04e-09

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 54.12  E-value: 1.04e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207    19 LADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV 78
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
9-463 2.47e-94

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: 293.27  E-value: 2.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207   9 SRGSGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGE 88
Cdd:COG1167    7 RDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPAPAPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  89 QIDPLTVSLGG-TRVHDAPANKIRFDT-TAAPDLGQGKVIAGILAEIGEQHFSEISSYS--------RnfpsnwfEAGRL 158
Cdd:COG1167   87 PRAAAAVAAPAlRRLLEAAPGVIDLGSgAPDPDLFPLAALRRALRRALRRLPPALLGYGdpqglpelR-------EAIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 159 WLARSGWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERLCQQ 238
Cdd:COG1167  160 YLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLDALEAALRR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 239 QHPKIAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL--LASL-APDRTFLVNGLSKSVAAG 315
Cdd:COG1167  240 HRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPppLAALdAPGRVIYIGSFSKTLAPG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 316 VRGGWVACPPHFAQRIKVTHRMITGGLPFILAETCARLVESGTAHEIRKESVEELSRRVRLAREQLQ-----GFDFQSHP 390
Cdd:COG1167  320 LRLGYLVAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALArhlpdGLRVTGPP 399
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516732207 391 HAPFLWLKLPEPWMSGTFKNAAFRDGVLVDDEDEFkaARGEKTYHRVRIGFSSPkTGQELVSGLMILRRLLEN 463
Cdd:COG1167  400 GGLHLWLELPEGVDAEALAAAALARGILVAPGSAF--SADGPPRNGLRLGFGAP-SEEELEEALRRLAELLRE 469
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
159-459 2.30e-46

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: 164.44  E-value: 2.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 159 WLARS-GWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERL-- 235
Cdd:cd00609   48 WLGRRgGVDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLea 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 236 CQQQHPKIAFLMPtVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTP---LLASLAPDRTFLVNGLSKSV 312
Cdd:cd00609  128 AKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELVYDGEPppaLALLDAYERVIVLRSFSKTF 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 313 A-AGVRGGWVACPP-HFAQRIKVTHRMITGGLPFILAETCARLVESGTAHeiRKESVEELSRRVRLAREQLQGFDF---Q 387
Cdd:cd00609  207 GlPGLRIGYLIAPPeELLERLKKLLPYTTSGPSTLSQAAAAAALDDGEEH--LEELRERYRRRRDALLEALKELGPlvvV 284
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516732207 388 SHPHAPFLWLKLPEPWMSGTFKNAAFRDGVLVDDEDEFkaarGEKTYHRVRIGFSSPKtgQELVSGLMILRR 459
Cdd:cd00609  285 KPSGGFFLWLDLPEGDDEEFLERLLLEAGVVVRPGSAF----GEGGEGFVRLSFATPE--EELEEALERLAE 350
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
171-454 1.00e-15

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 78.12  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  171 NIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVE---SDELGVIPEDFERLCQQQHpkIAFLM 247
Cdd:pfam00155  65 AVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydSNDFHLDFDALEAALKEKP--KVVLH 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  248 PTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGM---SGDDTPLLASLAP-DRTFLVNGLSKS-VAAGVRGGWVA 322
Cdd:pfam00155 143 TSPHNPTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFvfgSPDAVATRALLAEgPNLLVVGSFSKAfGLAGWRVGYIL 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  323 CPPHFAQRIKVTHRmitgglPFILAETCARLVESGTAHEIR-----KESVEELSRRVRLAREQLQ--GFDFQSHPHAPFL 395
Cdd:pfam00155 223 GNAAVISQLRKLAR------PFYSSTHLQAAAAAALSDPLLvaselEEMRQRIKERRDYLRDGLQaaGLSVLPSQAGFFL 296
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516732207  396 WLKLPEPWMSGTFKNAAFRDGVLVDDEDEFKAARgektyhRVRIGFS--SPKTGQELVSGL 454
Cdd:pfam00155 297 LTGLDPETAKELAQVLLEEVGVYVTPGSSPGVPG------WLRITVAggTEEELEELLEAI 351
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
8-78 1.79e-15

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 72.13  E-value: 1.79e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516732207   8 ISRGSG-PVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYA-LVHErGLVAGEVGRGTYV 78
Cdd:COG1725    3 IDFDSGvPIYEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYReLEDE-GLIETRRGKGTFV 74
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
251-405 2.62e-15

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: 77.48  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 251 HNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMS--GDDTPLLASL--APDRTFLVNGLSKSVA-AGVRGGWVACPP 325
Cdd:COG0436  173 NNPTGAVYSREELEALAELAREHDLLVISDEIYEELVydGAEHVSILSLpgLKDRTIVINSFSKSYAmTGWRIGYAVGPP 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 326 HFAQRIKVTHRMITGGLPFILAETCARLVESGTAHeiRKESVEELSRRVRLAREQLQ--GFDFqSHPHAPF-LWLKLPEP 402
Cdd:COG0436  253 ELIAALLKLQSNLTSCAPTPAQYAAAAALEGPQDY--VEEMRAEYRRRRDLLVEGLNeiGLSV-VKPEGAFyLFADVPEL 329

                 ...
gi 516732207 403 WMS 405
Cdd:COG0436  330 GLD 332
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
14-78 1.29e-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: 65.55  E-value: 1.29e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732207  14 PVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV 78
Cdd:cd07377    1 PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFV 65
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
21-400 2.98e-13

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 71.23  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  21 DSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVlnRSETPPGEQidplTVSLGGT 100
Cdd:PRK15481  12 DSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVI--RGSPSPVAL----EGGDPGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 101 RVHD-APANKirfDTTAAPDLGQgkVIAGILAE---IGEQHFS-EISSYsrnfpsnwfeaGRLWLARSgwMPEAENIVPT 175
Cdd:PRK15481  86 PLHDlAGGNP---DPQRLPDLSR--YFARLSRTprlYGDAPVSpELHAW-----------AARWLRDD--CPVAFEIDLT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 176 LGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVIPEDFERLCQQQhPKIAFLMPTVHNPTV 255
Cdd:PRK15481 148 SGAIDAIERLLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQG-ARAVILTPRAHNPTG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 256 SIMPYERRVTIAAIARKH-GVWLIEDDLYGGMSGDD-TPLLASLAPdRTFLVNGLSKSVAAGVRGGWVACPPHFAQRIKV 333
Cdd:PRK15481 227 CSLSARRAAALRNLLARYpQVLVIIDDHFALLSSSPyHSVIPQTTQ-RWALIRSVSKALGPDLRLAFVASDSATSARLRL 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516732207 334 THRMITGGLPFILAE-TCARLVESGTAHEIRKESVEELSRRVRLARE-QLQGFDFQSHPHAPFLWLKLP 400
Cdd:PRK15481 306 RLNSGTQWVSHLLQDlVYACLTDPEYQARLAQARLFYAQRRQKLARAlQQYGIAIPSPGDGLNLWLPLD 374
PRK05764 PRK05764
aspartate aminotransferase; Provisional
251-325 3.49e-11

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 64.76  E-value: 3.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 251 HNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL--LASLAP---DRTFLVNGLSKSVA-AGVRGGWVACP 324
Cdd:PRK05764 174 SNPTGAVYSPEELEAIADVAVEHDIWVLSDEIYEKLVYDGAEFtsIASLSPelrDRTITVNGFSKAYAmTGWRLGYAAGP 253

                 .
gi 516732207 325 P 325
Cdd:PRK05764 254 K 254
C_P_lyase_phnF TIGR02325
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for ...
8-81 9.75e-11

phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond. [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]


Pssm-ID: 131378 [Multi-domain]  Cd Length: 238  Bit Score: 61.72  E-value: 9.75e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732207    8 ISRGSGP-VYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNR 81
Cdd:TIGR02325   1 IERTSGVaLWRQIADKIEQEIAAGHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGTFVAAR 75
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
167-339 1.69e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 62.43  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 167 PEAEnIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVESDELGVI--PEDFERLCQQQHPKI- 243
Cdd:PRK07309  90 PENE-ILVTIGATEALSASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVltPEMLEKAILEQGDKLk 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 244 AFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGM--SGDDTPLLASLAPDRTFLVNGLSKSVA-AGVRGGW 320
Cdd:PRK07309 169 AVILNYPANPTGVTYSREQIKALADVLKKYDIFVISDEVYSELtyTGEPHVSIAEYLPDQTILINGLSKSHAmTGWRIGL 248
                        170       180
                 ....*....|....*....|
gi 516732207 321 VACPPHF-AQRIKVTHRMIT 339
Cdd:PRK07309 249 IFAPAEFtAQLIKSHQYLVT 268
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
10-119 3.77e-10

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 59.88  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  10 RGSGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGEQ 89
Cdd:COG2188    1 SSPVPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEPKIEYPLSR 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 516732207  90 IDPLTVSLG------GTRVhdapankIRFDTTAAPD 119
Cdd:COG2188   81 LTSFTEELRargrepSTRV-------LSAERVPADE 109
PRK07682 PRK07682
aminotransferase;
167-329 8.67e-10

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 60.13  E-value: 8.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 167 PEAENIVpTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTVES---DELGVIPEDFERLCQQQHPKI 243
Cdd:PRK07682  80 PNDEIIV-TVGASQALDVAMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATtleNEFKVQPAQIEAAITAKTKAI 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 244 AFLMPTvhNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL-LASLA--PDRTFLVNGLSKSVA-AGVRGG 319
Cdd:PRK07682 159 LLCSPN--NPTGAVLNKSELEEIAVIVEKHDLIVLSDEIYAELTYDEAYTsFASIKgmRERTILISGFSKGFAmTGWRLG 236
                        170
                 ....*....|
gi 516732207 320 WVACPPHFAQ 329
Cdd:PRK07682 237 FIAAPVYFSE 246
PRK07324 PRK07324
transaminase; Validated
169-463 8.75e-10

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 60.34  E-value: 8.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 169 AENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGrrtLTVE----SDELGVIPeDFERLCQQQHPK-- 242
Cdd:PRK07324  80 PENILQTNGATGANFLVLYALVEPGDHVISVYPTYQQLYDIPESLG---AEVDywqlKEENGWLP-DLDELRRLVRPNtk 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 243 -IAFLMPtvHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGG-MSGDDTPLLASLApDRTFLVNGLSKSVA-AGVRGG 319
Cdd:PRK07324 156 lICINNA--NNPTGALMDRAYLEEIVEIARSVDAYVLSDEVYRPlDEDGSTPSIADLY-EKGISTNSMSKTYSlPGIRVG 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 320 WVACPPHFAQRIKvTHR---MITGGlpfILAETCARLVesgTAHeirKESVeeLSRRVRLAREQLQGFD--FQSHPHA-- 392
Cdd:PRK07324 233 WIAANEEVIDILR-KYRdytMICAG---VFDDMLASLA---LEH---RDAI--LERNRKIVRTNLAILDewVAKEPRVsy 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 393 --P------FLWLKLPEPwmSGTFKNAAFRD-GVLVDDEDEFkaargEKTYHrVRIGFSSPKtgQELVSGLMILRRLLEN 463
Cdd:PRK07324 301 vkPkavstsFVKLDVDMP--SEDFCLKLLKEtGVLLVPGNRF-----DLEGH-VRIGYCCDT--ETLKKGLKKLSEFLRE 370
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
19-78 1.04e-09

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 54.12  E-value: 1.04e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207    19 LADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV 78
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
PLN00175 PLN00175
aminotransferase family protein; Provisional
192-339 1.10e-08

aminotransferase family protein; Provisional


Pssm-ID: 215089 [Multi-domain]  Cd Length: 413  Bit Score: 57.18  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 192 PGDKIVFEHLTYTQVSRSARLLGR--RTLTVESDELGViPEDFERLCQQQHPKiAFLMPTVHNPTVSIMPYERRVTIAAI 269
Cdd:PLN00175 138 PGDEVILFAPFYDSYEATLSMAGAkiKTVTLRPPDFAV-PEDELKAAFTSKTR-AILINTPHNPTGKMFTREELELIASL 215
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516732207 270 ARKHGVWLIEDDLYGGMSGD-DTPLLASLAP--DRTFLVNGLSKSVA-AGVRGGWVACPPHFAQRIKVTHRMIT 339
Cdd:PLN00175 216 CKENDVLAFTDEVYDKLAFEgDHISMASLPGmyERTVTMNSLGKTFSlTGWKIGWAIAPPHLTWGVRQAHSFLT 289
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
12-93 1.32e-08

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 55.32  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  12 SGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGEQID 91
Cdd:COG2186    5 RRSLAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSPWALLDPLA 84

                 ..
gi 516732207  92 PL 93
Cdd:COG2186   85 LL 86
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
16-78 1.73e-08

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: 50.69  E-value: 1.73e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516732207   16 YLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV 78
Cdd:pfam00392   2 YEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
192-331 2.47e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 52.64  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 192 PGDKIVFEHLTYTQVSRSARLLGRRTLTVESD-ELGVIPEDFERLCQQQHPKI-AFLMPTVHNPTVSIMPYERRVTIAAI 269
Cdd:PRK06108 107 PGDEVVAVTPLWPNLVAAPKILGARVVCVPLDfGGGGWTLDLDRLLAAITPRTrALFINSPNNPTGWTASRDDLRAILAH 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516732207 270 ARKHGVWLIEDDLYGGMSGDDTPLLASL----AP-DRTFLVNGLSKSVA-AGVRGGWVACPPHFAQRI 331
Cdd:PRK06108 187 CRRHGLWIVADEVYERLYYAPGGRAPSFldiaEPdDRIIFVNSFSKNWAmTGWRLGWLVAPPALGQVL 254
PRK09265 PRK09265
aminotransferase AlaT; Validated
252-322 5.94e-07

aminotransferase AlaT; Validated


Pssm-ID: 181738  Cd Length: 404  Bit Score: 51.35  E-value: 5.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516732207 252 NPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDD---TPlLASLAPDR---TFlvNGLSKSV-AAGVRGGWVA 322
Cdd:PRK09265 179 NPTGAVYSKELLEEIVEIARQHNLIIFADEIYDKILYDGavhIS-IASLAPDLlcvTF--NGLSKAYrVAGFRVGWMV 253
PRK08361 PRK08361
aspartate aminotransferase; Provisional
168-405 4.02e-06

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 48.72  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 168 EAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTV---ESDELGVIPEDFERLCQQQHPKIA 244
Cdd:PRK08361  92 DVDNVIVTAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIplrEENEFQPDPDELLELITKRTRMIV 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 245 FLMPtvHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDT---PLLaSLAPDRTFLVNGLSKSVA-AGVRGGW 320
Cdd:PRK08361 172 INYP--NNPTGATLDKEVAKAIADIAEDYNIYILSDEPYEHFLYEGAkhyPMI-KYAPDNTILANSFSKTFAmTGWRLGF 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 321 VACPPHFAQRIKVTHRMITGGLPF---ILAETCARLVESGTA-HEIRKESVEElsRRVRLAR-EQLQGFDFQSHPHAPFL 395
Cdd:PRK08361 249 VIAPEQVIKDMIKLHAYIIGNVASfvqIAGIEALRSKESWKAvEEMRKEYNER--RKLVLKRlKEMPHIKVFEPKGAFYV 326
                        250
                 ....*....|
gi 516732207 396 WLKLPEPWMS 405
Cdd:PRK08361 327 FANIDETGMS 336
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
252-320 5.64e-06

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 48.58  E-value: 5.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732207 252 NPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDD---TPlLASLAPDrTFLV--NGLSKS-VAAGVRGGW 320
Cdd:PRK13355 292 NPTGALYPREVLQQIVDIAREHQLIIFSDEIYDRLVMDGlehTS-IASLAPD-LFCVtfSGLSKShMIAGYRIGW 364
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
252-349 7.91e-06

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: 48.11  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  252 NPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL--LASLAPDRTFLV-NGLSKS-VAAGVRGGWVAC-PPH 326
Cdd:TIGR01265 180 NPCGSVFSRDHLQKIAEVAEKLGIPIIADEIYGHMVFGDAPFipMASFASIVPVLSlGGISKRwVVPGWRLGWIIIhDPH 259
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 516732207  327 -------------FAQRIKVTHRMITGGLPFILAET 349
Cdd:TIGR01265 260 gifrdtvlqglknLLQRILGPATIVQGALPDILENT 295
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
219-345 1.34e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 47.41  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 219 TVESDELGVIPEDFERLCQqqHPKIAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPL-LASL 297
Cdd:PRK06348 142 TYEEDGFQINVKKLEALIT--SKTKAIILNSPNNPTGAVFSKETLEEIAKIAIEYDLFIISDEVYDGFSFYEDFVpMATL 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516732207 298 A--PDRTFLVNGLSKSVA-AGVRGGWVACPPHFAQRIKVTHRMITGGLPFI 345
Cdd:PRK06348 220 AgmPERTITFGSFSKDFAmTGWRIGYVIAPDYIIETAKIINEGICFSAPTI 270
PLN00145 PLN00145
tyrosine/nicotianamine aminotransferase; Provisional
243-349 8.83e-05

tyrosine/nicotianamine aminotransferase; Provisional


Pssm-ID: 215074 [Multi-domain]  Cd Length: 430  Bit Score: 44.76  E-value: 8.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 243 IAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPLL-----ASLAPDRTflVNGLSKS-VAAGV 316
Cdd:PLN00145 192 VAMVIINPNNPCGSVYSYEHLAKIAETARKLGILVIADEVYDHLTFGSKPFVpmgvfGEVAPVLT--LGSISKRwVVPGW 269
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 516732207 317 RGGWVA-CPPH-FAQRIKV-----THRMIT--------GGLPFILAET 349
Cdd:PLN00145 270 RLGWIAtCDPNgILKETKVvdsirNYLNIStdpatfvqGAIPQIIANT 317
PRK09764 PRK09764
GntR family transcriptional regulator;
11-78 1.64e-04

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 43.28  E-value: 1.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516732207  11 GSGPVYLRLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV 78
Cdd:PRK09764   2 GHKPLYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYV 69
PRK06107 PRK06107
aspartate transaminase;
252-324 1.79e-04

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 43.57  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 252 NPTVSIMPYERRVTIAAIARKH-GVWLIEDDLYGGMSGDDTPL--LASLAP---DRTFLVNGLSKSVA-AGVRGGWVACP 324
Cdd:PRK06107 177 NPTGAVYSRAELRALADVLLRHpHVLVLTDDIYDHIRFDDEPTphLLAAAPelrDRVLVTNGVSKTYAmTGWRIGYAAGP 256
MalY COG1168
Bifunctional PLP-dependent enzyme with beta-cystathionase and maltose regulon repressor ...
144-311 3.58e-04

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: 42.77  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 144 YSRNFPSnWFEAGRLWLA-RSGWMPEAENIVPTLGAHAAAISVIAAVSAPGDKIVFEHLTYTQVSRSARLLGRRTLTV-- 220
Cdd:COG1168   62 YTAPPDE-YYEAIIDWLKrRHGWEIDPEWIVFTPGVVPGLALAIRAFTEPGDGVLIQTPVYPPFFKAIENNGRELVENpl 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 221 -ESDELGVIP-EDFERLCQQqHPKiAFLM--PtvHNPTvsimpyeRRV-------TIAAIARKHGVWLIED----DL-YG 284
Cdd:COG1168  141 iLEDGRYRIDfDDLEAKLDP-GVK-LLLLcnP--HNPT-------GRVwtreeleRLAELCERHDVLVISDeihaDLvLP 209
                        170       180       190
                 ....*....|....*....|....*....|
gi 516732207 285 GMSgdDTPlLASLAP---DRTFLVNGLSKS 311
Cdd:COG1168  210 GHK--HTP-FASLSEeaaDRTITLTSPSKT 236
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
229-395 3.60e-04

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 42.55  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 229 PEDFERLCQQ---QHPKIAFLMPTVHNPTVSIMPYERrvtIAAIARKHGVWLIEDDLYG-GMSGDD--TPLLASLAPDRT 302
Cdd:cd06454  117 MEDLEKLLREarrPYGKKLIVTEGVYSMDGDIAPLPE---LVDLAKKYGAILFVDEAHSvGVYGPHgrGVEEFGGLTDDV 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 303 FLVNG-LSKsvAAGVRGGWVACPPHFAQRIKVTHRmitgglPFILAETCARLVESGTAHEIRK-----ESVEELSRRVRL 376
Cdd:cd06454  194 DIIMGtLGK--AFGAVGGYIAGSKELIDYLRSYAR------GFIFSTSLPPAVAAAALAALEVlqggpERRERLQENVRY 265
                        170       180
                 ....*....|....*....|....
gi 516732207 377 AREQLQ--GFDF---QSHPHAPFL 395
Cdd:cd06454  266 LRRGLKelGFPVggsPSHIIPPLI 289
PRK09990 PRK09990
DNA-binding transcriptional regulator GlcC; Provisional
20-86 6.80e-04

DNA-binding transcriptional regulator GlcC; Provisional


Pssm-ID: 182186 [Multi-domain]  Cd Length: 251  Bit Score: 41.29  E-value: 6.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516732207  20 ADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPP 86
Cdd:PRK09990  13 AERIERLIVDGVLKVGQALPSERRLCEKLGFSRSALREGLTVLRGRGIIETAQGRGSFVARLNRVQD 79
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
169-402 7.16e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 41.72  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 169 AENIVPTLGAHAAAISVIAAVSAPGDK-IVF-----EHLTYTQVSrsarllGRRTLTVESDELGVIPeDFERLCQQQHPK 242
Cdd:PRK06836  96 ADHIVMTCGAAGALNVALKAILNPGDEvIVFapyfvEYRFYVDNH------GGKLVVVPTDTDTFQP-DLDALEAAITPK 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 243 I-AFLMPTVHNPTVSIMPYERRVTIAAIARK------HGVWLIEDDLYGGMSGDDTpLLASLAP--DRTFLVNGLSKSVA 313
Cdd:PRK06836 169 TkAVIINSPNNPTGVVYSEETLKALAALLEEkskeygRPIYLISDEPYREIVYDGA-EVPYIFKyyDNSIVVYSFSKSLS 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 314 -AGVRGGWVACPPHFAQRIKVTHRMI--TGGLPFIlaetCA-----RLVesgtAHEIRKES-VEELSRRVRLAREQLQ-- 382
Cdd:PRK06836 248 lPGERIGYIAVNPEMEDADDLVAALVfaNRILGFV----NApalmqRVV----AKCLDATVdVSIYKRNRDLLYDGLTel 319
                        250       260
                 ....*....|....*....|
gi 516732207 383 GFDFQSHPHAPFLWLKLPEP 402
Cdd:PRK06836 320 GFECVKPQGAFYLFPKSPEE 339
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
18-93 8.76e-04

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 40.91  E-value: 8.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516732207  18 RLADSIESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYVLNRSETPPGEQI-DPL 93
Cdd:PRK10421   6 EVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRWRHETWSEQNIvQPL 82
PLN03026 PLN03026
histidinol-phosphate aminotransferase; Provisional
192-395 1.27e-03

histidinol-phosphate aminotransferase; Provisional


Pssm-ID: 178597  Cd Length: 380  Bit Score: 40.84  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 192 PGDKIVFEHLTYTQVSRSARLLGRRTLTV-ESDELGVIPEDFERLCQQQHPKIAFLMpTVHNPTVSIMPYERRVTIAAIA 270
Cdd:PLN03026 126 PGDKIIDCPPTFGMYVFDAAVNGAEVIKVpRTPDFSLDVPRIVEAVETHKPKLLFLT-SPNNPDGSIISDDDLLKILELP 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 271 rkhgVWLIEDDLYGGMSGDDTPLlaSLAPDRTFLV--NGLSKSVA-AGVRGGWVACPPHFAQ---RIKVthrmitgglPF 344
Cdd:PLN03026 205 ----ILVVLDEAYIEFSTQESRM--KWVKKYDNLIvlRTFSKRAGlAGLRVGYGAFPLSIIEylwRAKQ---------PY 269
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516732207 345 ---ILAET--CARLVESGTAHEIRKESVEElsrRVRLAReQLQGFDF-QSHP-HAPFL 395
Cdd:PLN03026 270 nvsVAAEVaaCAALSNPKYLEDVKNALVEE---RERLFG-LLKEVPFlEPYPsDANFI 323
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
252-349 1.46e-03

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: 40.92  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207  252 NPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGM--SGDDTPLLASLAPDRTFLV-NGLSKS-VAAGVRGGWVACPPHF 327
Cdd:TIGR01264 179 NPCGSVFSRQHLEEILAVAERQCLPIIADEIYGDMvfSGATFEPLASLSSTVPILScGGLAKRwLVPGWRLGWIIIHDRR 258
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 516732207  328 -------------AQRIKVTHRMITGGLPFILAET 349
Cdd:TIGR01264 259 gilrdirdglvklSQRILGPCTIVQGALPSILLRT 293
PRK07683 PRK07683
aminotransferase A; Validated
246-336 1.97e-03

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 40.48  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 246 LMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTPLlaSLA-----PDRTFLVNGLSKSVA-AGVRGG 319
Cdd:PRK07683 166 VLPYPSNPTGVTLSKEELQDIADVLKDKNIFVLSDEIYSELVYEQPHT--SIAhfpemREKTIVINGLSKSHSmTGWRIG 243
                         90
                 ....*....|....*..
gi 516732207 320 WVACPPHFAQRIKVTHR 336
Cdd:PRK07683 244 FLFAPSYLAKHILKVHQ 260
pdhR PRK09464
pyruvate dehydrogenase complex transcriptional repressor PdhR;
18-86 2.35e-03

pyruvate dehydrogenase complex transcriptional repressor PdhR;


Pssm-ID: 181879 [Multi-domain]  Cd Length: 254  Bit Score: 39.62  E-value: 2.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516732207  18 RLADSI----ESAISSGALPAGSKLPPQRNLAYDIGVTIGTIGRAYALVHERGLVAGEVGRGTYV---LNRSETPP 86
Cdd:PRK09464  10 KLSDVIeqqlEFLILEGTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGGGTFVqssLWQSFSDP 85
PRK08636 PRK08636
LL-diaminopimelate aminotransferase;
230-402 2.42e-03

LL-diaminopimelate aminotransferase;


Pssm-ID: 236316  Cd Length: 403  Bit Score: 40.07  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 230 EDFERLCQQQHPKIAFLM---PtvHNPT---VSIMPYERRVtiaAIARKHGVWLIEDDLYGGMSGDD--TP--LLASLAP 299
Cdd:PRK08636 163 ENLEKALRESSPKPKYVVvnfP--HNPTtatVEKSFYERLV---ALAKKERFYIISDIAYADITFDGykTPsiLEVEGAK 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 300 DRTFLVNGLSKSV-AAGVRGGWVACPPHFA---QRIK--VTHRMITgglPFILAETCARLVESGTAHEIRKesVEELSRR 373
Cdd:PRK08636 238 DVAVESYTLSKSYnMAGWRVGFVVGNKKLVgalKKIKswLDYGMFT---PIQVAATIALDGDQSCVEEIRE--TYRKRRD 312
                        170       180
                 ....*....|....*....|....*....
gi 516732207 374 VRLAREQLQGFDFQSHPHAPFLWLKLPEP 402
Cdd:PRK08636 313 VLIESFANAGWELQKPRASMFVWAKIPEP 341
PLN00143 PLN00143
tyrosine/nicotianamine aminotransferase; Provisional
243-366 2.49e-03

tyrosine/nicotianamine aminotransferase; Provisional


Pssm-ID: 165711 [Multi-domain]  Cd Length: 409  Bit Score: 40.00  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 243 IAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTP-----LLASLAPDRTflVNGLSKS-VAAGV 316
Cdd:PLN00143 172 IAMVIINPGNPCGSVYSYEHLNKIAETARKLGILVIADEVYGHIVFGSKPfvpmgLFASIVPVIT--LGSISKRwMIPGW 249
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516732207 317 RGGW-VACPP-------HFAQRIK-------VTHRMITGGLPFILAETCARLVeSGTAHEIRKES 366
Cdd:PLN00143 250 GLGWlVTCDPsgllqicEIADSIKkalnpapFPPTFIQAAIPEILEKTTEDFF-SKTINILRAAL 313
PRK07681 PRK07681
LL-diaminopimelate aminotransferase;
192-463 4.32e-03

LL-diaminopimelate aminotransferase;


Pssm-ID: 181081  Cd Length: 399  Bit Score: 39.40  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 192 PGDKIVFEHLTYTQVSRSARLLGRRT----LTVESD---ELGVIPEDFerlcqQQHPKIAFL-MPTVHNPTVSIMPYERR 263
Cdd:PRK07681 116 PGDIILVPDPGYTAYETGIQMAGATSyympLKKENDflpDLELIPEEI-----ADKAKMMILnFPGNPVPAMAHEDFFKE 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 264 VTiaAIARKHGVWLIEDDLYGGMSGDDTPLLASLAPDRTFLV----NGLSKSVA-AGVRGGWVACPPHFAQRIKVTHRMI 338
Cdd:PRK07681 191 VI--AFAKKHNIIVVHDFAYAEFYFDGNKPISFLSVPGAKEVgveiNSLSKSYSlAGSRIGYMIGNEEIVRALTQFKSNT 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 339 TGGLPFILAETCARLVESGTAHEIRKESVEELSRRVRLAREQLQGFDFQSHPHAPFLWLKLPEPWMSGTFKNAAF-RDGV 417
Cdd:PRK07681 269 DYGVFLPIQKAACAALRNGAAFCEKNRGIYQERRDTLVDGFRTFGWNVDKPAGSMFVWAEIPKGWTSLSFAYALMdRANV 348
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 516732207 418 LVDDEDEFkAARGEKTyhrVRIGFSSPKTgqelvsglmILRRLLEN 463
Cdd:PRK07681 349 VVTPGHAF-GPHGEGF---VRIALVQDEE---------VLQQAVEN 381
PLN02656 PLN02656
tyrosine transaminase
243-393 7.95e-03

tyrosine transaminase


Pssm-ID: 178262 [Multi-domain]  Cd Length: 409  Bit Score: 38.37  E-value: 7.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 243 IAFLMPTVHNPTVSIMPYERRVTIAAIARKHGVWLIEDDLYGGMSGDDTP-----LLASLAPDRTflVNGLSKS-VAAGV 316
Cdd:PLN02656 171 VALVIINPGNPCGNVYSYQHLKKIAETAEKLKILVIADEVYGHLAFGSNPfvpmgVFGSIVPVLT--LGSLSKRwIVPGW 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516732207 317 RGGWVACP--------PHFAQRIKVTHRMITGGLPFILAeTCARLVESgTAHEIRKESVEELSRRVRLAREQLQGFDFQS 388
Cdd:PLN02656 249 RLGWFVTTdpsgsfrdPKIVERIKKYFDILGGPATFIQA-AVPTILEQ-TDESFFKKTINILKQSSDICCDRIKEIPCIT 326

                 ....*
gi 516732207 389 HPHAP 393
Cdd:PLN02656 327 CPHKP 331
 
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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