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Conserved domains on  [gi|1340571705|gb|POX04802|]
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PLP-dependent aminotransferase family protein [Serratia marcescens]

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 ...
 1-478 8.49e-155

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: 448.51  E-value: 8.49e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705   1 MTLLDETPDTRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPA 80
Cdd:COG1167     3 IRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  81 LkmASAPSGRIEPPADDVLALIdtvfaaQQNPAFTNIALACPQTSDFyPGGKLGRMLSSQLRRQPDLIGQYSLPPGSLRL 160
Cdd:COG1167    83 P--APAPRAAAAVAAPALRRLL------EAAPGVIDLGSGAPDPDLF-PLAALRRALRRALRRLPPALLGYGDPQGLPEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 161 RQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQlGLSLDA 240
Cdd:COG1167   154 REAIARYLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDED-GLDLDA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 241 LELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGWVLFCSSF 320
Cdd:COG1167   233 LEAALRRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 321 TKTLAPDFRVGWI-CGGRFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDEARALIARHFPRG 399
Cdd:COG1167   313 SKTLAPGLRLGYLvAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDG 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340571705 400 TLATQPAGGFVFWVEFPPNVDSVALFHQLLEEQICLTPGTLYSPSGRYRNALRLSCCYPFNARYTQALARLGARACEMS 478
Cdd:COG1167   393 LRVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLRELA 471
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 1-478 8.49e-155

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: 448.51  E-value: 8.49e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705   1 MTLLDETPDTRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPA 80
Cdd:COG1167     3 IRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  81 LkmASAPSGRIEPPADDVLALIdtvfaaQQNPAFTNIALACPQTSDFyPGGKLGRMLSSQLRRQPDLIGQYSLPPGSLRL 160
Cdd:COG1167    83 P--APAPRAAAAVAAPALRRLL------EAAPGVIDLGSGAPDPDLF-PLAALRRALRRALRRLPPALLGYGDPQGLPEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 161 RQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQlGLSLDA 240
Cdd:COG1167   154 REAIARYLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDED-GLDLDA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 241 LELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGWVLFCSSF 320
Cdd:COG1167   233 LEAALRRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 321 TKTLAPDFRVGWI-CGGRFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDEARALIARHFPRG 399
Cdd:COG1167   313 SKTLAPGLRLGYLvAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDG 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340571705 400 TLATQPAGGFVFWVEFPPNVDSVALFHQLLEEQICLTPGTLYSPSGRYRNALRLSCCYPFNARYTQALARLGARACEMS 478
Cdd:COG1167   393 LRVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLRELA 471
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 140-472 3.22e-50

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: 174.84  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 140 QLRRQPDLIGQYSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLL 218
Cdd:cd00609    21 AAAALRAGLLGYYPDPGLPELREAIAEWlGRRGGVDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 219 ASLGLKALEIPTDPQLG-LSLDALELLLNEKRLNAVIAMPtVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQF 297
Cdd:cd00609   101 RLAGAEVVPVPLDEEGGfLLDLELLEAAKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELVY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 298 GGALSPAVKAFDRDGWVLFCSSFTKTLA-PDFRVGWICG--GRFHEALRKLKAVSSMSESQLLSETLATFLESGgyDHHL 374
Cdd:cd00609   180 DGEPPPALALLDAYERVIVLRSFSKTFGlPGLRIGYLIAppEELLERLKKLLPYTTSGPSTLSQAAAAAALDDG--EEHL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 375 RNLRKRYAAQVDEARALIARHFPRGTlaTQPAGGFVFWVEFPPNVDSVALFHQLLEEQICLTPGTLYSPSGryRNALRLS 454
Cdd:cd00609   258 EELRERYRRRRDALLEALKELGPLVV--VKPSGGFFLWLDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGG--EGFVRLS 333

                         330
                  ....*....|....*...
gi 1340571705 455 CCYPFnARYTQALARLGA 472
Cdd:cd00609   334 FATPE-EELEEALERLAE 350
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 17-424 3.04e-24

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 104.74  E-value: 3.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  17 DTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPALKMASAPSGrieppad 96
Cdd:PRK15481   12 DSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPG------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  97 dvLALIDTvfaAQQNPAFTNIalacPQTSDFYPGgklgrmlssqLRRQPDLIGQYSLPPGslrlRQQIARRSMTLGMlLE 176
Cdd:PRK15481   85 --TPLHDL---AGGNPDPQRL----PDLSRYFAR----------LSRTPRLYGDAPVSPE----LHAWAARWLRDDC-PV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 177 PGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQLGLSLDALELLLNEKRlnAVIAM 256
Cdd:PRK15481  141 AFEIDLTSGAIDAIERLLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGAR--AVILT 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 257 PTVQNPLGCTMPLAAKKRLARLMNDH-QVPLIEDGLYAEIQFGGALSPAVKAFDRdgWVLFcSSFTKTLAPDFRVGWI-C 334
Cdd:PRK15481  219 PRAHNPTGCSLSARRAAALRNLLARYpQVLVIIDDHFALLSSSPYHSVIPQTTQR--WALI-RSVSKALGPDLRLAFVaS 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 335 GGRFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDE-ARALIARHFPRGTlatqPAGGFVFWV 413
Cdd:PRK15481  296 DSATSARLRLRLNSGTQWVSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKlARALQQYGIAIPS----PGDGLNLWL 371

                         410
                  ....*....|.
gi 1340571705 414 EFPPNVDSVAL 424
Cdd:PRK15481  372 PLDTDSQATAL 382
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
150-470 4.55e-16

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 79.27  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 150 QYSLPPGSLRLRQQIAR-RSMTLGMLLEPGD-VVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALE 227
Cdd:pfam00155  34 LYGPTDGHPELREALAKfLGRSPVLKLDREAaVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 228 IPTDPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKA 307
Cdd:pfam00155 114 YPLYDSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRA 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 308 F-DRDGWVLFCSSFTKTLA-PDFRVGWICGgrfHEALRK--LKAVSSMSESQLLSETLATFLE-SGGYDHHLRNLRKRYA 382
Cdd:pfam00155 194 LlAEGPNLLVVGSFSKAFGlAGWRVGYILG---NAAVISqlRKLARPFYSSTHLQAAAAAALSdPLLVASELEEMRQRIK 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 383 AQVDEARALIARhfpRGTLATQPAGGFVFWVEFPPNVDsVALFHQLLEEQ-ICLTPGTLYSPSGRyrnaLRLSCCYPFNA 461
Cdd:pfam00155 271 ERRDYLRDGLQA---AGLSVLPSQAGFFLLTGLDPETA-KELAQVLLEEVgVYVTPGSSPGVPGW----LRITVAGGTEE 342


                  ....*....
gi 1340571705 462 RYTQALARL 470
Cdd:pfam00155 343 ELEELLEAI 351
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
 156-448 4.55e-16

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: 79.83  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 156 GSLRLRQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTY--FYLLPLLASLGLKALEIPTDPQ 233
Cdd:TIGR01264  74 GALSAREAIASYYHNPDGPIEADDVVLCSGCSHAIEMCIAALANAGQNILVPRPGFplYETLAESMGIEVKLYNLLPDKS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 234 LGLSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGW 313
Cdd:TIGR01264 154 WEIDLKQLESLIDEKTAALIVNNPS--NPCGSVFSRQHLEEILAVAERQCLPIIADEIYGDMVFSGATFEPLASLSSTVP 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 314 VLFCSSFTKT-LAPDFRVGWIC----GGRFHEALRKLKAVS-------SMSESQLLSETLATfleSGGYDHHLRNLRKRY 381
Cdd:TIGR01264 232 ILSCGGLAKRwLVPGWRLGWIIihdrRGILRDIRDGLVKLSqrilgpcTIVQGALPSILLRT---PQEYFDGTLSVLESN 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340571705 382 AAQVDEARALIarhfpRGTLATQPAGGFVFWV-----EFPPNVDSVALFHQLLEEQ--ICLtPGTLYSPSGRYR 448
Cdd:TIGR01264 309 AMLCYGALAAV-----PGLRPVMPSGAMYMMVgiemeHFPEFKNDVEFTERLVAEQsvFCL-PGSCFEYPGFFR 376
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
15-74 1.63e-13

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 64.90  E-value: 1.63e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705   15 LADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYV 74
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
 
Name Accession Description Interval E-value
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 1-478 8.49e-155

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: 448.51  E-value: 8.49e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705   1 MTLLDETPDTRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPA 80
Cdd:COG1167     3 IRLDRDSSGPLYLQLADALREAILSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAARLPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  81 LkmASAPSGRIEPPADDVLALIdtvfaaQQNPAFTNIALACPQTSDFyPGGKLGRMLSSQLRRQPDLIGQYSLPPGSLRL 160
Cdd:COG1167    83 P--APAPRAAAAVAAPALRRLL------EAAPGVIDLGSGAPDPDLF-PLAALRRALRRALRRLPPALLGYGDPQGLPEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 161 RQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQlGLSLDA 240
Cdd:COG1167   154 REAIARYLARRGVPASPDQILITSGAQQALDLALRALLRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDED-GLDLDA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 241 LELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGWVLFCSSF 320
Cdd:COG1167   233 LEAALRRHRPRAVYVTPSHQNPTGATMSLERRRALLELARRHGVPIIEDDYDSELRYDGRPPPPLAALDAPGRVIYIGSF 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 321 TKTLAPDFRVGWI-CGGRFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDEARALIARHFPRG 399
Cdd:COG1167   313 SKTLAPGLRLGYLvAPGRLIERLARLKRATDLGTSPLTQLALAEFLESGHYDRHLRRLRREYRARRDLLLAALARHLPDG 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340571705 400 TLATQPAGGFVFWVEFPPNVDSVALFHQLLEEQICLTPGTLYSPSGRYRNALRLSCCYPFNARYTQALARLGARACEMS 478
Cdd:COG1167   393 LRVTGPPGGLHLWLELPEGVDAEALAAAALARGILVAPGSAFSADGPPRNGLRLGFGAPSEEELEEALRRLAELLRELA 471
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 140-472 3.22e-50

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: 174.84  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 140 QLRRQPDLIGQYSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLL 218
Cdd:cd00609    21 AAAALRAGLLGYYPDPGLPELREAIAEWlGRRGGVDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 219 ASLGLKALEIPTDPQLG-LSLDALELLLNEKRLNAVIAMPtVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQF 297
Cdd:cd00609   101 RLAGAEVVPVPLDEEGGfLLDLELLEAAKTPKTKLLYLNN-PNNPTGAVLSEEELEELAELAKKHGILIISDEAYAELVY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 298 GGALSPAVKAFDRDGWVLFCSSFTKTLA-PDFRVGWICG--GRFHEALRKLKAVSSMSESQLLSETLATFLESGgyDHHL 374
Cdd:cd00609   180 DGEPPPALALLDAYERVIVLRSFSKTFGlPGLRIGYLIAppEELLERLKKLLPYTTSGPSTLSQAAAAAALDDG--EEHL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 375 RNLRKRYAAQVDEARALIARHFPRGTlaTQPAGGFVFWVEFPPNVDSVALFHQLLEEQICLTPGTLYSPSGryRNALRLS 454
Cdd:cd00609   258 EELRERYRRRRDALLEALKELGPLVV--VKPSGGFFLWLDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGG--EGFVRLS 333

                         330
                  ....*....|....*...
gi 1340571705 455 CCYPFnARYTQALARLGA 472
Cdd:cd00609   334 FATPE-EELEEALERLAE 350
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 150-472 3.98e-25

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: 106.75  E-value: 3.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 150 QYSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEI 228
Cdd:COG0436    62 GYTPSAGIPELREAIAAYyKRRYGVDLDPDEILVTNGAKEALALALLALLNPGDEVLVPDPGYPSYRAAVRLAGGKPVPV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 229 PTDPQLGlsldaleLLLNEKRLNAVIAMPTV-------QNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGAl 301
Cdd:COG0436   142 PLDEENG-------FLPDPEALEAAITPRTKaivlnspNNPTGAVYSREELEALAELAREHDLLVISDEIYEELVYDGA- 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 302 sPAVKAFDRDGW---VLFCSSFTKTLA-PDFRVGWICGG-RFHEALRKLKAVSSMSESQLLSETLATFLEsgGYDHHLRN 376
Cdd:COG0436   214 -EHVSILSLPGLkdrTIVINSFSKSYAmTGWRIGYAVGPpELIAALLKLQSNLTSCAPTPAQYAAAAALE--GPQDYVEE 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 377 LRKRYAAQVDEARALIARHfprGTLATQPAGGFVFWVEFPP-NVDSVALFHQLLEEQ-ICLTPGTLYSPSGryRNALRLS 454
Cdd:COG0436   291 MRAEYRRRRDLLVEGLNEI---GLSVVKPEGAFYLFADVPElGLDSEEFAERLLEEAgVAVVPGSAFGPAG--EGYVRIS 365

                         330
                  ....*....|....*...
gi 1340571705 455 CCYPfNARYTQALARLGA 472
Cdd:COG0436   366 YATS-EERLEEALERLAR 382
PRK15481 PRK15481
transcriptional regulatory protein PtsJ; Provisional
 17-424 3.04e-24

transcriptional regulatory protein PtsJ; Provisional


Pssm-ID: 185378 [Multi-domain]  Cd Length: 431  Bit Score: 104.74  E-value: 3.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  17 DTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPALKMASAPSGrieppad 96
Cdd:PRK15481   12 DSIRQLIQAGRLRPGDSLPPVRELASELGVNRNTVAAAYKRLVTAGLAQSQGRNGTVIRGSPSPVALEGGDPG------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  97 dvLALIDTvfaAQQNPAFTNIalacPQTSDFYPGgklgrmlssqLRRQPDLIGQYSLPPGslrlRQQIARRSMTLGMlLE 176
Cdd:PRK15481   85 --TPLHDL---AGGNPDPQRL----PDLSRYFAR----------LSRTPRLYGDAPVSPE----LHAWAARWLRDDC-PV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 177 PGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQLGLSLDALELLLNEKRlnAVIAM 256
Cdd:PRK15481  141 AFEIDLTSGAIDAIERLLCAHLLPGDSVAVEDPCFLSSINMLRYAGFSASPVSVDAEGMQPEKLERALAQGAR--AVILT 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 257 PTVQNPLGCTMPLAAKKRLARLMNDH-QVPLIEDGLYAEIQFGGALSPAVKAFDRdgWVLFcSSFTKTLAPDFRVGWI-C 334
Cdd:PRK15481  219 PRAHNPTGCSLSARRAAALRNLLARYpQVLVIIDDHFALLSSSPYHSVIPQTTQR--WALI-RSVSKALGPDLRLAFVaS 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 335 GGRFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDE-ARALIARHFPRGTlatqPAGGFVFWV 413
Cdd:PRK15481  296 DSATSARLRLRLNSGTQWVSHLLQDLVYACLTDPEYQARLAQARLFYAQRRQKlARALQQYGIAIPS----PGDGLNLWL 371

                         410
                  ....*....|.
gi 1340571705 414 EFPPNVDSVAL 424
Cdd:PRK15481  372 PLDTDSQATAL 382
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 10-75 5.34e-21

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: 86.35  E-value: 5.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1340571705  10 TRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVR 75
Cdd:cd07377     1 PLYEQIADQLREAILSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
12-82 7.48e-21

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 87.54  E-value: 7.48e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340571705  12 YLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPALK 82
Cdd:COG1725    12 YEQIADQIKEAIASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFVAEDARELL 82
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
150-470 4.55e-16

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 79.27  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 150 QYSLPPGSLRLRQQIAR-RSMTLGMLLEPGD-VVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALE 227
Cdd:pfam00155  34 LYGPTDGHPELREALAKfLGRSPVLKLDREAaVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 228 IPTDPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKA 307
Cdd:pfam00155 114 YPLYDSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRA 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 308 F-DRDGWVLFCSSFTKTLA-PDFRVGWICGgrfHEALRK--LKAVSSMSESQLLSETLATFLE-SGGYDHHLRNLRKRYA 382
Cdd:pfam00155 194 LlAEGPNLLVVGSFSKAFGlAGWRVGYILG---NAAVISqlRKLARPFYSSTHLQAAAAAALSdPLLVASELEEMRQRIK 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 383 AQVDEARALIARhfpRGTLATQPAGGFVFWVEFPPNVDsVALFHQLLEEQ-ICLTPGTLYSPSGRyrnaLRLSCCYPFNA 461
Cdd:pfam00155 271 ERRDYLRDGLQA---AGLSVLPSQAGFFLLTGLDPETA-KELAQVLLEEVgVYVTPGSSPGVPGW----LRITVAGGTEE 342


                  ....*....
gi 1340571705 462 RYTQALARL 470
Cdd:pfam00155 343 ELEELLEAI 351
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
 156-448 4.55e-16

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: 79.83  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 156 GSLRLRQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTY--FYLLPLLASLGLKALEIPTDPQ 233
Cdd:TIGR01264  74 GALSAREAIASYYHNPDGPIEADDVVLCSGCSHAIEMCIAALANAGQNILVPRPGFplYETLAESMGIEVKLYNLLPDKS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 234 LGLSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGW 313
Cdd:TIGR01264 154 WEIDLKQLESLIDEKTAALIVNNPS--NPCGSVFSRQHLEEILAVAERQCLPIIADEIYGDMVFSGATFEPLASLSSTVP 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 314 VLFCSSFTKT-LAPDFRVGWIC----GGRFHEALRKLKAVS-------SMSESQLLSETLATfleSGGYDHHLRNLRKRY 381
Cdd:TIGR01264 232 ILSCGGLAKRwLVPGWRLGWIIihdrRGILRDIRDGLVKLSqrilgpcTIVQGALPSILLRT---PQEYFDGTLSVLESN 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340571705 382 AAQVDEARALIarhfpRGTLATQPAGGFVFWV-----EFPPNVDSVALFHQLLEEQ--ICLtPGTLYSPSGRYR 448
Cdd:TIGR01264 309 AMLCYGALAAV-----PGLRPVMPSGAMYMMVgiemeHFPEFKNDVEFTERLVAEQsvFCL-PGSCFEYPGFFR 376
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
15-74 1.63e-13

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 64.90  E-value: 1.63e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705   15 LADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYV 74
Cdd:smart00345   1 VAERLREDIVSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
6-76 1.82e-12

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 66.81  E-value: 1.82e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340571705   6 ETPDTRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRS 76
Cdd:COG2188     1 SSPVPLYLQIADALRERIESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAE 71
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 12-74 2.87e-12

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


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 61.48  E-value: 2.87e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340571705  12 YLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYV 74
Cdd:pfam00392   2 YEQVYARLREDILSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
10-80 6.48e-12

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 65.34  E-value: 6.48e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340571705  10 TRYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPA 80
Cdd:COG2186     7 SLAEQVAEQLRELILSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVREPSPW 77
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 151-448 2.09e-10

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: 62.36  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTY--FYLLPLLASLGLKALE 227
Cdd:TIGR01265  69 YAPSVGALAAREAVAEYlSSDLPGKLTADDVVLTSGCSQAIEICIEALANPGANILVPRPGFplYDTRAAFSGLEVRLYD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 228 IPTDPQLGLSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKA 307
Cdd:TIGR01265 149 LLPEKDWEIDLDGLESLADEKTVAIVVINPS--NPCGSVFSRDHLQKIAEVAEKLGIPIIADEIYGHMVFGDAPFIPMAS 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 308 FDRDGWVLFCSSFTKT-LAPDFRVGWIC----GGRF-HEALRKLKAVSSMS--ESQLLSETLATFLESG--GYDHHLRNL 377
Cdd:TIGR01265 227 FASIVPVLSLGGISKRwVVPGWRLGWIIihdpHGIFrDTVLQGLKNLLQRIlgPATIVQGALPDILENTpqEFFDGKISV 306

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1340571705 378 RKRYAAQVDEARALIarhfpRGTLATQPAGGFVFWVE-----FPPNVDSVALFHQLLEEQ--ICLtPGTLYSPSGRYR 448
Cdd:TIGR01265 307 LKSNAELCYEELKDI-----PGLVCPKPEGAMYLMVKlelelFPEIKDDVDFCEKLAREEsvICL-PGSAFGLPNWVR 378
PRK08363 PRK08363
alanine aminotransferase; Validated
 151-409 1.88e-09

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 59.44  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARRSMT-LGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIP 229
Cdd:PRK08363   66 YGPSEGLPELREAIVKREKRkNGVDITPDDVRVTAAVTEALQLIFGALLDPGDEILIPGPSYPPYTGLVKFYGGVPVEYR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 230 TDPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGA-LSPAvkAF 308
Cdd:PRK08363  146 TIEEEGWQPDIDDIRKKITEKTKAIAVINPNNPTGALYEKKTLKEILDIAGEHDLPVISDEIYDLMTYEGKhVSPG--SL 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 309 DRDGWVLFCSSFTKT-LAPDFRVGWICGGRFHEALRKLK-AVSSMSESQLLSETLATFLESGGYDHHLRNLrKRYAAQVD 386
Cdd:PRK08363  224 TKDVPVIVMNGLSKVyFATGWRLGYIYFVDPEGKLAEVReAIDKLARIRLCPNTPAQFAAIAGLTGPMDYL-EEYMKKLK 302

                         250       260
                  ....*....|....*....|....*
gi 1340571705 387 EARALIARHFPR--GTLATQPAGGF 409
Cdd:PRK08363  303 ERRDYIYKRLNEipGISTTKPQGAF 327
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 139-433 8.39e-08

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: 53.98  E-value: 8.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 139 SQLRRQPDligqyslpPGSLRLRQQIARRsmtLGmlLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLL 218
Cdd:COG0079    40 DALNRYPD--------PDATALREALAEY---YG--VPPEQVLVGNGSDELIQLLARAFLGPGDEVLVPEPTFSEYPIAA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 219 ASLGLKALEIPTDPQLGLSLDALELLLNEK-RLnAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHqVPLIEDGLYAEiqF 297
Cdd:COG0079   107 RAAGAEVVEVPLDEDFSLDLDALLAAITERtDL-VFLCNPN--NPTGTLLPREELEALLEALPAD-GLVVVDEAYAE--F 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 298 GGALSPAVKAFDRDGWVLFCSSFTKTLA-PDFRVGWICGgrfH----EALRKLK---AVSSmsesqlLSETLATF-LEsg 368
Cdd:COG0079   181 VPEEDSALPLLARYPNLVVLRTFSKAYGlAGLRLGYAIA---SpeliAALRRVRgpwNVNS------LAQAAALAaLE-- 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1340571705 369 gYDHHLRnlrkRYAAQVDEARALIARHFPRGTLATQPAGG-FVfWVEFPPnvDSVALFHQLLEEQI 433
Cdd:COG0079   250 -DRAYLE----ETRARLRAERERLAAALRALGLTVYPSQAnFV-LVRVPE--DAAELFEALLERGI 307
PRK07550 PRK07550
aminotransferase;
151-473 9.27e-08

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 54.19  E-value: 9.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIP 229
Cdd:PRK07550   63 YGPVEGLPELREAYAAHySRLYGAAISPEQVHITSGCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGIRPVYLP 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 230 TDPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGAlsPAVKAFD 309
Cdd:PRK07550  143 CDEGPGLLPDPAAAEALITPRTRAIALVTPNNPTGVVYPPELLHELYDLARRHGIALILDETYRDFDSGGG--APHDLFA 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 310 RDGW---VLFCSSFTKTLA-PDFRVGWICGG--RFHEAlrkLKAVSSMS--ESQLLSETLATFLEsggydhHLRNLRKRY 381
Cdd:PRK07550  221 DPDWddtLVHLYSFSKSYAlTGHRVGAVVASpaRIAEI---EKFMDTVAicAPRIGQIAVAWGLP------NLADWRAGN 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 382 AAQVDEARALIARHFPR-GTLATQPAGGFVFWVEFP-PNVDSVALFHQLLEEQ--ICLtPGTLYSPSGryRNALRLSccy 457
Cdd:PRK07550  292 RAEIARRRDAFRAVFARlPGWELLASGAYFAYVRHPfPDRPSREVARRLAKEAgiLCL-PGTMFGPGQ--EGYLRLA--- 365

                         330
                  ....*....|....*..
gi 1340571705 458 pF-NARyTQALARLGAR 473
Cdd:PRK07550  366 -FaNAD-VAGIGELVER 380
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
161-439 1.57e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 53.27  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 161 RQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTY----FYllplLASLGLKALEIPTDP--- 232
Cdd:PRK06836   79 REAIAESlNRRFGTPLTADHIVMTCGAAGALNVALKAILNPGDEVIVFAPYFveyrFY----VDNHGGKLVVVPTDTdtf 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 233 QLGLSLDalelllnEKRLN----AVIaMPTVQNPLGCTMPLAAKKRLARLMND------HQVPLIEDGLYAEIQFGGALS 302
Cdd:PRK06836  155 QPDLDAL-------EAAITpktkAVI-INSPNNPTGVVYSEETLKALAALLEEkskeygRPIYLISDEPYREIVYDGAEV 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 303 PAV-KAFDRdgwVLFCSSFTKTLA-PDFRVGWIcggrfhealrklkAVSS-MSESQLLSETL-------------ATFle 366
Cdd:PRK06836  227 PYIfKYYDN---SIVVYSFSKSLSlPGERIGYI-------------AVNPeMEDADDLVAALvfanrilgfvnapALM-- 288

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1340571705 367 sggydhhLRNLRKRYAAQVD-----EARALIARHFPR-GTLATQPAGGFVFWVEfPPNVDSVALFHQLLEEQICLTPGT 439
Cdd:PRK06836  289 -------QRVVAKCLDATVDvsiykRNRDLLYDGLTElGFECVKPQGAFYLFPK-SPEEDDVAFCEKAKKHNLLLVPGS 359
PRK07682 PRK07682
aminotransferase;
151-445 4.19e-07

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 52.04  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARR-SMTLGMLLEPGD-VVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEI 228
Cdd:PRK07682   53 YTANAGLLELRQEIAKYlKKRFAVSYDPNDeIIVTVGASQALDVAMRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPV 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 229 PT--DPQLGLSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALS--PA 304
Cdd:PRK07682  133 ATtlENEFKVQPAQIEAAITAKTKAILLCSPN--NPTGAVLNKSELEEIAVIVEKHDLIVLSDEIYAELTYDEAYTsfAS 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 305 VKAFdRDGWVLFcSSFTKTLA-PDFRVGWICG-GRFHEALRKLKAVSSMSesqllSETLATF-----LESGGYDhhLRNL 377
Cdd:PRK07682  211 IKGM-RERTILI-SGFSKGFAmTGWRLGFIAApVYFSEAMLKIHQYSMMC-----APTMAQFaaleaLRAGNDD--VIRM 281

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1340571705 378 RKRYAAQvdeaRALIARHFPR-GTLATQPAGGF-VFwvefpPNVDSVALFHQ------LLEEQICLTPGTLYSPSG 445
Cdd:PRK07682  282 RDSYRKR----RNFFVTSFNEiGLTCHVPGGAFyAF-----PSISSTGLSSEefaeqlLLEEKVAVVPGSVFGESG 348
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
14-76 4.94e-07

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 50.69  E-value: 4.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340571705  14 QLADTLAEAIRRGTLLPGDRLpSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRS 76
Cdd:COG1802    15 QVYEALREAILSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAP 76
PRK09764 PRK09764
GntR family transcriptional regulator;
11-75 1.10e-06

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 49.83  E-value: 1.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340571705  11 RYLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVR 75
Cdd:PRK09764    6 LYRQIADRIREQIARGELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYVK 70
PTZ00433 PTZ00433
tyrosine aminotransferase; Provisional
 254-448 1.89e-06

tyrosine aminotransferase; Provisional


Pssm-ID: 185613  Cd Length: 412  Bit Score: 50.17  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 254 IAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFDRDGWVLFCSSFTKTL-APDFRVGW 332
Cdd:PTZ00433  181 LIMTNPSNPCGSNFSRKHVEDIIRLCEELRLPLISDEIYAGMVFNGATFTSVADFDTTVPRVILGGTAKNLvVPGWRLGW 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 333 IC-------GGRFHEALRKLKAVSSMSESqLLSETLATFLESGGYDHHlrnlrKRYAAQVDEARALIARHFPR--GTLAT 403
Cdd:PTZ00433  261 LLlvdphgnGGDFLDGMKRLGMLVCGPCS-VVQAALGEALLNTPQEHL-----EQIVAKLEEGAMVLYNHIGEciGLSPT 334

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1340571705 404 QPAGGFVFWV-----EFPPNVDSVALFHQLLEEQ-ICLTPGTLYSPSGRYR 448
Cdd:PTZ00433  335 MPRGSMFLMSrldleKFRDIKSDVEFYEKLLEEEnVQVLPGEIFHMPGFTR 385
PRK11523 PRK11523
transcriptional regulator ExuR;
12-92 2.31e-06

transcriptional regulator ExuR;


Pssm-ID: 183176 [Multi-domain]  Cd Length: 253  Bit Score: 49.07  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705  12 YLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPalKMASAPSGRI 91
Cdd:PRK11523   10 YQQLAAELKERIEQGVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSGIHVVSNQP--RHQQAADNNM 87


                  .
gi 1340571705  92 E 92
Cdd:PRK11523   88 E 88
avtA PRK09440
valine--pyruvate transaminase; Provisional
 253-438 4.96e-06

valine--pyruvate transaminase; Provisional


Pssm-ID: 236517  Cd Length: 416  Bit Score: 48.70  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 253 VIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEiQFGGALSPAVKAFDRDGWVLfCSSFTKTLAPDFRVGW 332
Cdd:PRK09440  184 CVSRPT--NPTGNVLTDEELEKLDALARQHNIPLLIDNAYGP-PFPGIIFSEATPLWNPNIIL-CMSLSKLGLPGVRCGI 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 333 ICGG-RFHEALRKLKAVSSMSESQLLSETLATFLESGGYDHHLRN-LRKRYAAQVDEARALIARHFPR-GTLATQPAGGF 409
Cdd:PRK09440  260 VIADeEIIEALSNMNGIISLAPGRLGPAIAAEMIESGDLLRLSETvIRPFYRQKVQLAIALLRRYLPDePCLIHKPEGAI 339

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1340571705 410 VFWVEFP--PnVDSVALFHQLLEEQICLTPG 438
Cdd:PRK09440  340 FLWLWFKdlP-ITTEELYQRLKARGVLVVPG 369
PRK09276 PRK09276
LL-diaminopimelate aminotransferase; Provisional
 261-470 8.58e-06

LL-diaminopimelate aminotransferase; Provisional


Pssm-ID: 181749  Cd Length: 385  Bit Score: 47.98  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 261 NPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFD--RDGWVLFcSSFTKTL-APDFRVGWICGGR 337
Cdd:PRK09276  177 NPTGAVADLEFFEEVVDFAKKYDIIVCHDAAYSEIAYDGYKPPSFLEVPgaKDVGIEF-HSLSKTYnMTGWRIGFAVGNA 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 338 -FHEALRKLKavSSMSESQLLSETLATFLESGGYDHHLRNLRKRYAAQVDearALIARHFPRGTLATQPAGGFVFWVEFP 416
Cdd:PRK09276  256 dLIAGLGKVK--SNVDSGVFQAIQEAGIAALNGPQEVVEELRKIYQERRD---ILVEGLRKLGLEVEPPKATFYVWAPVP 330

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340571705 417 PNVDSVALFHQLLEEQ-ICLTPGTLYSPSGR-YrnaLRLSCCYPfNARYTQALARL 470
Cdd:PRK09276  331 KGYTSAEFATLLLDKAgVVVTPGNGFGEYGEgY---FRIALTVP-DERIEEAVERI 382
PRK08960 PRK08960
pyridoxal phosphate-dependent aminotransferase;
160-470 9.89e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181595  Cd Length: 387  Bit Score: 47.74  E-value: 9.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 160 LRQQIAR-RSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPTDPQLGLSL 238
Cdd:PRK08960   74 LREAIAGfYAQRYGVDVDPERILVTPGGSGALLLASSLLVDPGKHWLLADPGYPCNRHFLRLVEGAAQLVPVGPDSRYQL 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 239 DALELLL--NEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGAlSPAVKAFDRDGWVLf 316
Cdd:PRK08960  154 TPALVERhwNADTVGALVASPA--NPTGTLLSRDELAALSQALRARGGHLVVDEIYHGLTYGVD-AASVLEVDDDAFVL- 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 317 cSSFTKTLA-PDFRVGWICG-GRFHEALRKLK-----AVSSMSESQLLS----ETLATFLESggydhhlrnlRKRYAAQV 385
Cdd:PRK08960  230 -NSFSKYFGmTGWRLGWLVApPAAVPELEKLAqnlyiSASTPAQHAALAcfepETLAILEAR----------RAEFARRR 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 386 DE-ARALIARHFprgTLATQPAGGFVFWVEFPP-NVDSVALFHQLLE-EQICLTPGTLYspsGRYR--NALRLSccypfn 460
Cdd:PRK08960  299 DFlLPALRELGF---GIAVEPQGAFYLYADISAfGGDAFAFCRHFLEtEHVAFTPGLDF---GRHQagQHVRFA------ 366

                         330
                  ....*....|
gi 1340571705 461 arYTQALARL 470
Cdd:PRK08960  367 --YTQSLPRL 374
PLN00145 PLN00145
tyrosine/nicotianamine aminotransferase; Provisional
 151-381 1.23e-05

tyrosine/nicotianamine aminotransferase; Provisional


Pssm-ID: 215074 [Multi-domain]  Cd Length: 430  Bit Score: 47.46  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIP 229
Cdd:PLN00145   90 YSTCVGLLPARRAIAEYlSRDLPYELSTDDIYLTAGCAQAIEIIMSVLAQPGANILLPRPGYPLYEARAVFSGLEVRHFD 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 230 TDPQLG--LSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKA 307
Cdd:PLN00145  170 LLPERGweVDLEGVEALADENTVAMVIINPN--NPCGSVYSYEHLAKIAETARKLGILVIADEVYDHLTFGSKPFVPMGV 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340571705 308 FDRDGWVLFCSSFTKT-LAPDFRVGWICGGRFHEALRKLKAVSSMSESQLLSETLATFLEsGGYDHHLRNLRKRY 381
Cdd:PLN00145  248 FGEVAPVLTLGSISKRwVVPGWRLGWIATCDPNGILKETKVVDSIRNYLNISTDPATFVQ-GAIPQIIANTKEEF 321
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
150-470 1.74e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 46.86  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 150 QYSLPPgslrLRQQIARRSMTL-GMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEI 228
Cdd:PRK06108   60 NLGIPE----LREALARYVSRLhGVATPPERIAVTSSGVQALMLAAQALVGPGDEVVAVTPLWPNLVAAPKILGARVVCV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 229 PTDPQLGLSLDALelllnEKRLNAV------IAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGAls 302
Cdd:PRK06108  136 PLDFGGGGWTLDL-----DRLLAAItprtraLFINSPNNPTGWTASRDDLRAILAHCRRHGLWIVADEVYERLYYAPG-- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 303 PAVKAF----DRDGWVLFCSSFTKTLA-PDFRVGWICGGR-FHEALRKLKAVSSMSESQLLSETLATFLESGgyDHHLRN 376
Cdd:PRK06108  209 GRAPSFldiaEPDDRIIFVNSFSKNWAmTGWRLGWLVAPPaLGQVLEKLIEYNTSCVAQFVQRAAVAALDEG--EDFVAE 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 377 LRKRYAAQVDE-ARALIArhFPRGTLAtQPAGGFVFWVEFPPNVDSVALFHQLLEE-QICLTPGTLYSPSGryRNALRLs 454
Cdd:PRK06108  287 LVARLRRSRDHlVDALRA--LPGVEVA-KPDGAMYAFFRIPGVTDSLALAKRLVDEaGLGLAPGTAFGPGG--EGFLRW- 360

                         330
                  ....*....|....*..
gi 1340571705 455 cCYPFN-ARYTQALARL 470
Cdd:PRK06108  361 -CFARDpARLDEAVERL 376
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 150-445 1.92e-05

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 46.79  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 150 QYSLPPGSLRLRQQIARRSMTL-GMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEI 228
Cdd:PRK08361   65 HYTPNAGIPELREAIAEYYKKFyGVDVDVDNVIVTAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEAKPIRI 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 229 PTDPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAF 308
Cdd:PRK08361  145 PLREENEFQPDPDELLELITKRTRMIVINYPNNPTGATLDKEVAKAIADIAEDYNIYILSDEPYEHFLYEGAKHYPMIKY 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 309 DRDGWVLfCSSFTKTLApdfRVGWicggRFHEALRKLKAVSSMSE-SQLLSETLATFLESGGYD--------HHLRNLRK 379
Cdd:PRK08361  225 APDNTIL-ANSFSKTFA---MTGW----RLGFVIAPEQVIKDMIKlHAYIIGNVASFVQIAGIEalrskeswKAVEEMRK 296

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340571705 380 RYaaqvDEARALIARHFPR--GTLATQPAGGFVFWvefpPNVDSVAL----FHQLLEEQ--ICLTPGTLYSPSG 445
Cdd:PRK08361  297 EY----NERRKLVLKRLKEmpHIKVFEPKGAFYVF----ANIDETGMssedFAEWLLEKarVVVIPGTAFGKAG 362
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
151-337 2.03e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 46.67  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARrsmTLGmlLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPT 230
Cdd:PRK06225   62 YPPPEGFPELRELILK---DLG--LDDDEALITAGATESLYLVMRAFLSPGDNAVTPDPGYLIIDNFASRFGAEVIEVPI 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 231 -DPQLGLSLDALELLLNEKRLNAVIAMPTVQNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEiqFGGALSPAVKaFD 309
Cdd:PRK06225  137 ySEECNYKLTPELVKENMDENTRLIYLIDPLNPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRD--FAREHTLAAE-YA 213

                         170       180
                  ....*....|....*....|....*....
gi 1340571705 310 RDGWVLfCSSFTKTLA-PDFRVGWICGGR 337
Cdd:PRK06225  214 PEHTVT-SYSFSKIFGmAGLRIGAVVATP 241
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
 14-76 3.49e-04

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 42.45  E-value: 3.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340571705  14 QLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRS 76
Cdd:PRK10421    6 EVADRVRALIEEKNLEAGMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFIRW 68
PLN00143 PLN00143
tyrosine/nicotianamine aminotransferase; Provisional
 151-367 3.83e-04

tyrosine/nicotianamine aminotransferase; Provisional


Pssm-ID: 165711 [Multi-domain]  Cd Length: 409  Bit Score: 42.69  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 151 YSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIP 229
Cdd:PLN00143   70 YAPTGGILPARRAIADYlSNDLPYQLSPDDVYLTLGCKHAAEIIIKVLARPEANILLPRPGFPDVETYAIFHHLEIRHFD 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 230 TDPQLG--LSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKA 307
Cdd:PLN00143  150 LLPEKGweVDLDAVEAIADENTIAMVIINPG--NPCGSVYSYEHLNKIAETARKLGILVIADEVYGHIVFGSKPFVPMGL 227

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340571705 308 FDRDGWVLFCSSFTKT-LAPDFRVGWICGGRFHEALRKLKAVSSMSESQLLSETLATFLES 367
Cdd:PLN00143  228 FASIVPVITLGSISKRwMIPGWGLGWLVTCDPSGLLQICEIADSIKKALNPAPFPPTFIQA 288
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
151-202 6.77e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 41.76  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1340571705 151 YSLPPGSLRLRQQIARRSMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGD 202
Cdd:PRK07568   62 YSHSQGIPELREAFAKYYKKWGIDVEPDEILITNGGSEAILFAMMAICDPGD 113
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
156-470 1.09e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 41.25  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 156 GSLRLRQQIARRSMT-LGMLLEPGDVVL-THGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLGLKALEIPT--- 230
Cdd:PRK07309   68 GLLELRQAAADFVKEkYNLDYAPENEILvTIGATEALSASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTten 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 231 DPQLGLSLDALELLLNEKRLNAVIA-MPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGALSPAVKAFD 309
Cdd:PRK07309  148 DFVLTPEMLEKAILEQGDKLKAVILnYPA--NPTGVTYSREQIKALADVLKKYDIFVISDEVYSELTYTGEPHVSIAEYL 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 310 RDGWVLFcSSFTKTLA-PDFRVGWICGGR-FHEALRK-----LKAVSSMSESQLLsETLatfleSGGYDHHLrNLRKRYA 382
Cdd:PRK07309  226 PDQTILI-NGLSKSHAmTGWRIGLIFAPAeFTAQLIKshqylVTAATTMAQFAAV-EAL-----TNGKDDAL-PMKKEYI 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 383 AQVDearALIARHFPRGTLATQPAGGFVFWVEFPP--NVDSVALFHQLLEEQ-ICLTPGTLYSPSGR-YrnaLRLSccYP 458
Cdd:PRK07309  298 KRRD---YIIEKMTDLGFKIIKPDGAFYIFAKIPAgyNQDSFKFLQDFARKKaVAFIPGAAFGPYGEgY---VRLS--YA 369

                         330
                  ....*....|...
gi 1340571705 459 FN-ARYTQALARL 470
Cdd:PRK07309  370 ASmETIKEAMKRL 382
PRK10225 PRK10225
Uxu operon transcriptional regulator;
12-86 2.75e-03

Uxu operon transcriptional regulator;


Pssm-ID: 182318 [Multi-domain]  Cd Length: 257  Bit Score: 39.62  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340571705  12 YLQLADTLAEAIRRGTLLPGDRLPSVRRCAQTHRVSINTVVSAYRTLEDRGLIEARPQSGFYVRSTLPALKMASA 86
Cdd:PRK10225   11 YQEVGAMIRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAGIYVLDSSGSHNTDSP 85
PLN02656 PLN02656
tyrosine transaminase
 144-332 4.64e-03

tyrosine transaminase


Pssm-ID: 178262 [Multi-domain]  Cd Length: 409  Bit Score: 39.14  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 144 QPDLIGQYSLPPGSLRLRQQIARR-SMTLGMLLEPGDVVLTHGCMEALQLALRVTTKPGDCVGLESPTYFYLLPLLASLG 222
Cdd:PLN02656   62 QSNKFNGYAPTVGLPQARRAIAEYlSRDLPYKLSLDDVFITSGCTQAIDVALSMLARPGANILLPRPGFPIYELCAAFRH 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 223 LKALEIPTDPQLG--LSLDALELLLNEKRLNAVIAMPTvqNPLGCTMPLAAKKRLARLMNDHQVPLIEDGLYAEIQFGGA 300
Cdd:PLN02656  142 LEVRYVDLLPEKGweVDLDAVEALADQNTVALVIINPG--NPCGNVYSYQHLKKIAETAEKLKILVIADEVYGHLAFGSN 219

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1340571705 301 LSPAVKAFDRDGWVLFCSSFTKT-LAPDFRVGW 332
Cdd:PLN02656  220 PFVPMGVFGSIVPVLTLGSLSKRwIVPGWRLGW 252
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 174-326 9.15e-03

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 36.98  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340571705 174 LLEPGD--VVLTHGCMEALQLALRVTTKPGDCV-GLESPTYFYLLPLLASLGLKALEIPTDPQLGLSLDALELLLNEKRL 250
Cdd:cd01494    12 LLQPGNdkAVFVPSGTGANEAALLALLGPGDEViVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGLDVAILEELKAKP 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340571705 251 NAVIAMPTVQNPLGCTmpLAAKKRLARLMNDHQVPLIEDGLYAeiqfgGALSPAVKAFDRDGWVLFC-SSFTKTLAP 326
Cdd:cd01494    92 NVALIVITPNTTSGGV--LVPLKEIRKIAKEYGILLLVDAASA-----GGASPAPGVLIPEGGADVVtFSLHKNLGG 161
 
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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