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Conserved domains on  [gi|1225552194|ref|WP_093559879|]
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amino acid aminotransferase [Pseudoduganella namucuonensis]

Protein Classification

similar to aspartate aminotransferase, mitochondrial( domain architecture ID 10787683)

protein similar to aspartate aminotransferase, mitochondrial

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
1-393 0e+00

Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


:

Pssm-ID: 441057  Cd Length: 396  Bit Score: 695.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   1 MFKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVRE 80
Cdd:COG1448     1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  81 LTFGG---AVPADRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:COG1448    81 LLFGAdspAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFA 237
Cdd:COG1448   161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:COG1448   241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:COG1448   321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
 
Name Accession Description Interval E-value
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
1-393 0e+00

Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 441057  Cd Length: 396  Bit Score: 695.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   1 MFKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVRE 80
Cdd:COG1448     1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  81 LTFGG---AVPADRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:COG1448    81 LLFGAdspAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFA 237
Cdd:COG1448   161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:COG1448   241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:COG1448   321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PRK09257 PRK09257
aromatic amino acid transaminase;
1-393 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 686.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   1 MFKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVRE 80
Cdd:PRK09257    1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  81 LTFGGAVP---ADRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:PRK09257   81 LLFGADSPalaAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFA 237
Cdd:PRK09257  161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:PRK09257  241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:PRK09257  321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-388 4.17e-85

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 263.01  E-value: 4.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  26 PHKINLSIGVYLNEAGKmpamgAVLRAESALAADLGTRPYLPMEGNAAYRAAVRELTFGG-AVPADRVAIAQTLGGSGAL 104
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP-----AVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSpVLKLDREAAVVFGSGAGAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 105 KVGADFIArYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFPGMLAALEALPagdVVLLHACCHNPTGA 184
Cdd:pfam00155  76 IEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPTGT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 185 DLDELQWRELAALVKRRGLLPFFDMAYQGFGKGvDEDAFAIRHFAAEGIPLFAATSFSKNFSLYGERCGSLSVVCAdare 264
Cdd:pfam00155 152 VATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNAA---- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 265 agnVLGQLKATIRRNYSSppTHGARIIARVLDDAALRAEWraeLEGMRTRVADMRAGLYEALRERrpdgDFGYLVKQTGM 344
Cdd:pfam00155 227 ---VISQLRKLARPFYSS--THLQAAAAAALSDPLLVASE---LEEMRQRIKERRDYLRDGLQAA----GLSVLPSQAGF 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 345 FSFTGLTPAEV----ERLREESAVYLV--------GSGRLCLAALTRRTIAPTADA 388
Cdd:pfam00155 295 FLLTGLDPETAkelaQVLLEEVGVYVTpgsspgvpGWLRITVAGGTEEELEELLEA 350
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
29-378 5.56e-48

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: 166.75  E-value: 5.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  29 INLSIGVYLNEAGKmpamgAVLRAESALAADLGTRPYLPMEGNAAYRAAVRELTFG-GAVPADRVAIAQTLGGSGALKVG 107
Cdd:cd00609     1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRrGGVDVPPEEIVVTNGAQEALSLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 108 ADFIARyfPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAatGHVDFPGMLAALEALPAGDVVLLHACcHNPTGADLD 187
Cdd:cd00609    76 LRALLN--PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEE--GGFLLDLELLEAAKTPKTKLLYLNNP-NNPTGAVLS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 188 ELQWRELAALVKRRGLLPFFDMAYQGFGKgvDEDAFAIRHFAAEGIPLFAATSFSKNFSLYGERCGSLSVVCADAREagn 267
Cdd:cd00609   151 EEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGYLIAPPEELLE--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 268 vlgQLKATIRRNYSSPPTHGARIIARVLDDAAlraewrAELEGMRTRVADMRAGLYEALRERRPDgdfGYLVKQTGMFSF 347
Cdd:cd00609   226 ---RLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPL---VVVKPSGGFFLW 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1225552194 348 TGLTP----AEVERLREESAVYLV----------GSGRLCLAALT 378
Cdd:cd00609   294 LDLPEgddeEFLERLLLEAGVVVRpgsafgeggeGFVRLSFATPE 338
DAPAT_plant TIGR03542
LL-diaminopimelate aminotransferase; This clade of the pfam00155 superfamily of ...
16-258 3.06e-06

LL-diaminopimelate aminotransferase; This clade of the pfam00155 superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (GenProp0125). This clade includes characterized species in plants and Chlamydia. Every member of this clade is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh).


Pssm-ID: 163316  Cd Length: 402  Bit Score: 48.95  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  16 LNENFGADPRPHKINLSIGvylneAGKMPAMGAVLRAESALAADLGT----RPYLPMEGNAAYRAAVRELTFGGAVPADR 91
Cdd:TIGR03542  23 VAEFRKKNPSADIIRLGIG-----DTTQPLPASVIEAFHNAVDELASpetfRGYGPEQGYPFLREAIAENDYRGRIDPEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  92 VAIaqtlggSGALKVGADFIARYF-PKAGVWVSDPTWD--NHYSIFAGAGLPVQKYRYYD-----AATGHVDFpgmLAAL 163
Cdd:TIGR03542  98 IFI------SDGAKCDVFRLQSLFgPDNTVAVQDPVYPayLDSNVMAGRAGVLDDDGRYSkitylPCTAENNF---IPEL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 164 EALPAGDVVLLhacC--HNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFgkgVDEDAFAIRHFAAEGIPLFAA--T 239
Cdd:TIGR03542 169 PEEPHIDIIYL---CspNNPTGTVLTKEQLKELVDYANEHGSLILFDAAYSAF---ISDPSLPHSIFEIPGARFCAIefR 242
                         250
                  ....*....|....*....
gi 1225552194 240 SFSKNFSLYGERCGsLSVV 258
Cdd:TIGR03542 243 SFSKTAGFTGVRLG-WTVV 260
 
Name Accession Description Interval E-value
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
1-393 0e+00

Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 441057  Cd Length: 396  Bit Score: 695.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   1 MFKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVRE 80
Cdd:COG1448     1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  81 LTFGG---AVPADRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:COG1448    81 LLFGAdspAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFA 237
Cdd:COG1448   161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:COG1448   241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:COG1448   321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PRK09257 PRK09257
aromatic amino acid transaminase;
1-393 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 686.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   1 MFKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVRE 80
Cdd:PRK09257    1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  81 LTFGGAVP---ADRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:PRK09257   81 LLFGADSPalaAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFA 237
Cdd:PRK09257  161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:PRK09257  241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:PRK09257  321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL 396
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
2-393 3.01e-176

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 496.75  E-value: 3.01e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   2 FKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVREL 81
Cdd:PTZ00376    5 FSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSFIEAAQKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  82 TFGGAVPA---DRVAIAQTLGGSGALKVGADFIARYFPKAG-VWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFP 157
Cdd:PTZ00376   85 LFGEASYAlaeKRIATVQALSGTGALRLGFEFLKRFLPAGTtVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGLDFD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 158 GMLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKG-VDEDAFAIRHFAAEGIPLF 236
Cdd:PTZ00376  165 GMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGdLDKDAYAIRLFAERGVEFL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 237 AATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVA 316
Cdd:PTZ00376  245 VAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRIQ 324
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225552194 317 DMRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARVL 393
Cdd:PTZ00376  325 NMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVV 401
PLN02397 PLN02397
aspartate transaminase
2-392 1.04e-163

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 465.59  E-value: 1.04e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194   2 FKHVEAYPGDPILTLNENFGADPRPHKINLSIGVYLNEAGKMPAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAVREL 81
Cdd:PLN02397   24 FEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAKL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  82 TFGGAVPA---DRVAIAQTLGGSGALKVGADFIARYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFPG 158
Cdd:PLN02397  104 AYGADSPAikeNRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDFDG 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 159 MLAALEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKG-VDEDAFAIRHFAAEGIPLFA 237
Cdd:PLN02397  184 LLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGdLDADAQSVRMFVEDGHEILV 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 238 ATSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEGMRTRVAD 317
Cdd:PLN02397  264 AQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRIIS 343
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1225552194 318 MRAGLYEALRERRPDGDFGYLVKQTGMFSFTGLTPAEVERLREESAVYLVGSGRLCLAALTRRTIAPTADAMARV 392
Cdd:PLN02397  344 MRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAV 418
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-388 4.17e-85

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 263.01  E-value: 4.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  26 PHKINLSIGVYLNEAGKmpamgAVLRAESALAADLGTRPYLPMEGNAAYRAAVRELTFGG-AVPADRVAIAQTLGGSGAL 104
Cdd:pfam00155   1 TDKINLGSNEYLGDTLP-----AVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSpVLKLDREAAVVFGSGAGAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 105 KVGADFIArYFPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAATGHVDFPGMLAALEALPagdVVLLHACCHNPTGA 184
Cdd:pfam00155  76 IEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPTGT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 185 DLDELQWRELAALVKRRGLLPFFDMAYQGFGKGvDEDAFAIRHFAAEGIPLFAATSFSKNFSLYGERCGSLSVVCAdare 264
Cdd:pfam00155 152 VATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNAA---- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 265 agnVLGQLKATIRRNYSSppTHGARIIARVLDDAALRAEWraeLEGMRTRVADMRAGLYEALRERrpdgDFGYLVKQTGM 344
Cdd:pfam00155 227 ---VISQLRKLARPFYSS--THLQAAAAAALSDPLLVASE---LEEMRQRIKERRDYLRDGLQAA----GLSVLPSQAGF 294
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1225552194 345 FSFTGLTPAEV----ERLREESAVYLV--------GSGRLCLAALTRRTIAPTADA 388
Cdd:pfam00155 295 FLLTGLDPETAkelaQVLLEEVGVYVTpgsspgvpGWLRITVAGGTEEELEELLEA 350
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
29-378 5.56e-48

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: 166.75  E-value: 5.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  29 INLSIGVYLNEAGKmpamgAVLRAESALAADLGTRPYLPMEGNAAYRAAVRELTFG-GAVPADRVAIAQTLGGSGALKVG 107
Cdd:cd00609     1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRrGGVDVPPEEIVVTNGAQEALSLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 108 ADFIARyfPKAGVWVSDPTWDNHYSIFAGAGLPVQKYRYYDAatGHVDFPGMLAALEALPAGDVVLLHACcHNPTGADLD 187
Cdd:cd00609    76 LRALLN--PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEE--GGFLLDLELLEAAKTPKTKLLYLNNP-NNPTGAVLS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 188 ELQWRELAALVKRRGLLPFFDMAYQGFGKgvDEDAFAIRHFAAEGIPLFAATSFSKNFSLYGERCGSLSVVCADAREagn 267
Cdd:cd00609   151 EEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGYLIAPPEELLE--- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 268 vlgQLKATIRRNYSSPPTHGARIIARVLDDAAlraewrAELEGMRTRVADMRAGLYEALRERRPDgdfGYLVKQTGMFSF 347
Cdd:cd00609   226 ---RLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPL---VVVKPSGGFFLW 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1225552194 348 TGLTP----AEVERLREESAVYLV----------GSGRLCLAALT 378
Cdd:cd00609   294 LDLPEgddeEFLERLLLEAGVVVRpgsafgeggeGFVRLSFATPE 338
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
29-395 5.79e-14

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: 72.86  E-value: 5.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  29 INLSIGvylnEAGKMPAMGAVLRAESALAAdlGTRPYLPMEGNAAYRAAVRELT---FGGAVPADRVAIaqTLGGSGALk 105
Cdd:COG0436    33 IDLGIG----EPDFPTPDHIREAAIEALDD--GVTGYTPSAGIPELREAIAAYYkrrYGVDLDPDEILV--TNGAKEAL- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 106 vgaDFIARYFPKAG--VWVSDPTWDNHYSI--FAGAglpvqKYRYYDAATGHvDFPGMLAALEAL--PAGDVVLLhacC- 178
Cdd:COG0436   104 ---ALALLALLNPGdeVLVPDPGYPSYRAAvrLAGG-----KPVPVPLDEEN-GFLPDPEALEAAitPRTKAIVL---Ns 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 179 -HNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFG------------KGVDEDAFAIrhfaaegiplfaaTSFSKNF 245
Cdd:COG0436   172 pNNPTGAVYSREELEALAELAREHDLLVISDEIYEELVydgaehvsilslPGLKDRTIVI-------------NSFSKSY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 246 SLYGERCGSLsVVCADAREAgnvLGQLKATIRrnySSPPTHGARIIArvlddAALRAEwRAELEGMRTRVADMRAGLYEA 325
Cdd:COG0436   239 AMTGWRIGYA-VGPPELIAA---LLKLQSNLT---SCAPTPAQYAAA-----AALEGP-QDYVEEMRAEYRRRRDLLVEG 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 326 LRE-----RRPDGDFgYL-VKqtgmFSFTGLTPAE-VERLREESAVYLV-GSG---------RLCLAAlTRRTIAPTADA 388
Cdd:COG0436   306 LNEiglsvVKPEGAF-YLfAD----VPELGLDSEEfAERLLEEAGVAVVpGSAfgpagegyvRISYAT-SEERLEEALER 379

                  ....*..
gi 1225552194 389 MARVLGR 395
Cdd:COG0436   380 LARFLER 386
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
45-396 1.78e-11

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: 65.24  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  45 AMGAVLRAESALAADlgtrpYLPMEGNAAYRAAVRE--LTFGGAVPADRVAIaqTLGGSGALkvgaDFIARYFPKAG--V 120
Cdd:COG1167   129 ALRRALRRLPPALLG-----YGDPQGLPELREAIARylARRGVPASPDQILI--TSGAQQAL----DLALRALLRPGdtV 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 121 WVSDPTWDNHYSIFAGAGL---PVQkyryydaatghVDFPGM-LAALEAL---PAGDVVLLHACCHNPTGADLDELQWRE 193
Cdd:COG1167   198 AVESPTYPGALAALRAAGLrlvPVP-----------VDEDGLdLDALEAAlrrHRPRAVYVTPSHQNPTGATMSLERRRA 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 194 LAALVKRRGLLPFFDMAYQGFgkgvdedafairHFAAEGIPLFAA----------TSFSKNFS--LygeRCGSLSVvcad 261
Cdd:COG1167   267 LLELARRHGVPIIEDDYDSEL------------RYDGRPPPPLAAldapgrviyiGSFSKTLApgL---RLGYLVA---- 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 262 areAGNVLGQLKATIRRNYSSPPTHGARIIARVLDDaalrAEWRAELEGMRTRVADMRAGLYEALRERRPDGdFGYLVKQ 341
Cdd:COG1167   328 ---PGRLIERLARLKRATDLGTSPLTQLALAEFLES----GHYDRHLRRLRREYRARRDLLLAALARHLPDG-LRVTGPP 399
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1225552194 342 TGMFsFTGLTPAEV------ERLREE------SAVYLVGSG-----RLCLAALTRRTIAPTADAMARVLGRR 396
Cdd:COG1167   400 GGLH-LWLELPEGVdaealaAAALARgilvapGSAFSADGPprnglRLGFGAPSEEELEEALRRLAELLREL 470
PRK08960 PRK08960
pyridoxal phosphate-dependent aminotransferase;
52-346 1.58e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181595  Cd Length: 387  Bit Score: 52.75  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  52 AESALAAdlGTRPYLPMEGNAAYRAAVREL---TFGGAVPADRVAIaqTLGGSGALKVGADFIARyfPKAGVWVSDPTW- 127
Cdd:PRK08960   54 GQAALAA--GHTRYTAARGLPALREAIAGFyaqRYGVDVDPERILV--TPGGSGALLLASSLLVD--PGKHWLLADPGYp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 128 -DNHY-SIFAGA--GLPVQKYRYYDAATGHVDF---PGMLAALEALPAgdvvllhacchNPTGADLDELQWRELAALVKR 200
Cdd:PRK08960  128 cNRHFlRLVEGAaqLVPVGPDSRYQLTPALVERhwnADTVGALVASPA-----------NPTGTLLSRDELAALSQALRA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 201 RGLLPFFDMAYQGFGKG--------VDEDAFAIrhfaaegiplfaaTSFSKNFSLYGERCGSLsVVCADAREAGNVLGQl 272
Cdd:PRK08960  197 RGGHLVVDEIYHGLTYGvdaasvleVDDDAFVL-------------NSFSKYFGMTGWRLGWL-VAPPAAVPELEKLAQ- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 273 katirRNYSSPPThgariIARVLDDAALRAEWRAELEGMRTRVADMRAGLYEALRE------RRPDGDFgYLVKQTGMFS 346
Cdd:PRK08960  262 -----NLYISAST-----PAQHAALACFEPETLAILEARRAEFARRRDFLLPALRElgfgiaVEPQGAF-YLYADISAFG 330
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
75-257 6.32e-07

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: 48.92  E-value: 6.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  75 RAAVRELTFGGAVpadrvAIAQTLGGSGALKVGADFIARyfPKAGVWVSDPTWDNHYSIFA---GAGL-PVQKYRYYDAA 150
Cdd:cd01494     6 EEKLARLLQPGND-----KAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAelaGAKPvPVPVDDAGYGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 151 TGHVDFPgmlaalEALPAGDVVLLHAccHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGkgvdedAFAIRHFAA 230
Cdd:cd01494    79 LDVAILE------ELKAKPNVALIVI--TPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGA------SPAPGVLIP 144
                         170       180
                  ....*....|....*....|....*..
gi 1225552194 231 EGIPLFAATSFSKNFSlyGERCGSLSV 257
Cdd:cd01494   145 EGGADVVTFSLHKNLG--GEGGGVVIV 169
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
51-328 1.04e-06

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: 50.13  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  51 RAESALAADLGTRPYLPMEGNAAYRAAVRELtFGgaVPADRVAIAqtlGGSGALkvgADFIARYFPKAG--VWVSDPTWD 128
Cdd:COG0079    30 KVLEAIAAALDALNRYPDPDATALREALAEY-YG--VPPEQVLVG---NGSDEL---IQLLARAFLGPGdeVLVPEPTFS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 129 NHYSIFAGAGLPVQKYRYydAATGHVDFPGMLAALEALPagDVVLLhacC--HNPTGADLDELQWRELAALVKRRGLLpF 206
Cdd:COG0079   101 EYPIAARAAGAEVVEVPL--DEDFSLDLDALLAAITERT--DLVFL---CnpNNPTGTLLPREELEALLEALPADGLV-V 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 207 FDMAYQGFGKGVDEdafairhfaaeGIPLFAAT-------SFSKNFSLYGERCGslsVVCADAreagnvlgQLKATIRR- 278
Cdd:COG0079   173 VDEAYAEFVPEEDS-----------ALPLLARYpnlvvlrTFSKAYGLAGLRLG---YAIASP--------ELIAALRRv 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1225552194 279 ----NYSSPpthgARIIARvlddAALRAewRAELEGMRTRVADMRAGLYEALRE 328
Cdd:COG0079   231 rgpwNVNSL----AQAAAL----AALED--RAYLEETRARLRAERERLAAALRA 274
DAPAT_plant TIGR03542
LL-diaminopimelate aminotransferase; This clade of the pfam00155 superfamily of ...
16-258 3.06e-06

LL-diaminopimelate aminotransferase; This clade of the pfam00155 superfamily of aminotransferases includes several which are adjacent to elements of the lysine biosynthesis via diaminopimelate pathway (GenProp0125). This clade includes characterized species in plants and Chlamydia. Every member of this clade is from a genome which possesses most of the lysine biosynthesis pathway but lacks any of the known succinylases, desuccinylases, acetylases or deacetylases typical of the acylated versions of this pathway nor do they have the direct, NADPH-dependent enzyme (ddh).


Pssm-ID: 163316  Cd Length: 402  Bit Score: 48.95  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  16 LNENFGADPRPHKINLSIGvylneAGKMPAMGAVLRAESALAADLGT----RPYLPMEGNAAYRAAVRELTFGGAVPADR 91
Cdd:TIGR03542  23 VAEFRKKNPSADIIRLGIG-----DTTQPLPASVIEAFHNAVDELASpetfRGYGPEQGYPFLREAIAENDYRGRIDPEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  92 VAIaqtlggSGALKVGADFIARYF-PKAGVWVSDPTWD--NHYSIFAGAGLPVQKYRYYD-----AATGHVDFpgmLAAL 163
Cdd:TIGR03542  98 IFI------SDGAKCDVFRLQSLFgPDNTVAVQDPVYPayLDSNVMAGRAGVLDDDGRYSkitylPCTAENNF---IPEL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 164 EALPAGDVVLLhacC--HNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFgkgVDEDAFAIRHFAAEGIPLFAA--T 239
Cdd:TIGR03542 169 PEEPHIDIIYL---CspNNPTGTVLTKEQLKELVDYANEHGSLILFDAAYSAF---ISDPSLPHSIFEIPGARFCAIefR 242
                         250
                  ....*....|....*....
gi 1225552194 240 SFSKNFSLYGERCGsLSVV 258
Cdd:TIGR03542 243 SFSKTAGFTGVRLG-WTVV 260
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
65-338 5.16e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 48.27  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  65 YLPMEGNAAYRAAVREL---TFGGAVPADRVAIaqTLGGSGALKV--------GADFI--ARYFPKAGVWVsdptwDNHy 131
Cdd:PRK06836   69 YMPNAGYPEVREAIAESlnrRFGTPLTADHIVM--TCGAAGALNValkailnpGDEVIvfAPYFVEYRFYV-----DNH- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 132 sifaGAGLPVqkyryydAATGHVDFPGMLAALEAL--PAGDVVLLHACcHNPTGADLDELQWRELAALVKRRGllpffdm 209
Cdd:PRK06836  141 ----GGKLVV-------VPTDTDTFQPDLDALEAAitPKTKAVIINSP-NNPTGVVYSEETLKALAALLEEKS------- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 210 ayQGFGKGV----DEdafAIRHFAAEGI---PLFAA-------TSFSKNFSLYGERCGSLSV---------VCADAREAG 266
Cdd:PRK06836  202 --KEYGRPIylisDE---PYREIVYDGAevpYIFKYydnsivvYSFSKSLSLPGERIGYIAVnpemedaddLVAALVFAN 276
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225552194 267 NVLGqlkatirrnYSSPPTHGARIIARVLDDaalraewRAELEGMRTRvadmRAGLYEALRE-----RRPDGDFgYL 338
Cdd:PRK06836  277 RILG---------FVNAPALMQRVVAKCLDA-------TVDVSIYKRN----RDLLYDGLTElgfecVKPQGAF-YL 332
PRK07550 PRK07550
aminotransferase;
44-322 2.48e-05

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 46.10  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  44 PAMGAVLRAESALAADLGTRPYLPMEGNAAYRAAV----RELtFGGAVPADRVAIaqTLGGSGALKVGADFIARyfpkAG 119
Cdd:PRK07550   42 PPPPELLRALAEAAADPAAHLYGPVEGLPELREAYaahySRL-YGAAISPEQVHI--TSGCNQAFWAAMVTLAG----AG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 120 --VWVSDPTWDNHYSIFAGAGL-PVqkYRYYDAATGHVDFPGMLAALeaLPAGDVVLLHACCHNPTGADLDELQWRELAA 196
Cdd:PRK07550  115 deVILPLPWYFNHKMWLDMLGIrPV--YLPCDEGPGLLPDPAAAEAL--ITPRTRAIALVTPNNPTGVVYPPELLHELYD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 197 LVKRRGLLPFFDMAYQGF--GKGVDEDAFAIRHFAAEGIPLFaatSFSKNFSLYGERCGSLSVVCADAREAGNVLGQLKA 274
Cdd:PRK07550  191 LARRHGIALILDETYRDFdsGGGAPHDLFADPDWDDTLVHLY---SFSKSYALTGHRVGAVVASPARIAEIEKFMDTVAI 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1225552194 275 TIRRNysspPTHGARIIARVLDDaalraeWRAELEGMRTRVAD-MRAGL 322
Cdd:PRK07550  268 CAPRI----GQIAVAWGLPNLAD------WRAGNRAEIARRRDaFRAVF 306
PRK08637 PRK08637
hypothetical protein; Provisional
27-324 5.92e-05

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 44.95  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  27 HKINLSIGVYLNEAGKM--PAMGAVLraeSALAADlGTRPYLPMEGNAAYRAAVRELTF-------GGAVPADRVAIAQT 97
Cdd:PRK08637    4 TKYNATIGMATEKGGPMylSSLQDLL---NDLTPD-EIFPYAPPQGIPELRDLWQEKMLrenpslsGKKMSLPIVTNALT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  98 LGgsgaLKVGADFiaryFPKAG--VWVSDPTWDNHYSIFAGA-GLPVQKYRYYDAAtGHVDFPGMLAALEALPAGD-VVL 173
Cdd:PRK08637   80 HG----LSLVADL----FVDQGdtVLLPDHNWGNYKLTFNTRrGAEIVTYPIFDED-GGFDTDALKEALQAAYNKGkVIV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 174 LHACCHNPTGADLDELQWRELAALVK---RRG--LLPFFDMAYQG-----------FGK--GVDEDAFAIRhfaaegipL 235
Cdd:PRK08637  151 ILNFPNNPTGYTPTEKEATAIVEAIKelaDAGtkVVAVVDDAYFGlfyedsykeslFAAlaNLHSNILAVK--------L 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 236 FAATsfsKNFSLYGERCGSLSvvCAD-AREAGNVLGQL----KATIRRNYSSPPTHGARIIARVLDDAALRAEWRAELEG 310
Cdd:PRK08637  223 DGAT---KEEFVWGFRVGFIT--FGTkAGSSQTVKEALekkvKGLIRSNISNGPHPSQSAVLRALNSPEFDKEKQEKFQI 297
                         330
                  ....*....|....
gi 1225552194 311 MRTRVADMRAGLYE 324
Cdd:PRK08637  298 LKERYEKTKEVLYD 311
PRK07324 PRK07324
transaminase; Validated
55-253 1.51e-04

transaminase; Validated


Pssm-ID: 235989  Cd Length: 373  Bit Score: 43.39  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  55 ALAADLGTRP--YLPMEGNAAYRAAVRELTfggavpaDRVAIAQTLGGSGAlkVGADFIARYF---PKAGVWVSDPTWDN 129
Cdd:PRK07324   46 AFYQELGQKKltYGWIEGSPEFKEAVASLY-------QNVKPENILQTNGA--TGANFLVLYAlvePGDHVISVYPTYQQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 130 HYSIFAGAGLPVQKYRYYDAAtghvDFPGMLAALEAL--PAGDVVLLHACcHNPTGADLDELQWRELAALVKRRGLLPFF 207
Cdd:PRK07324  117 LYDIPESLGAEVDYWQLKEEN----GWLPDLDELRRLvrPNTKLICINNA-NNPTGALMDRAYLEEIVEIARSVDAYVLS 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1225552194 208 DMAYQGFGKgvDEDAFAIRHFAAEGIplfAATSFSKNFSLYGERCG 253
Cdd:PRK07324  192 DEVYRPLDE--DGSTPSIADLYEKGI---STNSMSKTYSLPGIRVG 232
hisC TIGR01141
histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; ...
109-253 4.60e-04

histidinol-phosphate aminotransferase; Alternate names: histidinol-phosphate transaminase; imidazole acetol-phosphate transaminase Histidinol-phosphate aminotransferase is a pyridoxal-phosphate dependent enzyme. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273467  Cd Length: 350  Bit Score: 41.87  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 109 DFIARYF--PKAGVWVSDPTWDnHYSIFA-GAGLPVQKYRYYDaatghvDFPGMLAALEALPAGDVVLLHACC-HNPTGA 184
Cdd:TIGR01141  86 DLLIRAFlePGDAVLVPPPTYS-MYEISAkIHGAEVVKVPLDE------DGQLDLEDILVAIDDKPKLVFLCSpNNPTGN 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 185 DLDELQWRELAALVKRRGLLpFFDMAYQGFGKGVDEDAFAIRHfaaegiP-LFAATSFSKNFSLYGERCG 253
Cdd:TIGR01141 159 LFSRGDIEAVLERTPGDALV-VVDEAYGEFSGEPSTLPLLAEY------PnLIVLRTLSKAFGLAGLRIG 221
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
65-304 1.97e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 40.12  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  65 YLPMEGNAAYRAAVRElTFGgaVPADRVAIaqTLGGSGALKVGADFIARyfPKAGVWVSDPTW---DNHYSIFAGAglpV 141
Cdd:PRK06225   62 YPPPEGFPELRELILK-DLG--LDDDEALI--TAGATESLYLVMRAFLS--PGDNAVTPDPGYliiDNFASRFGAE---V 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 142 QKYRYYDAATGHVDFPGMLaaLEALPAGDVVLLHACCHNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFGKGvded 221
Cdd:PRK06225  132 IEVPIYSEECNYKLTPELV--KENMDENTRLIYLIDPLNPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDFARE---- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 222 afaiRHFAAEGIPLFAAT--SFSKNFSLYGERCGSLsVVCADareagnVLGQLKATIRRNYssppthGARIIARVLDDAA 299
Cdd:PRK06225  206 ----HTLAAEYAPEHTVTsySFSKIFGMAGLRIGAV-VATPD------LIEVVKSIVINDL------GTNVIAQEAAIAG 268

                  ....*..
gi 1225552194 300 L--RAEW 304
Cdd:PRK06225  269 LkvKDEW 275
PRK08361 PRK08361
aspartate aminotransferase; Provisional
179-346 2.86e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 39.48  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 179 HNPTGADLDELQWRELAALVKRRGLLPFFDMAYQGFgkgVDEDA--FAIRHFAAEGIPLfaATSFSKNFSLYGERCGSLS 256
Cdd:PRK08361  176 NNPTGATLDKEVAKAIADIAEDYNIYILSDEPYEHF---LYEGAkhYPMIKYAPDNTIL--ANSFSKTFAMTGWRLGFVI 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 257 VVCADAREagnvLGQLKATIRRNYSSppthgariIARVLDDAALRAE--WRAeLEGMRTRVADMRAGLYEALRE------ 328
Cdd:PRK08361  251 APEQVIKD----MIKLHAYIIGNVAS--------FVQIAGIEALRSKesWKA-VEEMRKEYNERRKLVLKRLKEmphikv 317
                         170       180
                  ....*....|....*....|.
gi 1225552194 329 RRPDGDFgYL---VKQTGMFS 346
Cdd:PRK08361  318 FEPKGAF-YVfanIDETGMSS 337
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
45-272 4.58e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 38.77  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194  45 AMGAVLRAESALAADLGTrPYLpMEGNAAYRAAVreltFGGAVPADRVAIaqTLGGSGALKVGADFIARyfPKAGVWVSD 124
Cdd:PRK06108   46 AAAALADGETFYTHNLGI-PEL-REALARYVSRL----HGVATPPERIAV--TSSGVQALMLAAQALVG--PGDEVVAVT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225552194 125 PTWDNHYSIFAGAGL-PVQKYRYYDAATGHVDFPGMLAALEalPAGDVVLLHACcHNPTG--ADLDELQwrELAALVKRR 201
Cdd:PRK06108  116 PLWPNLVAAPKILGArVVCVPLDFGGGGWTLDLDRLLAAIT--PRTRALFINSP-NNPTGwtASRDDLR--AILAHCRRH 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1225552194 202 GLLPFFDMAYQGFGKGVDEDAFAIRHFAAEGIPLFAATSFSKNFSLYGERCGSLSVvcadAREAGNVLGQL 272
Cdd:PRK06108  191 GLWIVADEVYERLYYAPGGRAPSFLDIAEPDDRIIFVNSFSKNWAMTGWRLGWLVA----PPALGQVLEKL 257
 
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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