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Conserved domains on  [gi|16128895|ref|NP_415448|]
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aspartate aminotransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

amino acid aminotransferase( domain architecture ID 10013160)

pyridoxal-5'-phosphate (PLP)-dependent amino acid aminotransferase such as tyrosine transaminase, aspartate transaminase, and aromatic-amino-acid aminotransferase

CATH:  3.90.1150.10|3.40.640.10
EC:  2.6.1.-
Gene Ontology:  GO:0030170|GO:0008483
PubMed:  8112347|10800595|10673430|11933250
SCOP:  4000670

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK09257 PRK09257
aromatic amino acid transaminase;
1-396 0e+00

aromatic amino acid transaminase;


:

Pssm-ID: 181731  Cd Length: 396  Bit Score: 795.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    1 MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   81 LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895  321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:PRK09257 321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL 396
 
Name Accession Description Interval E-value
PRK09257 PRK09257
aromatic amino acid transaminase;
1-396 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 795.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    1 MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   81 LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895  321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:PRK09257 321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL 396
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 1-396 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: 777.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   1 MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE 80
Cdd:COG1448   1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  81 LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:COG1448  81 LLFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV 240
Cdd:COG1448 161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:COG1448 241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895 321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:COG1448 321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-392 1.72e-107

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 320.02  E-value: 1.72e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    26 PGKINLGIGVYKDETgktpvLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGkgSALINDKRARTAQTPGGTG 105
Cdd:pfam00155   1 TDKINLGSNEYLGDT-----LPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGR--SPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   106 ALRVAADFLAKNTSvKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQagdVVLFHGCCHNPT 185
Cdd:pfam00155  74 ANIEALIFLLANPG-DAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   186 GIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGlEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTlvaads 265
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYIL------ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   266 eTVDRAFSQMKAAIRANYSnpPAHGASVVATILSNDALRAiweQELTDMRQRIQRMRQLFVNTLQEKGanrdFSFIIKQN 345
Cdd:pfam00155 223 -GNAAVISQLRKLARPFYS--STHLQAAAAAALSDPLLVA---SELEEMRQRIKERRDYLRDGLQAAG----LSVLPSQA 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128895   346 GMFSFSGLTKEQVLR----LREEFGVYAVA--------SGRVNVAGMTPDNMAPLCEAI 392
Cdd:pfam00155 293 GFFLLTGLDPETAKElaqvLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 29-392 3.89e-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: 172.14  E-value: 3.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  29 INLGIGVYKDETGKtpvltSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSalINDKRARTAQTPGGTGALR 108
Cdd:cd00609   1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGG--VDVPPEEIVVTNGAQEALS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 109 VAADFLAKNTsvKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAqaGDVVLFHgCCHNPTGID 188
Cdd:cd00609  74 LLLRALLNPG--DEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPK--TKLLYLN-NPNNPTGAV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 189 PTLEQWQTLAQLSVEKGWLPLFDFAYQGFARglEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGActLVAADsetv 268
Cdd:cd00609 149 LSEEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPP---- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 269 DRAFSQMKAAIRANYSNPPAHGASVVATILSNDalraiwEQELTDMRQRIQRMRQLFVNTLQEKGanrDFSFIIKQNGMF 348
Cdd:cd00609 221 EELLERLKKLLPYTTSGPSTLSQAAAAAALDDG------EEHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGFF 291

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128895 349 SF----SGLTKEQVLRLREEFGVYAVASG----------RVNVAGmTPDNMAPLCEAI 392
Cdd:cd00609 292 LWldlpEGDDEEFLERLLLEAGVVVRPGSafgeggegfvRLSFAT-PEEELEEALERL 348
 
Name Accession Description Interval E-value
PRK09257 PRK09257
aromatic amino acid transaminase;
1-396 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 795.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    1 MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   81 LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895  321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:PRK09257 321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAVL 396
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 1-396 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: 777.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   1 MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQE 80
Cdd:COG1448   1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  81 LLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:COG1448  81 LLFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIV 240
Cdd:COG1448 161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:COG1448 241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895 321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:COG1448 321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
 2-396 3.81e-180

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 506.77  E-value: 3.81e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    2 FENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQEL 81
Cdd:PTZ00376   5 FSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSFIEAAQKL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   82 LFGKGSALINDKRARTAQTPGGTGALRVAADFLAK-NTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFD 160
Cdd:PTZ00376  85 LFGEASYALAEKRIATVQALSGTGALRLGFEFLKRfLPAGTTVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGLDFD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  161 ALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG-LEEDAEGLRAFAAMHKELI 239
Cdd:PTZ00376 165 GMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGdLDKDAYAIRLFAERGVEFL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  240 VASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQ 319
Cdd:PTZ00376 245 VAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRIQ 324

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128895  320 RMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:PTZ00376 325 NMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVV 401
PLN02397 PLN02397
aspartate transaminase
 2-395 2.03e-172

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 487.93  E-value: 2.03e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    2 FENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQEL 81
Cdd:PLN02397  24 FEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAKL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   82 LFGKGSALINDKRARTAQTPGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDA 161
Cdd:PLN02397 104 AYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDFDG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  162 LINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG-LEEDAEGLRAFAAMHKELIV 240
Cdd:PLN02397 184 LLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGdLDADAQSVRMFVEDGHEILV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  241 ASSYSKNFGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PLN02397 264 AQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRIIS 343

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128895  321 MRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAV 395
Cdd:PLN02397 344 MRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAV 418
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-392 1.72e-107

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 320.02  E-value: 1.72e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895    26 PGKINLGIGVYKDETgktpvLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGkgSALINDKRARTAQTPGGTG 105
Cdd:pfam00155   1 TDKINLGSNEYLGDT-----LPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGR--SPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   106 ALRVAADFLAKNTSvKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAQagdVVLFHGCCHNPT 185
Cdd:pfam00155  74 ANIEALIFLLANPG-DAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   186 GIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGlEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTlvaads 265
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYIL------ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   266 eTVDRAFSQMKAAIRANYSnpPAHGASVVATILSNDALRAiweQELTDMRQRIQRMRQLFVNTLQEKGanrdFSFIIKQN 345
Cdd:pfam00155 223 -GNAAVISQLRKLARPFYS--STHLQAAAAAALSDPLLVA---SELEEMRQRIKERRDYLRDGLQAAG----LSVLPSQA 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 16128895   346 GMFSFSGLTKEQVLR----LREEFGVYAVA--------SGRVNVAGMTPDNMAPLCEAI 392
Cdd:pfam00155 293 GFFLLTGLDPETAKElaqvLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 29-392 3.89e-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: 172.14  E-value: 3.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  29 INLGIGVYKDETGKtpvltSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSalINDKRARTAQTPGGTGALR 108
Cdd:cd00609   1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGG--VDVPPEEIVVTNGAQEALS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 109 VAADFLAKNTsvKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLNEAqaGDVVLFHgCCHNPTGID 188
Cdd:cd00609  74 LLLRALLNPG--DEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPK--TKLLYLN-NPNNPTGAV 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 189 PTLEQWQTLAQLSVEKGWLPLFDFAYQGFARglEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGActLVAADsetv 268
Cdd:cd00609 149 LSEEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPP---- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 269 DRAFSQMKAAIRANYSNPPAHGASVVATILSNDalraiwEQELTDMRQRIQRMRQLFVNTLQEKGanrDFSFIIKQNGMF 348
Cdd:cd00609 221 EELLERLKKLLPYTTSGPSTLSQAAAAAALDDG------EEHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGFF 291

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16128895 349 SF----SGLTKEQVLRLREEFGVYAVASG----------RVNVAGmTPDNMAPLCEAI 392
Cdd:cd00609 292 LWldlpEGDDEEFLERLLLEAGVVVRPGSafgeggegfvRLSFAT-PEEELEEALERL 348
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 5-373 8.70e-15

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


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 75.17  E-value: 8.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   5 ITAAPADPILGLADLFRADERPGK--INLGIGvykDETGKTPvlTSVKKAEQYLLENETTKnYLGIDGIPEFgRctqell 82
Cdd:COG0436   7 LARLPPSPIREVSALAAELKAAGEdvIDLGIG---EPDFPTP--DHIREAAIEALDDGVTG-YTPSAGIPEL-R------ 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  83 fgkgSALINDKRART---------AQTPGGTGALRVAA-------DflakntsvkRVWVSNPSWPNHKSVFNSAGLEVRE 146
Cdd:COG0436  74 ----EAIAAYYKRRYgvdldpdeiLVTNGAKEALALALlallnpgD---------EVLVPDPGYPSYRAAVRLAGGKPVP 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 147 YAYYDAENHTLDFDALINSLNEAQAGdVVLfhgcC--HNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGlEED 224
Cdd:COG0436 141 VPLDEENGFLPDPEALEAAITPRTKA-IVL----NspNNPTGAVYSREELEALAELAREHDLLVISDEIYEELVYD-GAE 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 225 AEGLRAFAAMHKELIVASSYSKNFGLYNERVGACtlvAADSETVDrafsQMKAAIRANYSNPPAHGASVVATILSNDalr 304
Cdd:COG0436 215 HVSILSLPGLKDRTIVINSFSKSYAMTGWRIGYA---VGPPELIA----ALLKLQSNLTSCAPTPAQYAAAAALEGP--- 284

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128895 305 aiwEQELTDMRQRIQRMRQLFVNTLQEKGanrdFSFIIKQNGMF---SFSGLTK---EQVLRLREEFGVyAVASG 373
Cdd:COG0436 285 ---QDYVEEMRAEYRRRRDLLVEGLNEIG----LSVVKPEGAFYlfaDVPELGLdseEFAERLLEEAGV-AVVPG 351
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 73-249 5.08e-10

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: 58.16  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  73 EFGRCTQELLFGKGSALIndkrartaQTPGGTGALRVAADFLAKN-TSVkrVWVSNPSWPNHKSVFNSAGLEVREYAYYD 151
Cdd:cd01494   4 ELEEKLARLLQPGNDKAV--------FVPSGTGANEAALLALLGPgDEV--IVDANGHGSRYWVAAELAGAKPVPVPVDD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 152 AENHTLDFDALINSLNEAQAGDVVlFHGCCHNPTGIDPTLEqwqtLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGlraf 231
Cdd:cd01494  74 AGYGGLDVAILEELKAKPNVALIV-ITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAASAGGASPAPGVLIP---- 144

                       170
                ....*....|....*...
gi 16128895 232 aaMHKELIVASSYSKNFG 249
Cdd:cd01494 145 --EGGADVVTFSLHKNLG 160
PRK08637 PRK08637
hypothetical protein; Provisional
 70-332 1.61e-09

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 59.20  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895   70 GIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAAD-FLAKNTSVkrvWVSNPSWPNHKSVFNSA-GLEVREY 147
Cdd:PRK08637  45 GIPELRDLWQEKMLRENPSLSGKKMSLPIVTNALTHGLSLVADlFVDQGDTV---LLPDHNWGNYKLTFNTRrGAEIVTY 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  148 AYYDAENHtLDFDALINSLNEAQAGD-VVLFHGCCHNPTGIDPTLEQWQTLAQL---SVEKGW--LPLFDFAYQGFargL 221
Cdd:PRK08637 122 PIFDEDGG-FDTDALKEALQAAYNKGkVIVILNFPNNPTGYTPTEKEATAIVEAikeLADAGTkvVAVVDDAYFGL---F 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  222 EEDA--EGL-RAFAAMHKELI---VASSYSKNF--GLyneRVGACTL--VAADSETVDRAFSQ-MKAAIRANYSNPPAHG 290
Cdd:PRK08637 198 YEDSykESLfAALANLHSNILavkLDGATKEEFvwGF---RVGFITFgtKAGSSQTVKEALEKkVKGLIRSNISNGPHPS 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 16128895  291 ASVVatilsndaLRAIWEQELtdmrqriQRMRQLFVNTLQEK 332
Cdd:PRK08637 275 QSAV--------LRALNSPEF-------DKEKQEKFQILKER 301
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 100-396 2.55e-08

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: 55.61  E-value: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 100 TPGGTGALRVAADFLAKNTSVkrVWVSNPSWPNHKSVFNSAGLEVREYAyYDAENhtLDFDALINSLNEAQAgDVVLFHG 179
Cdd:COG1167 176 TSGAQQALDLALRALLRPGDT--VAVESPTYPGALAALRAAGLRLVPVP-VDEDG--LDLDALEAALRRHRP-RAVYVTP 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 180 CCHNPTGIDPTLEQWQTLAQLSVEKG-WL----PLFDFAYQGfargleedaEGLRAFAAM-HKEL-IVASSYSKNF--GL 250
Cdd:COG1167 250 SHQNPTGATMSLERRRALLELARRHGvPIieddYDSELRYDG---------RPPPPLAALdAPGRvIYIGSFSKTLapGL 320

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 251 yneRVGActlVAADSETVDRafsqMKAAIRANYSNPPAHGASVVATILSNDALRAIweqeLTDMRQRIQRMRQLFVNTLQ 330
Cdd:COG1167 321 ---RLGY---LVAPGRLIER----LARLKRATDLGTSPLTQLALAEFLESGHYDRH----LRRLRREYRARRDLLLAALA 386

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 331 EKgANRDFSFIIKQNGMFSF----SGLTKEQVLRLREEFGVyAVASG-------------RVNVAGMTPDNMAPLCEAIV 393
Cdd:COG1167 387 RH-LPDGLRVTGPPGGLHLWlelpEGVDAEALAAAALARGI-LVAPGsafsadgpprnglRLGFGAPSEEELEEALRRLA 464


                ...
gi 16128895 394 AVL 396
Cdd:COG1167 465 ELL 467
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 121-314 3.18e-07

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: 51.67  E-value: 3.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 121 KRVWVSNPSWPNHKSVFNSAGLEVREYAYydAENHTLDFDALINSLNEAqaGDVVLFhgcC--HNPTGIDPTLEQWQTLA 198
Cdd:COG0079  90 DEVLVPEPTFSEYPIAARAAGAEVVEVPL--DEDFSLDLDALLAAITER--TDLVFL---CnpNNPTGTLLPREELEALL 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895 199 QLSVEKGWLpLFDFAYQGFArgleEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGactLVAADSETVDR-------- 270
Cdd:COG0079 163 EALPADGLV-VVDEAYAEFV----PEEDSALPLLARYPNLVVLRTFSKAYGLAGLRLG---YAIASPELIAAlrrvrgpw 234

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 16128895 271 ---AFSQMkAAIRAnysnpPAHGASVVATILSNDALRAIWEQELTDM 314
Cdd:COG0079 235 nvnSLAQA-AALAA-----LEDRAYLEETRARLRAERERLAAALRAL 275
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
100-321 9.05e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 50.52  E-value: 9.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  100 TPGGTGALRVAADFLAKNTSvkRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAE-NHTLDFDALINSLNEAQAgdvVLFH 178
Cdd:PRK06225  89 TAGATESLYLVMRAFLSPGD--NAVTPDPGYLIIDNFASRFGAEVIEVPIYSEEcNYKLTPELVKENMDENTR---LIYL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  179 GCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG----LEEDAEGlrafaamhkeLIVASSYSKNFGLYNER 254
Cdd:PRK06225 164 IDPLNPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDFAREhtlaAEYAPEH----------TVTSYSFSKIFGMAGLR 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128895  255 VGActlVAADSETVDrafsQMKAAIRANYsnppahGASVVATILSNDAL--RAIWEQELTDMRQRIQRM 321
Cdd:PRK06225 234 IGA---VVATPDLIE----VVKSIVINDL------GTNVIAQEAAIAGLkvKDEWIDRIRRTTFKNQKL 289
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
146-348 3.66e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 39.02  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  146 EYAYYdAENH--------------TLDFDALINSLNEAQAGDVVlfhGCCHNPTGIDPTLEQWQTLAQLSVEKG------ 205
Cdd:PRK06836 132 EYRFY-VDNHggklvvvptdtdtfQPDLDALEAAITPKTKAVII---NSPNNPTGVVYSEETLKALAALLEEKSkeygrp 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  206 -WL----PLFDFAYQGfargleedAEGLRAFAAmHKELIVASSYSKNFGLYNERVGactLVAADSETVDRAfSQMKAAIR 280
Cdd:PRK06836 208 iYLisdePYREIVYDG--------AEVPYIFKY-YDNSIVVYSFSKSLSLPGERIG---YIAVNPEMEDAD-DLVAALVF 274

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128895  281 AN----YSNPPAHGASVVATILSNDALRAIWEqeltdmrqriqRMRQLFVNTLQEKGanrdFSFiIKQNGMF 348
Cdd:PRK06836 275 ANrilgFVNAPALMQRVVAKCLDATVDVSIYK-----------RNRDLLYDGLTELG----FEC-VKPQGAF 330
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
183-256 8.00e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 38.16  E-value: 8.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128895  183 NPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFArgLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVG 256
Cdd:PRK06348 173 NPTGAVFSKETLEEIAKIAIEYDLFIISDEVYDGFS--FYEDFVPMATLAGMPERTITFGSFSKDFAMTGWRIG 244
PRK07682 PRK07682
aminotransferase;
183-333 9.12e-03

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 37.79  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128895  183 NPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFArgLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGactLVA 262
Cdd:PRK07682 165 NPTGAVLNKSELEEIAVIVEKHDLIVLSDEIYAELT--YDEAYTSFASIKGMRERTILISGFSKGFAMTGWRLG---FIA 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128895  263 ADSETVD-----RAFSQMKAAIRANYSnppahgasvvatilSNDALRAiWEQELTDMRQRIQRMRQLFVNTLQEKG 333
Cdd:PRK07682 240 APVYFSEamlkiHQYSMMCAPTMAQFA--------------ALEALRA-GNDDVIRMRDSYRKRRNFFVTSFNEIG 300
 
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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