NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489126028|ref|WP_003035825|]
View 

MULTISPECIES: aspartate transaminase [Citrobacter]

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

show extra options »

Show site features     Horizontal zoom: ×

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: 793.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   1 MFENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  81 LLFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 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: 793.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   1 MFENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  81 LLFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 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: 775.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   1 MFENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQE 80
Cdd:COG1448    1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  81 LLFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:COG1448   81 LLFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELIV 240
Cdd:COG1448  161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:COG1448  241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:COG1448  321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-392 6.06e-105

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 313.47  E-value: 6.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   26 PGKINLGIGVYKDETgktpvLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQELLFgkTSSLINDKRARTAQTPGGTG 105
Cdd:pfam00155   1 TDKINLGSNEYLGDT-----LPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLG--RSPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  106 ALRVAADFLARNTSaKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFDALLASLSEAQagdVVLFHGCCHNPT 185
Cdd:pfam00155  74 ANIEALIFLLANPG-DAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  186 GIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGlEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGACTlvaada 265
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYIL------ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  266 eTVDRAFSQMKSAIRANYSnpPAHGASVVATILSNDALRAiweQELTDMRQRIQRMRLLFVNTLQEKGanrdFSFIIKQN 345
Cdd:pfam00155 223 -GNAAVISQLRKLARPFYS--STHLQAAAAAALSDPLLVA---SELEEMRQRIKERRDYLRDGLQAAG----LSVLPSQA 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489126028  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 1.73e-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: 167.90  E-value: 1.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  29 INLGIGVYKDETGKtpvltSVKKAEQYILENETTKNYLGIDGIPEFGRCTQELLFGKTSslINDKRARTAQTPGGTGALR 108
Cdd:cd00609    1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGG--VDVPPEEIVVTNGAQEALS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 109 VAADFLARNtsAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFDALLASLSEAqaGDVVLFHgCCHNPTGID 188
Cdd:cd00609   74 LLLRALLNP--GDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPK--TKLLYLN-NPNNPTGAV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 189 PTLEQWQTLAQLSVEKGWLPLFDFAYQGFARglEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGActLVAADAEtv 268
Cdd:cd00609  149 LSEEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPPEE-- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 269 drAFSQMKSAIRANYSNPPAHGASVVATILSNDalraiwEQELTDMRQRIQRMRLLFVNTLQEKGanrDFSFIIKQNGMF 348
Cdd:cd00609  223 --LLERLKKLLPYTTSGPSTLSQAAAAAALDDG------EEHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGFF 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489126028 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: 793.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   1 MFENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQE 80
Cdd:PRK09257   1 MFEHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  81 LLFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:PRK09257  81 LLFGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELIV 240
Cdd:PRK09257 161 AMLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDGLEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 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: 775.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   1 MFENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQE 80
Cdd:COG1448    1 MFEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  81 LLFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:COG1448   81 LLFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELIV 240
Cdd:COG1448  161 GMLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGLEEDAAGLRLFAEAGPEFLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:COG1448  241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:COG1448  321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
 2-396 0e+00

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 510.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   2 FENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQEL 81
Cdd:PTZ00376   5 FSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSFIEAAQKL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  82 LFGKTSSLINDKRARTAQTPGGTGALRVAADFLAR-NTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFD 160
Cdd:PTZ00376  85 LFGEASYALAEKRIATVQALSGTGALRLGFEFLKRfLPAGTTVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGLDFD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 161 ALLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG-LEEDAEGLRAFAALHKELI 239
Cdd:PTZ00376 165 GMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGdLDKDAYAIRLFAERGVEFL 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 240 VASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQ 319
Cdd:PTZ00376 245 VAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRIQ 324

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489126028 320 RMRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL 396
Cdd:PTZ00376 325 NMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVV 401
PLN02397 PLN02397
aspartate transaminase
 2-395 1.29e-171

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 485.62  E-value: 1.29e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   2 FENITAAPADPILGLADLFRADDRPGKINLGIGVYKDETGKTPVLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQEL 81
Cdd:PLN02397  24 FEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAKL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  82 LFGKTSSLINDKRARTAQTPGGTGALRVAADFLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFDA 161
Cdd:PLN02397 104 AYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDFDG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 162 LLASLSEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG-LEEDAEGLRAFAALHKELIV 240
Cdd:PLN02397 184 LLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGdLDADAQSVRMFVEDGHEILV 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 241 ASSYSKNFGLYNERVGACTLVAADAETVDRAFSQMKSAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQR 320
Cdd:PLN02397 264 AQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRIIS 343

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489126028 321 MRLLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAV 395
Cdd:PLN02397 344 MRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAV 418
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
26-392 6.06e-105

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 313.47  E-value: 6.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   26 PGKINLGIGVYKDETgktpvLTSVKKAEQYILENETTKNYLGIDGIPEFGRCTQELLFgkTSSLINDKRARTAQTPGGTG 105
Cdd:pfam00155   1 TDKINLGSNEYLGDT-----LPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLG--RSPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  106 ALRVAADFLARNTSaKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFDALLASLSEAQagdVVLFHGCCHNPT 185
Cdd:pfam00155  74 ANIEALIFLLANPG-DAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  186 GIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARGlEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGACTlvaada 265
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFG-SPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYIL------ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  266 eTVDRAFSQMKSAIRANYSnpPAHGASVVATILSNDALRAiweQELTDMRQRIQRMRLLFVNTLQEKGanrdFSFIIKQN 345
Cdd:pfam00155 223 -GNAAVISQLRKLARPFYS--STHLQAAAAAALSDPLLVA---SELEEMRQRIKERRDYLRDGLQAAG----LSVLPSQA 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489126028  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 1.73e-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: 167.90  E-value: 1.73e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  29 INLGIGVYKDETGKtpvltSVKKAEQYILENETTKNYLGIDGIPEFGRCTQELLFGKTSslINDKRARTAQTPGGTGALR 108
Cdd:cd00609    1 IDLSIGEPDFPPPP-----EVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGG--VDVPPEEIVVTNGAQEALS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 109 VAADFLARNtsAKRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAANHSLDFDALLASLSEAqaGDVVLFHgCCHNPTGID 188
Cdd:cd00609   74 LLLRALLNP--GDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLELLEAAKTPK--TKLLYLN-NPNNPTGAV 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 189 PTLEQWQTLAQLSVEKGWLPLFDFAYQGFARglEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGActLVAADAEtv 268
Cdd:cd00609  149 LSEEELEELAELAKKHGILIISDEAYAELVY--DGEPPPALALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPPEE-- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 269 drAFSQMKSAIRANYSNPPAHGASVVATILSNDalraiwEQELTDMRQRIQRMRLLFVNTLQEKGanrDFSFIIKQNGMF 348
Cdd:cd00609  223 --LLERLKKLLPYTTSGPSTLSQAAAAAALDDG------EEHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGFF 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489126028 349 SF----SGLTKEQVLRLREEFGVYAVASG----------RVNVAGmTPDNMAPLCEAI 392
Cdd:cd00609  292 LWldlpEGDDEEFLERLLLEAGVVVRPGSafgeggegfvRLSFAT-PEEELEEALERL 348
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 5-373 8.35e-13

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: 69.00  E-value: 8.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028   5 ITAAPADPILGLADLFRADDRPGK--INLGIGvykDETGKTPvlTSVKKAEQYILENETTKnYLGIDGIPEFgrctqell 82
Cdd:COG0436    7 LARLPPSPIREVSALAAELKAAGEdvIDLGIG---EPDFPTP--DHIREAAIEALDDGVTG-YTPSAGIPEL-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  83 fgktsslindkRARTAQ-----------------TPGGTGALRVAA-------DflarntsakRVWVSNPSWPNHKSVFN 138
Cdd:COG0436   73 -----------REAIAAyykrrygvdldpdeilvTNGAKEALALALlallnpgD---------EVLVPDPGYPSYRAAVR 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 139 SAGLEVREYNYYDAANHSLDFDALLASLSEAQAGdVVLfhgcC--HNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQG 216
Cdd:COG0436  133 LAGGKPVPVPLDEENGFLPDPEALEAAITPRTKA-IVL----NspNNPTGAVYSREELEALAELAREHDLLVISDEIYEE 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 217 FARGlEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGACtlvAADAETVdRAFSQMKSAIRANYSNPPAHGAsvvAT 296
Cdd:COG0436  208 LVYD-GAEHVSILSLPGLKDRTIVINSFSKSYAMTGWRIGYA---VGPPELI-AALLKLQSNLTSCAPTPAQYAA---AA 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 297 ILSNDalraiwEQELTDMRQRIQRMRLLFVNTLQEKGanrdFSFIIKQNGMF---SFSGLTK---EQVLRLREEFGVyAV 370
Cdd:COG0436  280 ALEGP------QDYVEEMRAEYRRRRDLLVEGLNEIG----LSVVKPEGAFYlfaDVPELGLdseEFAERLLEEAGV-AV 348


                 ...
gi 489126028 371 ASG 373
Cdd:COG0436  349 VPG 351
PRK08637 PRK08637
hypothetical protein; Provisional
 70-287 5.03e-11

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 63.82  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  70 GIPEFGRCTQELLFGKTSSLINDKRARTAQTPGGTGALRVAAD-FLarnTSAKRVWVSNPSWPNHKSVFNSA-GLEVREY 147
Cdd:PRK08637  45 GIPELRDLWQEKMLRENPSLSGKKMSLPIVTNALTHGLSLVADlFV---DQGDTVLLPDHNWGNYKLTFNTRrGAEIVTY 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 148 NYYDAANHsLDFDALLASLSEAQAGD-VVLFHGCCHNPTGIDPTLEQWQTLAQL---SVEKGW--LPLFDFAYQGFargL 221
Cdd:PRK08637 122 PIFDEDGG-FDTDALKEALQAAYNKGkVIVILNFPNNPTGYTPTEKEATAIVEAikeLADAGTkvVAVVDDAYFGL---F 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489126028 222 EEDA--EGL-RAFAALHKELI---VASSYSKNF--GLyneRVGACTL--VAADAETVDRAFSQ-MKSAIRANYSNPP 287
Cdd:PRK08637 198 YEDSykESLfAALANLHSNILavkLDGATKEEFvwGF---RVGFITFgtKAGSSQTVKEALEKkVKGLIRSNISNGP 271
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 73-249 6.70e-08

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: 52.00  E-value: 6.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  73 EFGRCTQELLfgktssliNDKRARTAQTPGGTGALRVAADFLARN-TSAkrVWVSNPSWPNHKSVFNSAGLEVREYNYYD 151
Cdd:cd01494    4 ELEEKLARLL--------QPGNDKAVFVPSGTGANEAALLALLGPgDEV--IVDANGHGSRYWVAAELAGAKPVPVPVDD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 152 AAnhslDFDALLASLSEAQAGD---VVLFHGCCHNPTGIDPTLEqwqtLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGl 228
Cdd:cd01494   74 AG----YGGLDVAILEELKAKPnvaLIVITPNTTSGGVLVPLKE----IRKIAKEYGILLLVDAASAGGASPAPGVLIP- 144

                        170       180
                 ....*....|....*....|.
gi 489126028 229 rafaaLHKELIVASSYSKNFG 249
Cdd:cd01494  145 -----EGGADVVTFSLHKNLG 160
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 100-396 8.48e-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: 54.06  E-value: 8.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 100 TPGGTGALRVAADFLARNTSakRVWVSNPSWPNHKSVFNSAGLEVREYNyYDAanHSLDFDALLASLSEAQAgDVVLFHG 179
Cdd:COG1167  176 TSGAQQALDLALRALLRPGD--TVAVESPTYPGALAALRAAGLRLVPVP-VDE--DGLDLDALEAALRRHRP-RAVYVTP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 180 CCHNPTGIDPTLEQWQTLAQLSVEKG-WL----PLFDFAYQGfargleedaEGLRAFAAL-HKEL-IVASSYSKNF--GL 250
Cdd:COG1167  250 SHQNPTGATMSLERRRALLELARRHGvPIieddYDSELRYDG---------RPPPPLAALdAPGRvIYIGSFSKTLapGL 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 251 yneRVGActlVAADAETVDRafsqMKSAIRANYSNPPAHGASVVATILSNDALRAIweqeLTDMRQRIQRMRLLFVNTLQ 330
Cdd:COG1167  321 ---RLGY---LVAPGRLIER----LARLKRATDLGTSPLTQLALAEFLESGHYDRH----LRRLRREYRARRDLLLAALA 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 331 EKgANRDFSFIIKQNGMFSF----SGLTKEQVLRLREEFGVyAVASG-------------RVNVAGMTPDNMAPLCEAIV 393
Cdd:COG1167  387 RH-LPDGLRVTGPPGGLHLWlelpEGVDAEALAAAALARGI-LVAPGsafsadgpprnglRLGFGAPSEEELEEALRRLA 464


                 ...
gi 489126028 394 AVL 396
Cdd:COG1167  465 ELL 467
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
100-321 3.66e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 51.68  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 100 TPGGTGALRVAADFLARNTSakRVWVSNPSWPNHKSVFNSAGLEVREYNYYDAA-NHSLDFDALLASLSEAQAgdvVLFH 178
Cdd:PRK06225  89 TAGATESLYLVMRAFLSPGD--NAVTPDPGYLIIDNFASRFGAEVIEVPIYSEEcNYKLTPELVKENMDENTR---LIYL 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 179 GCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGFARG----LEEDAEGlrafaalhkeLIVASSYSKNFGLYNER 254
Cdd:PRK06225 164 IDPLNPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRDFAREhtlaAEYAPEH----------TVTSYSFSKIFGMAGLR 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489126028 255 VGActLVAADAetvdrAFSQMKSAIRANYsnppahGASVVATILSNDAL--RAIWEQELTDMRQRIQRM 321
Cdd:PRK06225 234 IGA--VVATPD-----LIEVVKSIVINDL------GTNVIAQEAAIAGLkvKDEWIDRIRRTTFKNQKL 289
HisC COG0079
Histidinol-phosphate/aromatic aminotransferase or cobyric acid decarboxylase [Amino acid ...
 113-270 7.93e-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: 50.52  E-value: 7.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 113 FLARNTSAKRVWVSNPSWPNHKSVFNSAGLEVREYNYydAANHSLDFDALLASLSEAqaGDVVLFhgcC--HNPTGIDPT 190
Cdd:COG0079   82 ARAFLGPGDEVLVPEPTFSEYPIAARAAGAEVVEVPL--DEDFSLDLDALLAAITER--TDLVFL---CnpNNPTGTLLP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 191 LEQWQTLAQLSVEKGWLpLFDFAYQGFArgleEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGactLVAADAETVDR 270
Cdd:COG0079  155 REELEALLEALPADGLV-VVDEAYAEFV----PEEDSALPLLARYPNLVVLRTFSKAYGLAGLRLG---YAIASPELIAA 226
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
96-256 1.02e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 41.08  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028  96 RTAQTPGGTGALRVAADFLARntSAKRVWVSNPSWPNHKSVFNSAGLEVREYNY-YDAANHSLDFDALLASLSEAQAgdv 174
Cdd:PRK06108  86 RIAVTSSGVQALMLAAQALVG--PGDEVVAVTPLWPNLVAAPKILGARVVCVPLdFGGGGWTLDLDRLLAAITPRTR--- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 175 VLFHGCCHNPTGIDPTLEQWQTLAQLSVEKG-WLpLFDFAYQGFARGLEEDAEGLRAFAALHKELIVASSYSKNFGLYNE 253
Cdd:PRK06108 161 ALFINSPNNPTGWTASRDDLRAILAHCRRHGlWI-VADEVYERLYYAPGGRAPSFLDIAEPDDRIIFVNSFSKNWAMTGW 239


                 ...
gi 489126028 254 RVG 256
Cdd:PRK06108 240 RLG 242
PRK05166 PRK05166
histidinol-phosphate transaminase;
122-334 3.91e-03

histidinol-phosphate transaminase;


Pssm-ID: 179950  Cd Length: 371  Bit Score: 38.96  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 122 RVWVSNPSWPNHKSVFNSAGLEVREYNYYDAAnhSLDFDALLASLSEAQAgdvVLFHGCCHNPTGIDPTLEQWQT-LAQL 200
Cdd:PRK05166 114 RVVTLYPSFPLHEDYPTMMGARVERVTVTPDL--GFDLDALCAAVARAPR---MLMFSNPSNPVGSWLTADQLARvLDAT 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126028 201 SVEKgwLPLFDFAYQGFARGlEEDAEGLRAFAALHKELIVASSYSKNFGLYNERVGACtlVAADAETV---DRA---FSQ 274
Cdd:PRK05166 189 PPET--LIVVDEAYAEYAAG-DDYPSALTLLKARGLPWIVLRTFSKAYGLAGLRVGYG--LVSDPELVgllDRVrtpFNV 263

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489126028 275 MKSAIRANYS--NPPAHGASVVATILsndALRAIWEQELTDMRQRI--QRMRLLFVNTLQEKGA 334
Cdd:PRK05166 264 NGAAQAAALAalDDEEHLAKGVALAL---AERERLKKELAEMGYRIapSRANFLFFDARRPASA 324
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH