NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|443542|pdb|7AAT|A]
View 

Chain A, ASPARTATE AMINOTRANSFERASE

Protein Classification

aspartate aminotransferase( domain architecture ID 10791343)

aspartate aminotransferase catalyzes the conversion of 2-oxoglutarate and L-aspartate to L-glutamate and oxaloacetate and plays a major role in the metabolism of amino acids and organic acids related to the Krebs cycle

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
1-401 0e+00

aspartate transaminase


:

Pssm-ID: 215222  Cd Length: 423  Bit Score: 715.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         1 SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRAS 80
Cdd:PLN02397  21 SSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        81 AELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRdVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSL 160
Cdd:PLN02397 101 AKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       161 DFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGI 240
Cdd:PLN02397 180 DFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       241 DVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMAD 320
Cdd:PLN02397 260 EILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMAD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       321 RIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT 400
Cdd:PLN02397 340 RIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVV 419

                 .
7AAT_A       401 K 401
Cdd:PLN02397 420 T 420
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
1-401 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 715.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         1 SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRAS 80
Cdd:PLN02397  21 SSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        81 AELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRdVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSL 160
Cdd:PLN02397 101 AKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       161 DFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGI 240
Cdd:PLN02397 180 DFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       241 DVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMAD 320
Cdd:PLN02397 260 EILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMAD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       321 RIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT 400
Cdd:PLN02397 340 RIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVV 419

                 .
7AAT_A       401 K 401
Cdd:PLN02397 420 T 420
TyrB COG1448
Aspartate/tyrosine/aromatic aminotransferase [Amino acid transport and metabolism];
5-399 0e+00

Aspartate/tyrosine/aromatic aminotransferase [Amino acid transport and metabolism];


Pssm-ID: 224365  Cd Length: 396  Bit Score: 568.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        5 SHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELA 84
Cdd:COG1448   3 EKIEAAPADPILGLKEAFKADPRPNKVNLGIGVYKDEDGKTPVLRAVKKAEKRLLEQEKTKNYLPIEGLPEFLEAVQKLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       85 LGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKfSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTG 164
Cdd:COG1448  83 FGADSPALAEDRVATVQTLGGTGALRVAADFLARFFP-DATVWISDPTWPNHKAIFEAAGLEVETYPYYDAETKGLDFDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      165 AMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGdINRDAWALRHFIEQGIDVVL 244
Cdd:COG1448 162 MLADLKTAPEGSVVLLHGCCHNPTGIDPTEEQWQELADLIKERGLIPFFDIAYQGFADG-LEEDAYALRLFAEVGPELLV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      245 SQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIIS 324
Cdd:COG1448 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKAIIRTNYSNPPAHGAAVVATILNNPELRAEWEQELEEMRQRILE 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7AAT_A      325 MRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQV 399
Cdd:COG1448 321 MRQALVDALKALGAPRNFDFIISQRGMFSYTGLSPEQVDRLREEFGIYLVASGRINVAGLNTSNIDYVAKAIAAV 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
28-396 6.71e-96

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 290.75  E-value: 6.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         28 SKKMNLGVGAYRDDngkpyVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKsgRYVTVQGISGTG 107
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSPVLKLD--REAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        108 SLRVGANFLqrFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPeksIILLHACAHNP 187
Cdd:pfam00155  74 ANIEALIFL--LANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        188 TGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDinRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICr 267
Cdd:pfam00155 149 TGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGS--PDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNA- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        268 daeeakRVESQLKILIRPMYSnpPMNGARIASLILNTPELRKEWLVEvkgMADRIISMRTQLVSNLKKEGsshnWQHITD 347
Cdd:pfam00155 226 ------AVISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPS 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
7AAT_A        348 QIGMFCFTGLKPEQV----ERLTKEFSIYMTK--------DGRISVAGVASSNVGYLAHAI 396
Cdd:pfam00155 291 QAGFFLLTGLDPETAkelaQVLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
31-383 3.49e-43

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: 154.04  E-value: 3.49e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       31 MNLGVGAYRDDNGKPyvlncVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRyvTVQGISGTGSLR 110
Cdd:cd00609   1 IDLSIGEPDFPPPPE-----VLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEE--IVVTNGAQEALS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      111 VGANFlqrFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFtgAMEDISKIPEKSIILLHACaHNPTGV 190
Cdd:cd00609  74 LLLRA---LLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDL--ELLEAAKTPKTKLLYLNNP-NNPTGA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      191 DPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAwalRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVicrdae 270
Cdd:cd00609 148 VLSEEELEELAELAKKHGILIISDEAYAELVYDGEPPPA---LALLDAYERVIVLRSFSKTFGLPGLRIGYLIA------ 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      271 EAKRVESQLKILIRPMYSNPPMNGARIASLILNTPElrkewlVEVKGMADRIISMRTQLVSNLKKEGSSHNwqhITDQIG 350
Cdd:cd00609 219 PPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPLVV---VKPSGG 289
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
7AAT_A      351 MFCFTGLKP----EQVERLTKEFSIYMTKDG----------RISVAG 383
Cdd:cd00609 290 FFLWLDLPEgddeEFLERLLLEAGVVVRPGSafgeggegfvRLSFAT 336
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
1-401 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 715.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         1 SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRAS 80
Cdd:PLN02397  21 SSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        81 AELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRdVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSL 160
Cdd:PLN02397 101 AKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       161 DFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGI 240
Cdd:PLN02397 180 DFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       241 DVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMAD 320
Cdd:PLN02397 260 EILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMAD 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       321 RIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT 400
Cdd:PLN02397 340 RIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVV 419

                 .
7AAT_A       401 K 401
Cdd:PLN02397 420 T 420
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
1-401 0e+00

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 674.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         1 SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRAS 80
Cdd:PTZ00376   2 DSLFSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSFIEAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        81 AELALGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSL 160
Cdd:PTZ00376  82 QKLLFGEASYALAEKRIATVQALSGTGALRLGFEFLKRFLPAGTTVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       161 DFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGI 240
Cdd:PTZ00376 162 DFDGMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGDLDKDAYAIRLFAERGV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       241 DVVLSQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMAD 320
Cdd:PTZ00376 242 EFLVAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       321 RIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT 400
Cdd:PTZ00376 322 RIQNMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVV 401

                 .
7AAT_A       401 K 401
Cdd:PTZ00376 402 R 402
PRK09257 PRK09257
aromatic amino acid transaminase;
5-399 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 568.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         5 SHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELA 84
Cdd:PRK09257   3 EHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQELL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        85 LGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKfSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTG 164
Cdd:PRK09257  83 FGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFP-DAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       165 AMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGdINRDAWALRHFIEQGIDVVL 244
Cdd:PRK09257 162 MLADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDG-LEEDAYGLRAFAAAGLELLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       245 SQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIIS 324
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7AAT_A       325 MRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQV 399
Cdd:PRK09257 321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAV 395
TyrB COG1448
Aspartate/tyrosine/aromatic aminotransferase [Amino acid transport and metabolism];
5-399 0e+00

Aspartate/tyrosine/aromatic aminotransferase [Amino acid transport and metabolism];


Pssm-ID: 224365  Cd Length: 396  Bit Score: 568.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        5 SHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELA 84
Cdd:COG1448   3 EKIEAAPADPILGLKEAFKADPRPNKVNLGIGVYKDEDGKTPVLRAVKKAEKRLLEQEKTKNYLPIEGLPEFLEAVQKLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       85 LGENSEAFKSGRYVTVQGISGTGSLRVGANFLQRFFKfSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTG 164
Cdd:COG1448  83 FGADSPALAEDRVATVQTLGGTGALRVAADFLARFFP-DATVWISDPTWPNHKAIFEAAGLEVETYPYYDAETKGLDFDG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      165 AMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGdINRDAWALRHFIEQGIDVVL 244
Cdd:COG1448 162 MLADLKTAPEGSVVLLHGCCHNPTGIDPTEEQWQELADLIKERGLIPFFDIAYQGFADG-LEEDAYALRLFAEVGPELLV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      245 SQSYAKNMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASLILNTPELRKEWLVEVKGMADRIIS 324
Cdd:COG1448 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKAIIRTNYSNPPAHGAAVVATILNNPELRAEWEQELEEMRQRILE 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7AAT_A      325 MRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQV 399
Cdd:COG1448 321 MRQALVDALKALGAPRNFDFIISQRGMFSYTGLSPEQVDRLREEFGIYLVASGRINVAGLNTSNIDYVAKAIAAV 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
28-396 6.71e-96

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 290.75  E-value: 6.71e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A         28 SKKMNLGVGAYRDDngkpyVLNCVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKsgRYVTVQGISGTG 107
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLGRSPVLKLD--REAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        108 SLRVGANFLqrFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFTGAMEDISKIPeksIILLHACAHNP 187
Cdd:pfam00155  74 ANIEALIFL--LANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        188 TGVDPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDinRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVICr 267
Cdd:pfam00155 149 TGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGS--PDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNA- 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A        268 daeeakRVESQLKILIRPMYSnpPMNGARIASLILNTPELRKEWLVEvkgMADRIISMRTQLVSNLKKEGsshnWQHITD 347
Cdd:pfam00155 226 ------AVISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPS 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
7AAT_A        348 QIGMFCFTGLKPEQV----ERLTKEFSIYMTK--------DGRISVAGVASSNVGYLAHAI 396
Cdd:pfam00155 291 QAGFFLLTGLDPETAkelaQVLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
31-383 3.49e-43

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: 154.04  E-value: 3.49e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       31 MNLGVGAYRDDNGKPyvlncVRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRyvTVQGISGTGSLR 110
Cdd:cd00609   1 IDLSIGEPDFPPPPE-----VLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEE--IVVTNGAQEALS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      111 VGANFlqrFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAYRYYDPKTCSLDFtgAMEDISKIPEKSIILLHACaHNPTGV 190
Cdd:cd00609  74 LLLRA---LLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDL--ELLEAAKTPKTKLLYLNNP-NNPTGA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      191 DPRQEQWKELASVVKKRNLLAYFDMAYQGFASGDINRDAwalRHFIEQGIDVVLSQSYAKNMGLYGERAGAFTVicrdae 270
Cdd:cd00609 148 VLSEEELEELAELAKKHGILIISDEAYAELVYDGEPPPA---LALLDAYERVIVLRSFSKTFGLPGLRIGYLIA------ 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      271 EAKRVESQLKILIRPMYSNPPMNGARIASLILNTPElrkewlVEVKGMADRIISMRTQLVSNLKKEGSSHNwqhITDQIG 350
Cdd:cd00609 219 PPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPLVV---VKPSGG 289
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
7AAT_A      351 MFCFTGLKP----EQVERLTKEFSIYMTKDG----------RISVAG 383
Cdd:cd00609 290 FFLWLDLPEgddeEFLERLLLEAGVVVRPGSafgeggegfvRLSFAT 336
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
90-264 4.43e-11

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: 60.86  E-value: 4.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       90 EAFKSGRYVTVQGISGTGSLRVGANFLqrfFKFSRDVYLPKPSWGNHTPIFRD-AGLQLQAYRYyDPKTCSLDFTGAMED 168
Cdd:cd01494  11 RLLQPGNDKAVFVPSGTGANEAALLAL---LGPGDEVIVDANGHGSRYWVAAElAGAKPVPVPV-DDAGYGGLDVAILEE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      169 ISKIPEKSIILLHACAHNPTGVDPRqeqwKELASVVKKRNLLAYFDMAYQGFASGdinrdaWALRHFIEQGIDVVlSQSY 248
Cdd:cd01494  87 LKAKPNVALIVITPNTTSGGVLVPL----KEIRKIAKEYGILLLVDAASAGGASP------APGVLIPEGGADVV-TFSL 155
                       170
                ....*....|....*.
7AAT_A      249 AKNMGlyGERAGAFTV 264
Cdd:cd01494 156 HKNLG--GEGGGVVIV 169
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism];
55-276 2.00e-07

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism];


Pssm-ID: 223513 [Multi-domain]  Cd Length: 393  Bit Score: 52.66  E-value: 2.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A       55 EAMIAAKKMDKE-YLPIAGLADFTRASAELALGENSEAFKSGRYVTVqGISGTGSLrvgANFLQRFFKFSRDVYLPKPSW 133
Cdd:COG0436  48 EAAIEALEEGGThYTPSAGIPELREAIAEKYKRRYGLDVDPEEEIIV-TAGAKEAL---FLAFLALLNPGDEVLIPDPGY 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7AAT_A      134 GNHTPIFRDAGLQLqayRYYDPKTCSLDFTGAMEDI-SKIPEKSIILLHACAHNPTGVDPRQEQWKELASVVKKRNLLAY 212
Cdd:COG0436 124 PSYEAAVKLAGGKP---VPVPLDEEENGFKPDLEDLeAAITPKTKAIILNSPNNPTGAVYSKEELKAIVELAREHDIIII 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
7AAT_A      213 FDMAYQGFASGDinRDAWALRHFIEQGIDVVLSQSYAKNMGLYGERAGAftVICRDAEEAKRVE 276
Cdd:COG0436 201 SDEIYEELVYDG--AEHPSILELAGARDRTITINSFSKTYGMTGWRIGW--VVGPPEELIAALR 260
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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