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Conserved domains on  [gi|1376909036|ref|XP_002965036|]
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aspartate aminotransferase, mitochondrial [Selaginella moellendorffii]

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

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List of domain hits

Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
13-428 0e+00

aspartate transaminase


:

Pssm-ID: 215222  Cd Length: 423  Bit Score: 824.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  13 FMSTAAAPASSVPAGARSGWWEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQ-IIAGKQ 91
Cdd:PLN02397    4 FLKAKSRSRSSMAAAAASSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQrLLAGSR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  92 NMEYLPMGGLVKFNDLSVKLAYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDAR 171
Cdd:PLN02397   84 NKEYLPIEGLAEFNKLSAKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 172 VEAHTFRYYKPSTRGLDFEGLMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGD 251
Cdd:PLN02397  164 VPVRTYRYYDPKTRGLDFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 252 TVRDAQAIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSD 331
Cdd:PLN02397  244 LDADAQSVRMFVEDGHEILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 332 PELKEQWYKEVKVMADRIIGMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGV 411
Cdd:PLN02397  324 PELFSEWTKELKGMADRIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGL 403
                         410
                  ....*....|....*..
gi 1376909036 412 TTGNVEYLANAIHEVTK 428
Cdd:PLN02397  404 SSKNVPYLADAIHAVVT 420
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
13-428 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 824.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  13 FMSTAAAPASSVPAGARSGWWEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQ-IIAGKQ 91
Cdd:PLN02397    4 FLKAKSRSRSSMAAAAASSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQrLLAGSR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  92 NMEYLPMGGLVKFNDLSVKLAYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDAR 171
Cdd:PLN02397   84 NKEYLPIEGLAEFNKLSAKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 172 VEAHTFRYYKPSTRGLDFEGLMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGD 251
Cdd:PLN02397  164 VPVRTYRYYDPKTRGLDFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 252 TVRDAQAIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSD 331
Cdd:PLN02397  244 LDADAQSVRMFVEDGHEILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 332 PELKEQWYKEVKVMADRIIGMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGV 411
Cdd:PLN02397  324 PELFSEWTKELKGMADRIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGL 403
                         410
                  ....*....|....*..
gi 1376909036 412 TTGNVEYLANAIHEVTK 428
Cdd:PLN02397  404 SSKNVPYLADAIHAVVT 420
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
33-427 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: 561.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  33 WEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQIIAGKQ-NMEYLPMGGLVKFNDLSVKL 111
Cdd:COG1448     2 FEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETEtTKSYLPIEGDAAFNDAVQKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 112 AYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEG 191
Cdd:COG1448    82 LFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 192 LMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASG-DtvRDAQAIRIFMEDGHQLA 270
Cdd:COG1448   162 MLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGlE--EDAAGLRLFAEAGPEFL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 271 CAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPELKEQWYKEVKVMADRII 350
Cdd:COG1448   240 VASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIK 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376909036 351 GMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGVTTGNVEYLANAIHEVT 427
Cdd:COG1448   320 AMRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-423 8.37e-104

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 311.93  E-value: 8.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  57 PKKVNVGVGAYRNDegkpvVLECVRKAE-QIIAGKQNMEYLPMGGLVKFNDLSVKLAYGDtaPVLEEKRVAAVQTLSGTG 135
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEkDALAGGTRNLYGPTDGHPELREALAKFLGRS--PVLKLDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 136 ACRLFADFQKRFkPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEGLMEDLKKAPegsFVLLHACAHNPT 215
Cdd:pfam00155  74 ANIEALIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 216 GVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGDtvRDAQAIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLSVVCDn 295
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGS--PDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNAA- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 296 sqqavnVKSQLQQIARPMYSnpPLHGAQIVTTVLSDPELKEQWYKEvkvMADRIIGMREALKSNLEKLGsslpWKHITEQ 375
Cdd:pfam00155 227 ------VISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPSQ 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 376 IGMFCYSGLT----EDQVDRLTKEFHIYMTRN--------GRISMAGVTTGNVEYLANAI 423
Cdd:pfam00155 292 AGFFLLTGLDpetaKELAQVLLEEVGVYVTPGsspgvpgwLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
60-425 4.99e-44

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: 157.12  E-value: 4.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  60 VNVGVGAYRNDEGKPVVLECVRKAEQiiagKQNMEYLPMGGLVKFNDLSVKLAYGDTAPVLEEKRVaaVQTLSGTGACRL 139
Cdd:cd00609     1 IDLSIGEPDFPPPPEVLEALAAAALR----AGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEI--VVTNGAQEALSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 140 FADFqkrF-KPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEglMEDLKKAPEGSFVLLHACaHNPTGVD 218
Cdd:cd00609    75 LLRA---LlNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLE--LLEAAKTPKTKLLYLNNP-NNPTGAV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 219 PTADQWKEMSQLFKSNGLFPFFDMAYQGFASGDTVRDaqaIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLsvVCDNSQq 298
Cdd:cd00609   149 LSEEELEELAELAKKHGILIISDEAYAELVYDGEPPP---ALALLDAYERVIVLRSFSKTFGLPGLRIGYL--IAPPEE- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 299 avnVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPElkeqwyKEVKVMADRIIGMREALKSNLEKLGsslPWKHITEQIGM 378
Cdd:cd00609   223 ---LLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGF 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376909036 379 FCY----SGLTEDQVDRLTKEFHIYMTRNG----------RISMAGVTTgNVEYLANAIHE 425
Cdd:cd00609   291 FLWldlpEGDDEEFLERLLLEAGVVVRPGSafgeggegfvRLSFATPEE-ELEEALERLAE 350
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
13-428 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 824.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  13 FMSTAAAPASSVPAGARSGWWEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQ-IIAGKQ 91
Cdd:PLN02397    4 FLKAKSRSRSSMAAAAASSRFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQrLLAGSR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  92 NMEYLPMGGLVKFNDLSVKLAYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDAR 171
Cdd:PLN02397   84 NKEYLPIEGLAEFNKLSAKLAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGSTIYIPNPTWGNHHNIFRDAG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 172 VEAHTFRYYKPSTRGLDFEGLMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGD 251
Cdd:PLN02397  164 VPVRTYRYYDPKTRGLDFDGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 252 TVRDAQAIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSD 331
Cdd:PLN02397  244 LDADAQSVRMFVEDGHEILVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGD 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 332 PELKEQWYKEVKVMADRIIGMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGV 411
Cdd:PLN02397  324 PELFSEWTKELKGMADRIISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGL 403
                         410
                  ....*....|....*..
gi 1376909036 412 TTGNVEYLANAIHEVTK 428
Cdd:PLN02397  404 SSKNVPYLADAIHAVVT 420
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
32-428 0e+00

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 640.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  32 WWEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQIIAGK-QNMEYLPMGGLVKFNDLSVK 110
Cdd:PTZ00376    4 LFSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKnLDKEYLPIEGLQSFIEAAQK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 111 LAYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRF-KPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDF 189
Cdd:PTZ00376   84 LLFGEASYALAEKRIATVQALSGTGALRLGFEFLKRFlPAGTTVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGLDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 190 EGLMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGDTVRDAQAIRIFMEDGHQL 269
Cdd:PTZ00376  164 DGMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGDLDKDAYAIRLFAERGVEF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 270 ACAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPELKEQWYKEVKVMADRI 349
Cdd:PTZ00376  244 LVAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRI 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376909036 350 IGMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGVTTGNVEYLANAIHEVTK 428
Cdd:PTZ00376  324 QNMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVVR 402
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
33-427 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: 561.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  33 WEAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQIIAGKQ-NMEYLPMGGLVKFNDLSVKL 111
Cdd:COG1448     2 FEHLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETEtTKSYLPIEGDAAFNDAVQKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 112 AYGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEG 191
Cdd:COG1448    82 LFGADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDATVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 192 LMEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASG-DtvRDAQAIRIFMEDGHQLA 270
Cdd:COG1448   162 MLADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGFGDGlE--EDAAGLRLFAEAGPEFL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 271 CAQSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPELKEQWYKEVKVMADRII 350
Cdd:COG1448   240 VASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIK 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376909036 351 GMREALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGVTTGNVEYLANAIHEVT 427
Cdd:COG1448   320 AMRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PRK09257 PRK09257
aromatic amino acid transaminase;
34-426 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 550.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  34 EAVQPAARDPILGVTEAFLADSDPKKVNVGVGAYRNDEGKPVVLECVRKAEQIIAGKQ-NMEYLPMGGLVKFNDLSVKLA 112
Cdd:PRK09257    3 EHLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETEtTKNYLPIEGLAAYRQAVQELL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 113 YGDTAPVLEEKRVAAVQTLSGTGACRLFADFQKRFKPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEGL 192
Cdd:PRK09257   83 FGADSPALAAGRVATVQTPGGTGALRVGADFLKRAFPDAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFDAM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 193 MEDLKKAPEGSFVLLHACAHNPTGVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGdTVRDAQAIRIFMEDGHQLACA 272
Cdd:PRK09257  163 LADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGFGDG-LEEDAYGLRAFAAAGLELLVA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 273 QSFAKNMGLYGQRVGCLSVVCDNSQQAVNVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPELKEQWYKEVKVMADRIIGM 352
Cdd:PRK09257  242 SSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKAM 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376909036 353 REALKSNLEKLGSSLPWKHITEQIGMFCYSGLTEDQVDRLTKEFHIYMTRNGRISMAGVTTGNVEYLANAIHEV 426
Cdd:PRK09257  322 RQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAV 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-423 8.37e-104

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 311.93  E-value: 8.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  57 PKKVNVGVGAYRNDegkpvVLECVRKAE-QIIAGKQNMEYLPMGGLVKFNDLSVKLAYGDtaPVLEEKRVAAVQTLSGTG 135
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEkDALAGGTRNLYGPTDGHPELREALAKFLGRS--PVLKLDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 136 ACRLFADFQKRFkPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEGLMEDLKKAPegsFVLLHACAHNPT 215
Cdd:pfam00155  74 ANIEALIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNPT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 216 GVDPTADQWKEMSQLFKSNGLFPFFDMAYQGFASGDtvRDAQAIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLSVVCDn 295
Cdd:pfam00155 150 GTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGS--PDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNAA- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 296 sqqavnVKSQLQQIARPMYSnpPLHGAQIVTTVLSDPELKEQWYKEvkvMADRIIGMREALKSNLEKLGsslpWKHITEQ 375
Cdd:pfam00155 227 ------VISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPSQ 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 376 IGMFCYSGLT----EDQVDRLTKEFHIYMTRN--------GRISMAGVTTGNVEYLANAI 423
Cdd:pfam00155 292 AGFFLLTGLDpetaKELAQVLLEEVGVYVTPGsspgvpgwLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
60-425 4.99e-44

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: 157.12  E-value: 4.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036  60 VNVGVGAYRNDEGKPVVLECVRKAEQiiagKQNMEYLPMGGLVKFNDLSVKLAYGDTAPVLEEKRVaaVQTLSGTGACRL 139
Cdd:cd00609     1 IDLSIGEPDFPPPPEVLEALAAAALR----AGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEEI--VVTNGAQEALSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 140 FADFqkrF-KPDSRIYIPVPTWANHHNIWRDARVEAHTFRYYKPSTRGLDFEglMEDLKKAPEGSFVLLHACaHNPTGVD 218
Cdd:cd00609    75 LLRA---LlNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEGGFLLDLE--LLEAAKTPKTKLLYLNNP-NNPTGAV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 219 PTADQWKEMSQLFKSNGLFPFFDMAYQGFASGDTVRDaqaIRIFMEDGHQLACAQSFAKNMGLYGQRVGCLsvVCDNSQq 298
Cdd:cd00609   149 LSEEELEELAELAKKHGILIISDEAYAELVYDGEPPP---ALALLDAYERVIVLRSFSKTFGLPGLRIGYL--IAPPEE- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 299 avnVKSQLQQIARPMYSNPPLHGAQIVTTVLSDPElkeqwyKEVKVMADRIIGMREALKSNLEKLGsslPWKHITEQIGM 378
Cdd:cd00609   223 ---LLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELG---PLVVVKPSGGF 290
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376909036 379 FCY----SGLTEDQVDRLTKEFHIYMTRNG----------RISMAGVTTgNVEYLANAIHE 425
Cdd:cd00609   291 FLWldlpEGDDEEFLERLLLEAGVVVRPGSafgeggegfvRLSFATPEE-ELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
115-280 8.69e-14

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: 68.95  E-value: 8.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 115 DTAPVLEEKRVAAVQTLSGTGAcrLFADFQKRFKPDSRIYIPVPTWANHHNI--------WRDARveahtfryYKPSTRG 186
Cdd:cd01494     8 KLARLLQPGNDKAVFVPSGTGA--NEAALLALLGPGDEVIVDANGHGSRYWVaaelagakPVPVP--------VDDAGYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376909036 187 LDFEGLMEDLKKAPEGSFVLLHACAHNPTGVDPTadqwKEMSQLFKSNGLFPFFDMAYQGFASGdtvrdaqAIRIFMEDG 266
Cdd:cd01494    78 GLDVAILEELKAKPNVALIVITPNTTSGGVLVPL----KEIRKIAKEYGILLLVDAASAGGASP-------APGVLIPEG 146
                         170
                  ....*....|....
gi 1376909036 267 HQLACAQSFAKNMG 280
Cdd:cd01494   147 GADVVTFSLHKNLG 160
 
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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