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Conserved domains on  [gi|73486658|ref|NP_002071|]
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aspartate aminotransferase, mitochondrial isoform 1 precursor [Homo sapiens]

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
 32-430 0e+00

aspartate transaminase


:

Pssm-ID: 215222  Cd Length: 423  Bit Score: 719.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAE 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  112 LALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRdVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDF 191
Cdd:PLN02397 103 LAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  192 TGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINV 271
Cdd:PLN02397 182 DGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGHEI 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  272 CLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRI 351
Cdd:PLN02397 262 LVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRI 341

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73486658  352 IGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK 430
Cdd:PLN02397 342 ISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVVT 420
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
 32-430 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 719.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAE 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  112 LALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRdVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDF 191
Cdd:PLN02397 103 LAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  192 TGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINV 271
Cdd:PLN02397 182 DGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGHEI 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  272 CLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRI 351
Cdd:PLN02397 262 LVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRI 341

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73486658  352 IGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK 430
Cdd:PLN02397 342 ISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVVT 420
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 35-429 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: 587.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELAL 114
Cdd:COG1448   4 HLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQKLLF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 115 GENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRdVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGA 194
Cdd:COG1448  84 GADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDAT-VWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFDGM 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 195 VEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFasGDG-DKDAWAVRHFIEQGINVCL 273
Cdd:COG1448 163 LADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGF--GDGlEEDAAGLRLFAEAGPEFLV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 274 CQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIG 353
Cdd:COG1448 241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73486658 354 MRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVT 429
Cdd:COG1448 321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-425 3.99e-106

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 317.71  E-value: 3.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658    57 SKKMNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALgeNSEVLKSGRFVTVQTISGTG 136
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLG--RSPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   137 ALRIGASFLqrFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPeqsVLLLHACAHNP 216
Cdd:pfam00155  74 ANIEALIFL--LANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   217 TGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASgdGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCk 296
Cdd:pfam00155 149 TGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVF--GSPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNA- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   297 dadeakRVESQLKILIRPMYSnpPLNGARIAAAILNTPDLRKQWLQEvkvMADRIIGMRTQLVSNLKKEGsthnWQHITD 376
Cdd:pfam00155 226 ------AVISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPS 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73486658   377 QIGMFCFTGLKPEQV----ERLIKEFSIYMTK--------DGRISVAGVTSSNVGYLAHAI 425
Cdd:pfam00155 291 QAGFFLLTGLDPETAkelaQVLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 60-427 9.15e-49

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: 169.44  E-value: 9.15e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  60 MNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRfvTVQTISGTGALR 139
Cdd:cd00609   1 IDLSIGEPDFP-----PPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEE--IVVTNGAQEALS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 140 IGASFlqrFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKtcGFDFTGAVEDISKIPEQSVLLLHACaHNPTGV 219
Cdd:cd00609  74 LLLRA---LLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEG--GFLLDLELLEAAKTPKTKLLYLNNP-NNPTGA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 220 DPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAwavRHFIEQGINVCLCQSYAKNMGLYGERVGAftMVCKDad 299
Cdd:cd00609 148 VLSEEELEELAELAKKHGILIISDEAYAELVYDGEPPPA---LALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPP-- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 300 eaKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDlrkqwlQEVKVMADRIIGMRTQLVSNLKKEGSTHNwqhITDQIG 379
Cdd:cd00609 221 --EELLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPLVV---VKPSGG 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73486658 380 MFCFTGLKP----EQVERLIKEFSIYMTKDG----------RISVAGVTSSNVgYLAHAIHQ 427
Cdd:cd00609 290 FFLWLDLPEgddeEFLERLLLEAGVVVRPGSafgeggegfvRLSFATPEEELE-EALERLAE 350
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
 32-430 0e+00

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 719.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAE 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNKLSAK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  112 LALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRdVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDF 191
Cdd:PLN02397 103 LAYGADSPAIKENRVATVQCLSGTGSLRLGAEFLARFYPGST-IYIPNPTWGNHHNIFRDAGVPVRTYRYYDPKTRGLDF 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  192 TGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINV 271
Cdd:PLN02397 182 DGLLEDLKAAPDGSFVLLHACAHNPTGVDPTPEQWEQISDLIKSKNHLPFFDSAYQGFASGDLDADAQSVRMFVEDGHEI 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  272 CLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRI 351
Cdd:PLN02397 262 LVAQSYAKNMGLYGERVGALSVVCKSADVAVRVKSQLKLIARPMYSNPPIHGASIVATILGDPELFSEWTKELKGMADRI 341

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73486658  352 IGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK 430
Cdd:PLN02397 342 ISMRQKLYDALEARGSPGDWSHITKQIGMFSFTGLNKEQVDRMTKEYHIYMTRDGRISMAGLSSKNVPYLADAIHAVVT 420
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
 32-430 0e+00

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 673.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAE 111
Cdd:PTZ00376   4 LFSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSFIEAAQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  112 LALGENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDF 191
Cdd:PTZ00376  84 LLFGEASYALAEKRIATVQALSGTGALRLGFEFLKRFLPAGTTVYVSNPTWPNHVNIFKSAGLNVKEYRYYDPKTKGLDF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  192 TGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINV 271
Cdd:PTZ00376 164 DGMLEDLRTAPNGSVVLLHACAHNPTGVDPTEEQWKEIADVMKRKNLIPFFDMAYQGFASGDLDKDAYAIRLFAERGVEF 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  272 CLCQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRI 351
Cdd:PTZ00376 244 LVAQSFSKNMGLYGERIGALHIVCANKEEAANVLSQLKLIIRPMYSSPPIHGARIADRILSDPELRAEWLSELKEMSGRI 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73486658  352 IGMRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVTK 430
Cdd:PTZ00376 324 QNMRQLLYDELKALGSPGDWEHIINQIGMFSFTGLTKEQVERLIEKYHIYLLDNGRISVAGLTSKNVDYVAEAIHDVVR 402
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 35-429 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: 587.83  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELAL 114
Cdd:COG1448   4 HLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFNDAVQKLLF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 115 GENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKFSRdVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGA 194
Cdd:COG1448  84 GADSPAVAAGRVATVQTPGGTGALRVGADFLKRAFPDAT-VWVSDPTWPNHRAIFEAAGLEVKTYPYYDAETGGVDFDGM 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 195 VEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFasGDG-DKDAWAVRHFIEQGINVCL 273
Cdd:COG1448 163 LADLKQLPAGDVVLLHGCCHNPTGADLTPEQWQEVAELLKERGLIPFLDIAYQGF--GDGlEEDAAGLRLFAEAGPEFLV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 274 CQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIG 353
Cdd:COG1448 241 ASSFSKNFGLYRERVGALSVVAADAEEADRVLSQLKALIRTNYSNPPDHGAAIVATILNDPELRALWEAELAEMRERIKA 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73486658 354 MRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQVT 429
Cdd:COG1448 321 MRQQLVDALRAKGPSRDFSFIARQRGMFSYLGLSPEQVDRLREEFGIYMVGSGRINVAGLNESNIDYVAEAIAAVL 396
PRK09257 PRK09257
aromatic amino acid transaminase;
35-428 0e+00

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 577.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELAL 114
Cdd:PRK09257   4 HLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQAVQELLF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  115 GENSEVLKSGRFVTVQTISGTGALRIGASFLQRFFKfSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGA 194
Cdd:PRK09257  84 GADSPALAAGRVATVQTPGGTGALRVGADFLKRAFP-DAKVWVSDPTWPNHRAIFEAAGLEVKTYPYYDAATKGLDFDAM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  195 VEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFasGDG-DKDAWAVRHFIEQGINVCL 273
Cdd:PRK09257 163 LADLSQAPAGDVVLLHGCCHNPTGADLTPEQWDELAELLKERGLIPFLDIAYQGF--GDGlEEDAYGLRAFAAAGLELLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  274 CQSYAKNMGLYGERVGAFTMVCKDADEAKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIG 353
Cdd:PRK09257 241 ASSFSKNFGLYGERVGALSVVAEDAEEADRVLSQLKATIRTNYSNPPAHGAAIVATILNDPELRAEWEAELEEMRERIKA 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73486658  354 MRTQLVSNLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGYLAHAIHQV 428
Cdd:PRK09257 321 MRQLLVEALKAKGPSRDFDFIARQRGMFSYSGLTPEQVDRLREEFGVYAVGSGRINVAGLNESNIDYVAEAIAAV 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-425 3.99e-106

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 317.71  E-value: 3.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658    57 SKKMNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALgeNSEVLKSGRFVTVQTISGTG 136
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELREALAKFLG--RSPVLKLDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   137 ALRIGASFLqrFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFTGAVEDISKIPeqsVLLLHACAHNP 216
Cdd:pfam00155  74 ANIEALIFL--LANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSNDFHLDFDALEAALKEKP---KVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   217 TGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASgdGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCk 296
Cdd:pfam00155 149 TGTVATLEELEKLLDLAKEHNILLLVDEAYAGFVF--GSPDAVATRALLAEGPNLLVVGSFSKAFGLAGWRVGYILGNA- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   297 dadeakRVESQLKILIRPMYSnpPLNGARIAAAILNTPDLRKQWLQEvkvMADRIIGMRTQLVSNLKKEGsthnWQHITD 376
Cdd:pfam00155 226 ------AVISQLRKLARPFYS--STHLQAAAAAALSDPLLVASELEE---MRQRIKERRDYLRDGLQAAG----LSVLPS 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73486658   377 QIGMFCFTGLKPEQV----ERLIKEFSIYMTK--------DGRISVAGVTSSNVGYLAHAI 425
Cdd:pfam00155 291 QAGFFLLTGLDPETAkelaQVLLEEVGVYVTPgsspgvpgWLRITVAGGTEEELEELLEAI 351
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 60-427 9.15e-49

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: 169.44  E-value: 9.15e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  60 MNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEVLKSGRfvTVQTISGTGALR 139
Cdd:cd00609   1 IDLSIGEPDFP-----PPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVPPEE--IVVTNGAQEALS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 140 IGASFlqrFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYRYYDPKtcGFDFTGAVEDISKIPEQSVLLLHACaHNPTGV 219
Cdd:cd00609  74 LLLRA---LLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEG--GFLLDLELLEAAKTPKTKLLYLNNP-NNPTGA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 220 DPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAwavRHFIEQGINVCLCQSYAKNMGLYGERVGAftMVCKDad 299
Cdd:cd00609 148 VLSEEELEELAELAKKHGILIISDEAYAELVYDGEPPPA---LALLDAYERVIVLRSFSKTFGLPGLRIGY--LIAPP-- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 300 eaKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDlrkqwlQEVKVMADRIIGMRTQLVSNLKKEGSTHNwqhITDQIG 379
Cdd:cd00609 221 --EELLERLKKLLPYTTSGPSTLSQAAAAAALDDGE------EHLEELRERYRRRRDALLEALKELGPLVV---VKPSGG 289

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73486658 380 MFCFTGLKP----EQVERLIKEFSIYMTKDG----------RISVAGVTSSNVgYLAHAIHQ 427
Cdd:cd00609 290 FFLWLDLPEgddeEFLERLLLEAGVVVRPGSafgeggegfvRLSFATPEEELE-EALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 119-293 2.58e-09

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: 56.24  E-value: 2.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 119 EVLKSGRFVTVQTISGTGALRIGASFLqrfFKFSRDVFLPKPTWGNHTPIFRD-AGMQLQGYRYyDPKTCGFDFTGAVED 197
Cdd:cd01494  11 RLLQPGNDKAVFVPSGTGANEAALLAL---LGPGDEVIVDANGHGSRYWVAAElAGAKPVPVPV-DDAGYGGLDVAILEE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 198 ISKIPEQSVLLLHACAHNPTGVDPRpeqwKEIATVVKKRNLFAFFDMAYQGFASGdgdkdaWAVRHFIEQGINVCLcQSY 277
Cdd:cd01494  87 LKAKPNVALIVITPNTTSGGVLVPL----KEIRKIAKEYGILLLVDAASAGGASP------APGVLIPEGGADVVT-FSL 155

                       170
                ....*....|....*.
gi 73486658 278 AKNMGlyGERVGAFTM 293
Cdd:cd01494 156 HKNLG--GEGGGVVIV 169
PRK08637 PRK08637
hypothetical protein; Provisional
 57-350 1.15e-07

hypothetical protein; Provisional


Pssm-ID: 181512  Cd Length: 388  Bit Score: 53.42  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   57 SKKMNLGVGAYRDDNGKPYvLPSVRKAEAQIAAKNLdKEYLPIGGLAEFCKASAELALGENSEvLKSgrfvtvQTISG-- 134
Cdd:PRK08637   3 ATKYNATIGMATEKGGPMY-LSSLQDLLNDLTPDEI-FPYAPPQGIPELRDLWQEKMLRENPS-LSG------KKMSLpi 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  135 -TGALRIGASFLQRFFKFSRD-VFLPKPTWGNHTPIFRDA-GMQLQGYRYYDpKTCGFDFTGAVE--DISKIPEQSVLLL 209
Cdd:PRK08637  74 vTNALTHGLSLVADLFVDQGDtVLLPDHNWGNYKLTFNTRrGAEIVTYPIFD-EDGGFDTDALKEalQAAYNKGKVIVIL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  210 HAcAHNPTGVDPRPEQWKEIATVVKK-----RNLFAFFDMAYQGFASGDGDKdawavrhfieQGINVCLCQSY------- 277
Cdd:PRK08637 153 NF-PNNPTGYTPTEKEATAIVEAIKEladagTKVVAVVDDAYFGLFYEDSYK----------ESLFAALANLHsnilavk 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  278 ----AKNMGLYGERVGAFTMVCK--DADEAKRV-ESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADR 350
Cdd:PRK08637 222 ldgaTKEEFVWGFRVGFITFGTKagSSQTVKEAlEKKVKGLIRSNISNGPHPSQSAVLRALNSPEFDKEKQEKFQILKER 301
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 155-397 3.86e-06

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: 48.59  E-value: 3.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 155 VFLPKPTWGNHTPIFRDAGMQLqgyRYYDPK-TCGFDFTgaVEDI-SKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATV 232
Cdd:COG0436 117 VLVPDPGYPSYRAAVRLAGGKP---VPVPLDeENGFLPD--PEALeAAITPRTKAIVLNSPNNPTGAVYSREELEALAEL 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 233 VKKRNLFAFFDMAYQGFASgDGDK--DAWAVRHFIEQGInvcLCQSYAKNMGLYGERVGAftMVCKDA--DEAKRVESQl 308
Cdd:COG0436 192 AREHDLLVISDEIYEELVY-DGAEhvSILSLPGLKDRTI---VINSFSKSYAMTGWRIGY--AVGPPEliAALLKLQSN- 264

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658 309 kilirpMYSNPPLNGARIAAAILNTPDlrkqwlQEVKVMADRIIGMRTQLVSNLKKEGsthnWQHITDQIGMFCFTGLKP 388
Cdd:COG0436 265 ------LTSCAPTPAQYAAAAALEGPQ------DYVEEMRAEYRRRRDLLVEGLNEIG----LSVVKPEGAFYLFADVPE 328

                       250
                ....*....|....*
gi 73486658 389 ------EQVERLIKE 397
Cdd:COG0436 329 lgldseEFAERLLEE 343
PRK07683 PRK07683
aminotransferase A; Validated
 72-246 7.36e-04

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 41.63  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658   72 GKP-YVLPSVRKAEAQIAAKNLDKEYLPIGGLAE-------FCKASAELALGENSEVLKsgrfvtvqTISGTGALRIGas 143
Cdd:PRK07683  36 GQPdFPTPSHVKEAAKRAITENYTSYTHNAGLLElrkaacnFVKDKYDLHYSPESEIIV--------TIGASEAIDIA-- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  144 fLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQgyrYYDPKTCGFDFTG-AVEDIskIPEQSVLLLHACAHNPTGVDPR 222
Cdd:PRK07683 106 -FRTILEPGTEVILPAPIYPGYEPIIRLCGAKPV---FIDTRSTGFRLTAeALENA--ITEKTRCVVLPYPSNPTGVTLS 179

                        170       180
                 ....*....|....*....|....
gi 73486658  223 PEQWKEIATVVKKRNLFAFFDMAY 246
Cdd:PRK07683 180 KEELQDIADVLKDKNIFVLSDEIY 203
PRK07337 PRK07337
pyridoxal phosphate-dependent aminotransferase;
204-289 4.22e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180937  Cd Length: 388  Bit Score: 39.27  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  204 QSVLLlhACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVrhfieqGINVCLCQSYAKNMGL 283
Cdd:PRK07337 165 RGVLL--ASPSNPTGTSIAPDELRRIVEAVRARGGFTIVDEIYQGLSYDAAPVSALSL------GDDVITINSFSKYFNM 236


                 ....*.
gi 73486658  284 YGERVG 289
Cdd:PRK07337 237 TGWRLG 242
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
215-289 5.98e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 38.55  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  215 NPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGF---------ASGDGDKDawavrHFIEQGinvclcqSYAKNMGLYG 285
Cdd:PRK06348 173 NPTGAVFSKETLEEIAKIAIEYDLFIISDEVYDGFsfyedfvpmATLAGMPE-----RTITFG-------SFSKDFAMTG 240


                 ....
gi 73486658  286 ERVG 289
Cdd:PRK06348 241 WRIG 244
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
215-335 6.04e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 38.68  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73486658  215 NPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASgdGDKDAWAVRHF--IEQgiNVCLCQSYAKNMGLYGERVGAFt 292
Cdd:PRK07568 173 NPTGVVYTKEELEMLAEIAKKHDLFLISDEVYREFVY--DGLKYTSALSLegLED--RVIIIDSVSKRYSACGARIGCL- 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 73486658  293 mVCKDADEAKRV--ESQLKIlirpmysNPPLNGARIAAAILNTPD 335
Cdd:PRK07568 248 -ISKNKELIAAAmkLCQARL-------SPPTLEQIGAAALLDTPE 284
 
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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