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Conserved domains on  [gi|1063700331|ref|NP_001318216|]
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alanine:glyoxylate aminotransferase [Arabidopsis thaliana]

Protein Classification

alanine--glyoxylate aminotransferase family protein( domain architecture ID 11476754)

alanine--glyoxylate aminotransferase (AGAT) family protein such as AGAT, serine--glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
1-401 0e+00

serine--glyoxylate aminotransaminase


:

Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 815.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331   1 MDYMYGPGRHHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNT 80
Cdd:PLN02409    1 MDYVYAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  81 LSPGDRIVSFLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDENHTIKAICIVHNETATGVTNDISAVR 160
Cdd:PLN02409   81 LSPGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNHKIKAVCVVHNETSTGVTNDLAGVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 161 TLLDHYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKF 240
Cdd:PLN02409  161 KLLDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTQKEEWISNTVTAVMVPPHIDGS 320
Cdd:PLN02409  241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 321 EIVRRAWQRYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYLQHHIPLIPSR 400
Cdd:PLN02409  321 EIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTTPLIPSR 400

                  .
gi 1063700331 401 I 401
Cdd:PLN02409  401 I 401
 
Name Accession Description Interval E-value
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
1-401 0e+00

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 815.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331   1 MDYMYGPGRHHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNT 80
Cdd:PLN02409    1 MDYVYAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  81 LSPGDRIVSFLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDENHTIKAICIVHNETATGVTNDISAVR 160
Cdd:PLN02409   81 LSPGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNHKIKAVCVVHNETSTGVTNDLAGVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 161 TLLDHYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKF 240
Cdd:PLN02409  161 KLLDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTQKEEWISNTVTAVMVPPHIDGS 320
Cdd:PLN02409  241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 321 EIVRRAWQRYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYLQHHIPLIPSR 400
Cdd:PLN02409  321 EIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTTPLIPSR 400

                  .
gi 1063700331 401 I 401
Cdd:PLN02409  401 I 401
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
11-371 0e+00

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 514.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  11 HLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNTLSPGDRIVSF 90
Cdd:cd06451     1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  91 LIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQdenHTIKAICIVHNETATGVTNDISAVRTLLdhYKHPA 170
Cdd:cd06451    81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQ---HDIKAVTLTHNETSTGVLNPLEGIGALA--KKHDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 171 LLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKT-SKSLKVFFDWNDYLKFYKLGTYWPY 249
Cdd:cd06451   156 LLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKkTKPKGFYFDLLLLLKYWGEGYSYPH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 250 TPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTqKEEWISNTVTAVMVPPHIDGSEIVRRAWQR 329
Cdd:cd06451   236 TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLA-KPELRSPTVTAVLVPEGVDGDEVVRRLMKR 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1063700331 330 YNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILK 371
Cdd:cd06451   315 YNIEIAGGLGPTAGKVFRIGHMGEATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
10-390 1.24e-169

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 479.20  E-value: 1.24e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  10 HHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTsGTPFLFPTTGTGAWESALTNTLSPGDRIVS 89
Cdd:COG0075     1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTE-NDVVILTGSGTGAMEAALANLVSPGDKVLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  90 FLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLsqDENHTIKAICIVHNETATGVTNDISAVRTLLDhyKHP 169
Cdd:COG0075    80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEAL--AADPDIKAVAVVHNETSTGVLNPLEEIGALAK--EHG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 170 ALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKFYKLGtYWPY 249
Cdd:COG0075   156 ALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWEKG-QTPY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 250 TPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTqKEEWISNTVTAVMVPPHIDGSEIVRRAWQR 329
Cdd:COG0075   235 TPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFA-EEEYRSPTVTAVRVPEGVDAAALRKRLKER 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063700331 330 YNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYL 390
Cdd:COG0075   314 YGIEIAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVL 374
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
12-281 3.69e-21

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 93.85  E-value: 3.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  12 LFVPGPVNIPEPVIRAMNRNNEDYRSPAIPAL------TKTLLEDVKKIFKTTSGTPF----LFpTTGTGawES------ 75
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVhtlgkeATQAYEEAREKVAEFINAPSndeiIF-TSGTT--EAinlval 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  76 ALTNTLSPGDRIVSFLIGQFS--LLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLsqdeNHTIKAICIVHNETATGVT 153
Cdd:pfam00266  80 SLGRSLKPGDEIVITEMEHHAnlVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLI----TPKTKLVAITHVSNVTGTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 154 NDISAVRTLLDHYKhpALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSlPTGLGIVCASPKALEATKTSKSL--KVF 231
Cdd:pfam00266 156 QPVPEIGKLAHQYG--ALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYG-PTGIGVLYGRRDLLEKMPPLLGGggMIE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063700331 232 FDWNDYLKFYklGTYWPY---TPSIQLLYGLRAALDLIFEEGLENIIARHARL 281
Cdd:pfam00266 233 TVSLQESTFA--DAPWKFeagTPNIAGIIGLGAALEYLSEIGLEAIEKHEHEL 283
 
Name Accession Description Interval E-value
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
1-401 0e+00

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 815.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331   1 MDYMYGPGRHHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNT 80
Cdd:PLN02409    1 MDYVYAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  81 LSPGDRIVSFLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDENHTIKAICIVHNETATGVTNDISAVR 160
Cdd:PLN02409   81 LSPGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTNHKIKAVCVVHNETSTGVTNDLAGVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 161 TLLDHYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKF 240
Cdd:PLN02409  161 KLLDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTQKEEWISNTVTAVMVPPHIDGS 320
Cdd:PLN02409  241 YKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGIDSA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 321 EIVRRAWQRYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYLQHHIPLIPSR 400
Cdd:PLN02409  321 EIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTTPLIPSR 400

                  .
gi 1063700331 401 I 401
Cdd:PLN02409  401 I 401
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
11-371 0e+00

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 514.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  11 HLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNTLSPGDRIVSF 90
Cdd:cd06451     1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  91 LIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQdenHTIKAICIVHNETATGVTNDISAVRTLLdhYKHPA 170
Cdd:cd06451    81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQ---HDIKAVTLTHNETSTGVLNPLEGIGALA--KKHDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 171 LLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKT-SKSLKVFFDWNDYLKFYKLGTYWPY 249
Cdd:cd06451   156 LLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKkTKPKGFYFDLLLLLKYWGEGYSYPH 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 250 TPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTqKEEWISNTVTAVMVPPHIDGSEIVRRAWQR 329
Cdd:cd06451   236 TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLA-KPELRSPTVTAVLVPEGVDGDEVVRRLMKR 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1063700331 330 YNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILK 371
Cdd:cd06451   315 YNIEIAGGLGPTAGKVFRIGHMGEATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
10-390 1.24e-169

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 479.20  E-value: 1.24e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  10 HHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTsGTPFLFPTTGTGAWESALTNTLSPGDRIVS 89
Cdd:COG0075     1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTE-NDVVILTGSGTGAMEAALANLVSPGDKVLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  90 FLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLsqDENHTIKAICIVHNETATGVTNDISAVRTLLDhyKHP 169
Cdd:COG0075    80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEAL--AADPDIKAVAVVHNETSTGVLNPLEEIGALAK--EHG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 170 ALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKFYKLGtYWPY 249
Cdd:COG0075   156 ALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWEKG-QTPY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 250 TPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTqKEEWISNTVTAVMVPPHIDGSEIVRRAWQR 329
Cdd:COG0075   235 TPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFA-EEEYRSPTVTAVRVPEGVDAAALRKRLKER 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063700331 330 YNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYL 390
Cdd:COG0075   314 YGIEIAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVL 374
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
12-281 3.69e-21

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 93.85  E-value: 3.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  12 LFVPGPVNIPEPVIRAMNRNNEDYRSPAIPAL------TKTLLEDVKKIFKTTSGTPF----LFpTTGTGawES------ 75
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVhtlgkeATQAYEEAREKVAEFINAPSndeiIF-TSGTT--EAinlval 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  76 ALTNTLSPGDRIVSFLIGQFS--LLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLsqdeNHTIKAICIVHNETATGVT 153
Cdd:pfam00266  80 SLGRSLKPGDEIVITEMEHHAnlVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLI----TPKTKLVAITHVSNVTGTI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 154 NDISAVRTLLDHYKhpALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSlPTGLGIVCASPKALEATKTSKSL--KVF 231
Cdd:pfam00266 156 QPVPEIGKLAHQYG--ALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYG-PTGIGVLYGRRDLLEKMPPLLGGggMIE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063700331 232 FDWNDYLKFYklGTYWPY---TPSIQLLYGLRAALDLIFEEGLENIIARHARL 281
Cdd:pfam00266 233 TVSLQESTFA--DAPWKFeagTPNIAGIIGLGAALEYLSEIGLEAIEKHEHEL 283
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
12-280 2.68e-13

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 70.71  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  12 LFVPGPVNIPEPVIRAMNRN----NEDYRspaipALTKTLLEDVKKIFKTTSG-TPFLFPTTGTGAWESALtNTLSP--- 83
Cdd:PRK13479    8 LLTPGPLTTSRTVREAMLRDwgswDDDFN-----ALTASVRAKLVAIATGEEGyTCVPLQGSGTFSVEAAI-GSLVPrdg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  84 ----------GDRIVSFLigqfsllwidqqKRLNFNVDVVESDWGQGANLQVLASKLSQDEnhTIKAICIVHNETATGVT 153
Cdd:PRK13479   82 kvlvpdngayGARIAQIA------------EYLGIAHVVLDTGEDEPPDAAEVEAALAADP--RITHVALVHCETTTGIL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 154 NDISAVRTLLdhYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATK-TSKSLKV-F 231
Cdd:PRK13479  148 NPLDEIAAVA--KRHGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKgNSRSLSLdL 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063700331 232 FDWNDYLkfyKLGTYWPYTPSIQLLYGLRAALDLIFEEGleNIIARHAR 280
Cdd:PRK13479  226 YDQWAYM---EKTGQWRFTPPTHVVAAFYQALLELEEEG--GVPARGAR 269
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
79-292 5.72e-13

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 69.78  E-value: 5.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  79 NTLSPGDRIV-------SFLIGqfsllWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDenhtIKAICIVHNETATG 151
Cdd:COG0520    98 GRLKPGDEILitemehhSNIVP-----WQELAERTGAEVRVIPLDEDGELDLEALEALLTPR----TKLVAVTHVSNVTG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 152 VTNDISAVRTLLdHyKHPALLLVDGVSSICALDFRMDEWGVD-VALTGsQKALSlPTGLGIVCASPKALEATKTskslkV 230
Cdd:COG0520   169 TVNPVKEIAALA-H-AHGALVLVDGAQSVPHLPVDVQALGCDfYAFSG-HKLYG-PTGIGVLYGKRELLEALPP-----F 239
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 231 FFDWNDYLKFYKLGTYW---PY-----TPSIQLLYGLRAALDLIFEEGLENIIARHARLgkaTRLAVEAW 292
Cdd:COG0520   240 LGGGGMIEWVSFDGTTYadlPRrfeagTPNIAGAIGLGAAIDYLEAIGMEAIEAREREL---TAYALEGL 306
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
69-213 1.33e-08

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 53.93  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  69 GTGAWESALTNTLSPGDRIVSFLIGQFSLLWIdqqKRLNFNVDVVESD-WGQGANLQVLASKLSQDENHTIKAICIVHNE 147
Cdd:cd01494    26 GTGANEAALLALLGPGDEVIVDANGHGSRYWV---AAELAGAKPVPVPvDDAGYGGLDVAILEELKAKPNVALIVITPNT 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331 148 TATGVTNDISAVRTLLDHYKhpALLLVDGVS----SICALDFRMDEwGVDVALTGSQKALSLPtGLGIVC 213
Cdd:cd01494   103 TSGGVLVPLKEIRKIAKEYG--ILLLVDAASaggaSPAPGVLIPEG-GADVVTFSLHKNLGGE-GGGVVI 168
PRK03080 PRK03080
phosphoserine transaminase;
70-220 2.57e-07

phosphoserine transaminase;


Pssm-ID: 235103  Cd Length: 378  Bit Score: 52.11  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700331  70 TGAWESALTNTLspGDRIVSFLI-GQFSLLWI-DQQKRLNF-NVDVVESDWGQGANLQvlASKLSQDenhtikaICIVHN 146
Cdd:PRK03080   77 TGAWEMALWSLL--GARRVDHLAwESFGSKWAtDVVKQLKLeDPRVLEADYGSLPDLS--AVDFDRD-------VVFTWN 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063700331 147 ETATGV----TNDISAVRTlldhykhpALLLVDGVSSICALDFRMDEwgVDVALTGSQKALSLPTGLGIVCASPKALE 220
Cdd:PRK03080  146 GTTTGVrvpvARWIGADRE--------GLTICDATSAAFALPLDWSK--LDVYTFSWQKVLGGEGGHGMAILSPRAVE 213
 
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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