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Conserved domains on  [gi|50539730|ref|NP_001002331|]
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alanine--glyoxylate and serine--pyruvate aminotransferase a [Danio rerio]

Protein Classification

alanine--glyoxylate aminotransferase family protein( domain architecture ID 10157834)

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
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 22-384 2.03e-159

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: 452.13  E-value: 2.03e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  22 LMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVTLAVSGPGHAAMECAIFNSLEPGDKILIA 101
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 102 VNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKYRPAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFLVD 181
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 182 SVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERAcHKIFNRKTKPISYFLDLNWLANYWGCDDkpvrSYHH 261
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERA-LERIKKKTKPKGFYFDLLLLLKYWGEGY----SYPH 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 262 TGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDkKARLPTVTTIVAPPGYDWREITGYIMKT 341
Cdd:cd06451 236 TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKP-ELRSPTVTAVLVPEGVDGDEVVRRLMKR 314

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 50539730 342 FNIEISGGLGPSAGMVLRVGLMGCnSNKANVDKVLEALADALK 384
Cdd:cd06451 315 YNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 22-384 2.03e-159

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: 452.13  E-value: 2.03e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  22 LMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVTLAVSGPGHAAMECAIFNSLEPGDKILIA 101
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 102 VNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKYRPAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFLVD 181
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 182 SVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERAcHKIFNRKTKPISYFLDLNWLANYWGCDDkpvrSYHH 261
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERA-LERIKKKTKPKGFYFDLLLLLKYWGEGY----SYPH 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 262 TGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDkKARLPTVTTIVAPPGYDWREITGYIMKT 341
Cdd:cd06451 236 TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKP-ELRSPTVTAVLVPEGVDGDEVVRRLMKR 314

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 50539730 342 FNIEISGGLGPSAGMVLRVGLMGCnSNKANVDKVLEALADALK 384
Cdd:cd06451 315 YNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 21-384 5.29e-143

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: 411.02  E-value: 5.29e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  21 RLMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVtLAVSGPGHAAMECAIFNSLEPGDKILI 100
Cdd:COG0075   1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDV-VILTGSGTGAMEAALANLVSPGDKVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 101 AVNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKYR-PAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFL 179
Cdd:COG0075  80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 180 VDSVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERACHKIfnRKTKPISYFLDLNWLANYWgcdDKpvRSY 259
Cdd:COG0075 160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYW---EK--GQT 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 260 HHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDkKARLPTVTTIVAPPGYDWREITGYIM 339
Cdd:COG0075 233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 50539730 340 KTFNIEISGGLGPSAGMVLRVGLMGcNSNKANVDKVLEALADALK 384
Cdd:COG0075 312 ERYGIEIAGGLGPLKGKIFRIGHMG-YVNPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 16-384 2.24e-107

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 321.32  E-value: 2.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   16 FPVPQRLMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVTLAVSGPGHAAMECAIFNSLEPG 95
Cdd:PLN02409   5 YAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   96 DKILIAVNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNK---YRPAVFFLTHGESSTGVVHPIDGIGPL-- 170
Cdd:PLN02409  85 DKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLld 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  171 CRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERACHKIFNRKTKPISY----FLDLNWLA 246
Cdd:PLN02409 165 CAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKLG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  247 NYWGcddkpvrsyhHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDKKARLPTVTTIVAP 326
Cdd:PLN02409 245 TYWP----------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVP 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50539730  327 PGYDWREITGYIMKTFNIEISGGLGPSAGMVLRVGLMGcNSNK-------ANVDKVLEALADALK 384
Cdd:PLN02409 315 EGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLG-NVNElqllgalAGVEMVLKDVGYPVK 378
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 25-375 6.17e-50

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: 172.05  E-value: 6.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730    25 GPGPSNVPARISAAGAQ----------PMLGHLHTETIEIMNQIKSGIQYAFQTK-NRVTLAVSGPGHAaMECAI---FN 90
Cdd:pfam00266   5 SAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEA-INLVAlslGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730    91 SLEPGDKILIAVNGIWGER--ASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAVFFLTHGESSTGVVHPIDGIG 168
Cdd:pfam00266  84 SLKPGDEIVITEMEHHANLvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVPEIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   169 PLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKvLNAPPGTAPISFSERACHKIfnRKTKPISYFLDLNWLaNY 248
Cdd:pfam00266 163 KLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL-QE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   249 WGCDDKPVRSYHHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDKkaRLPTVTTIVApPG 328
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNF-KG 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50539730   329 YDWREItGYIMKTFNIEISGGL---GPSAGM-----VLRVGLmGCNSNKANVDKV 375
Cdd:pfam00266 316 VHPHDV-ATLLDESGIAVRSGHhcaQPLMVRlglggTVRASF-YIYNTQEDVDRL 368
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 22-384 2.03e-159

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: 452.13  E-value: 2.03e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  22 LMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVTLAVSGPGHAAMECAIFNSLEPGDKILIA 101
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 102 VNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKYRPAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFLVD 181
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 182 SVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERAcHKIFNRKTKPISYFLDLNWLANYWGCDDkpvrSYHH 261
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERA-LERIKKKTKPKGFYFDLLLLLKYWGEGY----SYPH 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 262 TGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDkKARLPTVTTIVAPPGYDWREITGYIMKT 341
Cdd:cd06451 236 TPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKP-ELRSPTVTAVLVPEGVDGDEVVRRLMKR 314

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 50539730 342 FNIEISGGLGPSAGMVLRVGLMGCnSNKANVDKVLEALADALK 384
Cdd:cd06451 315 YNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 21-384 5.29e-143

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: 411.02  E-value: 5.29e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  21 RLMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVtLAVSGPGHAAMECAIFNSLEPGDKILI 100
Cdd:COG0075   1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDV-VILTGSGTGAMEAALANLVSPGDKVLV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 101 AVNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKYR-PAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFL 179
Cdd:COG0075  80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 180 VDSVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERACHKIfnRKTKPISYFLDLNWLANYWgcdDKpvRSY 259
Cdd:COG0075 160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYW---EK--GQT 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 260 HHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDkKARLPTVTTIVAPPGYDWREITGYIM 339
Cdd:COG0075 233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 50539730 340 KTFNIEISGGLGPSAGMVLRVGLMGcNSNKANVDKVLEALADALK 384
Cdd:COG0075 312 ERYGIEIAGGLGPLKGKIFRIGHMG-YVNPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 16-384 2.24e-107

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 321.32  E-value: 2.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   16 FPVPQRLMLGPGPSNVPARISAAGAQPMLGHLHTETIEIMNQIKSGIQYAFQTKNRVTLAVSGPGHAAMECAIFNSLEPG 95
Cdd:PLN02409   5 YAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   96 DKILIAVNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNK---YRPAVFFLTHGESSTGVVHPIDGIGPL-- 170
Cdd:PLN02409  85 DKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLld 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  171 CRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLNAPPGTAPISFSERACHKIFNRKTKPISY----FLDLNWLA 246
Cdd:PLN02409 165 CAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKLG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  247 NYWGcddkpvrsyhHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDKKARLPTVTTIVAP 326
Cdd:PLN02409 245 TYWP----------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVP 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50539730  327 PGYDWREITGYIMKTFNIEISGGLGPSAGMVLRVGLMGcNSNK-------ANVDKVLEALADALK 384
Cdd:PLN02409 315 EGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLG-NVNElqllgalAGVEMVLKDVGYPVK 378
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 25-375 6.17e-50

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: 172.05  E-value: 6.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730    25 GPGPSNVPARISAAGAQ----------PMLGHLHTETIEIMNQIKSGIQYAFQTK-NRVTLAVSGPGHAaMECAI---FN 90
Cdd:pfam00266   5 SAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTEA-INLVAlslGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730    91 SLEPGDKILIAVNGIWGER--ASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAVFFLTHGESSTGVVHPIDGIG 168
Cdd:pfam00266  84 SLKPGDEIVITEMEHHANLvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVPEIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   169 PLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKvLNAPPGTAPISFSERACHKIfnRKTKPISYFLDLNWLaNY 248
Cdd:pfam00266 163 KLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL-QE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   249 WGCDDKPVRSYHHTGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQMGLKLFVQDKkaRLPTVTTIVApPG 328
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNF-KG 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50539730   329 YDWREItGYIMKTFNIEISGGL---GPSAGM-----VLRVGLmGCNSNKANVDKV 375
Cdd:pfam00266 316 VHPHDV-ATLLDESGIAVRSGHhcaQPLMVRlglggTVRASF-YIYNTQEDVDRL 368
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 55-216 1.22e-24

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: 98.99  E-value: 1.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  55 MNQIKSGIQYAFQTKNRVTLAVSGpGHAAMECAIFNSLEPGDKILIAVNGIWGERASeIAERIGAKVNTVETMAGGYLTN 134
Cdd:cd01494   2 LEELEEKLARLLQPGNDKAVFVPS-GTGANEAALLALLGPGDEVIVDANGHGSRYWV-AAELAGAKPVPVPVDDAGYGGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 135 E--EIEKALNKYRPAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAP---ICMDEQGIDILYTGSQKVL 209
Cdd:cd01494  80 DvaILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNL 159


                ....*..
gi 50539730 210 NAPPGTA 216
Cdd:cd01494 160 GGEGGGV 166
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 78-333 1.16e-16

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 80.73  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   78 GPGHAAMECAIFNSLEPGDKILIAVNGIWGERASEIAERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAV--FFLTHGE 155
Cdd:PRK13479  63 GSGTFSVEAAIGSLVPRDGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAA-DPRIthVALVHCE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  156 SSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLNAPPGtapISFserachkIFNRKT-- 233
Cdd:PRK13479 142 TTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPG---FGF-------VIARRSel 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  234 ---KPISYFLDLNwLANYWGCDDKPVRsYHHTGPVSSFYALRESLAIL-AETGLENSWKRHKEVAEYFHKGLEQMGLKLF 309
Cdd:PRK13479 212 eacKGNSRSLSLD-LYDQWAYMEKTGQ-WRFTPPTHVVAAFYQALLELeEEGGVPARGARYANNQRTLVAGMRALGFEPL 289

                        250       260
                 ....*....|....*....|....*.
gi 50539730  310 VQDkKARLPTVTTIVAP--PGYDWRE 333
Cdd:PRK13479 290 LDA-EIQSPIIVTFHAPadPAYDFKE 314
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
89-385 1.23e-15

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 77.87  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  89 FNSLEPGDKILIAVNgiwgERAS------EIAERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAVFFLTHGESSTGVVH 162
Cdd:COG0520  97 LGRLKPGDEILITEM----EHHSnivpwqELAERTGAEVRVIPLDEDGELDLEALEALLTP-RTKLVAVTHVSNVTGTVN 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 163 PIDGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLnAPPGTAPISFSERACHKIfnrktKPisyfldl 242
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLY-GPTGIGVLYGKRELLEAL-----PP------- 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 243 nWLANYWGCDDkpVRSYHH------------TGPVSSFYALRESLAILAETGLENSWKRHKEVAEYFHKGLEQM-GLKLF 309
Cdd:COG0520 239 -FLGGGGMIEW--VSFDGTtyadlprrfeagTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIpGVRIL 315

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 310 -VQDKKARLPTVTTIVAppGYDWREItGYIMKTFNIEISGGLGPSAGMVLRVGLMGC--------NsNKANVDKVLEALA 380
Cdd:COG0520 316 gPADPEDRSGIVSFNVD--GVHPHDV-AALLDDEGIAVRAGHHCAQPLMRRLGVPGTvrasfhlyN-TEEEIDRLVEALK 391


                ....*
gi 50539730 381 DALKH 385
Cdd:COG0520 392 KLAEL 396
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 90-215 3.84e-11

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 64.02  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  90 NSLEPGDKILIAVNgiwgERASEI------AERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAVFFLTHGESSTGVVHP 163
Cdd:cd06453  83 RANKPGDEIVTSVM----EHHSNIvpwqqlAERTGAKLKVVPVDDDGQLDLEALEKLLTE-RTKLVAVTHVSNVLGTINP 157

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 50539730 164 IDGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDIL-YTGsQKVLnAPPGT 215
Cdd:cd06453 158 VKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLaFSG-HKML-GPTGI 208
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 115-215 1.71e-07

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 52.74  E-value: 1.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 115 ERIGAKVNTVETMAGGYLTNEEIEKALNKyRPAVFFLTHGESSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPICMD 194
Cdd:COG1104 111 EKEGFEVTYLPVDEDGRVDLEALEAALRP-DTALVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVK 189

                        90       100
                ....*....|....*....|..
gi 50539730 195 EQGIDiLYTGS-QKvLNAPPGT 215
Cdd:COG1104 190 ELGVD-LLSLSaHK-IYGPKGV 209
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
115-208 6.79e-07

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 51.10  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  115 ERIGAKVNTVETMAGGYLTNEEIEKALnkyRPAVFFLT--HGESSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPIC 192
Cdd:PRK14012 115 EREGFEVTYLDPQSNGIIDLEKLEAAM---RDDTILVSimHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPID 191

                         90
                 ....*....|....*.
gi 50539730  193 MDEQGIDILYTGSQKV 208
Cdd:PRK14012 192 LSKLKVDLMSFSAHKI 207
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
115-208 1.42e-06

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 49.73  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  115 ERIGAKVNTVETMAGGYLTNEEIEKALnkyRPAVFFLT--HGESSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPIC 192
Cdd:PRK02948 109 ESQGYTVTEIPVDKSGLIRLVDLERAI---TPDTVLASiqHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPID 185

                         90
                 ....*....|....*.
gi 50539730  193 MDEQGIDILYTGSQKV 208
Cdd:PRK02948 186 VFEMGIDSLSVSAHKI 201
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 93-234 2.37e-05

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 45.84  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  93 EPGDKILIAVNGIWGERASeiAERIGAKVNTVETMA--GGYLTNEE----IEKALNK--YRPAVFFLTHGESSTGVVHPI 164
Cdd:cd06452  81 EKGDWVVVDGLAHYTSYVA--AERAGLNVREVPNTGhpEYHITPEGyaevIEEVKDEfgKPPALALLTHVDGNYGNLHDA 158

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50539730 165 DGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLNAPpgtAPI---SFSERACHKIFnRKTK 234
Cdd:cd06452 159 KKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAAS---APIgvlATTEEWADIVF-RTSQ 227
PLN02651 PLN02651
cysteine desulfurase
 135-216 3.17e-04

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 42.33  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  135 EEIEKALnkyRPAVFFLT--HGESSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVlNAP 212
Cdd:PLN02651 129 DELAAAI---RPDTALVSvmAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKI-YGP 204


                 ....
gi 50539730  213 PGTA 216
Cdd:PLN02651 205 KGVG 208
PTZ00125 PTZ00125
ornithine aminotransferase-like protein; Provisional
 135-219 4.83e-04

ornithine aminotransferase-like protein; Provisional


Pssm-ID: 240281 [Multi-domain]  Cd Length: 400  Bit Score: 41.97  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  135 EEIEKALNKYRPAVFFLTHGESSTGVVHPIDGIGP----LCRKYSCLFLVDSV-AALG--GAPICMDEQGI--DILYTGs 205
Cdd:PTZ00125 168 EALEKLLQDPNVAAFIVEPIQGEAGVIVPDDGYLKqvyeLCKKYNVLLIVDEIqTGLGrtGKLLAHDHEGVkpDIVLLG- 246

                         90
                 ....*....|....
gi 50539730  206 qKVLNAppGTAPIS 219
Cdd:PTZ00125 247 -KALSG--GLYPIS 257
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
 87-234 5.06e-04

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 41.84  E-value: 5.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730   87 AIFNSL-EPGDKILIAVNGIWGERASeiAERigAKVNTVETMAGGYLTN--------EEIEKALNK--YRPAVFFLTHGE 155
Cdd:PRK09331  93 AVMHSLcKKGDYVVLDGLAHYTSYVA--AER--AGLNVREVPKTGYPEYkitpeayaEKIEEVKEEtgKPPALALLTHVD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730  156 SSTGVVHPIDGIGPLCRKYSCLFLVDSVAALGGAPICMDEQGIDILYTGSQKVLNAPpgtAPI---SFSERACHKIFnRK 232
Cdd:PRK09331 169 GNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHKSMAAS---APSgvlATTEEYADKVF-RT 244


                 ..
gi 50539730  233 TK 234
Cdd:PRK09331 245 SR 246
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 108-199 3.30e-03

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 39.11  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50539730 108 ERASEIAERigaKVNTVETMAGGYLTNEEIEKALNKYRPA---VFFL--THGESSTGVVHPIDGIGPLCRKYSCLFLVDs 182
Cdd:cd06450 109 EKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVvaTAGTTDTGAIDPLEEIADLAEKYDLWLHVD- 184

                        90
                ....*....|....*...
gi 50539730 183 vAALGG-APICMDEQGID 199
Cdd:cd06450 185 -AAYGGfLLPFPEPRHLD 201
 
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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