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Conserved domains on  [gi|111038130|ref|NP_057911|]
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alanine--glyoxylate aminotransferase isoform 1 precursor [Mus musculus]

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 ...
 46-407 5.37e-166

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: 469.85  E-value: 5.37e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  46 LLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTG 125
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 126 TNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVD 205
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 206 SVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKyKVYSRKTKPVSFYTDITYLAKLWGCEGETrviHHT 285
Cdd:cd06451  161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERAL-ERIKKKTKPKGFYFDLLLLLKYWGEGYSY---PHT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 286 TPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVLDHF 365
Cdd:cd06451  237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 111038130 366 SIEISGGLGPTEERVLRIGLLGYnATTENVDRVAEALREALQ 407
Cdd:cd06451  316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 46-407 5.37e-166

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: 469.85  E-value: 5.37e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  46 LLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTG 125
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 126 TNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVD 205
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 206 SVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKyKVYSRKTKPVSFYTDITYLAKLWGCEGETrviHHT 285
Cdd:cd06451  161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERAL-ERIKKKTKPKGFYFDLLLLLKYWGEGYSY---PHT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 286 TPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVLDHF 365
Cdd:cd06451  237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 111038130 366 SIEISGGLGPTEERVLRIGLLGYnATTENVDRVAEALREALQ 407
Cdd:cd06451  316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 45-407 5.82e-137

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: 396.77  E-value: 5.82e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  45 RLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPlTLVVSGSGHCAMETALFNLLEPGDSFLT 124
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 125 GTNGIWGMRAAEIADRIGARVHqMIKKP-GEHYTLQEVEEGLAQHKPV-LLFLVHGESSTGVVQPLDGFGELCHRYQCLL 202
Cdd:COG0075   80 LVNGAFGERWAEIAERYGAEVV-VLEVPwGEAVDPEEVEEALAADPDIkAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 203 LVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVysRKTKPVSFYTDITYLAKLWGcEGETrvi 282
Cdd:COG0075  159 IVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYWE-KGQT--- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 283 HHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDpEIRLPTITTVTVPAGYNWRDIVSYVL 362
Cdd:COG0075  233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 111038130 363 DHFSIEISGGLGPTEERVLRIGLLGYNaTTENVDRVAEALREALQ 407
Cdd:COG0075  312 ERYGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 40-390 3.83e-97

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 295.90  E-value: 3.83e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  40 LSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPG 119
Cdd:PLN02409   5 YAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 120 DSFLTGTNGIWGMRAAEIADRIGARVhQMIKKP-GEHYTLQEVEEGLAQ---HKPVLLFLVHGESSTGVVQPLDGFGEL- 194
Cdd:PLN02409  85 DKVVSFRIGQFSLLWIDQMQRLNFDV-DVVESPwGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLl 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 195 -CHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSF----YTDITYL 269
Cdd:PLN02409 164 dCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 270 AKLWGcegetrvihHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVP 349
Cdd:PLN02409 244 GTYWP---------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVP 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 111038130 350 AGYNWRDIVSYVLDHFSIEISGGLGPTEERVLRIGLLGYNA 390
Cdd:PLN02409 315 EGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 47-398 6.39e-61

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: 201.32  E-value: 6.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130   47 LLGPGPSNLAPRVLAAGSL----------RMIGHMQKEMLQIMEEIKQGIQYVFQTR-NPLTLVVSGSGHcAMETALFNL 115
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTE-AINLVALSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  116 ---LEPGDSFLTGTNGIWG--MRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAqHKPVLLFLVHGESSTGVVQPLDG 190
Cdd:pfam00266  82 grsLKPGDEIVITEMEHHAnlVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  191 FGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKvLNAPPGISLISFNDKAKYKVysRKTKPVSFYTDITYLa 270
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  271 KLWGCEGETRVIHH-TTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPeiRLPTITTVTVP 349
Cdd:pfam00266 237 QESTFADAPWKFEAgTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 111038130  350 aGYNWRDIVSYvLDHFSIEISGGL---GPTEER-----VLRIGLLGYNaTTENVDRV 398
Cdd:pfam00266 315 -GVHPHDVATL-LDESGIAVRSGHhcaQPLMVRlglggTVRASFYIYN-TQEDVDRL 368
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 46-407 5.37e-166

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: 469.85  E-value: 5.37e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  46 LLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTG 125
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 126 TNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVD 205
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 206 SVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKyKVYSRKTKPVSFYTDITYLAKLWGCEGETrviHHT 285
Cdd:cd06451  161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERAL-ERIKKKTKPKGFYFDLLLLLKYWGEGYSY---PHT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 286 TPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKdPEIRLPTITTVTVPAGYNWRDIVSYVLDHF 365
Cdd:cd06451  237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 111038130 366 SIEISGGLGPTEERVLRIGLLGYnATTENVDRVAEALREALQ 407
Cdd:cd06451  316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 45-407 5.82e-137

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: 396.77  E-value: 5.82e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  45 RLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPlTLVVSGSGHCAMETALFNLLEPGDSFLT 124
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 125 GTNGIWGMRAAEIADRIGARVHqMIKKP-GEHYTLQEVEEGLAQHKPV-LLFLVHGESSTGVVQPLDGFGELCHRYQCLL 202
Cdd:COG0075   80 LVNGAFGERWAEIAERYGAEVV-VLEVPwGEAVDPEEVEEALAADPDIkAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 203 LVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVysRKTKPVSFYTDITYLAKLWGcEGETrvi 282
Cdd:COG0075  159 IVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYWE-KGQT--- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 283 HHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDpEIRLPTITTVTVPAGYNWRDIVSYVL 362
Cdd:COG0075  233 PYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLK 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 111038130 363 DHFSIEISGGLGPTEERVLRIGLLGYNaTTENVDRVAEALREALQ 407
Cdd:COG0075  312 ERYGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 40-390 3.83e-97

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 295.90  E-value: 3.83e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  40 LSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPG 119
Cdd:PLN02409   5 YAPGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 120 DSFLTGTNGIWGMRAAEIADRIGARVhQMIKKP-GEHYTLQEVEEGLAQ---HKPVLLFLVHGESSTGVVQPLDGFGEL- 194
Cdd:PLN02409  85 DKVVSFRIGQFSLLWIDQMQRLNFDV-DVVESPwGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLl 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 195 -CHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSF----YTDITYL 269
Cdd:PLN02409 164 dCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 270 AKLWGcegetrvihHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVP 349
Cdd:PLN02409 244 GTYWP---------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVP 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 111038130 350 AGYNWRDIVSYVLDHFSIEISGGLGPTEERVLRIGLLGYNA 390
Cdd:PLN02409 315 EGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 47-398 6.39e-61

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: 201.32  E-value: 6.39e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130   47 LLGPGPSNLAPRVLAAGSL----------RMIGHMQKEMLQIMEEIKQGIQYVFQTR-NPLTLVVSGSGHcAMETALFNL 115
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTE-AINLVALSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  116 ---LEPGDSFLTGTNGIWG--MRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAqHKPVLLFLVHGESSTGVVQPLDG 190
Cdd:pfam00266  82 grsLKPGDEIVITEMEHHAnlVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  191 FGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKvLNAPPGISLISFNDKAKYKVysRKTKPVSFYTDITYLa 270
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  271 KLWGCEGETRVIHH-TTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPeiRLPTITTVTVP 349
Cdd:pfam00266 237 QESTFADAPWKFEAgTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 111038130  350 aGYNWRDIVSYvLDHFSIEISGGL---GPTEER-----VLRIGLLGYNaTTENVDRV 398
Cdd:pfam00266 315 -GVHPHDVATL-LDESGIAVRSGHhcaQPLMVRlglggTVRASFYIYN-TQEDVDRL 368
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 79-238 3.92e-34

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: 124.80  E-value: 3.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  79 MEEIKQGIQYVFQTRNPLTLVVSgSGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAeIADRIGARVHQMIKKPGEHYTL 158
Cdd:cd01494    2 LEELEEKLARLLQPGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV-AAELAGAKPVPVPVDDAGYGGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 159 --QEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVP---IYMDQQGIDIMYSSSQKVL 233
Cdd:cd01494   80 dvAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNL 159


                 ....*
gi 111038130 234 NAPPG 238
Cdd:cd01494  160 GGEGG 164
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 46-355 5.88e-23

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 99.22  E-value: 5.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  46 LLLGPGPSNLAPRVLAAgSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLV-VSGSGHCAMETALFNLLEPGDSFLT 124
Cdd:PRK13479   7 LLLTPGPLTTSRTVREA-MLRDWGSWDDDFNALTASVRAKLVAIATGEEGYTCVpLQGSGTFSVEAAIGSLVPRDGKVLV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 125 GTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVL-LFLVHGESSTGVVQPLDGFGELCHRYQCLLL 203
Cdd:PRK13479  86 PDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRIThVALVHCETTTGILNPLDEIAAVAKRHGKRLI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 204 VDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLisfndkakykVYSRKtkpvsfytditylAKLWGCEGETRV-- 281
Cdd:PRK13479 166 VDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGF----------VIARR-------------SELEACKGNSRSls 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 282 --IHH-------------TTPVTSLYCLRESLA-LIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVkDPEIRLPTITT 345
Cdd:PRK13479 223 ldLYDqwaymektgqwrfTPPTHVVAAFYQALLeLEEEGGVPARGARYANNQRTLVAGMRALGFEPLL-DAEIQSPIIVT 301

                        330
                 ....*....|
gi 111038130 346 VTVPAGYNWR 355
Cdd:PRK13479 302 FHAPADPAYD 311
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
113-408 4.40e-12

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 67.09  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 113 FNLLEPGDSFLTGT----NGIWGMRaaEIADRIGARVHQMIKKPGEHYTLQEVEEGLaQHKPVLLFLVHGESSTGVVQPL 188
Cdd:COG0520   97 LGRLKPGDEILITEmehhSNIVPWQ--ELAERTGAEVRVIPLDEDGELDLEALEALL-TPRTKLVAVTHVSNVTGTVNPV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 189 DGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLnAPPGI-SLIsfndkAKYKVYsRKTKP-------- 259
Cdd:COG0520  174 KEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLY-GPTGIgVLY-----GKRELL-EALPPflggggmi 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 260 --VSFyTDITYLaklwgcEGETRvihH---TTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEM-GLKFF- 332
Cdd:COG0520  247 ewVSF-DGTTYA------DLPRR---FeagTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIpGVRILg 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 333 VKDPEIRLPtITTVTVpAGYNWRDIVSYvLDHFSIEISGGL---GPTEER-----VLRIGLLGYNaTTENVDRVAEALRE 404
Cdd:COG0520  317 PADPEDRSG-IVSFNV-DGVHPHDVAAL-LDDEGIAVRAGHhcaQPLMRRlgvpgTVRASFHLYN-TEEEIDRLVEALKK 392


                 ....
gi 111038130 405 ALQH 408
Cdd:COG0520  393 LAEL 396
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 182-408 1.47e-11

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: 65.45  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 182 TGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKvLNAPPGISLIsfndkakykVYSRKTKPVS 261
Cdd:COG1104  153 TGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IYGPKGVGAL---------YVRKGVRLEP 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 262 FytditylakLWGCEGETRvihhttpvtslycLR---ESLALI---------AEQGLENCWRRHREATAHLHKHLQEM-- 327
Cdd:COG1104  223 L---------IHGGGQERG-------------LRsgtENVPGIvglgkaaelAAEELEEEAARLRALRDRLEEGLLAAip 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 328 GLKFFVkDPEIRLPTITTVTVPaGYNWRDIVSYvLDHFSIEISGG----------------LGPTEERV---LRIGlLGY 388
Cdd:COG1104  281 GVVING-DPENRLPNTLNFSFP-GVEGEALLLA-LDLAGIAVSSGsacssgslepshvllaMGLDEELAhgsIRFS-LGR 356

                        250       260
                 ....*....|....*....|
gi 111038130 389 NATTENVDRVAEALREALQH 408
Cdd:COG1104  357 FTTEEEIDRAIEALKEIVAR 376
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
162-232 2.91e-08

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 55.12  E-value: 2.91e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111038130 162 EEGLAQH---KPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKV 232
Cdd:PRK02948 128 LVDLERAitpDTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKI 201
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
171-239 9.85e-06

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 47.24  E-value: 9.85e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111038130 171 VLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLnAPPGI 239
Cdd:PRK14012 146 ILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIY-GPKGI 213
PLN02651 PLN02651
cysteine desulfurase
 172-239 2.75e-05

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 45.80  E-value: 2.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111038130 172 LLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVlNAPPGI 239
Cdd:PLN02651 141 LVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKI-YGPKGV 207
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 137-402 1.58e-04

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: 43.61  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 137 IADRIGARVHqmIKKPGEHYTL--QEVEEGLAQhKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVP 214
Cdd:cd06453  108 LAERTGAKLK--VVPVDDDGQLdlEALEKLLTE-RTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMP 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 215 IYMDQQGIDiMYS-SSQKVLnAPPGISLIsfndkakykvYSRKtkpvsfytDItyLAKL--WGCEGETRVIHHTTPVTSL 291
Cdd:cd06453  185 VDVQDLGCD-FLAfSGHKML-GPTGIGVL----------YGKE--------EL--LEEMppYGGGGEMIEEVSFEETTYA 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 292 YC----------------LRESLALIAEQGLENCWRRHREATAHLHKHLQEM-GLKFFvKDPEIRLPtITTVTVPaGYNW 354
Cdd:cd06453  243 DLphkfeagtpniagaigLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIpGVRVY-GDAEDRAG-VVSFNLE-GIHP 319

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 111038130 355 RDiVSYVLDHFSIEISGGL---GPTEER-----VLRIGLLGYNaTTENVDRVAEAL 402
Cdd:cd06453  320 HD-VATILDQYGIAVRAGHhcaQPLMRRlgvpgTVRASFGLYN-TEEEIDALVEAL 373
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 99-258 1.82e-03

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: 40.07  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130  99 VVSGSGHcAMETALFNLLEPGDSFLTGTNGIWGMRAAeiADRIGARVHQMIK--KPGEHYTLQEVEEGLAQHK------P 170
Cdd:cd06452   64 VTPGARE-GKFAVMHSLCEKGDWVVVDGLAHYTSYVA--AERAGLNVREVPNtgHPEYHITPEGYAEVIEEVKdefgkpP 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038130 171 VLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKY 250
Cdd:cd06452  141 ALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASAPIGVLATTEEWAD 220


                 ....*...
gi 111038130 251 KVYsRKTK 258
Cdd:cd06452  221 IVF-RTSQ 227
 
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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