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Conserved domains on  [gi|612978108|gb|EZV88499|]
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hypothetical protein U894_00314 [Staphylococcus aureus 22825]

Protein Classification

pyridoxal-phosphate-dependent aminotransferase family protein( domain architecture ID 11414660)

pyridoxal-phosphate-dependent aminotransferase family protiein similar to alanine--glyoxylate aminotransferase (AGAT)

CATH:  3.90.1150.10|3.40.640.10
EC:  2.6.1.-
Gene Ontology:  GO:0030170
PubMed:  35697072|38885378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 6-384 3.50e-158

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: 449.54  E-value: 3.50e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   6 PLLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQNDVLILTSSGTSVLEASMLNIVNPEDHFVVI 85
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDVVILTGSGTGAMEAALANLVSPGDKVLVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  86 VSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTlNVEVKAVFSQYCETSTTVLHPIHELGNAINQFNsnIY 165
Cdd:COG0075   81 VNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAA-DPDIKAVAVVHNETSTGVLNPLEEIGALAKEHG--AL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 166 FVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPKFYLDLNKYISSQADNSTPFTPN 245
Cdd:COG0075  158 LIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWEKGQTPYTPP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 246 VSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVTAFKPNTNDEVKIIKDELKNRFKIT 325
Cdd:COG0075  238 VSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIE 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612978108 326 IAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIILTEHRKVNYIGKGISKYMEVIHE 384
Cdd:COG0075  318 IAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 6-384 3.50e-158

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: 449.54  E-value: 3.50e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   6 PLLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQNDVLILTSSGTSVLEASMLNIVNPEDHFVVI 85
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDVVILTGSGTGAMEAALANLVSPGDKVLVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  86 VSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTlNVEVKAVFSQYCETSTTVLHPIHELGNAINQFNsnIY 165
Cdd:COG0075   81 VNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAA-DPDIKAVAVVHNETSTGVLNPLEEIGALAKEHG--AL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 166 FVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPKFYLDLNKYISSQADNSTPFTPN 245
Cdd:COG0075  158 LIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWEKGQTPYTPP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 246 VSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVTAFKPNTNDEVKIIKDELKNRFKIT 325
Cdd:COG0075  238 VSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIE 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612978108 326 IAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIILTEHRKVNYIGKGISKYMEVIHE 384
Cdd:COG0075  318 IAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 7-362 6.40e-100

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: 300.36  E-value: 6.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   7 LLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQN-DVLILTSSGTSVLEASMLNIVNPEDHFVVI 85
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENgLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  86 VSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTLnvEVKAVFSQYCETSTTVLHPIHELGNAINQFNSniY 165
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQH--DIKAVTLTHNETSTGVLNPLEGIGALAKKHDA--L 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 166 FVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPK-FYLDLNKYISSQ-ADNSTPFT 243
Cdd:cd06451  157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKgFYFDLLLLLKYWgEGYSYPHT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 244 PNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVTAFK-PNTNDEVKIIKdELKNRF 322
Cdd:cd06451  237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLvPEGVDGDEVVR-RLMKRY 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 612978108 323 KITIAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIIL 362
Cdd:cd06451  316 NIEIAGGLGPTAGKVFRIGHMGEATREDVLGVLSALEEAL 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 2-386 1.03e-68

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 221.94  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   2 YYHQP---LLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQNDV-LILTSSGTSVLEASMLNIVN 77
Cdd:PLN02409   3 YVYAPgrnHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTpFIFPTTGTGAWESALTNTLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  78 PEDHFVVIVSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYL-STLNVEVKAVFSQYCETSTTVLHPIHELGNA 156
Cdd:PLN02409  83 PGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLrQDTNHKIKAVCVVHNETSTGVTNDLAGVRKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 157 INQFNSNIYFVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPKFYLDLNKYISS-Q 235
Cdd:PLN02409 163 LDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKFyK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 236 ADNSTPFTPNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLV-NDKDASPTVTAFK-PNTNDEVKI 313
Cdd:PLN02409 243 LGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTkKPEWRSDTVTAVVvPEGIDSAEI 322

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612978108 314 IKDELKnRFKITIAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIILTEHRKVNYIGKGISKYMEVIHEAI 386
Cdd:PLN02409 323 VKNAWK-KYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTT 394
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 8-301 9.30e-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: 92.31  E-value: 9.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108    8 LLTPGPTPVPDAIMREIQA----------PMVGHRSKDFEDIAQQAFQGLKPIFGSQNDVLIL-TSSGTSVLEA---SML 73
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIfTSGTTEAINLvalSLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   74 NIVNPEDHFVVIVSGAFGNRF--KQIAQTYYKNVHIYDVTWGEAVDVKDFinyLSTLNVEVKAVFSQYCETSTTVLHPIH 151
Cdd:pfam00266  83 RSLKPGDEIVITEMEHHANLVpwQELAKRTGARVRVLPLDEDGLLDLDEL---EKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  152 ELGNAINQfnSNIYFVVDGVSCIGAVDVDINKDKIDVLVSGSQKaIMLPPGLAFVAYSHRAKERFKEVTTPKFYLD---L 228
Cdd:pfam00266 160 EIGKLAHQ--YGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPPLLGGGGMIEtvsL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612978108  229 NKYisSQADNSTPF---TPNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVT 301
Cdd:pfam00266 237 QES--TFADAPWKFeagTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIIS 310
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 6-384 3.50e-158

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: 449.54  E-value: 3.50e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   6 PLLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQNDVLILTSSGTSVLEASMLNIVNPEDHFVVI 85
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTENDVVILTGSGTGAMEAALANLVSPGDKVLVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  86 VSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTlNVEVKAVFSQYCETSTTVLHPIHELGNAINQFNsnIY 165
Cdd:COG0075   81 VNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAA-DPDIKAVAVVHNETSTGVLNPLEEIGALAKEHG--AL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 166 FVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPKFYLDLNKYISSQADNSTPFTPN 245
Cdd:COG0075  158 LIVDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARKLPSYYLDLKLWLKYWEKGQTPYTPP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 246 VSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVTAFKPNTNDEVKIIKDELKNRFKIT 325
Cdd:COG0075  238 VSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERYGIE 317

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 612978108 326 IAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIILTEHRKVNYIGKGISKYMEVIHE 384
Cdd:COG0075  318 IAGGLGPLKGKIFRIGHMGYVNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 7-362 6.40e-100

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: 300.36  E-value: 6.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   7 LLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQN-DVLILTSSGTSVLEASMLNIVNPEDHFVVI 85
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENgLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  86 VSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTLnvEVKAVFSQYCETSTTVLHPIHELGNAINQFNSniY 165
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQH--DIKAVTLTHNETSTGVLNPLEGIGALAKKHDA--L 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 166 FVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPK-FYLDLNKYISSQ-ADNSTPFT 243
Cdd:cd06451  157 LIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKgFYFDLLLLLKYWgEGYSYPHT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 244 PNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVTAFK-PNTNDEVKIIKdELKNRF 322
Cdd:cd06451  237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLvPEGVDGDEVVR-RLMKRY 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 612978108 323 KITIAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIIL 362
Cdd:cd06451  316 NIEIAGGLGPTAGKVFRIGHMGEATREDVLGVLSALEEAL 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 2-386 1.03e-68

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 221.94  E-value: 1.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   2 YYHQP---LLLTPGPTPVPDAIMREIQAPMVGHRSKDFEDIAQQAFQGLKPIFGSQNDV-LILTSSGTSVLEASMLNIVN 77
Cdd:PLN02409   3 YVYAPgrnHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTpFIFPTTGTGAWESALTNTLS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  78 PEDHFVVIVSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYL-STLNVEVKAVFSQYCETSTTVLHPIHELGNA 156
Cdd:PLN02409  83 PGDKVVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLrQDTNHKIKAVCVVHNETSTGVTNDLAGVRKL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 157 INQFNSNIYFVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVTTPKFYLDLNKYISS-Q 235
Cdd:PLN02409 163 LDCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFDWADYLKFyK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 236 ADNSTPFTPNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLV-NDKDASPTVTAFK-PNTNDEVKI 313
Cdd:PLN02409 243 LGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTkKPEWRSDTVTAVVvPEGIDSAEI 322

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612978108 314 IKDELKnRFKITIAGGQGHLKGQILRIGHMGKISPFDILSVVSALEIILTEHRKVNYIGKGISKYMEVIHEAI 386
Cdd:PLN02409 323 VKNAWK-KYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGALAGVEMVLKDVGYPVKLGSGVAAAQAYLQKTT 394
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 4-357 3.25e-23

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 99.60  E-value: 3.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   4 HQPLLLTPGP----TPVPDAIMREIqapmvGHRSKDFEDIAQQAFQGLKPIFGSQND---VLiLTSSGTSVLEASMLNIV 76
Cdd:PRK13479   4 NDPLLLTPGPlttsRTVREAMLRDW-----GSWDDDFNALTASVRAKLVAIATGEEGytcVP-LQGSGTFSVEAAIGSLV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  77 NPEDHFVVIVSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFINYLSTlNVEVKAVFSQYCETSTTVLHPIHELGNA 156
Cdd:PRK13479  78 PRDGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAA-DPRITHVALVHCETTTGILNPLDEIAAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 157 INQFNSNiyFVVDGVSCIGAVDVDINKDKIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVtTPKFYLDL-NKYISSQ 235
Cdd:PRK13479 157 AKRHGKR--LIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPGFGFVIARRSELEACKGN-SRSLSLDLyDQWAYME 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 236 ADNSTPFTPNVSLFRGVNAYVETVKAEGfnHVIARH--YAiRN--ALRSALKALDLTLLVNDKDASPTVTAF-KPNTND- 309
Cdd:PRK13479 234 KTGQWRFTPPTHVVAAFYQALLELEEEG--GVPARGarYA-NNqrTLVAGMRALGFEPLLDAEIQSPIIVTFhAPADPAy 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 612978108 310 EVKIIKDELKNR-F-----KITIAggqghlkgQILRIGHMGKISPFDILSVVSA 357
Cdd:PRK13479 311 DFKEFYERLKEQgFviypgKLTQV--------DTFRIGCIGDVDAADIRRLVAA 356
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 8-301 9.30e-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: 92.31  E-value: 9.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108    8 LLTPGPTPVPDAIMREIQA----------PMVGHRSKDFEDIAQQAFQGLKPIFGSQNDVLIL-TSSGTSVLEA---SML 73
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEyytdyngnvhRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIfTSGTTEAINLvalSLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108   74 NIVNPEDHFVVIVSGAFGNRF--KQIAQTYYKNVHIYDVTWGEAVDVKDFinyLSTLNVEVKAVFSQYCETSTTVLHPIH 151
Cdd:pfam00266  83 RSLKPGDEIVITEMEHHANLVpwQELAKRTGARVRVLPLDEDGLLDLDEL---EKLITPKTKLVAITHVSNVTGTIQPVP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  152 ELGNAINQfnSNIYFVVDGVSCIGAVDVDINKDKIDVLVSGSQKaIMLPPGLAFVAYSHRAKERFKEVTTPKFYLD---L 228
Cdd:pfam00266 160 EIGKLAHQ--YGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKMPPLLGGGGMIEtvsL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612978108  229 NKYisSQADNSTPF---TPNVSLFRGVNAYVETVKAEGFNHVIARHYAIRNALRSALKALDLTLLVNDKDASPTVT 301
Cdd:pfam00266 237 QES--TFADAPWKFeagTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIIS 310
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 45-202 3.80e-12

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: 63.94  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  45 QGLKPIFGSQNDVLILTSSGTSVLEASMLNIVNPEDHfVVIVSGAFGNRFKQIAQTYYKNVHIYDVTWGEAV--DVKDFI 122
Cdd:cd01494    7 EKLARLLQPGNDKAVFVPSGTGANEAALLALLGPGDE-VIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGglDVAILE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 123 NYLSTLNveVKAVFSQYCETSTTVLHPIHELGNAInqFNSNIYFVVDGVSCIGAVD---VDINKDKIDVLVSGSQKAIML 199
Cdd:cd01494   86 ELKAKPN--VALIVITPNTTSGGVLVPLKEIRKIA--KEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNLGG 161


                 ...
gi 612978108 200 PPG 202
Cdd:cd01494  162 EGG 164
SerC COG1932
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
 11-246 6.02e-10

Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 441535  Cd Length: 358  Bit Score: 60.08  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  11 PGPTPVPDAIMREIQAPMV------------GHRSKDFEDIAQQAFQGLKPIFG--SQNDVLILtsSGTSVLEASM--LN 74
Cdd:COG1932    8 AGPAKLPEEVLEQAQAELLdwngsgmsvmemSHRSKPFKAIVEEAEADLRELLGipDGYEVLFL--QGGATAQFAMvpMN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  75 IVNPEDHFVVIVSGAFGNRFKQIAQTYyKNVHiydVTWGEAVDVKDFINYLSTLNVEVKAVFSQYC--ETST-TVLHPIH 151
Cdd:COG1932   86 LLRGGKKADYLVTGEWSKKAIKEAKKY-GEVN---VVASSEDDNFGYIPKPEEWQLSPDADYVHYTsnETITgVEFHELP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 152 ELGNAInqfnsniyFVVDGVSCIGAVDVDINkdKIDVLVSGSQKAIMlPPGLAFVAYSHRAKERFKEvTTPKFyLDLnky 231
Cdd:COG1932  162 DVGDVP--------LVADMSSDILSRPVDVS--KFGLIYAGAQKNIG-PAGLTVVIVRPDLLGRAER-AIPSM-LDY--- 225

                        250
                 ....*....|....*.
gi 612978108 232 iSSQADN-STPFTPNV 246
Cdd:COG1932  226 -KTHADNdSMYNTPPT 240
PLN02452 PLN02452
phosphoserine transaminase
 11-206 3.65e-08

phosphoserine transaminase


Pssm-ID: 178071  Cd Length: 365  Bit Score: 54.70  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  11 PGPTPVPDAIMREIQAPMV------------GHRSKDFEDIAQQAFQGLKPIFG--SQNDVLILTSSGTSVLEASMLNIV 76
Cdd:PLN02452  13 AGPATLPANVLAKAQAELYnwegsgmsvmemSHRGKEFLSIIQKAEADLRELLDipDNYEVLFLQGGASTQFAAIPLNLC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  77 NPEDHFVVIVSGAFGNRFKQIAQTYYKNVHIYDVTWGEAVDVKDFinylSTLNVEVKAVFSQYCETSTtvlhpIHELgna 156
Cdd:PLN02452  93 KPGDKADFVVTGSWSKKAAKEAKKYCKTNVIASGKDEKYTKIPSV----SEWELTPDAKFVHICANET-----IHGV--- 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612978108 157 inQFNS-----NIYFVVDGVS--CIGAVDVdinkDKIDVLVSGSQKAIMlPPGLAFV 206
Cdd:PLN02452 161 --EFKDypdvgNVPLVADMSSnfLSKPVDV----SKYGVIYAGAQKNVG-PSGVTIV 210
PSAT_like cd00611
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ...
 11-206 1.38e-06

Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.


Pssm-ID: 99736 [Multi-domain]  Cd Length: 355  Bit Score: 49.60  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  11 PGPTPVPDAIMREIQAPMV------------GHRSKDFEDIAQQAFQGLKPIFG--SQNDVLILTSSGTSVLEASMLNIV 76
Cdd:cd00611    5 AGPAALPEEVLEQAQKELLdfnglgmsvmemSHRSKDFEAIVNEAESDLRELLNipDNYKVLFLQGGATGQFAAVPLNLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  77 NPEDHFVVIVSGAFGNRFKQIAQTYYKNVHIydvtwgeaVDVKDFINY-----LSTLNVEVKAVFSQYCETSTtvlhpIH 151
Cdd:cd00611   85 GDKGTADYVVTGAWSAKAAKEAKRYGGVVVI--------VAAKEEGKYtkipdVETWDLAPDAAYVHYCSNET-----IH 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 612978108 152 elGNAINQF--NSNIYFVVDGVSCIGAVDVDINkdKIDVLVSGSQKAIMlPPGLAFV 206
Cdd:cd00611  152 --GVEFDEVpdTGGVPLVADMSSNILSRPIDVS--KFGVIYAGAQKNLG-PAGVTVV 203
PRK05355 PRK05355
3-phosphoserine/phosphohydroxythreonine transaminase;
11-206 8.07e-05

3-phosphoserine/phosphohydroxythreonine transaminase;


Pssm-ID: 235428  Cd Length: 360  Bit Score: 44.32  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  11 PGPTPVPDAIMREIQAPM------------VGHRSKDFEDIAQQAFQGLKPIFGSQND--VLILTSSGTsvLEASM--LN 74
Cdd:PRK05355   9 AGPAMLPEEVLEQAQQELldwngsgmsvmeISHRSKEFEAVAEEAEADLRELLNIPDNykVLFLQGGAS--LQFAMvpMN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  75 IVNPEDHFVVIVSGAFGNRFKQIAQTyYKNVHIYDVTwgeAVDVKDFINYLSTLNVEVKAVFSQYCETST---TVLHPIH 151
Cdd:PRK05355  87 LLGGGKKADYVDTGSWSKKAIKEAKK-YGEVNVAASS---EDDGFTYIPPLDEWQLSDDAAYVHYTSNETidgTEFHELP 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 612978108 152 ELGNAInqfnsniyFVVDGVSCIGAVDVDINkdKIDVLVSGSQKAIMlPPGLAFV 206
Cdd:PRK05355 163 DTGDVP--------LVADMSSDILSRPIDVS--KFGLIYAGAQKNIG-PAGLTIV 206
PRK03080 PRK03080
phosphoserine transaminase;
31-230 1.42e-04

phosphoserine transaminase;


Pssm-ID: 235103  Cd Length: 378  Bit Score: 43.64  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108  31 HRSKDFEDIAQQAFQGLKPIFGSQND--VLILTSSGTSVLEASMLNIVNPE--DHFVVivsGAFGNRFKQ--IAQTYYKN 104
Cdd:PRK03080  41 HRQKPVKALLKRVIEGTRELLSLPEGyeVGIVPGSDTGAWEMALWSLLGARrvDHLAW---ESFGSKWATdvVKQLKLED 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612978108 105 VHIYDVTWGEAVDvkdfinyLSTLNVEVKAVFSQYcETSTTVLHPIHELGNAinqfNSNIYFVVDGVSCIGAVDVDInkD 184
Cdd:PRK03080 118 PRVLEADYGSLPD-------LSAVDFDRDVVFTWN-GTTTGVRVPVARWIGA----DREGLTICDATSAAFALPLDW--S 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 612978108 185 KIDVLVSGSQKAIMLPPGLAFVAYSHRAKERFKEVT----TPKFyLDLNK 230
Cdd:PRK03080 184 KLDVYTFSWQKVLGGEGGHGMAILSPRAVERLESYTparpIPKF-FRLTK 232
 
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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