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Conserved domains on  [gi|488317948|ref|WP_002387333|]
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MULTISPECIES: alanine--glyoxylate aminotransferase family protein [Enterococcus]

Protein Classification

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

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

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 ...
10-402 1.93e-153

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: 437.98  E-value: 1.93e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  10 RTIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQqAFAIDGTSRSGLEAGLFALIEPGDKVLV 89
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  90 PTYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKEH-QPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFV 168
Cdd:COG0075   80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 169 VDMVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADylagryqkelglgadARNERFIQSNYLDLSQLE 248
Cdd:COG0075  160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALE---------------AIEARKLPSYYLDLKLWL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 249 KYWGpERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDTKTPTVIPVVIPEGIDG 328
Cdd:COG0075  225 KYWE-KGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDA 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488317948 329 EKVRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYsSREDNVLHFLSAFETVLKHQGYQFEGGSGSTHALAEYLN 402
Cdd:COG0075  304 AALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
10-402 1.93e-153

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: 437.98  E-value: 1.93e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  10 RTIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQqAFAIDGTSRSGLEAGLFALIEPGDKVLV 89
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  90 PTYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKEH-QPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFV 168
Cdd:COG0075   80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 169 VDMVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADylagryqkelglgadARNERFIQSNYLDLSQLE 248
Cdd:COG0075  160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALE---------------AIEARKLPSYYLDLKLWL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 249 KYWGpERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDTKTPTVIPVVIPEGIDG 328
Cdd:COG0075  225 KYWE-KGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDA 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488317948 329 EKVRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYsSREDNVLHFLSAFETVLKHQGYQFEGGSGSTHALAEYLN 402
Cdd:COG0075  304 AALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
11-381 4.08e-115

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: 340.04  E-value: 4.08e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  11 TIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQQAFAIDGTSRSGLEAGLFALIEPGDKVLVP 90
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  91 TYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKEHQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVD 170
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 171 MVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADYLAGRYQKELGlgadarnerfiqsnYLDLSQLEKY 250
Cdd:cd06451  161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGF--------------YFDLLLLLKY 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 251 WGPERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDTKTPTVIPVVIPEGIDGEK 330
Cdd:cd06451  227 WGEGYSYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDE 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488317948 331 VRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYSSREDnVLHFLSAFETVLK 381
Cdd:cd06451  307 VVRRLMKRYNIEIAGGLGPTAGKVFRIGHMGEATRED-VLGVLSALEEALK 356
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
9-401 3.26e-75

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 239.27  E-value: 3.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948   9 RRTIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQQAFAIDGTSRSGLEAGLFALIEPGDKVL 88
Cdd:PLN02409   9 RNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  89 VPTYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKE---HQPKIVAMVHGETANAQMQPLDQIGAF--CREN 163
Cdd:PLN02409  89 SFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCAQH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 164 EIFFVVDMVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADYLagryqkelglgADARNER--FIQSNY 241
Cdd:PLN02409 169 PALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEAS-----------KTAKSPRvfFDWADY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 242 LDLSQLEKYWGperlnhHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDT-KTPTVIPV 320
Cdd:PLN02409 238 LKFYKLGTYWP------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEwRSDTVTAV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 321 VIPEGIDGEKVRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYSSrEDNVLHFLSAFETVLKHQGYQFEGGSGSTHAlAEY 400
Cdd:PLN02409 312 VVPEGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN-ELQLLGALAGVEMVLKDVGYPVKLGSGVAAA-QAY 389

                 .
gi 488317948 401 L 401
Cdd:PLN02409 390 L 390
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
39-335 3.82e-22

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: 96.55  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948   39 EFLQIMDEVREMIKVPFATKNQQA--FaIDGTSRSgLEA---GLFALIEPGDKVLVPTYGRFAYLLG--EICERARAEVI 111
Cdd:pfam00266  40 EATQAYEEAREKVAEFINAPSNDEiiF-TSGTTEA-INLvalSLGRSLKPGDEIVITEMEHHANLVPwqELAKRTGARVR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  112 YLEKDWLAPFEQTTVIEAIKEhQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKIDIAV 191
Cdd:pfam00266 118 VLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  192 AGTQKCVSvPSGLSLITynqrVADYLAGRYQKELGLGAdarnerFIQSNYLDLSQLEKywGPERLNHHTEATTMIYGLHE 271
Cdd:pfam00266 197 FSGHKLYG-PTGIGVLY----GRRDLLEKMPPLLGGGG------MIETVSLQESTFAD--APWKFEAGTPNIAGIIGLGA 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488317948  272 GLRLLLQEGMENVYARHRKNNRILVESLQKM-GLEIFGklDTKTPTVIPVVIpEGIDGEKVRSLL 335
Cdd:pfam00266 264 ALEYLSEIGLEAIEKHEHELAQYLYERLLSLpGIRLYG--PERRASIISFNF-KGVHPHDVATLL 325
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
10-402 1.93e-153

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: 437.98  E-value: 1.93e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  10 RTIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQqAFAIDGTSRSGLEAGLFALIEPGDKVLV 89
Cdd:COG0075    1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  90 PTYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKEH-QPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFV 168
Cdd:COG0075   80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 169 VDMVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADylagryqkelglgadARNERFIQSNYLDLSQLE 248
Cdd:COG0075  160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALE---------------AIEARKLPSYYLDLKLWL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 249 KYWGpERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDTKTPTVIPVVIPEGIDG 328
Cdd:COG0075  225 KYWE-KGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDA 303
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488317948 329 EKVRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYsSREDNVLHFLSAFETVLKHQGYQFEGGSGSTHALAEYLN 402
Cdd:COG0075  304 AALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
11-381 4.08e-115

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: 340.04  E-value: 4.08e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  11 TIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQQAFAIDGTSRSGLEAGLFALIEPGDKVLVP 90
Cdd:cd06451    1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  91 TYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKEHQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVD 170
Cdd:cd06451   81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 171 MVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADYLAGRYQKELGlgadarnerfiqsnYLDLSQLEKY 250
Cdd:cd06451  161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKTKPKGF--------------YFDLLLLLKY 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 251 WGPERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDTKTPTVIPVVIPEGIDGEK 330
Cdd:cd06451  227 WGEGYSYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDE 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488317948 331 VRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYSSREDnVLHFLSAFETVLK 381
Cdd:cd06451  307 VVRRLMKRYNIEIAGGLGPTAGKVFRIGHMGEATRED-VLGVLSALEEALK 356
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
9-401 3.26e-75

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 239.27  E-value: 3.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948   9 RRTIMTPGPVEAHPSVLRQMGQPILGQFDPEFLQIMDEVREMIKVPFATKNQQAFAIDGTSRSGLEAGLFALIEPGDKVL 88
Cdd:PLN02409   9 RNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  89 VPTYGRFAYLLGEICERARAEVIYLEKDWLAPFEQTTVIEAIKE---HQPKIVAMVHGETANAQMQPLDQIGAF--CREN 163
Cdd:PLN02409  89 SFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCAQH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 164 EIFFVVDMVATYGGVETKVDDWKIDIAVAGTQKCVSVPSGLSLITYNQRVADYLagryqkelglgADARNER--FIQSNY 241
Cdd:PLN02409 169 PALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEAS-----------KTAKSPRvfFDWADY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 242 LDLSQLEKYWGperlnhHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKMGLEIFGKLDT-KTPTVIPV 320
Cdd:PLN02409 238 LKFYKLGTYWP------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEwRSDTVTAV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 321 VIPEGIDGEKVRSLLLDHFKVEIASSFGDLKGKIWRVGNMGYSSrEDNVLHFLSAFETVLKHQGYQFEGGSGSTHAlAEY 400
Cdd:PLN02409 312 VVPEGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN-ELQLLGALAGVEMVLKDVGYPVKLGSGVAAA-QAY 389

                 .
gi 488317948 401 L 401
Cdd:PLN02409 390 L 390
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
39-335 3.82e-22

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: 96.55  E-value: 3.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948   39 EFLQIMDEVREMIKVPFATKNQQA--FaIDGTSRSgLEA---GLFALIEPGDKVLVPTYGRFAYLLG--EICERARAEVI 111
Cdd:pfam00266  40 EATQAYEEAREKVAEFINAPSNDEiiF-TSGTTEA-INLvalSLGRSLKPGDEIVITEMEHHANLVPwqELAKRTGARVR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  112 YLEKDWLAPFEQTTVIEAIKEhQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKIDIAV 191
Cdd:pfam00266 118 VLPLDEDGLLDLDELEKLITP-KTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  192 AGTQKCVSvPSGLSLITynqrVADYLAGRYQKELGLGAdarnerFIQSNYLDLSQLEKywGPERLNHHTEATTMIYGLHE 271
Cdd:pfam00266 197 FSGHKLYG-PTGIGVLY----GRRDLLEKMPPLLGGGG------MIETVSLQESTFAD--APWKFEAGTPNIAGIIGLGA 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488317948  272 GLRLLLQEGMENVYARHRKNNRILVESLQKM-GLEIFGklDTKTPTVIPVVIpEGIDGEKVRSLL 335
Cdd:pfam00266 264 ALEYLSEIGLEAIEKHEHELAQYLYERLLSLpGIRLYG--PERRASIISFNF-KGVHPHDVATLL 325
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
13-307 1.34e-17

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 83.42  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  13 MTPGPVEAHPSVLRQMgQPILGQFDPEFLQIMDEVRE-MIKVPFATKNQQAFAIDGTSRSGLEAGLFALIEPGDKVLVPT 91
Cdd:PRK13479   9 LTPGPLTTSRTVREAM-LRDWGSWDDDFNALTASVRAkLVAIATGEEGYTCVPLQGSGTFSVEAAIGSLVPRDGKVLVPD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  92 YGRFAYLLGEICER-ARAEVIYLEKDWLAPfeQTTVIEAIKEHQPKI--VAMVHGETANAQMQPLDQIGAFCRENEIFFV 168
Cdd:PRK13479  88 NGAYGARIAQIAEYlGIAHVVLDTGEDEPP--DAAEVEAALAADPRIthVALVHCETTTGILNPLDEIAAVAKRHGKRLI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 169 VDMVATYGGVETKVDDWKIDIAVAGTQKCVS-VPsGLSLITYNQRVADYLAGRyqkelglgadARnerfiqSNYLDL--- 244
Cdd:PRK13479 166 VDAMSSFGAIPIDIAELGIDALISSANKCIEgVP-GFGFVIARRSELEACKGN----------SR------SLSLDLydq 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488317948 245 -SQLEKYwGPERLnhhTEATTMIYGLHEGLRLLLQE-GMENVYARHRKNNRILVESLQKMGLEIF 307
Cdd:PRK13479 229 wAYMEKT-GQWRF---TPPTHVVAAFYQALLELEEEgGVPARGARYANNQRTLVAGMRALGFEPL 289
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
75-338 5.76e-09

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 57.46  E-value: 5.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  75 AGLFALIEPGDKVLVPTYGRFAYLLG--EICERARAEVIYLEKDwlapFEQTTVIEAIKEH---QPKIVAMVHGETANAQ 149
Cdd:COG0520   94 AYGLGRLKPGDEILITEMEHHSNIVPwqELAERTGAEVRVIPLD----EDGELDLEALEALltpRTKLVAVTHVSNVTGT 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 150 MQPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKIDIAVAGTQKCVSvPSGLSLITYNQRVAD----YLAGryqkel 225
Cdd:COG0520  170 VNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYG-PTGIGVLYGKRELLEalppFLGG------ 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 226 glGADARNERFIQSNYLDLsqlekywgPERLnhhtEATTM----IYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQK 301
Cdd:COG0520  243 --GGMIEWVSFDGTTYADL--------PRRF----EAGTPniagAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAA 308
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488317948 302 M-GLEIFGKLDTKTPT-VIPVVIpEGIDGEKVRSLLLDH 338
Cdd:COG0520  309 IpGVRILGPADPEDRSgIVSFNV-DGVHPHDVAALLDDE 346
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
44-196 1.32e-07

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: 50.84  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  44 MDEVREMIKVPFATKNQQAFAIDGtSRSGLEAGLFALIEPGDKVLVPTYGRFAYLlGEICERARAEVIYLEKD--WLAPF 121
Cdd:cd01494    2 LEELEEKLARLLQPGNDKAVFVPS-GTGANEAALLALLGPGDEVIVDANGHGSRY-WVAAELAGAKPVPVPVDdaGYGGL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488317948 122 EQTTVIEAIKEHQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVDMVATYGGV---ETKVDDWKIDIAVAGTQK 196
Cdd:cd01494   80 DVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASpapGVLIPEGGADVVTFSLHK 157
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
76-343 4.42e-06

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: 48.23  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  76 GLFALIEPGDKVLVPTYGRFAYLLG--EICERARAEViylekDWLAPFEQTTV-IEAIKEH---QPKIVAMVHGETANAQ 149
Cdd:cd06453   80 GLGRANKPGDEIVTSVMEHHSNIVPwqQLAERTGAKL-----KVVPVDDDGQLdLEALEKLlteRTKLVAVTHVSNVLGT 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 150 MQPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKIDIAVAGTQKcVSVPSGLSLITYNQRVADylagRYQKELGLGA 229
Cdd:cd06453  155 INPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHK-MLGPTGIGVLYGKEELLE----EMPPYGGGGE 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 230 DARNERFIQSNYLDLsqlekywgPERLNHHTEATTMIYGLHEGLRLLLQEGMENVYARHRKNNRILVESLQKM-GLEIFG 308
Cdd:cd06453  230 MIEEVSFEETTYADL--------PHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIpGVRVYG 301
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488317948 309 KLDTKTPtVIPVVIpEGIDGEKVrSLLLDHFKVEI 343
Cdd:cd06453  302 DAEDRAG-VVSFNL-EGIHPHDV-ATILDQYGIAV 333
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
69-172 2.02e-05

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 46.18  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  69 SRSGLEAGLFALIEPGDKVLVPTYGRFAYLlgEICERARAEVIYL----EKDWLAPFEQttvIEAIKEHQPKIVaMVH-- 142
Cdd:cd00609   68 AQEALSLLLRALLNPGDEVLVPDPTYPGYE--AAARLAGAEVVPVpldeEGGFLLDLEL---LEAAKTPKTKLL-YLNnp 141
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488317948 143 ----GETANAQmQpLDQIGAFCRENEIFFVVDMV 172
Cdd:cd00609  142 nnptGAVLSEE-E-LEELAELAKKHGILIISDEA 173
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
71-341 2.13e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 46.14  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948   71 SGLEAGLFALIEPGDKVLV--PTYGRFAyllgEICERARAEVI----YLEKDWLAPFEQttVIEAIKEhqpKIVAMVH-- 142
Cdd:pfam00155  74 ANIEALIFLLANPGDAILVpaPTYASYI----RIARLAGGEVVryplYDSNDFHLDFDA--LEAALKE---KPKVVLHts 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  143 -----GETANAQMqpLDQIGAFCRENEIFFVVDMVatYGGVetkvddwkidiaVAGTQKCVSVPSGLSlitynQRVADYL 217
Cdd:pfam00155 145 phnptGTVATLEE--LEKLLDLAKEHNILLLVDEA--YAGF------------VFGSPDAVATRALLA-----EGPNLLV 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  218 AGRYQKELGL-----GADARNERFIqsnyldlSQLEK----YWGPErlnhHTEATTMiyglhEGLR---LLLQEGMENVy 285
Cdd:pfam00155 204 VGSFSKAFGLagwrvGYILGNAAVI-------SQLRKlarpFYSST----HLQAAAA-----AALSdplLVASELEEMR- 266
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 488317948  286 ARHRKNNRILVESLQKMGLEIFGKlDTktpTVIPVVIPEGIDGEKVRSLLLDHFKV 341
Cdd:pfam00155 267 QRIKERRDYLRDGLQAAGLSVLPS-QA---GFFLLTGLDPETAKELAQVLLEEVGV 318
PLN02651 PLN02651
cysteine desulfurase
126-188 2.64e-05

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 45.80  E-value: 2.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488317948 126 VIEAIKEhQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKID 188
Cdd:PLN02651 131 LAAAIRP-DTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVD 192
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
72-306 7.07e-05

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 44.74  E-value: 7.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948  72 GLEAGLFALIEPGDKVLVP-----TYGRFAYLLGeicerarAEVIYL----EKDWLAPFEQttVIEAIKehqPKIVAMV- 141
Cdd:COG0436  102 ALALALLALLNPGDEVLVPdpgypSYRAAVRLAG-------GKPVPVpldeENGFLPDPEA--LEAAIT---PRTKAIVl 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 142 ------HGETANAQMqpLDQIGAFCRENEIFFVVDMV---ATYGGVET----KVDDWKidiavagtQKCVSVpSGLSLiT 208
Cdd:COG0436  170 nspnnpTGAVYSREE--LEALAELAREHDLLVISDEIyeeLVYDGAEHvsilSLPGLK--------DRTIVI-NSFSK-S 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 209 YN---QRVAdYLAGryqkelglgadarNERFIQS-----NYLDLSqlekywgperlnhhteATTMI-YGLHEGLRlLLQE 279
Cdd:COG0436  238 YAmtgWRIG-YAVG-------------PPELIAAllklqSNLTSC----------------APTPAqYAAAAALE-GPQD 286
                        250       260
                 ....*....|....*....|....*..
gi 488317948 280 GMENVYARHRKNNRILVESLQKMGLEI 306
Cdd:COG0436  287 YVEEMRAEYRRRRDLLVEGLNEIGLSV 313
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
151-188 2.95e-04

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: 42.73  E-value: 2.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488317948 151 QPLDQIGAFCRENEIFFVVDMVATYGGVETKVDDWKID 188
Cdd:COG1104  157 QPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVD 194
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
104-190 3.47e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 42.62  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488317948 104 ERARAEVIYLE--KDWLAPFEQttVIEAIKEhQPKIVAMVHGETANAQMQPLDQIGAFCRENEIFFVVDMVATYGGVETK 181
Cdd:PRK14012 115 EREGFEVTYLDpqSNGIIDLEK--LEAAMRD-DTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPID 191

                 ....*....
gi 488317948 182 VDDWKIDIA 190
Cdd:PRK14012 192 LSKLKVDLM 200
 
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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