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Conserved domains on  [gi|2168986039|ref|NP_001385605|]
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kynureninase isoform 1 [Mus musculus]

Protein Classification

kynureninase( domain architecture ID 11493179)

kynureninase catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
kynureninase TIGR01814
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
30-459 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


:

Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 611.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039  30 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 109
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 110 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 189
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 190 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 269
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 270 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 349
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 350 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVCDKRE 429
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIGDKRE 376
                         410       420       430
                  ....*....|....*....|....*....|
gi 2168986039 430 PDGIRVAPVPLYNSFHDVYKFIRLLTSILD 459
Cdd:TIGR01814 377 PSVIRVAPVPLYNTFVDVYDAVNVLEEILD 406
 
Name Accession Description Interval E-value
kynureninase TIGR01814
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
30-459 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 611.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039  30 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 109
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 110 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 189
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 190 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 269
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 270 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 349
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 350 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVCDKRE 429
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIGDKRE 376
                         410       420       430
                  ....*....|....*....|....*....|
gi 2168986039 430 PDGIRVAPVPLYNSFHDVYKFIRLLTSILD 459
Cdd:TIGR01814 377 PSVIRVAPVPLYNTFVDVYDAVNVLEEILD 406
Bna5 COG3844
Kynureninase [Amino acid transport and metabolism];
30-462 6.36e-175

Kynureninase [Amino acid transport and metabolism];


Pssm-ID: 443054 [Multi-domain]  Cd Length: 420  Bit Score: 496.95  E-value: 6.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039  30 ALRLDEEDKLSHFRNCFYIPkmrdlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEEL-DKWAKMGAYGHDvgKRP 108
Cdd:COG3844     8 ARALDAADPLAAFRDRFHLP---------------DDGVIYLDGNSLGLLPKAAAARLAEVLeEEWGELLIRGWN--EAP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 109 WI-----VGDesivsLMKDIVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDV 183
Cdd:COG3844    71 WFdlperLGD-----KLARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPRPGRTKILSEADNFPTDRYALEGQARLHGLDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 184 EksMRMVKPREGEeTLRMEDILEVIEEEgdsIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLH 263
Cdd:COG3844   146 E--LRLVEPRDGE-TLRPEDIEAALDDD---VALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 264 DWGVDFACWCSYKYLNSGAGGLAGAFVHEKHAHTVKPALVGWFGHDlsTRFNMDNKLQLIPGANGFRISNPPILLVCSLH 343
Cdd:COG3844   220 DWGVDFAVGCTYKYLNGGPGAPAFLYVHERHQDRLLQPLAGWWGHA--TPFAMEPGYEPAPGARRFQLGTPPILSMAALE 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 344 ASLEVFQQATMTALRRKSILLTGYLEYMLKHyhskdntENKGPIVNIITPSRAEERGCQLTLTfsIPK-KSVFKELEKRG 422
Cdd:COG3844   298 ASLDLFEEAGMDALRAKSLALTDYLIFLVEE-------RLAPLGLELITPRDPARRGSQVSLR--HPEaYAIFQALIERG 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2168986039 423 VVCDKREPDGIRVAPVPLYNSFHDVYKFIRLLTSILDSSE 462
Cdd:COG3844   369 VIGDFREPDVIRFGPTPLYTSFEDVWRAVEILREILEEGE 408
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
179-347 1.63e-05

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: 46.90  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 179 HGLDVE----KSMRMVKPREGEETLRMEDILEVIEEEGDSiavilfsglhfYTGQLFNIPAITKAGHAKGCFVGFDLAHA 254
Cdd:cd06451    96 YGADVDvvekPWGEAVSPEEIAEALEQHDIKAVTLTHNET-----------STGVLNPLEGIGALAKKHDALLIVDAVSS 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 255 VGNVELRLHDWGVDFACWCSYKYLNSGAGGLAGAFVHEkhahtvkpALVGWFGHDLSTRFNMDNKLQLIP-GANGFRISN 333
Cdd:cd06451   165 LGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSER--------ALERIKKKTKPKGFYFDLLLLLKYwGEGYSYPHT 236
                         170
                  ....*....|....
gi 2168986039 334 PPILLVCSLHASLE 347
Cdd:cd06451   237 PPVNLLYALREALD 250
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
227-369 7.59e-04

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: 41.46  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 227 TGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYKYLnsGAGGLAGAFVHEKHAHTVKPALVGwf 306
Cdd:pfam00266 152 TGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG-- 227
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168986039 307 GHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVFQQATMTALRRKSILLTGYLE 369
Cdd:pfam00266 228 GGMIETVSLQESTFADAP--WKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288
 
Name Accession Description Interval E-value
kynureninase TIGR01814
kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a ...
30-459 0e+00

kynureninase; This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130873 [Multi-domain]  Cd Length: 406  Bit Score: 611.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039  30 ALRLDEEDKLSHFRNCFYIPKMRDlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPW 109
Cdd:TIGR01814   1 ALELDEADPLRALRDEFHLPKIGD-----------ENAVIYLDGNSLGLMPKAARNALKEELDKWAKIAIRGHNTGKAPW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 110 IVGDESIVSLMKdiVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRM 189
Cdd:TIGR01814  70 FTLDESLLKLRL--VGAKEDEVVVMNTLTINLHLLLASFYKPTPKRYKILLEAKAFPSDHYAIESQLQLHGLTVEESMVQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 190 VKPREgEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDF 269
Cdd:TIGR01814 148 IEPRE-EETLRLEDILDTIEKNGDDIAVILLSGVQYYTGQLFDMAAITRAAHAKGALVGFDLAHAVGNVPLDLHDWGVDF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 270 ACWCSYKYLNsgAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVF 349
Cdd:TIGR01814 227 ACWCTYKYLN--AGPGAGAFVHEKHAHTERPRLAGWWGHARPTRFKMDNTLGLIP--CGFRISNPPILSVAALRGSLDIF 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 350 QQATMTALRRKSILLTGYLEYMLKHYHSKDntenkgPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVCDKRE 429
Cdd:TIGR01814 303 DQAGMEALRKKSLLLTDYLEELIKARCGGP------PVLTIITPRDHAQRGCQLSLTHPVPGKAVFQALIKRGVIGDKRE 376
                         410       420       430
                  ....*....|....*....|....*....|
gi 2168986039 430 PDGIRVAPVPLYNSFHDVYKFIRLLTSILD 459
Cdd:TIGR01814 377 PSVIRVAPVPLYNTFVDVYDAVNVLEEILD 406
Bna5 COG3844
Kynureninase [Amino acid transport and metabolism];
30-462 6.36e-175

Kynureninase [Amino acid transport and metabolism];


Pssm-ID: 443054 [Multi-domain]  Cd Length: 420  Bit Score: 496.95  E-value: 6.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039  30 ALRLDEEDKLSHFRNCFYIPkmrdlpsidlslvseDDDAIYFLGNSLGLQPKMVRTYLEEEL-DKWAKMGAYGHDvgKRP 108
Cdd:COG3844     8 ARALDAADPLAAFRDRFHLP---------------DDGVIYLDGNSLGLLPKAAAARLAEVLeEEWGELLIRGWN--EAP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 109 WI-----VGDesivsLMKDIVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDV 183
Cdd:COG3844    71 WFdlperLGD-----KLARLVGAAPGEVVVMDSTTVNLHKLLVAAYRPRPGRTKILSEADNFPTDRYALEGQARLHGLDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 184 EksMRMVKPREGEeTLRMEDILEVIEEEgdsIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLH 263
Cdd:COG3844   146 E--LRLVEPRDGE-TLRPEDIEAALDDD---VALVLLSHVNYRTGQLFDMAAITAAAHAAGALVGWDLAHSAGAVPVDLH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 264 DWGVDFACWCSYKYLNSGAGGLAGAFVHEKHAHTVKPALVGWFGHDlsTRFNMDNKLQLIPGANGFRISNPPILLVCSLH 343
Cdd:COG3844   220 DWGVDFAVGCTYKYLNGGPGAPAFLYVHERHQDRLLQPLAGWWGHA--TPFAMEPGYEPAPGARRFQLGTPPILSMAALE 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 344 ASLEVFQQATMTALRRKSILLTGYLEYMLKHyhskdntENKGPIVNIITPSRAEERGCQLTLTfsIPK-KSVFKELEKRG 422
Cdd:COG3844   298 ASLDLFEEAGMDALRAKSLALTDYLIFLVEE-------RLAPLGLELITPRDPARRGSQVSLR--HPEaYAIFQALIERG 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2168986039 423 VVCDKREPDGIRVAPVPLYNSFHDVYKFIRLLTSILDSSE 462
Cdd:COG3844   369 VIGDFREPDVIRFGPTPLYTSFEDVWRAVEILREILEEGE 408
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
198-459 2.74e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.45  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 198 TLRMEDILEVIeeeGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYK- 276
Cdd:COG0520   141 ELDLEALEALL---TPRTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKl 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 277 YLNSGAGGLagaFVHEKHAHTVKPALVGWFghdlSTRFNMDNKLQLIPGANGFRISNPPILLVCSLHASLEVFQQATMTA 356
Cdd:COG0520   218 YGPTGIGVL---YGKRELLEALPPFLGGGG----MIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEA 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 357 LRRKSILLTGYLEYMLKhyhskdntENKGpiVNIITPSRAEERGCqlTLTFSIPKKS---VFKELEKRGVV------C-- 425
Cdd:COG0520   291 IEARERELTAYALEGLA--------AIPG--VRILGPADPEDRSG--IVSFNVDGVHphdVAALLDDEGIAvraghhCaq 358
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2168986039 426 ---DKRE-PDGIRVAPVpLYNSFHDVYKFIRLLTSILD 459
Cdd:COG0520   359 plmRRLGvPGTVRASFH-LYNTEEEIDRLVEALKKLAE 395
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
179-347 1.63e-05

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: 46.90  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 179 HGLDVE----KSMRMVKPREGEETLRMEDILEVIEEEGDSiavilfsglhfYTGQLFNIPAITKAGHAKGCFVGFDLAHA 254
Cdd:cd06451    96 YGADVDvvekPWGEAVSPEEIAEALEQHDIKAVTLTHNET-----------STGVLNPLEGIGALAKKHDALLIVDAVSS 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 255 VGNVELRLHDWGVDFACWCSYKYLNSGAGGLAGAFVHEkhahtvkpALVGWFGHDLSTRFNMDNKLQLIP-GANGFRISN 333
Cdd:cd06451   165 LGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSER--------ALERIKKKTKPKGFYFDLLLLLKYwGEGYSYPHT 236
                         170
                  ....*....|....
gi 2168986039 334 PPILLVCSLHASLE 347
Cdd:cd06451   237 PPVNLLYALREALD 250
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
227-369 7.59e-04

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: 41.46  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168986039 227 TGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYKYLnsGAGGLAGAFVHEKHAHTVKPALVGwf 306
Cdd:pfam00266 152 TGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLY--GPTGIGVLYGRRDLLEKMPPLLGG-- 227
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2168986039 307 GHDLSTRFNMDNKLQLIPgaNGFRISNPPILLVCSLHASLEVFQQATMTALRRKSILLTGYLE 369
Cdd:pfam00266 228 GGMIETVSLQESTFADAP--WKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288
 
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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