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Conserved domains on  [gi|1868846809|ref|WP_179138133|]
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alanine--glyoxylate aminotransferase family protein [Candidatus Entotheonella palauensis]

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

 Zoom to residue level

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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 ...
 9-404 7.01e-163

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: 462.25  E-value: 7.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809   9 RLLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNeWALLVNGTARAGIEAALVSLLEPGDRVLV 88
Cdd:COG0075     1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEN-DVVILTGSGTGAMEAALANLVSPGDKVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  89 PIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHR-PSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLY 167
Cdd:COG0075    80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 168 VDATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgikpegfvpaaglpIQSNYFDLA 247
Cdd:COG0075   160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARK------------------LPSYYLDLK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 248 MLMDYWsPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELFGDQRHKMANVTGVVVPPG 327
Cdd:COG0075   222 LWLKYW-EKGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEG 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868846809 328 VQGDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYaCRKQNVLLCLGALEAALRQQGFPLGSGAAVDAAMQVYRD 404
Cdd:COG0075   301 VDAAALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 9-404 7.01e-163

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: 462.25  E-value: 7.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809   9 RLLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNeWALLVNGTARAGIEAALVSLLEPGDRVLV 88
Cdd:COG0075     1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEN-DVVILTGSGTGAMEAALANLVSPGDKVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  89 PIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHR-PSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLY 167
Cdd:COG0075    80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 168 VDATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgikpegfvpaaglpIQSNYFDLA 247
Cdd:COG0075   160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARK------------------LPSYYLDLK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 248 MLMDYWsPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELFGDQRHKMANVTGVVVPPG 327
Cdd:COG0075   222 LWLKYW-EKGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEG 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868846809 328 VQGDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYaCRKQNVLLCLGALEAALRQQGFPLGSGAAVDAAMQVYRD 404
Cdd:COG0075   301 VDAAALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 10-383 1.61e-111

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: 330.79  E-value: 1.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  10 LLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNEWALLVNGTARAGIEAALVSLLEPGDRVLVP 89
Cdd:cd06451     1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  90 IFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHRPSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVD 169
Cdd:cd06451    81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 170 ATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgiKPEGFvpaaglpiqsnYFDLAML 249
Cdd:cd06451   161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKT------KPKGF-----------YFDLLLL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 250 MDYWSPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELFGDQRHKMANVTGVVVPPGVQ 329
Cdd:cd06451   224 LKYWGEGYSYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVD 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1868846809 330 GDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYaCRKQNVLLCLGALEAALR 383
Cdd:cd06451   304 GDEVVRRLMKRYNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 6-398 2.67e-81

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 255.07  E-value: 2.67e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809   6 PAPRLLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNEWALLVNGTARAGIEAALVSLLEPGDR 85
Cdd:PLN02409    7 PGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  86 VLVPIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQ---HRPSVVAVVHGDTSTTMAQPLDGLGAI--CR 160
Cdd:PLN02409   87 VVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 161 HYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgiKPEGFVPAAglpiq 240
Cdd:PLN02409  167 QHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAK------SPRVFFDWA----- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 241 sNYFDLAMLMDYWSpqrlnhHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELF-GDQRHKMANV 319
Cdd:PLN02409  236 -DYLKFYKLGTYWP------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCtKKPEWRSDTV 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868846809 320 TGVVVPPGVQGDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYACRKQnVLLCLGALEAALRQQGFPLGSGAAVDAA 398
Cdd:PLN02409  309 TAVVVPEGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVNELQ-LLGALAGVEMVLKDVGYPVKLGSGVAAA 386
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 11-314 6.12e-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: 96.16  E-value: 6.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  11 LMGPGPVNADPRVLRAM-------------SMPLLGQfdaEFTGYMNDVMALLRRLFQTQNEWALL-VNGTARAgIEAAL 76
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIqeyytdyngnvhrGVHTLGK---EATQAYEEAREKVAEFINAPSNDEIIfTSGTTEA-INLVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  77 VSL---LEPGDRVLVPIFGRFGHLLC--EIARRCGADVQSIE-TEWGTVfDPQQIETAIQqHRPSVVAVVHGDTSTTMAQ 150
Cdd:pfam00266  79 LSLgrsLKPGDEIVITEMEHHANLVPwqELAKRTGARVRVLPlDEDGLL-DLDELEKLIT-PKTKLVAITHVSNVTGTIQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 151 PLDGLGAICRHYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKcLSGPSGsapITFndrvvkAIERRRHIEQGIKPEG 230
Cdd:pfam00266 157 PVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTG---IGV------LYGRRDLLEKMPPLLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 231 fvpaAGLPIQSNYFDLAMLMDywSPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAM-GLELF 309
Cdd:pfam00266 227 ----GGGMIETVSLQESTFAD--APWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLpGIRLY 300


                  ....*
gi 1868846809 310 GDQRH 314
Cdd:pfam00266 301 GPERR 305
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 9-404 7.01e-163

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: 462.25  E-value: 7.01e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809   9 RLLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNeWALLVNGTARAGIEAALVSLLEPGDRVLV 88
Cdd:COG0075     1 RLLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEN-DVVILTGSGTGAMEAALANLVSPGDKVLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  89 PIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHR-PSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLY 167
Cdd:COG0075    80 LVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 168 VDATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgikpegfvpaaglpIQSNYFDLA 247
Cdd:COG0075   160 VDAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAIEARK------------------LPSYYLDLK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 248 MLMDYWsPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELFGDQRHKMANVTGVVVPPG 327
Cdd:COG0075   222 LWLKYW-EKGQTPYTPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEG 300

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1868846809 328 VQGDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYaCRKQNVLLCLGALEAALRQQGFPLGSGAAVDAAMQVYRD 404
Cdd:COG0075   301 VDAAALRKRLKERYGIEIAGGLGPLKGKIFRIGHMGY-VNPEDVLRTLAALEEALRELGVPVELGAGVAAAQEVLAE 376
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 10-383 1.61e-111

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: 330.79  E-value: 1.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  10 LLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNEWALLVNGTARAGIEAALVSLLEPGDRVLVP 89
Cdd:cd06451     1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  90 IFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHRPSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVD 169
Cdd:cd06451    81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 170 ATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgiKPEGFvpaaglpiqsnYFDLAML 249
Cdd:cd06451   161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIKKKT------KPKGF-----------YFDLLLL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 250 MDYWSPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELFGDQRHKMANVTGVVVPPGVQ 329
Cdd:cd06451   224 LKYWGEGYSYPHTPPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVD 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1868846809 330 GDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYaCRKQNVLLCLGALEAALR 383
Cdd:cd06451   304 GDEVVRRLMKRYNIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 6-398 2.67e-81

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 255.07  E-value: 2.67e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809   6 PAPRLLMGPGPVNADPRVLRAMSMPLLGQFDAEFTGYMNDVMALLRRLFQTQNEWALLVNGTARAGIEAALVSLLEPGDR 85
Cdd:PLN02409    7 PGRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  86 VLVPIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQ---HRPSVVAVVHGDTSTTMAQPLDGLGAI--CR 160
Cdd:PLN02409   87 VVSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 161 HYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKCLSGPSGSAPITFNDRVVKAIERRRhieqgiKPEGFVPAAglpiq 240
Cdd:PLN02409  167 QHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAK------SPRVFFDWA----- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 241 sNYFDLAMLMDYWSpqrlnhHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAMGLELF-GDQRHKMANV 319
Cdd:PLN02409  236 -DYLKFYKLGTYWP------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCtKKPEWRSDTV 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1868846809 320 TGVVVPPGVQGDAIRHSLLEDFGIEIGTSFGPLHGRIWRIGAMGYACRKQnVLLCLGALEAALRQQGFPLGSGAAVDAA 398
Cdd:PLN02409  309 TAVVVPEGIDSAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVNELQ-LLGALAGVEMVLKDVGYPVKLGSGVAAA 386
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 11-314 6.12e-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: 96.16  E-value: 6.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  11 LMGPGPVNADPRVLRAM-------------SMPLLGQfdaEFTGYMNDVMALLRRLFQTQNEWALL-VNGTARAgIEAAL 76
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIqeyytdyngnvhrGVHTLGK---EATQAYEEAREKVAEFINAPSNDEIIfTSGTTEA-INLVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  77 VSL---LEPGDRVLVPIFGRFGHLLC--EIARRCGADVQSIE-TEWGTVfDPQQIETAIQqHRPSVVAVVHGDTSTTMAQ 150
Cdd:pfam00266  79 LSLgrsLKPGDEIVITEMEHHANLVPwqELAKRTGARVRVLPlDEDGLL-DLDELEKLIT-PKTKLVAITHVSNVTGTIQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 151 PLDGLGAICRHYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKcLSGPSGsapITFndrvvkAIERRRHIEQGIKPEG 230
Cdd:pfam00266 157 PVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTG---IGV------LYGRRDLLEKMPPLLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 231 fvpaAGLPIQSNYFDLAMLMDywSPQRLNHHTEASSMLYAARECARLVLREGLDACFERHALASRAMTTGLQAM-GLELF 309
Cdd:pfam00266 227 ----GGGMIETVSLQESTFAD--APWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLpGIRLY 300


                  ....*
gi 1868846809 310 GDQRH 314
Cdd:pfam00266 301 GPERR 305
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 43-204 5.70e-20

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: 86.28  E-value: 5.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  43 MNDVMALLRRLFQTQNEWALLVNGtARAGIEAALVSLLEPGDRVLVPIFGRFGHLLcEIARRCGA---DVQSIETEWGTV 119
Cdd:cd01494     2 LEELEEKLARLLQPGNDKAVFVPS-GTGANEAALLALLGPGDEVIVDANGHGSRYW-VAAELAGAkpvPVPVDDAGYGGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 120 fDPQQIETAIQQHRPSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVDATATLGGMTVP---VDAWQLDIVSAGLQKC 196
Cdd:cd01494    80 -DVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPgvlIPEGGADVVTFSLHKN 158


                  ....*...
gi 1868846809 197 LSGPSGSA 204
Cdd:cd01494   159 LGGEGGGV 166
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 10-202 4.14e-19

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 88.05  E-value: 4.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  10 LLMGPGPVNADPRVLRAMsMPLLGQFDAEFTGYMNDVMALLRRLFQTQNEW-ALLVNGTARAGIEAALVSLLEPGDRVLV 88
Cdd:PRK13479    7 LLLTPGPLTTSRTVREAM-LRDWGSWDDDFNALTASVRAKLVAIATGEEGYtCVPLQGSGTFSVEAAIGSLVPRDGKVLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  89 PIFGRFGHLLCEIARRCGADVQSIETEWGTVFDPQQIETAIQQHrPSV--VAVVHGDTSTTMAQPLDGLGAICRHYDALL 166
Cdd:PRK13479   86 PDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAAD-PRIthVALVHCETTTGILNPLDEIAAVAKRHGKRL 164

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1868846809 167 YVDATATLGGmtVPVDAWQLDI---VSAGlQKCLSGPSG 202
Cdd:PRK13479  165 IVDAMSSFGA--IPIDIAELGIdalISSA-NKCIEGVPG 200
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
74-203 7.40e-08

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 53.99  E-value: 7.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  74 AALVSLLEPGDRVLVPIfgrfghllCE----------IARRCGADVQSIE-TEWGTVfDPQQIETAIQqHRPSVVAVVHG 142
Cdd:COG0520    94 AYGLGRLKPGDEILITE--------MEhhsnivpwqeLAERTGAEVRVIPlDEDGEL-DLEALEALLT-PRTKLVAVTHV 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1868846809 143 DTSTTMAQPLDGLGAICRHYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKcLSGPSGS 203
Cdd:COG0520   164 SNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGI 223
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 21-237 1.34e-07

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 53.11  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  21 PRVLRAMSmpllgQFDAEFTGYMND-----VMALLRRLFQtqNEWALLV-NGTAraGIEAALVSLLEPGDRVLVpifGRF 94
Cdd:cd06502    12 PEMLEAMA-----AANVGDDVYGEDpttakLEARAAELFG--KEAALFVpSGTA--ANQLALAAHTQPGGSVIC---HET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  95 GHLLCE----IARRCGADVQSIETEWGTvFDPQQIETAIQQH------RPSVVAV---VHGDTSTTMAQpLDGLGAICRH 161
Cdd:cd06502    80 AHIYTDeagaPEFLSGVKLLPVPGENGK-LTPEDLEAAIRPRddihfpPPSLVSLentTEGGTVYPLDE-LKAISALAKE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 162 YDALLYVD------ATATLGgmtVPVDAWQ--LDIVSAGLQKCLSGPSGSapITFNDR--VVKAIERRRHIEQGIKPEGF 231
Cdd:cd06502   158 NGLPLHLDgarlanAAAALG---VALKTYKsgVDSVSFCLSKGGGAPVGA--VVVGNRdfIARARRRRKQAGGGMRQSGF 232


                  ....*.
gi 1868846809 232 VPAAGL 237
Cdd:cd06502   233 LAAAGL 238
PRK03080 PRK03080
phosphoserine transaminase;
46-199 2.57e-07

phosphoserine transaminase;


Pssm-ID: 235103  Cd Length: 378  Bit Score: 52.11  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  46 VMALLRRLFQTQNEWAL-LVNGTARAGIEAALVSLLEPgDRVLVPIFGRFG-----------HLlceiarrcgADVQSIE 113
Cdd:PRK03080   53 VIEGTRELLSLPEGYEVgIVPGSDTGAWEMALWSLLGA-RRVDHLAWESFGskwatdvvkqlKL---------EDPRVLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 114 TEWGTVFDPQQIETAiqqhrpSVVAVVHGDTSTTMAQPLDGLGAICRhyDALLYVDATATLGGMTVPVDawQLDIVSAGL 193
Cdd:PRK03080  123 ADYGSLPDLSAVDFD------RDVVFTWNGTTTGVRVPVARWIGADR--EGLTICDATSAAFALPLDWS--KLDVYTFSW 192


                  ....*.
gi 1868846809 194 QKCLSG 199
Cdd:PRK03080  193 QKVLGG 198
SerC COG1932
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ...
 37-202 6.82e-07

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: 50.84  E-value: 6.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  37 AEFTGYMNDVMALLRRLFQTQNEWA-LLVNGTARAGIEAALVSLLEPGDRVLVPIFGRFGHL-LCEIARRCGADV--QSI 112
Cdd:COG1932    43 KPFKAIVEEAEADLRELLGIPDGYEvLFLQGGATAQFAMVPMNLLRGGKKADYLVTGEWSKKaIKEAKKYGEVNVvaSSE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 113 ETEWGTVFDPQQIEtaiqqhRPSVVAVVHG---DTST-TMAQPLDGLGaicrhyDALLYVDATATLGGMtvPVDAWQLDI 188
Cdd:COG1932   123 DDNFGYIPKPEEWQ------LSPDADYVHYtsnETITgVEFHELPDVG------DVPLVADMSSDILSR--PVDVSKFGL 188

                         170
                  ....*....|....
gi 1868846809 189 VSAGLQKCLsGPSG 202
Cdd:COG1932   189 IYAGAQKNI-GPAG 201
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 51-169 1.74e-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: 46.57  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  51 RRLFQTQNEWALLVNGtARAGIEAALVSLLEPGDRVLVPIFGRFGHLlcEIARRCGADVQSIE-TEWGTVFDPQQIETAI 129
Cdd:cd00609    52 RGGVDVPPEEIVVTNG-AQEALSLLLRALLNPGDEVLVPDPTYPGYE--AAARLAGAEVVPVPlDEEGGFLLDLELLEAA 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1868846809 130 QQHRPSVVAVVHGD--TSTTMAQP-LDGLGAICRHYDALLYVD 169
Cdd:cd00609   129 KTPKTKLLYLNNPNnpTGAVLSEEeLEELAELAKKHGILIISD 171
PLN02651 PLN02651
cysteine desulfurase
 121-204 4.63e-05

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 45.03  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 121 DPQQIETAIQQHrPSVVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVDATATLGGMTVPVDAWQLDIVSAGLQKcLSGP 200
Cdd:PLN02651  127 DLDELAAAIRPD-TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK-IYGP 204


                  ....
gi 1868846809 201 SGSA 204
Cdd:PLN02651  205 KGVG 208
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 99-191 5.69e-05

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: 45.04  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  99 CEIARRCGADVQSIE-TEWGTVfDPQQIETAIqqhRPSVVAVvhgdtsTTMA--------QPLDGLGAICRHYDALLYVD 169
Cdd:COG1104   107 ARFLEKEGFEVTYLPvDEDGRV-DLEALEAAL---RPDTALV------SVMHannetgtiQPIAEIAEIAKEHGVLFHTD 176

                          90       100
                  ....*....|....*....|..
gi 1868846809 170 ATATLGGMTVPVDAWQLDIVSA 191
Cdd:COG1104   177 AVQAVGKIPVDVKELGVDLLSL 198
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 75-187 6.25e-05

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: 44.76  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  75 ALVSLLEPGDRV----------LVPIfgrfgHLLCEiarRCGADVQSIE-TEWGTVfDPQQIETAIQQhRPSVVAVVHGD 143
Cdd:cd06453    80 GLGRANKPGDEIvtsvmehhsnIVPW-----QQLAE---RTGAKLKVVPvDDDGQL-DLEALEKLLTE-RTKLVAVTHVS 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1868846809 144 TSTTMAQPLDGLGAICRHYDALLYVDATATLGGMTVPVDAWQLD 187
Cdd:cd06453   150 NVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCD 193
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
96-212 3.28e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 42.41  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  96 HLLCEIARRCGADVQSIETEWGTVFDPQQIETAIqqhRPS--VVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVDATAT 173
Cdd:PRK02948  102 HSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAI---TPDtvLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQT 178

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1868846809 174 LGGMTVPVDAWQLDIVSAGLQKcLSGPSGSAPITFNDRV 212
Cdd:PRK02948  179 FGKLPIDVFEMGIDSLSVSAHK-IYGPKGVGAVYINPQV 216
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
61-176 6.04e-04

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 41.59  E-value: 6.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  61 ALLV-NGTAraGIEAALVSL-LEPGDRVLVPIFGrFghllceIA-----RRCGADVqsietewgtVF----------DPQ 123
Cdd:COG0399    48 AVAVsSGTA--ALHLALRALgIGPGDEVITPAFT-F------VAtanaiLYVGATP---------VFvdidpdtyniDPE 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868846809 124 QIETAIQQhRPSVVAVVHgdtsttMA-QP--LDGLGAICRHYDALLYVDATATLGG 176
Cdd:COG0399   110 ALEAAITP-RTKAIIPVH------LYgQPadMDAIMAIAKKHGLKVIEDAAQALGA 158
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 22-166 1.02e-03

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 40.97  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  22 RVLRAMSMPLLGqfDAEFTGYMNDVMALLRRL----FQTQNEWALLVNGtARAGIEAALVSLLEPGDRVLV--PIFgrFG 95
Cdd:COG1167   132 RALRRLPPALLG--YGDPQGLPELREAIARYLarrgVPASPDQILITSG-AQQALDLALRALLRPGDTVAVesPTY--PG 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868846809  96 HLlcEIARRCGADVQSIET-EWGtvFDPQQIETAIQQHRPSVVAVV---HGDTSTTMaqPLD---GLGAICRHYDALL 166
Cdd:COG1167   207 AL--AALRAAGLRLVPVPVdEDG--LDLDALEAALRRHRPRAVYVTpshQNPTGATM--SLErrrALLELARRHGVPI 278
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
62-140 1.48e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 40.48  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  62 LLVNGTARAGIEAALVSLLEPGDRVLVPIFGRFGHLlcEIARRCGADVQSIET-EWGTVFDPQQIETAIQQHRPSVVAVV 140
Cdd:PRK07309   94 ILVTIGATEALSASLTAILEPGDKVLLPAPAYPGYE--PIVNLVGAEIVEIDTtENDFVLTPEMLEKAILEQGDKLKAVI 171
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
104-202 2.78e-03

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 39.54  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809 104 RCGADVQSIETEWGTVFDPQQIETAIqqhRPS--VVAVVHGDTSTTMAQPLDGLGAICRHYDALLYVDATATLGGMTVPV 181
Cdd:PRK14012  116 REGFEVTYLDPQSNGIIDLEKLEAAM---RDDtiLVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDL 192

                          90       100
                  ....*....|....*....|.
gi 1868846809 182 DAWQLDIVSAGLQKcLSGPSG 202
Cdd:PRK14012  193 SKLKVDLMSFSAHK-IYGPKG 212
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 74-175 7.60e-03

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 38.22  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  74 AALVSLLEPGDRVLVpifGRFGHL-LCEIARRCGADVQsietewgtVF---DPQQIETAIQQHRPSVVAVV-------HG 142
Cdd:PRK05958  114 AVLTALAGKGDLIVS---DKLNHAsLIDGARLSRARVR--------RYphnDVDALEALLAKWRAGRALIVtesvfsmDG 182

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1868846809 143 DTSttmaqPLDGLGAICRHYDALLYVD---ATATLG 175
Cdd:PRK05958  183 DLA-----PLAELVALARRHGAWLLVDeahGTGVLG 213
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
123-149 8.99e-03

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 38.12  E-value: 8.99e-03
                          10        20
                  ....*....|....*....|....*..
gi 1868846809 123 QQIETAIQQHRPSVVaVVHGDTSTTMA 149
Cdd:COG0381    78 EGLEEVLEEEKPDAV-LVHGDTNSTLA 103
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
55-169 9.83e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 37.67  E-value: 9.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868846809  55 QTQNEWALLVNGTARAGIEAALVSLLEPGDRVLVPIFGRFGHLlcEIARRCGADVQSIETEWGTVF--DPQQIETAIQQh 132
Cdd:pfam00155  59 KLDREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYI--RIARLAGGEVVRYPLYDSNDFhlDFDALEAALKE- 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1868846809 133 RPSVVAV--VHGDTSTTMAQP-LDGLGAICRHYDALLYVD 169
Cdd:pfam00155 136 KPKVVLHtsPHNPTGTVATLEeLEKLLDLAKEHNILLLVD 175
 
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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