NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446445211|ref|WP_000523066|]
View 

aminotransferase class V-fold PLP-dependent enzyme [Bacillus thuringiensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PucG super family cl33759
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 182-519 9.45e-57

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


The actual alignment was detected with superfamily member COG0075:

Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 193.77  E-value: 9.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 182 YTFLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVKKRLLQMTKAK-RVQIMLGTGTLANDAIalqLRSLKGKG---I 257
Cdd:COG0075    2 LLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEnDVVILTGSGTGAMEAA---LANLVSPGdkvL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 258 VLTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMESG-NYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKL 336
Cdd:COG0075   79 VLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 337 CVDCISSIGAVPIDLKD--IYFASGVSGKAIKSYTGLSFVFHNH----IVKINEAVPAYMDIGM---YEENESIPYSHSW 407
Cdd:COG0075  159 IVDAVSSLGGVPLDMDEwgIDVVVSGSQKCLMLPPGLAFVAVSEraleAIEARKLPSYYLDLKLwlkYWEKGQTPYTPPV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 408 NLIYALQEALKRFEDET---AFVKIKEIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSEGQSSKTIGDELALQ-GYIV 483
Cdd:COG0075  239 SLLYALREALDLILEEGlenRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERyGIEI 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446445211 484 -----HYesaylqKNNWIQIACLNHYKERDMKRMLNWLQMC 519
Cdd:COG0075  319 agglgPL------KGKIFRIGHMGYVNPEDVLRTLAALEEA 353
Acetyltransf_5 pfam13444
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 20-112 5.73e-17

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions.


:

Pssm-ID: 463880  Cd Length: 102  Bit Score: 76.49  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   20 LNYKTFVEEIPQHEET-KDRVRIDRFHEENTYLICLDDD--KLVGMVALRGKRPFSL---DYKISNLD-FYLQEHGENVY 92
Cdd:pfam13444   1 LRYRVFREEMGATGPAaLPGLDIDRFDAYCDHLLVWDDDtgEVVGTYRLLPPDAASGlggFYSATEFDlSALLALRGRLL 80

                          90       100
                  ....*....|....*....|
gi 446445211   93 EIRLLSVEREYRNGRALLGL 112
Cdd:pfam13444  81 ELGRSCVHPEYRNGRVLLLL 100
PhnO super family cl42766
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 84-160 5.05e-03

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


The actual alignment was detected with superfamily member COG0454:

Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  84 LQEHGENVYEIRLLSVEREYRN---GRALLgliRFLHRYLLLNGY---ELALISATTRELPLYEQMGFKAFHMLVGTEEA 157
Cdd:COG0454   51 LRRLDDKVLELKRLYVLPEYRGkgiGKALL---EALLEWARERGCtalELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127


                 ...
gi 446445211 158 AFQ 160
Cdd:COG0454  128 EFE 130
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 182-519 9.45e-57

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: 193.77  E-value: 9.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 182 YTFLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVKKRLLQMTKAK-RVQIMLGTGTLANDAIalqLRSLKGKG---I 257
Cdd:COG0075    2 LLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEnDVVILTGSGTGAMEAA---LANLVSPGdkvL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 258 VLTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMESG-NYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKL 336
Cdd:COG0075   79 VLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 337 CVDCISSIGAVPIDLKD--IYFASGVSGKAIKSYTGLSFVFHNH----IVKINEAVPAYMDIGM---YEENESIPYSHSW 407
Cdd:COG0075  159 IVDAVSSLGGVPLDMDEwgIDVVVSGSQKCLMLPPGLAFVAVSEraleAIEARKLPSYYLDLKLwlkYWEKGQTPYTPPV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 408 NLIYALQEALKRFEDET---AFVKIKEIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSEGQSSKTIGDELALQ-GYIV 483
Cdd:COG0075  239 SLLYALREALDLILEEGlenRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERyGIEI 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446445211 484 -----HYesaylqKNNWIQIACLNHYKERDMKRMLNWLQMC 519
Cdd:COG0075  319 agglgPL------KGKIFRIGHMGYVNPEDVLRTLAALEEA 353
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 184-472 2.46e-41

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: 152.06  E-value: 2.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 184 FLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVKKRLLQM--TKAKRVQIMLGTGTLANDAIALQLRSLKGKGIVLTN 261
Cdd:cd06451    3 LIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVfqTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVGVN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 262 GEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMESGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLCVDCI 341
Cdd:cd06451   83 GVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 342 SSIGAVPIDLK----DIYFaSGvSGKAIKSYTGLSFV-----FHNHIVKINEAVPAYMDIGMY----EENESIPYSHSWN 408
Cdd:cd06451  163 SSLGGEPFRMDewgvDVAY-TG-SQKALGAPPGLGPIafserALERIKKKTKPKGFYFDLLLLlkywGEGYSYPHTPPVN 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446445211 409 LIYALQEALKRFEDETAFVKIK---EIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSEGQSSKTI 472
Cdd:cd06451  241 LLYALREALDLILEEGLENRWArhrRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDEV 307
PhnW-AepZ TIGR03301
2-aminoethylphosphonate aminotransferase; This family includes a number of ...
 182-513 4.63e-33

2-aminoethylphosphonate aminotransferase; This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.


Pssm-ID: 274512 [Multi-domain]  Cd Length: 355  Bit Score: 129.03  E-value: 4.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  182 YTFLPGPVDIEENVRKAFsTKPISHRSKSFQVTMDNVKKRLLQMTKA--KRVQIML-GTGTLANDAIALQLRSLKGKGIV 258
Cdd:TIGR03301   1 ILLTPGPLSTSATVRDAM-LVDWCHWDSEFNDVTDQVRDRLLALAGGddNHTCVLLqGSGTFAVEATIGSLVPRDGKLLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  259 LTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVM-ESGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLC 337
Cdd:TIGR03301  80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALaADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  338 VDCISSIGAVPIDLK--DIYFASGVSGKAIKSYTGLSFVFHNHIVKINEAVPA---YMDI----GMYEENESIPYSHSWN 408
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEelDVDALIASANKCLEGVPGFGFVIARRDLLEASAGNArslYLDLydqwAYMEKTGKWRFTPPTH 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  409 LIYALQEALKRFEDETA----FVKIKEIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSE--GQSSKTIGDELALQGYI 482
Cdd:TIGR03301 240 TVYAFAQALEELEAEGGvparIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDdpDFDFDDFYQELKERGFV 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 446445211  483 VHyeSAYLQKNNWIQIACLNHYKERDMKRML 513
Cdd:TIGR03301 320 IY--PGKLTLADTFRIGTIGEIDAADIERLL 348
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 184-423 2.96e-20

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 92.90  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 184 FLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVK---KRLLQmTKAKRVQIMLGTGTLANDAIALQLRSLKGKGIVLT 260
Cdd:PLN02409  13 FVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLedvKYIFK-TKSGTPFIFPTTGTGAWESALTNTLSPGDKVVSFR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 261 NGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTEL-EKVMESGNYE--WLWFVHHETSTGMLNDLKELNVLTKKYQIK-- 335
Cdd:PLN02409  92 IGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILkSKLRQDTNHKikAVCVVHNETSTGVTNDLAGVRKLLDCAQHPal 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 336 LCVDCISSIGAVPIDLKDIYFASGVSG--KAIKSYTGLSFVFHN----HIVKINEAVPAYMDIG----MYEENESIPYSH 405
Cdd:PLN02409 172 LLVDGVSSIGALDFRMDEWGVDVALTGsqKALSLPTGLGIVCASpkalEASKTAKSPRVFFDWAdylkFYKLGTYWPYTP 251

                        250
                 ....*....|....*...
gi 446445211 406 SWNLIYALQEALKRFEDE 423
Cdd:PLN02409 252 SIQLLYGLRAALDLIFEE 269
Acetyltransf_5 pfam13444
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 20-112 5.73e-17

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions.


Pssm-ID: 463880  Cd Length: 102  Bit Score: 76.49  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   20 LNYKTFVEEIPQHEET-KDRVRIDRFHEENTYLICLDDD--KLVGMVALRGKRPFSL---DYKISNLD-FYLQEHGENVY 92
Cdd:pfam13444   1 LRYRVFREEMGATGPAaLPGLDIDRFDAYCDHLLVWDDDtgEVVGTYRLLPPDAASGlggFYSATEFDlSALLALRGRLL 80

                          90       100
                  ....*....|....*....|
gi 446445211   93 EIRLLSVEREYRNGRALLGL 112
Cdd:pfam13444  81 ELGRSCVHPEYRNGRVLLLL 100
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-147 8.19e-11

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.10  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  13 EFESIHKLNYKTFveeiPQHEETKDRVRIDRFHEENTYLICLDDDKLVGMVALRgkrPFSLDykisnldfylqeHGENVY 92
Cdd:COG3153    8 DAEAIAALLRAAF----GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALS---PVDID------------GEGPAL 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446445211  93 EIRLLSVEREYRN---GRALlglIRFLHRYLLLNGYELALISATTRELPLYEQMGFKA 147
Cdd:COG3153   69 LLGPLAVDPEYRGqgiGRAL---MRAALEAARERGARAVVLLGDPSLLPFYERFGFRP 123
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 204-475 8.38e-07

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: 51.09  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  204 ISHRSKSFQVTMDNVKKRLLQMTKAKRVQIMLGT--GTLANDAIALQL-RSLKGKG-IVLTNGEF-GNRL----VGHATR 274
Cdd:pfam00266  34 VHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTsgTTEAINLVALSLgRSLKPGDeIVITEMEHhANLVpwqeLAKRTG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  275 AQLHFdTYKKEMGEPFLyTELEKVMeSGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLCVDCISSIGAVPIDLK-- 352
Cdd:pfam00266 114 ARVRV-LPLDEDGLLDL-DELEKLI-TPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQkl 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  353 --DIYFASGVsgkaiKSY--TGLSFVfhnhIVK---INEAVPAYMDIGMYEE---NESIPYSHSWNL---------IYAL 413
Cdd:pfam00266 191 gvDFLAFSGH-----KLYgpTGIGVL----YGRrdlLEKMPPLLGGGGMIETvslQESTFADAPWKFeagtpniagIIGL 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446445211  414 QEALKRFED---ETAFVKIKEIYDYMEEAITTI-GLNLVSPKEHAAPIILTIQLSEGQSSKTIGDE 475
Cdd:pfam00266 262 GAALEYLSEiglEAIEKHEHELAQYLYERLLSLpGIRLYGPERRASIISFNFKGVHPHDVATLLDE 327
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 84-160 5.05e-03

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  84 LQEHGENVYEIRLLSVEREYRN---GRALLgliRFLHRYLLLNGY---ELALISATTRELPLYEQMGFKAFHMLVGTEEA 157
Cdd:COG0454   51 LRRLDDKVLELKRLYVLPEYRGkgiGKALL---EALLEWARERGCtalELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127


                 ...
gi 446445211 158 AFQ 160
Cdd:COG0454  128 EFE 130
 
Name Accession Description Interval E-value
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 182-519 9.45e-57

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: 193.77  E-value: 9.45e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 182 YTFLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVKKRLLQMTKAK-RVQIMLGTGTLANDAIalqLRSLKGKG---I 257
Cdd:COG0075    2 LLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEnDVVILTGSGTGAMEAA---LANLVSPGdkvL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 258 VLTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMESG-NYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKL 336
Cdd:COG0075   79 VLVNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 337 CVDCISSIGAVPIDLKD--IYFASGVSGKAIKSYTGLSFVFHNH----IVKINEAVPAYMDIGM---YEENESIPYSHSW 407
Cdd:COG0075  159 IVDAVSSLGGVPLDMDEwgIDVVVSGSQKCLMLPPGLAFVAVSEraleAIEARKLPSYYLDLKLwlkYWEKGQTPYTPPV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 408 NLIYALQEALKRFEDET---AFVKIKEIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSEGQSSKTIGDELALQ-GYIV 483
Cdd:COG0075  239 SLLYALREALDLILEEGlenRFARHRRLAEALRAGLEALGLELFAEEEYRSPTVTAVRVPEGVDAAALRKRLKERyGIEI 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 446445211 484 -----HYesaylqKNNWIQIACLNHYKERDMKRMLNWLQMC 519
Cdd:COG0075  319 agglgPL------KGKIFRIGHMGYVNPEDVLRTLAALEEA 353
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 184-472 2.46e-41

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: 152.06  E-value: 2.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 184 FLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVKKRLLQM--TKAKRVQIMLGTGTLANDAIALQLRSLKGKGIVLTN 261
Cdd:cd06451    3 LIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVfqTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVGVN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 262 GEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMESGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLCVDCI 341
Cdd:cd06451   83 GVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 342 SSIGAVPIDLK----DIYFaSGvSGKAIKSYTGLSFV-----FHNHIVKINEAVPAYMDIGMY----EENESIPYSHSWN 408
Cdd:cd06451  163 SSLGGEPFRMDewgvDVAY-TG-SQKALGAPPGLGPIafserALERIKKKTKPKGFYFDLLLLlkywGEGYSYPHTPPVN 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446445211 409 LIYALQEALKRFEDETAFVKIK---EIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSEGQSSKTI 472
Cdd:cd06451  241 LLYALREALDLILEEGLENRWArhrRLAKALREGLEALGLKLLAKPELRSPTVTAVLVPEGVDGDEV 307
PhnW-AepZ TIGR03301
2-aminoethylphosphonate aminotransferase; This family includes a number of ...
 182-513 4.63e-33

2-aminoethylphosphonate aminotransferase; This family includes a number of 2-aminoethylphosphonate aminotransferases, some of which are indicated to operate in the catabolism of 2-aminoethylphosphonate (AEP) and others which are involved in the biosynthesis of the same compound. The catabolic enzyme (PhnW) is known to use pyruvate:alanine as the transfer partner and is modeled by the equivalog-level model (TIGR02326). The PhnW family is apparently a branch of a larger tree including genes (AepZ) adjacent to others responsible for the biosynthesis of phosphonoacetaldehyde. The identity of the transfer partner is unknown for these enzymes and considering the reversed flux compared to PhnW, it may very well be different.


Pssm-ID: 274512 [Multi-domain]  Cd Length: 355  Bit Score: 129.03  E-value: 4.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  182 YTFLPGPVDIEENVRKAFsTKPISHRSKSFQVTMDNVKKRLLQMTKA--KRVQIML-GTGTLANDAIALQLRSLKGKGIV 258
Cdd:TIGR03301   1 ILLTPGPLSTSATVRDAM-LVDWCHWDSEFNDVTDQVRDRLLALAGGddNHTCVLLqGSGTFAVEATIGSLVPRDGKLLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  259 LTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVM-ESGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLC 337
Cdd:TIGR03301  80 LINGAYGERLAKICEYLGIPHTDLNFSEYEPPDLNRIEEALaADPDITHVATVHHETTTGILNPLEAIAKVARSHGAVLI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  338 VDCISSIGAVPIDLK--DIYFASGVSGKAIKSYTGLSFVFHNHIVKINEAVPA---YMDI----GMYEENESIPYSHSWN 408
Cdd:TIGR03301 160 VDAMSSFGAIPIDIEelDVDALIASANKCLEGVPGFGFVIARRDLLEASAGNArslYLDLydqwAYMEKTGKWRFTPPTH 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  409 LIYALQEALKRFEDETA----FVKIKEIYDYMEEAITTIGLNLVSPKEHAAPIILTIQLSE--GQSSKTIGDELALQGYI 482
Cdd:TIGR03301 240 TVYAFAQALEELEAEGGvparIARYRRNRELLVDGLRALGFQPLLPERWQSPIIVSFLYPDdpDFDFDDFYQELKERGFV 319

                         330       340       350
                  ....*....|....*....|....*....|.
gi 446445211  483 VHyeSAYLQKNNWIQIACLNHYKERDMKRML 513
Cdd:TIGR03301 320 IY--PGKLTLADTFRIGTIGEIDAADIERLL 348
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 184-423 2.96e-20

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 92.90  E-value: 2.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 184 FLPGPVDIEENVRKAFSTKPISHRSKSFQVTMDNVK---KRLLQmTKAKRVQIMLGTGTLANDAIALQLRSLKGKGIVLT 260
Cdd:PLN02409  13 FVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLedvKYIFK-TKSGTPFIFPTTGTGAWESALTNTLSPGDKVVSFR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 261 NGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTEL-EKVMESGNYE--WLWFVHHETSTGMLNDLKELNVLTKKYQIK-- 335
Cdd:PLN02409  92 IGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILkSKLRQDTNHKikAVCVVHNETSTGVTNDLAGVRKLLDCAQHPal 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 336 LCVDCISSIGAVPIDLKDIYFASGVSG--KAIKSYTGLSFVFHN----HIVKINEAVPAYMDIG----MYEENESIPYSH 405
Cdd:PLN02409 172 LLVDGVSSIGALDFRMDEWGVDVALTGsqKALSLPTGLGIVCASpkalEASKTAKSPRVFFDWAdylkFYKLGTYWPYTP 251

                        250
                 ....*....|....*...
gi 446445211 406 SWNLIYALQEALKRFEDE 423
Cdd:PLN02409 252 SIQLLYGLRAALDLIFEE 269
Acetyltransf_5 pfam13444
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 20-112 5.73e-17

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions.


Pssm-ID: 463880  Cd Length: 102  Bit Score: 76.49  E-value: 5.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   20 LNYKTFVEEIPQHEET-KDRVRIDRFHEENTYLICLDDD--KLVGMVALRGKRPFSL---DYKISNLD-FYLQEHGENVY 92
Cdd:pfam13444   1 LRYRVFREEMGATGPAaLPGLDIDRFDAYCDHLLVWDDDtgEVVGTYRLLPPDAASGlggFYSATEFDlSALLALRGRLL 80

                          90       100
                  ....*....|....*....|
gi 446445211   93 EIRLLSVEREYRNGRALLGL 112
Cdd:pfam13444  81 ELGRSCVHPEYRNGRVLLLL 100
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 234-375 8.60e-15

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 76.11  E-value: 8.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 234 MLGTGTLANDAIALQLRSLKGKGIVLTNGEFGNRLVGHATRAQLHFDTYKKEMGEPFLYTELEKVMES-GNYEWLWFVHH 312
Cdd:PRK13479  61 LQGSGTFSVEAAIGSLVPRDGKVLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAAdPRITHVALVHC 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446445211 313 ETSTGMLNDLKELNVLTKKYQIKLCVDCISSIGAVPIDLKDIYFASGVS--GKAIKSYTGLSFVF 375
Cdd:PRK13479 141 ETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAELGIDALISsaNKCIEGVPGFGFVI 205
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
13-147 8.19e-11

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 60.10  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  13 EFESIHKLNYKTFveeiPQHEETKDRVRIDRFHEENTYLICLDDDKLVGMVALRgkrPFSLDykisnldfylqeHGENVY 92
Cdd:COG3153    8 DAEAIAALLRAAF----GPGREAELVDRLREDPAAGLSLVAEDDGEIVGHVALS---PVDID------------GEGPAL 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446445211  93 EIRLLSVEREYRN---GRALlglIRFLHRYLLLNGYELALISATTRELPLYEQMGFKA 147
Cdd:COG3153   69 LLGPLAVDPEYRGqgiGRAL---MRAALEAARERGARAVVLLGDPSLLPFYERFGFRP 123
LasI COG3916
N-acyl-homoserine lactone synthase LasI (autoinducer biosynthesis) [Signal transduction ...
 13-147 9.30e-10

N-acyl-homoserine lactone synthase LasI (autoinducer biosynthesis) [Signal transduction mechanisms];


Pssm-ID: 443121 [Multi-domain]  Cd Length: 201  Bit Score: 58.41  E-value: 9.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  13 EFESIHKLNYKTFVEEIPQHEETKDRVRIDRFHEENT-YLICLD-DDKLVGMV-ALRGKRPFSLDYKISNL-DFYLQEHG 88
Cdd:COG3916   15 LLDEMFRLRHRVFVEELGWEVPVPDGLEIDQYDDPSAhYLLAHDeDGRVVGCVrLLPTTGPYMLEDVFPDLlDGGPAPRR 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446445211  89 ENVYEIRLLSVEREYR--------NGRALLGLIRFLHRYLLLNGYELALISATTRELPLYEQMGFKA 147
Cdd:COG3916   95 PDIWEISRFAVDKDFRrrlgerarRPRVALALFLAMVEYALENGITHLVAVMEPRLERLLRRLGWPF 161
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 204-475 8.38e-07

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: 51.09  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  204 ISHRSKSFQVTMDNVKKRLLQMTKAKRVQIMLGT--GTLANDAIALQL-RSLKGKG-IVLTNGEF-GNRL----VGHATR 274
Cdd:pfam00266  34 VHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTsgTTEAINLVALSLgRSLKPGDeIVITEMEHhANLVpwqeLAKRTG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  275 AQLHFdTYKKEMGEPFLyTELEKVMeSGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLCVDCISSIGAVPIDLK-- 352
Cdd:pfam00266 114 ARVRV-LPLDEDGLLDL-DELEKLI-TPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGHRPIDVQkl 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  353 --DIYFASGVsgkaiKSY--TGLSFVfhnhIVK---INEAVPAYMDIGMYEE---NESIPYSHSWNL---------IYAL 413
Cdd:pfam00266 191 gvDFLAFSGH-----KLYgpTGIGVL----YGRrdlLEKMPPLLGGGGMIETvslQESTFADAPWKFeagtpniagIIGL 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446445211  414 QEALKRFED---ETAFVKIKEIYDYMEEAITTI-GLNLVSPKEHAAPIILTIQLSEGQSSKTIGDE 475
Cdd:pfam00266 262 GAALEYLSEiglEAIEKHEHELAQYLYERLLSLpGIRLYGPERRASIISFNFKGVHPHDVATLLDE 327
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 45-146 5.40e-06

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 45.75  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  45 HEENTYLICLDDDKLVGMVALRgkrpfsldykisnldfylqEHGENVYEIRLLSVEREYRN---GRALLgliRFLHRYLL 121
Cdd:COG1246   25 EEIGEFWVAEEDGEIVGCAALH-------------------PLDEDLAELRSLAVHPDYRGrgiGRRLL---EALLAEAR 82

                         90       100
                 ....*....|....*....|....*
gi 446445211 122 LNGYELALISATTRELPLYEQMGFK 146
Cdd:COG1246   83 ELGLKRLFLLTTSAAIHFYEKLGFE 107
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 215-377 6.12e-06

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: 46.61  E-value: 6.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 215 MDNVKKRLLQMTKAKRVQIML-GTGTLANDAIALQLRSlKGKGIVLTNGEFGNRLVGHATRAQLHF-DTYKKEMGEPFLY 292
Cdd:cd01494    2 LEELEEKLARLLQPGNDKAVFvPSGTGANEAALLALLG-PGDEVIVDANGHGSRYWVAAELAGAKPvPVPVDDAGYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211 293 T-ELEKVMESGNYEWLWFVHHETSTGMLNDLKELNVLTKKYQIKLCVDCISSIGAVPIDLKDIYF--ASGVSGKAIKSYT 369
Cdd:cd01494   81 VaILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEggADVVTFSLHKNLG 160

                        170
                 ....*....|
gi 446445211 370 G--LSFVFHN 377
Cdd:cd01494  161 GegGGVVIVK 170
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 46-146 1.85e-05

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 43.21  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   46 EENTYLICLDDDKLVGMVALRgkrpfsldykisnldfylQEHGENVYEIRLLSVEREYRN---GRALLgliRFLHRYLLL 122
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALL------------------PLDDEGALAELRLAVHPEYRGqgiGRALL---EAAEAAAKE 59

                          90       100
                  ....*....|....*....|....
gi 446445211  123 NGYELALISATTRELPLYEQMGFK 146
Cdd:pfam13508  60 GGIKLLELETTNRAAAFYEKLGFE 83
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
12-148 5.69e-05

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 42.86  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  12 WEFESIHKLNYKTFVEE--IPQHEEtkdrvrIDRFHEENTYLICLDDDKLVGMVALRgkrpfsldykisnldfylqEHGE 89
Cdd:COG2153    2 EELYDALALRREVFVVEqgVPPYLE------LDGKDEDARHLLAYDDGELVATARLL-------------------PPGD 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446445211  90 NVYEIRLLSVEREYRN---GRALLgliRFLHRYLLLNGYELALISATTRELPLYEQMGFKAF 148
Cdd:COG2153   57 GEAKIGRVAVLPEYRGqglGRALM---EAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPV 115
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 14-145 1.95e-04

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 40.96  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   14 FESIHKLNYKTFVEEIPQHEEtkdRVRIDRFHEEN-TYLICLDDDKLVGMVAlrgkrpfsldykisnldFYLQEHGENVY 92
Cdd:pfam00583   1 LEALYELLSEEFPEPWPDEPL---DLLEDWDEDASeGFFVAEEDGELVGFAS-----------------LSIIDDEPPVG 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446445211   93 EIRLLSVEREYRN---GRALLgliRFLHRYLLLNGYE---LALISATTRELPLYEQMGF 145
Cdd:pfam00583  61 EIEGLAVAPEYRGkgiGTALL---QALLEWARERGCErifLEVAADNLAAIALYEKLGF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 23-162 5.76e-04

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 39.95  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211   23 KTFVEEIPQHEETKdrvRIDrfHEENTYLICLDDDKLVGMVALRGKRpfsldykisnldfylqeHgenvyeIRLLSVERE 102
Cdd:pfam13673  11 ETFYEFISPEALRE---RID--QGEYFFFVAFEGGQIVGVIALRDRG-----------------H------ISLLFVDPD 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446445211  103 YRN---GRALLGLIRflhRYLLLNGYELALIS--ATTRELPLYEQMGFKAfhmlVGTEEAA----FQPM 162
Cdd:pfam13673  63 YQGqgiGKALLEAVE---DYAEKDGIKLSELTvnASPYAVPFYEKLGFRA----TGPEQEFngirFVPM 124
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
24-160 3.63e-03

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 38.44  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  24 TFVEEIPQHEETKDRVRiDRFHEENTYLICLDDDKLVGMVALRGKRPFSLDYKISNLDFYlqehgenvyeirllsVEREY 103
Cdd:COG1247   29 TFETEPPSEEEREAWFA-AILAPGRPVLVAEEDGEVVGFASLGPFRPRPAYRGTAEESIY---------------VDPDA 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446445211 104 RN---GRALLgliRFLHRYLLLNGYElALISATTRE----LPLYEQMGFKafhmLVGTEEAAFQ 160
Cdd:COG1247   93 RGrgiGRALL---EALIERARARGYR-RLVAVVLADneasIALYEKLGFE----EVGTLPEVGF 148
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 84-160 5.05e-03

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 37.34  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446445211  84 LQEHGENVYEIRLLSVEREYRN---GRALLgliRFLHRYLLLNGY---ELALISATTRELPLYEQMGFKAFHMLVGTEEA 157
Cdd:COG0454   51 LRRLDDKVLELKRLYVLPEYRGkgiGKALL---EALLEWARERGCtalELDTLDGNPAAIRFYERLGFKEIERYVAYVGG 127


                 ...
gi 446445211 158 AFQ 160
Cdd:COG0454  128 EFE 130
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH