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Conserved domains on  [gi|446735576|ref|WP_000812832|]
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MULTISPECIES: aminotransferase class V-fold PLP-dependent enzyme [Staphylococcus]

Protein Classification

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 1001916)

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme similar to Staphylococcus aureus orn/lys/arg decarboxylase family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LdcC super family cl34388
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-445 1.20e-101

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


The actual alignment was detected with superfamily member COG1982:

Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 311.66  E-value: 1.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   1 MKQPILNKLESLNQEEAISLHVPGHKNmTIGHLSQLS-------MTMDKTEIPGLDDLHHPEEVILESMKQVEK--HSDY 71
Cdd:COG1982    5 LLTPLFDALKKYAERGPVSFHVPGHKG-GRGFGREFYdffgenvFRLDLTELPGLDDLHDPEGVIKEAQELAAEafGADR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  72 dAYFLVNGTTSGILSVIQSfSQKKGD-ILMARNVHKSVLHALDISQQEGHFIETHQSPLTN-----HYNKVNLSRLNNDG 145
Cdd:COG1982   84 -TFFLVNGTSSGNKAMILA-VCGPGDkVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGiiggiTPEAVEEALIEHPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 146 HKLAVLTYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGL-QGFPDSTLNYQADYVVQSFHKTLPALTMGSVLYIH 224
Cdd:COG1982  162 AKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFhPDLPRSAMEAGADLVVQSTHKTLGALTQSSMLHVK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 225 KNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEFYKTY---------DSTVFFDKRAQLI--------ECLEKKGFEML 287
Cdd:COG1982  242 GGRVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGEgeelldealELAIEARKEINKIpglyvfgpEDLGAPGVYDL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 288 qvdDPLKLLI--KYEGFTGHDIQNWFM-NAHIYLELADDYQALAILPLWHHDDTylFDSL---LRKIEDMILPKKSVSKV 361
Cdd:COG1982  322 ---DPTKLTIdvPGLGISGYEVAEYLReEYGIQVELADLYNILFLLSLGDTKED--IERLvaaLKELKRLYDKNAPLEEV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 362 KQTQLLTT--------EGNYKPKRfeyvtWCDLKKAKGKVLARHIVPYPPGIPIIFKGETITENMIELVNEYLETGMIVE 433
Cdd:COG1982  397 LPLAFPPLpelvmsprEAFFAETE-----LVPLEEAVGRIAAEMVIPYPPGIPLLMPGERITEEVIDYLRALEEAGGRFP 471
                        490
                 ....*....|....*
gi 446735576 434 GIKN---NKILVEDE 445
Cdd:COG1982  472 GFEDpelRTIRVVKE 486
 
Name Accession Description Interval E-value
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-445 1.20e-101

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 311.66  E-value: 1.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   1 MKQPILNKLESLNQEEAISLHVPGHKNmTIGHLSQLS-------MTMDKTEIPGLDDLHHPEEVILESMKQVEK--HSDY 71
Cdd:COG1982    5 LLTPLFDALKKYAERGPVSFHVPGHKG-GRGFGREFYdffgenvFRLDLTELPGLDDLHDPEGVIKEAQELAAEafGADR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  72 dAYFLVNGTTSGILSVIQSfSQKKGD-ILMARNVHKSVLHALDISQQEGHFIETHQSPLTN-----HYNKVNLSRLNNDG 145
Cdd:COG1982   84 -TFFLVNGTSSGNKAMILA-VCGPGDkVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGiiggiTPEAVEEALIEHPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 146 HKLAVLTYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGL-QGFPDSTLNYQADYVVQSFHKTLPALTMGSVLYIH 224
Cdd:COG1982  162 AKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFhPDLPRSAMEAGADLVVQSTHKTLGALTQSSMLHVK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 225 KNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEFYKTY---------DSTVFFDKRAQLI--------ECLEKKGFEML 287
Cdd:COG1982  242 GGRVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGEgeelldealELAIEARKEINKIpglyvfgpEDLGAPGVYDL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 288 qvdDPLKLLI--KYEGFTGHDIQNWFM-NAHIYLELADDYQALAILPLWHHDDTylFDSL---LRKIEDMILPKKSVSKV 361
Cdd:COG1982  322 ---DPTKLTIdvPGLGISGYEVAEYLReEYGIQVELADLYNILFLLSLGDTKED--IERLvaaLKELKRLYDKNAPLEEV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 362 KQTQLLTT--------EGNYKPKRfeyvtWCDLKKAKGKVLARHIVPYPPGIPIIFKGETITENMIELVNEYLETGMIVE 433
Cdd:COG1982  397 LPLAFPPLpelvmsprEAFFAETE-----LVPLEEAVGRIAAEMVIPYPPGIPLLMPGERITEEVIDYLRALEEAGGRFP 471
                        490
                 ....*....|....*
gi 446735576 434 GIKN---NKILVEDE 445
Cdd:COG1982  472 GFEDpelRTIRVVKE 486
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
4-264 8.47e-84

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 259.10  E-value: 8.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   4 PILNKLESLNQEEAISLHVPGHKNMTIGH------LSQLSMTMDKTEIPGLDDLHHPEEVILESMKQVEKH-SDYDAYFL 76
Cdd:cd00615    1 PLFEALKEYAKRGIISFHVPGHKGGRGFRksfyefYGENLFKADVTELTGLDDLLDPTGPIKEAQELAARAfGAKHTFFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  77 VNGTTSGILSVIQSFSQKKGDILMARNVHKSVLHALDISQQEGHFIETHQSPLTNHYNKVNLSR-----LNNDGHKLAVL 151
Cdd:cd00615   81 VNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGIPPETfkkalIEHPDAKAAVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 152 TYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGLQG-FPDSTLNYQADYVVQSFHKTLPALTMGSVLYIHKNAPYR 230
Cdd:cd00615  161 TNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPiLPSSAAMAGADIVVQSTHKTLPALTQGSMIHVKGDLVNP 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 446735576 231 ETIIEYLSYFQTSSPSYLIMASLESAAEFYKTYD 264
Cdd:cd00615  241 DRVNEALNLHQSTSPSYLILASLDVARAMMALEG 274
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
18-332 3.90e-48

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 169.99  E-value: 3.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   18 ISLHVPGHKNMTI-----------GHLSQLSMTMD-KTEIPGLDDLHHPEEVILESMKQVEK--HSDyDAYFLVNGTTSG 83
Cdd:pfam01276  16 YTFHCPGHQGGAGfqkhpagrffyDFFGENLLRIDvCIEDVELGDLLDHEGAIKEAQKYAARvfGAD-KSYFVVNGTSGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   84 ILSVIQSFSQKKGDILMARNVHKSVLHALDISQQEGHFIETHQSPL-------TNHYNKVNLSRL-----NNDGHKLAVL 151
Cdd:pfam01276  95 NKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPSRNAYgiiggipLHEFQEETLKEAiaevpDAKGPRLAVI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  152 TYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGLQGFPDSTLNYQAD-------YVVQSFHKTLPALTMGSvlYIH 224
Cdd:pfam01276 175 TNPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFIPIYADASPMGGEnengpgiFVTQSVHKLLAALSQAS--YIH 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  225 KNAPY---RETIIEYLSYFQTSSPSYLIMASLESAA--------------------------------EFYKTYDSTVFF 269
Cdd:pfam01276 253 KKEGHivnHDRFNEAFMMHATTSPSYPIFASLDVAAkmlegnsgrrlwnecveraiefrkaidtlnncEFFRPWNPEIVD 332
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446735576  270 DKRAQLIECLEK-KGFEMLQVD----DPLKLLI-----------KYEGFTGHDIQNWFMNAHIYLELADDYQALAILPL 332
Cdd:pfam01276 333 GKECWPFHPGETwHGFEGYADNqyflDPCKLTIltpgmdedgeySEFGVPATIVAKWLRENGIVPEKTDLNNILFLFTP 411
PRK15399 PRK15399
lysine decarboxylase;
73-416 9.50e-06

lysine decarboxylase;


Pssm-ID: 185297 [Multi-domain]  Cd Length: 713  Bit Score: 48.20  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  73 AYFLVNGTTSGIlSVIQSFSQKKGD-ILMARNVHKSVLHALDISQqeghFIETHQSPLTNHYN------KVNLSRlNNDG 145
Cdd:PRK15399 213 SYIVTNGTSTSN-KIVGMYAAPAGStLLIDRNCHKSLAHLLMMSD----VVPIWLKPTRNALGilggipRREFTR-DSIE 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 146 HKL-----------AVLTYPNYYGETFNVEEV-----IKSLHQLNIPVLIDEAHGAHFGLQGFPDSTLNYQADYVVQSFH 209
Cdd:PRK15399 287 EKVaattqaqwpvhAVITNSTYDGLLYNTDWIkqtldVPSIHFDSAWVPYTHFHPIYQGKSGMSGERVPGKVIFETQSTH 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 210 KTLPALTMGSVLYIhKNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEF------YKTYDSTV---------------- 267
Cdd:PRK15399 367 KMLAAFSQASLIHI-KGEYDEETFNEAFMMHTSTSPSYPIVASVETAAAMlrgnpgKRLINRSVeralhfrkevqrlree 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 268 ----FFD----KRAQLIECLEKK------GFEMLQVD----DPLKLLIKYEGFTGH-DIQNW---------FMNAH-IYL 318
Cdd:PRK15399 446 sdgwFFDiwqpENVDEAECWPVApgeqwhGFKDADADhmflDPVKVTILTPGMDEQgNMSEEgipaalvakFLDERgIVV 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 319 ELADDYQAL---------------------------------AILP-LWHHDDTYLFD----SLLRKIEDMI-------- 352
Cdd:PRK15399 526 EKTGPYNLLflfsigidktkamgllrgltefkraydlnlrvkNMLPdLYAEDPDFYRNmriqDLAQGIHKLIrkhdlpgl 605
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446735576 353 -------LPKKSVSKVKQTQLLTtEGNykpkrfeyVTWCDLKKAKGKVLARHIVPYPPGIPIIFKGETITE 416
Cdd:PRK15399 606 mlrafdvLPEMIMTPHQAWQRQI-KGE--------VETVALEQLVGRVSANMILPYPPGVPLLMPGEMITE 667
 
Name Accession Description Interval E-value
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
1-445 1.20e-101

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 311.66  E-value: 1.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   1 MKQPILNKLESLNQEEAISLHVPGHKNmTIGHLSQLS-------MTMDKTEIPGLDDLHHPEEVILESMKQVEK--HSDY 71
Cdd:COG1982    5 LLTPLFDALKKYAERGPVSFHVPGHKG-GRGFGREFYdffgenvFRLDLTELPGLDDLHDPEGVIKEAQELAAEafGADR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  72 dAYFLVNGTTSGILSVIQSfSQKKGD-ILMARNVHKSVLHALDISQQEGHFIETHQSPLTN-----HYNKVNLSRLNNDG 145
Cdd:COG1982   84 -TFFLVNGTSSGNKAMILA-VCGPGDkVLVPRNCHKSVIHGLILSGAIPVYLNPEIDNELGiiggiTPEAVEEALIEHPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 146 HKLAVLTYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGL-QGFPDSTLNYQADYVVQSFHKTLPALTMGSVLYIH 224
Cdd:COG1982  162 AKAVLITNPTYYGVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFhPDLPRSAMEAGADLVVQSTHKTLGALTQSSMLHVK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 225 KNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEFYKTY---------DSTVFFDKRAQLI--------ECLEKKGFEML 287
Cdd:COG1982  242 GGRVDHERVNEALMLLQSTSPSYLLMASLDVARRQMAGEgeelldealELAIEARKEINKIpglyvfgpEDLGAPGVYDL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 288 qvdDPLKLLI--KYEGFTGHDIQNWFM-NAHIYLELADDYQALAILPLWHHDDTylFDSL---LRKIEDMILPKKSVSKV 361
Cdd:COG1982  322 ---DPTKLTIdvPGLGISGYEVAEYLReEYGIQVELADLYNILFLLSLGDTKED--IERLvaaLKELKRLYDKNAPLEEV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 362 KQTQLLTT--------EGNYKPKRfeyvtWCDLKKAKGKVLARHIVPYPPGIPIIFKGETITENMIELVNEYLETGMIVE 433
Cdd:COG1982  397 LPLAFPPLpelvmsprEAFFAETE-----LVPLEEAVGRIAAEMVIPYPPGIPLLMPGERITEEVIDYLRALEEAGGRFP 471
                        490
                 ....*....|....*
gi 446735576 434 GIKN---NKILVEDE 445
Cdd:COG1982  472 GFEDpelRTIRVVKE 486
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
4-264 8.47e-84

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 259.10  E-value: 8.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   4 PILNKLESLNQEEAISLHVPGHKNMTIGH------LSQLSMTMDKTEIPGLDDLHHPEEVILESMKQVEKH-SDYDAYFL 76
Cdd:cd00615    1 PLFEALKEYAKRGIISFHVPGHKGGRGFRksfyefYGENLFKADVTELTGLDDLLDPTGPIKEAQELAARAfGAKHTFFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  77 VNGTTSGILSVIQSFSQKKGDILMARNVHKSVLHALDISQQEGHFIETHQSPLTNHYNKVNLSR-----LNNDGHKLAVL 151
Cdd:cd00615   81 VNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYGIAGGIPPETfkkalIEHPDAKAAVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 152 TYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGLQG-FPDSTLNYQADYVVQSFHKTLPALTMGSVLYIHKNAPYR 230
Cdd:cd00615  161 TNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPiLPSSAAMAGADIVVQSTHKTLPALTQGSMIHVKGDLVNP 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 446735576 231 ETIIEYLSYFQTSSPSYLIMASLESAAEFYKTYD 264
Cdd:cd00615  241 DRVNEALNLHQSTSPSYLILASLDVARAMMALEG 274
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
18-332 3.90e-48

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 169.99  E-value: 3.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   18 ISLHVPGHKNMTI-----------GHLSQLSMTMD-KTEIPGLDDLHHPEEVILESMKQVEK--HSDyDAYFLVNGTTSG 83
Cdd:pfam01276  16 YTFHCPGHQGGAGfqkhpagrffyDFFGENLLRIDvCIEDVELGDLLDHEGAIKEAQKYAARvfGAD-KSYFVVNGTSGS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   84 ILSVIQSFSQKKGDILMARNVHKSVLHALDISQQEGHFIETHQSPL-------TNHYNKVNLSRL-----NNDGHKLAVL 151
Cdd:pfam01276  95 NKTVGMAVCTPGDTILIDRNCHKSIHHALMLSGATPVYLEPSRNAYgiiggipLHEFQEETLKEAiaevpDAKGPRLAVI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  152 TYPNYYGETFNVEEVIKSLHQLNIPVLIDEAHGAHFGLQGFPDSTLNYQAD-------YVVQSFHKTLPALTMGSvlYIH 224
Cdd:pfam01276 175 TNPTYDGVLYNAKEIVDTLHHLSDPILFDSAWVGYEQFIPIYADASPMGGEnengpgiFVTQSVHKLLAALSQAS--YIH 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  225 KNAPY---RETIIEYLSYFQTSSPSYLIMASLESAA--------------------------------EFYKTYDSTVFF 269
Cdd:pfam01276 253 KKEGHivnHDRFNEAFMMHATTSPSYPIFASLDVAAkmlegnsgrrlwnecveraiefrkaidtlnncEFFRPWNPEIVD 332
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446735576  270 DKRAQLIECLEK-KGFEMLQVD----DPLKLLI-----------KYEGFTGHDIQNWFMNAHIYLELADDYQALAILPL 332
Cdd:pfam01276 333 GKECWPFHPGETwHGFEGYADNqyflDPCKLTIltpgmdedgeySEFGVPATIVAKWLRENGIVPEKTDLNNILFLFTP 411
PRK15399 PRK15399
lysine decarboxylase;
73-416 9.50e-06

lysine decarboxylase;


Pssm-ID: 185297 [Multi-domain]  Cd Length: 713  Bit Score: 48.20  E-value: 9.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  73 AYFLVNGTTSGIlSVIQSFSQKKGD-ILMARNVHKSVLHALDISQqeghFIETHQSPLTNHYN------KVNLSRlNNDG 145
Cdd:PRK15399 213 SYIVTNGTSTSN-KIVGMYAAPAGStLLIDRNCHKSLAHLLMMSD----VVPIWLKPTRNALGilggipRREFTR-DSIE 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 146 HKL-----------AVLTYPNYYGETFNVEEV-----IKSLHQLNIPVLIDEAHGAHFGLQGFPDSTLNYQADYVVQSFH 209
Cdd:PRK15399 287 EKVaattqaqwpvhAVITNSTYDGLLYNTDWIkqtldVPSIHFDSAWVPYTHFHPIYQGKSGMSGERVPGKVIFETQSTH 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 210 KTLPALTMGSVLYIhKNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEF------YKTYDSTV---------------- 267
Cdd:PRK15399 367 KMLAAFSQASLIHI-KGEYDEETFNEAFMMHTSTSPSYPIVASVETAAAMlrgnpgKRLINRSVeralhfrkevqrlree 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 268 ----FFD----KRAQLIECLEKK------GFEMLQVD----DPLKLLIKYEGFTGH-DIQNW---------FMNAH-IYL 318
Cdd:PRK15399 446 sdgwFFDiwqpENVDEAECWPVApgeqwhGFKDADADhmflDPVKVTILTPGMDEQgNMSEEgipaalvakFLDERgIVV 525
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 319 ELADDYQAL---------------------------------AILP-LWHHDDTYLFD----SLLRKIEDMI-------- 352
Cdd:PRK15399 526 EKTGPYNLLflfsigidktkamgllrgltefkraydlnlrvkNMLPdLYAEDPDFYRNmriqDLAQGIHKLIrkhdlpgl 605
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446735576 353 -------LPKKSVSKVKQTQLLTtEGNykpkrfeyVTWCDLKKAKGKVLARHIVPYPPGIPIIFKGETITE 416
Cdd:PRK15399 606 mlrafdvLPEMIMTPHQAWQRQI-KGE--------VETVALEQLVGRVSANMILPYPPGVPLLMPGEMITE 667
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
78-287 2.14e-05

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 46.53  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576   78 NGTTSGILSVIQSFSQKKGDILMARNVHKSVLHALDISQQEGHFIETHQSPlTNHYNKVNLSRLNNDGHKLAVLTYP-NY 156
Cdd:pfam00155  70 SGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDSN-DFHLDFDALEAALKEKPKVVLHTSPhNP 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  157 YGETFN---VEEVIKSLHQLNIPVLIDEAHGAH-FGLQGFPDSTLN---YQADYVVQSFHKT--LPALTMGSVLyihkna 227
Cdd:pfam00155 149 TGTVATleeLEKLLDLAKEHNILLLVDEAYAGFvFGSPDAVATRALlaeGPNLLVVGSFSKAfgLAGWRVGYIL------ 222
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446735576  228 pYRETIIEYL------SYFQTSSPSYLImASLESAAEFYKTYDSTV--FFDKRAQLIECLEKKGFEML 287
Cdd:pfam00155 223 -GNAAVISQLrklarpFYSSTHLQAAAA-AALSDPLLVASELEEMRqrIKERRDYLRDGLQAAGLSVL 288
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
76-225 4.19e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 45.52  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  76 LVNGTTSGILSVIQSFSQ-KKGD-ILMARNVHKSVLHA-LDISQQEGhfIETHQSPLTNHYnKVNLSRLN---NDGHKLA 149
Cdd:COG0520   82 FTRGTTEAINLVAYGLGRlKPGDeILITEMEHHSNIVPwQELAERTG--AEVRVIPLDEDG-ELDLEALEallTPRTKLV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 150 VLTY-PNYYGETFNVEEVIKSLHQLNIPVLIDeahGAhfglQGFPDSTLNYQA---DYVVQSFHKTL-PaltMGS-VLYI 223
Cdd:COG0520  159 AVTHvSNVTGTVNPVKEIAALAHAHGALVLVD---GA----QSVPHLPVDVQAlgcDFYAFSGHKLYgP---TGIgVLYG 228

                 ..
gi 446735576 224 HK 225
Cdd:COG0520  229 KR 230
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
54-223 6.42e-05

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: 43.53  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  54 PEEVILESMKQVEKHSDYDAYFlVNGTTSGILSVIQSFSQKKGDILMARNVHKSVLHALDISqqegHFIETHQSPLT-NH 132
Cdd:cd01494    1 KLEELEEKLARLLQPGNDKAVF-VPSGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAEL----AGAKPVPVPVDdAG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 133 YNKVNLS----RLNNDGHKLAVLTYPNY-YGETFNVEEVIKSLHQLNIPVLIDEAHGahFGLQGFP-DSTLNYQADYVVQ 206
Cdd:cd01494   76 YGGLDVAileeLKAKPNVALIVITPNTTsGGVLVPLKEIRKIAKEYGILLLVDAASA--GGASPAPgVLIPEGGADVVTF 153
                        170
                 ....*....|....*..
gi 446735576 207 SFHKTLpALTMGSVLYI 223
Cdd:cd01494  154 SLHKNL-GGEGGGVVIV 169
OKR_DC_1_C pfam03711
Orn/Lys/Arg decarboxylase, C-terminal domain;
379-416 1.23e-04

Orn/Lys/Arg decarboxylase, C-terminal domain;


Pssm-ID: 461020 [Multi-domain]  Cd Length: 132  Bit Score: 41.74  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446735576  379 EYVtwcDLKKAKGKVLARHIVPYPPGIPIIFKGETITE 416
Cdd:pfam03711  64 ELV---PLDELEGRIAAVGVLPYPPGIPLLMPGERFGE 98
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
75-285 3.81e-04

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: 42.33  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  75 FLVNGTTSGILSVIQSFSQKKGDILMAR---NVHKSVLHALDIsqqeghfiETHQSPLTNHYNKVN----LSRLNNDGHK 147
Cdd:cd00609   63 VVTNGAQEALSLLLRALLNPGDEVLVPDptyPGYEAAARLAGA--------EVVPVPLDEEGGFLLdlelLEAAKTPKTK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 148 LAVLTYPNY-YGETFNVEE---VIKSLHQLNIPVLIDEAHGaHFGLQGFPDSTLNYQADY----VVQSFHKT--LPALTM 217
Cdd:cd00609  135 LLYLNNPNNpTGAVLSEEEleeLAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYerviVLRSFSKTfgLPGLRI 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446735576 218 GsvlYIH-KNAPYRETIIEYLSYFQTSSPS---YLIMASLESAAEFYKTYdSTVFFDKRAQLIECLEKKGFE 285
Cdd:cd00609  214 G---YLIaPPEELLERLKKLLPYTTSGPSTlsqAAAAAALDDGEEHLEEL-RERYRRRRDALLEALKELGPL 281
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
147-214 1.41e-03

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 40.84  E-value: 1.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446735576 147 KLAVLTYPNY-YGETFNVEEVIKSLHQLNIPVLIDEAhgahFGLQGFPDSTLNYQADYVVQSFHKTLPA 214
Cdd:cd06452  141 ALALLTHVDGnYGNLHDAKKIAKVCHEYGVPLLLNGA----YTVGRMPVSGKELGADFIVGSGHKSMAA 205
PRK15400 PRK15400
lysine decarboxylase;
73-416 1.66e-03

lysine decarboxylase;


Pssm-ID: 185298 [Multi-domain]  Cd Length: 714  Bit Score: 40.99  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576  73 AYFLVNGTTSGIlSVIQSFSQKKGD-ILMARNVHKSVLHALDISQqeghFIETHQSPLTNHYN------KVNLSRL---- 141
Cdd:PRK15400 213 SYMVTNGTSTAN-KIVGMYSAPAGStVLIDRNCHKSLTHLMMMSD----VTPIYFRPTRNAYGilggipQSEFQHAtiak 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 142 ------NNDGHKLAVLTYPNYYGETFNVEEV-----IKSLHQLNIPVLIDEAHGAHFGLQGFPDSTLNYQADYVVQSFHK 210
Cdd:PRK15400 288 rvketpNATWPVHAVITNSTYDGLLYNTDFIkktldVKSIHFDSAWVPYTNFSPIYEGKCGMSGGRVEGKVIYETQSTHK 367
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 211 TLPALTMGSVLYIhKNAPYRETIIEYLSYFQTSSPSYLIMASLESAAEFYK----------TYDSTVFFDKRAQLIEClE 280
Cdd:PRK15400 368 LLAAFSQASMIHV-KGDVNEETFNEAYMMHTTTSPHYGIVASTETAAAMMKgnagkrlingSIERAIKFRKEIKRLRT-E 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 281 KKG--FEMLQVDD-------PLKLLIKYEGFTGHDiqnwfmNAHIYLelaDDYQALAILPLWHHDDTYLFD----SLLRK 347
Cdd:PRK15400 446 SDGwfFDVWQPDHidttecwPLRSDSTWHGFKNID------NEHMYL---DPIKVTLLTPGMKKDGTMSDFgipaSIVAK 516
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446735576 348 I--EDMILPKKS------------VSKVKQTQLLTTEGNYK--------------------PKRFE-------------- 379
Cdd:PRK15400 517 YldEHGIVVEKTgpynllflfsigIDKTKALSLLRALTDFKrafdlnlrvknmlpslyredPEFYEnmriqelaqnihkl 596
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446735576 380 ------------------------YVTW----------CDLKKAKGKVLARHIVPYPPGIPIIFKGETITE 416
Cdd:PRK15400 597 ivhhnlpdlmyrafevlptmvmtpYAAFqkelhgmteeVYLDEMVGRVNANMILPYPPGVPLVMPGEMITE 667
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
147-214 6.47e-03

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 38.76  E-value: 6.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446735576 147 KLAVLTYPNY-YGETFNVEEVIKSLHQLNIPVLIDEAHGAhfGLQGFPDSTLNyqADYVVQSFHKTLPA 214
Cdd:PRK09331 160 ALALLTHVDGnYGNLADAKKVAKVAHEYGIPFLLNGAYTV--GRMPVDGKKLG--ADFIVGSGHKSMAA 224
 
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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