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Conserved domains on  [gi|489010483|ref|WP_002921037|]
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MULTISPECIES: UDP-4-amino-4-deoxy-L-arabinose aminotransferase [Klebsiella]

Protein Classification

UDP-4-amino-4-deoxy-L-arabinose aminotransferase( domain architecture ID 10793601)

UDP-4-amino-4-deoxy-L-arabinose aminotransferase catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N), a modified arabinose that is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-379 0e+00

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


:

Pssm-ID: 183263  Cd Length: 379  Bit Score: 852.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   1 MSDFLPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  81 QTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 161 THYKGRHVGWQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAPQAEVITPGFKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 241 INAALALVQLEKLSHANQRRTEIAQRYLRELADTPFKPLSVPTWDHQHAWHLFIIRVDEAACGISRDALMEKLKAMGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489010483 321 GLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQLSGR 379
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
 
Name Accession Description Interval E-value
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-379 0e+00

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 852.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   1 MSDFLPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  81 QTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 161 THYKGRHVGWQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAPQAEVITPGFKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 241 INAALALVQLEKLSHANQRRTEIAQRYLRELADTPFKPLSVPTWDHQHAWHLFIIRVDEAACGISRDALMEKLKAMGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489010483 321 GLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQLSGR 379
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-375 3.16e-175

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 491.89  E-value: 3.16e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   4 FLPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTW 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  84 VSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHY 163
Cdd:COG0399   81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 164 KGRHVGWQGT-AIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGlgvdaydrqtHGRAPQAEVITPGFKYNLADIN 242
Cdd:COG0399  161 KGKKVGTFGDaGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHG----------RDRDAKYEHVELGYNYRMDELQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 243 AALALVQLEKLSHANQRRTEIAQRYLRELADTPFkpLSVPT--WDHQHAWHLFIIRVDEaacGISRDALMEKLKAMGIGT 320
Cdd:COG0399  231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPG--LTLPKvpPGAEHVYHLYVIRLDE---GEDRDELIAALKARGIGT 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489010483 321 GLHF-RAAHTQKYYRER-FPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQ 375
Cdd:COG0399  306 RVHYpIPLHLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-374 4.78e-168

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 473.69  E-value: 4.78e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   10 PSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWVSTLNM 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   90 ICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHYKGRHVG 169
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  170 WQGT-AIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHgrapqaevITPGFKYNLADINAALALV 248
Cdd:pfam01041 161 TLGDaATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWH--------EVLGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  249 QLEKLSHANQRRTEIAQRYLRELADTP-FKPLSVPTWDHQHAWHLFIIRVDEAAcgISRDALMEKLKAMGIGTGLHF-RA 326
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPgFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 489010483  327 AHTQKYYRERFPEVS--LPNTEWNSARICSLPLFPDMTDDDVTRVISALR 374
Cdd:pfam01041 311 LHLQPYYRDLFGYAPgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-374 6.22e-161

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 455.08  E-value: 6.22e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  16 ELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWVSTLNMICLLGA 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  96 TPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHYKGRHVGWQGT-A 174
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDaG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 175 IFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGvdaydrqthGRAPQAEVITPGFKYNLADINAALALVQLEKLS 254
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 255 HANQRRTEIAQRYLRELADTPFkpLSVPTW--DHQHAWHLFIIRVDEAAcGISRDALMEKLKAMGIGTGLHFRAAHTQKY 332
Cdd:cd00616  232 EIIARRREIAERYKELLADLPG--IRLPDVppGVKHSYHLYVIRLDPEA-GESRDELIEALKEAGIETRVHYPPLHHQPP 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 489010483 333 YRER--FPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALR 374
Cdd:cd00616  309 YKKLlgYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 5-376 1.16e-125

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 366.65  E-value: 1.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483    5 LPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWV 84
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   85 STLNMICLLGATPVMIDVDNDNLMITPAAVEAAITS----RTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  161 THYKGRHVG---WQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAP-QAEVITPGFKY 236
Cdd:TIGR03588 161 AEYGGKPVGncrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPwYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  237 NLADINAALALVQLEKLSHANQRRTEIAQRYLRELADTPFKPLSVPTWDHQHAWHLFIIRVDeAACGISRDALMEKLKAM 316
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLD-QEFGCTRKEVFEALRAA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  317 GIGTGLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQL 376
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
 
Name Accession Description Interval E-value
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-379 0e+00

UDP-4-amino-4-deoxy-L-arabinose aminotransferase;


Pssm-ID: 183263  Cd Length: 379  Bit Score: 852.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   1 MSDFLPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  81 QTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 161 THYKGRHVGWQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAPQAEVITPGFKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 241 INAALALVQLEKLSHANQRRTEIAQRYLRELADTPFKPLSVPTWDHQHAWHLFIIRVDEAACGISRDALMEKLKAMGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489010483 321 GLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQLSGR 379
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-375 3.16e-175

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 491.89  E-value: 3.16e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   4 FLPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTW 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  84 VSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHY 163
Cdd:COG0399   81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 164 KGRHVGWQGT-AIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGlgvdaydrqtHGRAPQAEVITPGFKYNLADIN 242
Cdd:COG0399  161 KGKKVGTFGDaGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHG----------RDRDAKYEHVELGYNYRMDELQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 243 AALALVQLEKLSHANQRRTEIAQRYLRELADTPFkpLSVPT--WDHQHAWHLFIIRVDEaacGISRDALMEKLKAMGIGT 320
Cdd:COG0399  231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPG--LTLPKvpPGAEHVYHLYVIRLDE---GEDRDELIAALKARGIGT 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489010483 321 GLHF-RAAHTQKYYRER-FPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQ 375
Cdd:COG0399  306 RVHYpIPLHLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-374 4.78e-168

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 473.69  E-value: 4.78e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   10 PSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWVSTLNM 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   90 ICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHYKGRHVG 169
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  170 WQGT-AIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHgrapqaevITPGFKYNLADINAALALV 248
Cdd:pfam01041 161 TLGDaATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWH--------EVLGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  249 QLEKLSHANQRRTEIAQRYLRELADTP-FKPLSVPTWDHQHAWHLFIIRVDEAAcgISRDALMEKLKAMGIGTGLHF-RA 326
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPgFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 489010483  327 AHTQKYYRERFPEVS--LPNTEWNSARICSLPLFPDMTDDDVTRVISALR 374
Cdd:pfam01041 311 LHLQPYYRDLFGYAPgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-374 6.22e-161

3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The members of this CD are involved in various biosynthetic pathways for secondary metabolites. Some well studied proteins in this CD are AHBA_synthase, protein product of pleiotropic regulatory gene degT, Arnb aminotransferase and pilin glycosylation protein. The prototype of this family, the AHBA_synthase, is a dimeric PLP dependent enzyme. AHBA_syn is the terminal enzyme of 3-amino-5-hydroxybenzoic acid (AHBA) formation which is involved in the biosynthesis of ansamycin antibiotics, including rifamycin B. Some members of this CD are involved in 4-amino-6-deoxy-monosaccharide D-perosamine synthesis. Perosamine is an important element in the glycosylation of several cell products, such as antibiotics and lipopolysaccharides of gram-positive and gram-negative bacteria. The pilin glycosylation protein encoded by gene pglA, is a galactosyltransferase involved in pilin glycosylation. Additionally, this CD consists of ArnB (PmrH) aminotransferase, a 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme. This CD also consists of several predicted pyridoxal phosphate-dependent enzymes apparently involved in regulation of cell wall biogenesis. The catalytic lysine which is present in all characterized PLP dependent enzymes is replaced by histidine in some members of this CD.


Pssm-ID: 99740 [Multi-domain]  Cd Length: 352  Bit Score: 455.08  E-value: 6.22e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  16 ELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWVSTLNMICLLGA 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  96 TPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHYKGRHVGWQGT-A 174
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDaG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 175 IFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGvdaydrqthGRAPQAEVITPGFKYNLADINAALALVQLEKLS 254
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 255 HANQRRTEIAQRYLRELADTPFkpLSVPTW--DHQHAWHLFIIRVDEAAcGISRDALMEKLKAMGIGTGLHFRAAHTQKY 332
Cdd:cd00616  232 EIIARRREIAERYKELLADLPG--IRLPDVppGVKHSYHLYVIRLDPEA-GESRDELIEALKEAGIETRVHYPPLHHQPP 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 489010483 333 YRER--FPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALR 374
Cdd:cd00616  309 YKKLlgYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 5-376 1.16e-125

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are aminotransferases of the pfam01041 family involved in the biosynthesis of pseudaminic acid. They convert UDP-4-keto-6-deoxy-N-acetylglucosamine into UDP-4-amino-4,6-dideoxy-N-acetylgalactose. Pseudaminic acid has a role in surface polysaccharide in Pseudomonas as well as in the modification of flagellin in Campylobacter and Helicobacter species.


Pssm-ID: 274662  Cd Length: 380  Bit Score: 366.65  E-value: 1.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483    5 LPFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGIGPGDEVITPSQTWV 84
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   85 STLNMICLLGATPVMIDVDNDNLMITPAAVEAAITS----RTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  161 THYKGRHVG---WQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAYDRQTHGRAP-QAEVITPGFKY 236
Cdd:TIGR03588 161 AEYGGKPVGncrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPwYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  237 NLADINAALALVQLEKLSHANQRRTEIAQRYLRELADTPFKPLSVPTWDHQHAWHLFIIRVDeAACGISRDALMEKLKAM 316
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLD-QEFGCTRKEVFEALRAA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  317 GIGTGLHFRAAHTQKYYRERFPEVSLPNTEWNSARICSLPLFPDMTDDDVTRVISALRQL 376
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKV 379
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 6-373 8.45e-87

TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional


Pssm-ID: 183283  Cd Length: 375  Bit Score: 267.47  E-value: 8.45e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   6 PFSRPSMGDAELAALREVLASGWIT-TGPKNQALEAAFCQLTGNRHAIAVSSATggmHVTLMA---LGIGPGDEVITPSQ 81
Cdd:PRK11706   3 PFNKPPVVGTELDYIQQAMSSGKLCgDGGFTRRCQQWLEQRFGSAKVLLTPSCT---AALEMAallLDIQPGDEVIMPSY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  82 TWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGT 161
Cdd:PRK11706  80 TFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 162 HYKGRHVGWQGT-AIFSFHAIKNMTCAEGGLIVTDDDELASR--I-------RSLKFHGLgVDAYDRQthgrapqaEVit 231
Cdd:PRK11706 160 TYKGRALGTIGHiGCFSFHETKNYTAGEGGALLINDPALIERaeIirekgtnRSQFFRGQ-VDKYTWV--------DI-- 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 232 pGFKYNLADINAALALVQLEKLSHANQRRTEIAQRY---LRELADTPFKPLSVPTWDHQHAWHLFIIRV-DEAacgiSRD 307
Cdd:PRK11706 229 -GSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYydaLAPLAEAGRIELPSIPDDCKHNAHMFYIKLrDLE----DRS 303

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489010483 308 ALMEKLKAMGIGTGLHFRAAHTQKYYRE--RFPEvSLPNTEWNSARICSLPLFPDMTDDDVTRVISAL 373
Cdd:PRK11706 304 ALINFLKEAGIMAVFHYIPLHSSPAGERfgRFHG-EDRYTTKESERLLRLPLFYNLTDVEQRTVIDTI 370
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 6-379 5.69e-55

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 186.63  E-value: 5.69e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   6 PFSRPSMGDAELAALreVLAS--GWITTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMAL--------GIGPGDE 75
Cdd:PRK15407  36 PPSGKVIDAKELQNL--VDASldFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALtspklgdrALKPGDE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  76 VITPSQTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGERHGISVIEDA 155
Cdd:PRK15407 114 VITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDN 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 156 AHAAGTHYKGRHVG-WQGTAIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGL------GVD-----AYDRQtHGR 223
Cdd:PRK15407 194 CDALGSTYDGRMTGtFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRdcwcapGCDntcgkRFGWQ-LGE 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 224 APQA---EVITPGFKYNL--ADINAALALVQLEKLSHANQRRTEiAQRYLRE-LAD-TPFKPLSVPTWDHQHAWHLFIIR 296
Cdd:PRK15407 273 LPFGydhKYTYSHLGYNLkiTDMQAAIGLAQLEKLPGFIEARKA-NFAYLKEgLASlEDFLILPEATPNSDPSWFGFPIT 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 297 VDEAAcGISRDALMEKLKAMGIGTGLHFRAAHT-QKYYRERFPEV--SLPNTE-------WnsaricsLPLFPDMTDDDV 366
Cdd:PRK15407 352 VKEDA-GFTRVELVKYLEENKIGTRLLFAGNLTrQPYFKGVKYRVvgELTNTDrimndtfW-------IGVYPGLTEEML 423

                        410
                 ....*....|...
gi 489010483 367 TRVISALRQLSGR 379
Cdd:PRK15407 424 DYVIEKIEEFFGL 436
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 34-195 4.33e-22

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: 92.06  E-value: 4.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  34 KNQALEAAFCQLT--GNRHAIAVSSATGGMHVTLMALGiGPGDEVITPSQTWVSTLN-MICLLGATPVMIDVDNDNLMIT 110
Cdd:cd01494    1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSRYWvAAELAGAKPVPVPVDDAGYGGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 111 PAA--VEAAITSRTKAIIPVHYAGAPADIDAIRAVGE---RHGISVIEDAAHAAGTHY-KGRHVGWQGTAIFSFHAIKNM 184
Cdd:cd01494   80 DVAilEELKAKPNVALIVITPNTTSGGVLVPLKEIRKiakEYGILLLVDAASAGGASPaPGVLIPEGGADVVTFSLHKNL 159

                        170
                 ....*....|.
gi 489010483 185 TCAEGGLIVTD 195
Cdd:cd01494  160 GGEGGGVVIVK 170
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 37-154 1.67e-18

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 85.95  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  37 ALEAAFCQLTGNRHAIAVSS-----ATGGMHV---TLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVD-NDNL 107
Cdd:PRK05764  72 ELREAIAAKLKRDNGLDYDPsqvivTTGAKQAlynAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGeENGF 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489010483 108 MITPAAVEAAITSRTKAII---PVHYAGA---PADIDAIRAVGERHGISVIED 154
Cdd:PRK05764 151 KLTVEQLEAAITPKTKALIlnsPSNPTGAvysPEELEAIADVAVEHDIWVLSD 203
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 52-154 8.52e-18

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


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 84.03  E-value: 8.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  52 IAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVD-NDNLMITPAAVEAAITSRTKAII---- 126
Cdd:COG0436   94 LVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDeENGFLPDPEALEAAITPRTKAIVlnsp 172

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489010483 127 --PvhyAGA---PADIDAIRAVGERHGISVIED 154
Cdd:COG0436  173 nnP---TGAvysREELEALAELAREHDLLVISD 202
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 6-318 1.35e-14

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: 74.30  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   6 PFSRPSMGDAELAALREVLASGWITTGPKNQALEAAFCQLTGNRHAIAV--------SSATGGMHVTLMALgIGPGDEVI 77
Cdd:cd00609    9 DFPPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGVDVppeeivvtNGAQEALSLLLRAL-LNPGDEVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  78 TPSQTWVSTLNMICLLGATPVMIDVDNDN-LMITPAAVEAAITSRTKAIIpVHYAGAP-------ADIDAIRAVGERHGI 149
Cdd:cd00609   88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGgFLLDLELLEAAKTPKTKLLY-LNNPNNPtgavlseEELEELAELAKKHGI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 150 SVIEDAAHaAGTHYKGRHVGWQGTAIFSFHAI------KNMtcAEGGL----IVTDDDELASRIRSLKfhglgvdaydrq 219
Cdd:cd00609  167 LIISDEAY-AELVYDGEPPPALALLDAYERVIvlrsfsKTF--GLPGLrigyLIAPPEELLERLKKLL------------ 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 220 thgraPQAEVITPGFkynladINAALALVQLEKLSHANQRRTEIAQRY---LRELADTPFKPLSVPtwdhQHAWHLFiIR 296
Cdd:cd00609  232 -----PYTTSGPSTL------SQAAAAAALDDGEEHLEELRERYRRRRdalLEALKELGPLVVVKP----SGGFFLW-LD 295

                        330       340
                 ....*....|....*....|..
gi 489010483 297 VDEaacGISRDALMEKLKAMGI 318
Cdd:cd00609  296 LPE---GDDEEFLERLLLEAGV 314
PRK07682 PRK07682
aminotransferase;
70-184 3.16e-12

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 67.07  E-value: 3.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  70 IGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDN-LMITPAAVEAAITSRTKAII---PVHYAGA---PADIDAIRA 142
Cdd:PRK07682 102 INPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAvlnKSELEEIAV 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489010483 143 VGERHGISVIEDAAHAAGThYKGRHVgwqgtaifSFHAIKNM 184
Cdd:PRK07682 182 IVEKHDLIVLSDEIYAELT-YDEAYT--------SFASIKGM 214
PRK06107 PRK06107
aspartate transaminase;
36-147 7.60e-11

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 63.22  E-value: 7.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  36 QALEAAFCQLTGNRHAIAVSSATGG----MHVTLMAlGIGPGDEVITPSQTWVSTLNMICLLGATPVMIDV-DNDNLMIT 110
Cdd:PRK06107  77 KAIIAKLERRNGLHYADNEITVGGGakqaIFLALMA-TLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACpEEQGFKLT 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489010483 111 PAAVEAAITSRTKAII---PVHYAGAP---ADIDAIRAVGERH 147
Cdd:PRK06107 156 PEALEAAITPRTRWLIlnaPSNPTGAVysrAELRALADVLLRH 198
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
36-216 5.75e-10

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 59.54  E-value: 5.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   36 QALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVIT--PSQTWVSTLNMICLL-GATPVMIDVDNDNLMiTPA 112
Cdd:pfam01212  35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgePAHIHFDETGGHAELgGVQPRPLDGDEAGNM-DLE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  113 AVEAAITSRTKAIIP----------VHYAG----APADIDAIRAVGERHGISVIED------AAHAAGTHYK--GRHVGw 170
Cdd:pfam01212 113 DLEAAIREVGADIFPptglislentHNSAGgqvvSLENLREIAALAREHGIPVHLDgarfanAAVALGVIVKeiTSYAD- 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 489010483  171 qgtaIFSFHAIKNMTCAEGGLIVTDDDELASRIRSLKFHGLGVDAY 216
Cdd:pfam01212 192 ----SVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLRQA 233
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 31-154 2.08e-09

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 58.57  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  31 TGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICL----LGATPVMIDVDNdn 106
Cdd:PRK05994  61 TNPTNAVLEERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHafksFGWQVRWADADD-- 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489010483 107 lmitPAAVEAAITSRTKAIIPVHYA---GAPADIDAIRAVGERHGISVIED 154
Cdd:PRK05994 138 ----PASFERAITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
53-163 2.62e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 58.19  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  53 AVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMID-VDNDNLMITPAAVEAAITSRTKAII---PV 128
Cdd:PRK06348  94 ATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPN 172

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489010483 129 HYAGA---PADIDAIRAVGERHGISVIEDAAHAAGTHY 163
Cdd:PRK06348 173 NPTGAvfsKETLEEIAKIAIEYDLFIISDEVYDGFSFY 210
PRK07683 PRK07683
aminotransferase A; Validated
 52-191 2.64e-09

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 58.20  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  52 IAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAII---PV 128
Cdd:PRK07683  93 IVTIGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPS 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489010483 129 HYAGAPAD---IDAIRAVGERHGISVIEDAAHAAGThYKGRHVgwqgtAIFSFHAIKNMTCAEGGL 191
Cdd:PRK07683 172 NPTGVTLSkeeLQDIADVLKDKNIFVLSDEIYSELV-YEQPHT-----SIAHFPEMREKTIVINGL 231
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
17-154 3.49e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 58.03  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  17 LAALREVLAsgwittgpknQALEAAFCQLTGNRHaIAVSSatGGMHVTLMALGI--GPGDEVITPSQTWVSTLNMICLLG 94
Cdd:PRK06108  63 IPELREALA----------RYVSRLHGVATPPER-IAVTS--SGVQALMLAAQAlvGPGDEVVAVTPLWPNLVAAPKILG 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489010483  95 ATPVMI--DVDNDNLMITPAAVEAAITSRTKAII------PVHYAGAPADIDAIRAVGERHGISVIED 154
Cdd:PRK06108 130 ARVVCVplDFGGGGWTLDLDRLLAAITPRTRALFinspnnPTGWTASRDDLRAILAHCRRHGLWIVAD 197
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
48-157 1.69e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 55.85  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  48 NRHAIAVSsATGGMHVTLMALGI-GPGDEVITPSQTWVSTLNMICLLGATPVMIDVDnDNLMITPAAVEAAITSRTKAII 126
Cdd:PRK05957  88 NEQAIVVT-AGSNMAFMNAILAItDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRAIV 165

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489010483 127 ---PVHYAGAPADIDAIRAVGE---RHGISVIEDAAH 157
Cdd:PRK05957 166 tisPNNPTGVVYPEALLRAVNQicaEHGIYHISDEAY 202
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
57-168 1.91e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 55.50  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  57 ATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSR---TKAIIpVHYAGA 133
Cdd:PRK07309 100 ATEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEQgdkLKAVI-LNYPAN 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489010483 134 P-------ADIDAIRAVGERHGISVIEDAAHAAGTHYKGRHV 168
Cdd:PRK07309 178 PtgvtysrEQIKALADVLKKYDIFVISDEVYSELTYTGEPHV 219
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
51-160 3.13e-08

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 54.62  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   51 AIAVSSATGGMHVTLMALGIGPGDEVITPSQTWVSTLNMICLLGATPVMIDV-DNDNLMITPAAVEAAITSRTKAII--- 126
Cdd:pfam00155  65 AVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAALKEKPKVVLhts 144

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 489010483  127 PVHYAGA---PADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:pfam00155 145 PHNPTGTvatLEELEKLLDLAKEHNILLLVDEAYAGF 181
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 30-208 6.68e-08

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 53.88  E-value: 6.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  30 TTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMIC-LLGATPVMIDVDNdnlM 108
Cdd:PRK07811  58 TGNPTRTALEEQLAALEGGAYGRAFSSGMAATDCLLRAV-LRPGDHIVIPNDAYGGTFRLIDkVFTRWGVEYTPVD---L 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 109 ITPAAVEAAITSRTKAI---IPVHYAGAPADIDAIRAVGERHGISVIEDAAHA-----------------AGTHYKGRHv 168
Cdd:PRK07811 134 SDLDAVRAAITPRTKLIwveTPTNPLLSITDIAALAELAHDAGAKVVVDNTFAspylqqplalgadvvvhSTTKYIGGH- 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489010483 169 gwqgtaifsfhaiknmTCAEGGLIVTDDDELASRIRSLKF 208
Cdd:PRK07811 213 ----------------SDVVGGALVTNDEELDEAFAFLQN 236
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
50-126 8.34e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 53.66  E-value: 8.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  50 HAIAVSSATGGMHVTLMALgIGPGDEVITPS------QTWVSTLnmicllGATPVMIDVDNDNLMITPAAVEAAITSRTK 123
Cdd:PRK06836  98 HIVMTCGAAGALNVALKAI-LNPGDEVIVFApyfveyRFYVDNH------GGKLVVVPTDTDTFQPDLDALEAAITPKTK 170


                 ...
gi 489010483 124 AII 126
Cdd:PRK06836 171 AVI 173
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 12-204 9.36e-08

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 53.36  E-value: 9.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  12 MGDAELAALREVLASGWI---TTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSqtwvstln 88
Cdd:cd00614   16 PSPAEAADLFALREGGYIysrIGNPTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASD-------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  89 miCLLGATPVMIDVDNDNLMIT--------PAAVEAAITSRTKAIipvhYAGAPA-------DIDAIRAVGERHGISVIE 153
Cdd:cd00614   87 --DLYGGTYRLFERLLPKLGIEvtfvdpddPEALEAAIKPETKLV----YVESPTnptlkvvDIEAIAELAHEHGALLVV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489010483 154 DA------------------AHAAgTHYKGRHvgwqGTAIfsfhaiknmtcaeGGLIVTDDDELASRIR 204
Cdd:cd00614  161 DNtfatpylqrplelgadivVHSA-TKYIGGH----SDVI-------------AGVVVGSGEALIQRLR 211
PRK12414 PRK12414
putative aminotransferase; Provisional
 15-154 9.61e-08

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 53.25  E-value: 9.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  15 AELAALREVLASgwittgpKNQALEAAfcQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLG 94
Cdd:PRK12414  66 AGIAALREALAE-------KTERLYGA--RYDPASEVTVIASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQG 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489010483  95 ATPVMIDVDNDNLMITPAAVEAAITSRTKAII------PVHYAGAPADIDAIRAVGERHGISVIED 154
Cdd:PRK12414 136 ATPVAIKLSPEDFRVNWDEVAAAITPRTRMIIvntphnPSATVFSAADLARLAQLTRNTDIVILSD 201
PRK07550 PRK07550
aminotransferase;
17-154 1.19e-07

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 53.04  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  17 LAALREVLASGW--------------ITTGPkNQALEAAfcqltgnrhaiavssatggmhvtLMALGiGPGDEVITPS-- 80
Cdd:PRK07550  69 LPELREAYAAHYsrlygaaispeqvhITSGC-NQAFWAA-----------------------MVTLA-GAGDEVILPLpw 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  81 ----QTWvstLNMiclLGATPVMIDVDNDN-LMITPAAVEAAITSRTKAII---PVHYAGA---PADIDAIRAVGERHGI 149
Cdd:PRK07550 124 yfnhKMW---LDM---LGIRPVYLPCDEGPgLLPDPAAAEALITPRTRAIAlvtPNNPTGVvypPELLHELYDLARRHGI 197


                 ....*
gi 489010483 150 SVIED 154
Cdd:PRK07550 198 ALILD 202
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 7-217 5.13e-07

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 51.20  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483   7 FSRPSMGDAELAALREvlASGWI---TTGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTW 83
Cdd:COG0626   31 FVFPSAEALAARFAGE--EGGYIysrYGNPTRRALEEALAALEGGEAALAFASGMAAISAVLLAL-LKAGDHVVASDDLY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  84 VSTLNMI--CL--LGATPVMIDVDNdnlmitPAAVEAAITSRTKAIipvhYAGAPA-------DIDAIRAVGERHGISVI 152
Cdd:COG0626  108 GGTRRLLdkVLarFGIEVTFVDPTD------LAAVEAAIRPNTKLV----FLETPSnptlevvDIAAIAAIAHAAGALLV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 153 ED------------------AAHAAgTHYkgrhVGWQGTAIfsfhaiknmtcaeGGLIVTDDDELASRIRSL-KFHGLGV 213
Cdd:COG0626  178 VDntfatpllqrplelgadiVVHSA-TKY----LGGHSDVL-------------GGAVVGRDEELAERLRFLqNALGAVL 239


                 ....
gi 489010483 214 DAYD 217
Cdd:COG0626  240 SPFD 243
PRK08248 PRK08248
homocysteine synthase;
15-154 1.09e-06

homocysteine synthase;


Pssm-ID: 236201 [Multi-domain]  Cd Length: 431  Bit Score: 50.23  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  15 AELAALREvlaSGWITT---GPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGiGPGDEVITPSQTWVSTLNMIC 91
Cdd:PRK08248  46 ANLFSLKE---FGNIYTrimNPTTDVFEKRIAALEGGIGALAVSSGQAAITYSILNIA-SAGDEIVSSSSLYGGTYNLFA 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489010483  92 L----LGATPVMIDVDNdnlmitPAAVEAAITSRTKAIIpVHYAGAPA----DIDAIRAVGERHGISVIED 154
Cdd:PRK08248 122 HtlpkLGITVKFVDPSD------PENFEAAITDKTKALF-AETIGNPKgdvlDIEAVAAIAHEHGIPLIVD 185
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
52-160 3.45e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.60  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  52 IAVSSATGGMHvtLMALGIG---PGDEVITPSQTWVSTLN---MICL-LGATPVMIDVDnDNLMITPAAVEAAITSRTK- 123
Cdd:COG0520   81 IFTRGTTEAIN--LVAYGLGrlkPGDEILITEMEHHSNIVpwqELAErTGAEVRVIPLD-EDGELDLEALEALLTPRTKl 157

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489010483 124 -AIIPVHYA-GAPADIDAIRAVGERHGISVIEDAAHAAG 160
Cdd:COG0520  158 vAVTHVSNVtGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
30-203 6.58e-06

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 47.77  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  30 TTGPKNQALEAAFCQLTGNRHAIAVSSatgGMHV--TLMALgIGPGDEVITPSQtwvstlnmicLLGATPVMIDVDNDNL 107
Cdd:PRK08247  49 TGNPTRGVLEQAIADLEGGDQGFACSS---GMAAiqLVMSL-FRSGDELIVSSD----------LYGGTYRLFEEHWKKW 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 108 MITP--------AAVEAAITSRTKAII---PVHYAGAPADIDAIRAVGERHGISVIED------------------AAHA 158
Cdd:PRK08247 115 NVRFvyvntaslKAIEQAITPNTKAIFietPTNPLMQETDIAAIAKIAKKHGLLLIVDntfytpvlqrpleegadiVIHS 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489010483 159 AgTHYKGRHvgwqgtaifsfhaikNMTCAegGLIVTDDDELASRI 203
Cdd:PRK08247 195 A-TKYLGGH---------------NDVLA--GLVVAKGQELCERL 221
PRK08912 PRK08912
aminotransferase;
55-154 1.53e-05

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 46.51  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  55 SSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDNLMITPAAVEAAITSRTKAII---PVHYA 131
Cdd:PRK08912  94 SGATEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnPLNPA 172

                         90       100
                 ....*....|....*....|....*.
gi 489010483 132 G---APADIDAIRAVGERHGISVIED 154
Cdd:PRK08912 173 GkvfPREELALLAEFCQRHDAVAICD 198
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 70-160 5.02e-04

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: 41.68  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  70 IGPGDEVITpsqtwvSTL----NMICLL------GATPVMIDVDNDNLmITPAAVEAAITSRTKAIIPVHYAGAPADIDA 139
Cdd:cd06453   85 NKPGDEIVT------SVMehhsNIVPWQqlaertGAKLKVVPVDDDGQ-LDLEALEKLLTERTKLVAVTHVSNVLGTINP 157

                         90       100
                 ....*....|....*....|....
gi 489010483 140 IRAVGE---RHGISVIEDAAHAAG 160
Cdd:cd06453  158 VKEIGEiahEAGVPVLVDGAQSAG 181
PRK06176 PRK06176
cystathionine gamma-synthase;
33-203 9.58e-04

cystathionine gamma-synthase;


Pssm-ID: 180443 [Multi-domain]  Cd Length: 380  Bit Score: 41.04  E-value: 9.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  33 PKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgiGPGDEVITPSQTWVSTLNMI-CLLGATPVMID-VDNDNLmit 110
Cdd:PRK06176  50 PTRFALEELIADLEGGVKGFAFASGLAGIHAVFSLF--QSGDHVLLGDDVYGGTFRLFdKVLVKNGLSCTiIDTSDL--- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 111 pAAVEAAITSRTKAIipvhYAGAPA-------DIDAIRAVGERHGISVIEDAAHAagTHYKGRHVGWqGTAIFSFHAIKN 183
Cdd:PRK06176 125 -SQIKKAIKPNTKAL----YLETPSnpllkitDLAQCASVAKDHGLLTIVDNTFA--TPYYQNPLLL-GADIVVHSGTKY 196

                        170       180
                 ....*....|....*....|...
gi 489010483 184 M---TCAEGGLIVTDDDELASRI 203
Cdd:PRK06176 197 LgghSDVVAGLVTTNNEALAQEI 219
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
46-213 1.48e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 40.51  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  46 TGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDND--NLMITPAAVEAAITSRTK 123
Cdd:PRK06225  81 LDDDEALITAGATESLYLVMRAF-LSPGDNAVTPDPGYLIIDNFASRFGAEVIEVPIYSEecNYKLTPELVKENMDENTR 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 124 AII------PVHYAGAPADIDAIRAVGERHGISVIEDAAHA--AGTHYKGRHVGWQGT-AIFSFHAIKNMTCAEGGLIVT 194
Cdd:PRK06225 160 LIYlidplnPLGSSYTEEEIKEFAEIARDNDAFLLHDCTYRdfAREHTLAAEYAPEHTvTSYSFSKIFGMAGLRIGAVVA 239

                        170
                 ....*....|....*....
gi 489010483 195 DDDELASrIRSLKFHGLGV 213
Cdd:PRK06225 240 TPDLIEV-VKSIVINDLGT 257
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
57-154 2.47e-03

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 39.64  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  57 ATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGAT--PVMIDVDNDNLMITPAAVEAAITSRTKAII---PVHYA 131
Cdd:PRK07777  94 ATEAIAAAVLGL-VEPGDEVLLIEPYYDSYAAVIAMAGAHrvPVPLVPDGRGFALDLDALRAAVTPRTRALIvnsPHNPT 172

                         90       100
                 ....*....|....*....|....*.
gi 489010483 132 GAPADIDAIRAVGE---RHGISVIED 154
Cdd:PRK07777 173 GTVLTAAELAAIAElavEHDLLVITD 198
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 36-275 2.53e-03

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: 39.62  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  36 QALEAAFCQLTGNRHAIAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNmiclLGATPV-----MIDVDNDNLMIT 110
Cdd:cd06502   35 AKLEARAAELFGKEAALFVPSGTAANQLALAAH-TQPGGSVICHETAHIYTDE----AGAPEFlsgvkLLPVPGENGKLT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 111 PAAVEAAIT-------SRTKAI---IPVHYAG--APADIDAIRAVGERHGISVIEDAAH--AAGTHYKGRHVGW-QGTAI 175
Cdd:cd06502  110 PEDLEAAIRprddihfPPPSLVsleNTTEGGTvyPLDELKAISALAKENGLPLHLDGARlaNAAAALGVALKTYkSGVDS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483 176 FSFHAIKNMtCAEGGLIVTDDDELASRIRSLKfhglgvdaydRQTHGRAPQAEVITPGFKYNLADInaalalVQLEKLSH 255
Cdd:cd06502  190 VSFCLSKGG-GAPVGAVVVGNRDFIARARRRR----------KQAGGGMRQSGFLAAAGLAALEND------LWLRRLRH 252

                        250       260
                 ....*....|....*....|
gi 489010483 256 ANQRRTEIAqRYLRELADTP 275
Cdd:cd06502  253 DHEMARRLA-EALEELGGLE 271
PRK09082 PRK09082
methionine aminotransferase; Validated
 36-154 2.98e-03

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 39.51  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  36 QALEAAFCQLTGNR----HAIAVSS-ATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDNLMIT 110
Cdd:PRK09082  74 EAIAAKTARLYGRQydadSEITVTAgATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVD 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489010483 111 PAAVEAAITSRTKAII---PVHYAGA---PADIDAIRAVGERHGISVIED 154
Cdd:PRK09082 153 WQRFAAAISPRTRLIIlntPHNPSGTvwsAADMRALWQLIAGTDIYVLSD 202
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 31-163 3.07e-03

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: 39.15  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  31 TGPKNQALEAAfCQLTGNRHA-IAVSSATGGMHVTLMALgIGPGDEVITPSQTWVSTLNMICLLGATPVMIDVDNDNLM- 108
Cdd:cd00615   58 TGPIKEAQELA-ARAFGAKHTfFLVNGTSSSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYg 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489010483 109 ----ITPAAVEAAITSRTKA----IIPVHYAGAPADIDAIRAVGERHGISVIEDAAHAAGTHY 163
Cdd:cd00615  136 iaggIPPETFKKALIEHPDAkaavITNPTYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRF 198
PRK05613 PRK05613
O-acetylhomoserine/O-acetylserine sulfhydrylase;
31-160 3.49e-03

O-acetylhomoserine/O-acetylserine sulfhydrylase;


Pssm-ID: 168128 [Multi-domain]  Cd Length: 437  Bit Score: 39.08  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  31 TGPKNQALEAAFCQLTGNRHAIAVSSATGGMHVTLMALGiGPGDEVITPSQTW--VSTLNMICL--LGATPVMIDVDNDn 106
Cdd:PRK05613  67 TNPTVEALENRIASLEGGVHAVAFASGQAAETAAILNLA-GAGDHIVTSPRLYggTETLFLVTLnrLGIEVTFVENPDD- 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489010483 107 lmitPAAVEAAITSRTKAIIPVHYAGAPADIDAIRAVGE---RHGISVIEDAAHAAG 160
Cdd:PRK05613 145 ----PESWQAAVQPNTKAFFGETFANPQADVLDIPAVAEvahRNQVPLIVDNTIATA 197
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
58-154 6.22e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 38.29  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489010483  58 TGGMHVTLMALG--IGPGDEVITPSQTWVSTLNMICLLGAT--PVMIDVDNDNLMITPAAVEAAITSRTKAII------P 127
Cdd:PRK07568  95 NGGSEAILFAMMaiCDPGDEILVPEPFYANYNGFATSAGVKivPVTTKIEEGFHLPSKEEIEKLITPKTKAILisnpgnP 174

                         90       100
                 ....*....|....*....|....*..
gi 489010483 128 VHYAGAPADIDAIRAVGERHGISVIED 154
Cdd:PRK07568 175 TGVVYTKEELEMLAEIAKKHDLFLISD 201
 
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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