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Conserved domains on  [gi|556424614|ref|WP_023309541|]
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MULTISPECIES: UDP-4-amino-4-deoxy-L-arabinose aminotransferase [Enterobacter]

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: 855.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   1 MSDFLPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  81 QTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 161 TYYKNRHVGWKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHGRAPQAEVIAPGYKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 241 INAALALVQLGKLKEANRRRQEIAERYLRELADTPFQPLTIPSWPHVHAWHLFIIRVDEARCGISRDNLMAALKEKGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556424614 321 GLHFRAAHTQKYYRERFPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQLAGH 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: 855.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   1 MSDFLPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  81 QTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 161 TYYKNRHVGWKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHGRAPQAEVIAPGYKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 241 INAALALVQLGKLKEANRRRQEIAERYLRELADTPFQPLTIPSWPHVHAWHLFIIRVDEARCGISRDNLMAALKEKGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556424614 321 GLHFRAAHTQKYYRERFPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQLAGH 379
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-375 7.75e-175

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 490.74  E-value: 7.75e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   4 FLPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTW 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  84 VSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYY 163
Cdd:COG0399   81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 164 KNRHVGWKGT-AIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGlgvdaydrqtHGRAPQAEVIAPGYKYNLADIN 242
Cdd:COG0399  161 KGKKVGTFGDaGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHG----------RDRDAKYEHVELGYNYRMDELQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 243 AALALVQLGKLKEANRRRQEIAERYLRELADTPFqpLTIPSWP--HVHAWHLFIIRVDEarcGISRDNLMAALKEKGIGT 320
Cdd:COG0399  231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPG--LTLPKVPpgAEHVYHLYVIRLDE---GEDRDELIAALKARGIGT 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556424614 321 GLHF-RAAHTQKYYRER-FPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQ 375
Cdd:COG0399  306 RVHYpIPLHLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-373 4.47e-166

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: 468.69  E-value: 4.47e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   10 PSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWVSTLNM 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   90 IVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHVG 169
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  170 WKGT-AIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHgrapqaevIAPGYKYNLADINAALALV 248
Cdd:pfam01041 161 TLGDaATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWH--------EVLGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  249 QLGKLKEANRRRQEIAERYLRELADTP-FQPLTIPSWPHVHAWHLFIIRVDEARcgISRDNLMAALKEKGIGTGLHF-RA 326
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPgFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 556424614  327 AHTQKYYRERFPDVS--LPNSEWNSARICSLPLFPDMTHDDTTRVITAL 373
Cdd:pfam01041 311 LHLQPYYRDLFGYAPgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-374 8.01e-158

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: 447.37  E-value: 8.01e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  16 EIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWVSTLNMIVLLGA 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  96 TPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHVGWKGT-A 174
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDaG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 175 IFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGvdaydrqthGRAPQAEVIAPGYKYNLADINAALALVQLGKLK 254
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 255 EANRRRQEIAERYLRELADTPFqpLTIPSWP--HVHAWHLFIIRVDEArCGISRDNLMAALKEKGIGTGLHFRAAHTQKY 332
Cdd:cd00616  232 EIIARRREIAERYKELLADLPG--IRLPDVPpgVKHSYHLYVIRLDPE-AGESRDELIEALKEAGIETRVHYPPLHHQPP 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 556424614 333 YRER--FPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALH 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 ...
 5-373 2.75e-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: 365.88  E-value: 2.75e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614    5 LPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWV 84
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   85 STLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAIT----PRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  161 TYYKNRHVG---WKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHGRAP-QAEVIAPGYKY 236
Cdd:TIGR03588 161 AEYGGKPVGncrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPwYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  237 NLADINAALALVQLGKLKEANRRRQEIAERYLRELADTP-FQPLTIPSwPHVHAWHLFIIRVDeARCGISRDNLMAALKE 315
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPyFTPLTIPL-GSKSAWHLYPILLD-QEFGCTRKEVFEALRA 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556424614  316 KGIGTGLHFRAAHTQKYYRERFPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITAL 373
Cdd:TIGR03588 319 AGIGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETL 376
 
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: 855.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   1 MSDFLPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPS 80
Cdd:PRK11658   1 MSDFLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  81 QTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:PRK11658  81 LTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 161 TYYKNRHVGWKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHGRAPQAEVIAPGYKYNLAD 240
Cdd:PRK11658 161 TYYKGRHIGARGTAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLGVDAFDRQTQGRAPQAEVLTPGYKYNLAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 241 INAALALVQLGKLKEANRRRQEIAERYLRELADTPFQPLTIPSWPHVHAWHLFIIRVDEARCGISRDNLMAALKEKGIGT 320
Cdd:PRK11658 241 INAAIALVQLAKLEALNARRREIAARYLQALADLPFQPLSLPAWPHQHAWHLFIIRVDEERCGISRDALMEALKERGIGT 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556424614 321 GLHFRAAHTQKYYRERFPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQLAGH 379
Cdd:PRK11658 321 GLHFRAAHTQKYYRERFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIAGQ 379
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
4-375 7.75e-175

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 490.74  E-value: 7.75e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   4 FLPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTW 83
Cdd:COG0399    1 MIPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  84 VSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYY 163
Cdd:COG0399   81 VATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 164 KNRHVGWKGT-AIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGlgvdaydrqtHGRAPQAEVIAPGYKYNLADIN 242
Cdd:COG0399  161 KGKKVGTFGDaGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHG----------RDRDAKYEHVELGYNYRMDELQ 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 243 AALALVQLGKLKEANRRRQEIAERYLRELADTPFqpLTIPSWP--HVHAWHLFIIRVDEarcGISRDNLMAALKEKGIGT 320
Cdd:COG0399  231 AAIGLAQLKRLDEFIARRRAIAARYREALADLPG--LTLPKVPpgAEHVYHLYVIRLDE---GEDRDELIAALKARGIGT 305

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556424614 321 GLHF-RAAHTQKYYRER-FPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQ 375
Cdd:COG0399  306 RVHYpIPLHLQPAYRDLgYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 10-373 4.47e-166

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: 468.69  E-value: 4.47e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   10 PSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWVSTLNM 89
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   90 IVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHVG 169
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  170 WKGT-AIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHgrapqaevIAPGYKYNLADINAALALV 248
Cdd:pfam01041 161 TLGDaATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWH--------EVLGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  249 QLGKLKEANRRRQEIAERYLRELADTP-FQPLTIPSWPHVHAWHLFIIRVDEARcgISRDNLMAALKEKGIGTGLHF-RA 326
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPgFTPLTTPPEADVHAWHLFPILVPEEA--INRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 556424614  327 AHTQKYYRERFPDVS--LPNSEWNSARICSLPLFPDMTHDDTTRVITAL 373
Cdd:pfam01041 311 LHLQPYYRDLFGYAPgdLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAV 359
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 16-374 8.01e-158

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: 447.37  E-value: 8.01e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  16 EIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWVSTLNMIVLLGA 95
Cdd:cd00616    1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  96 TPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHVGWKGT-A 174
Cdd:cd00616   81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDaG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 175 IFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGvdaydrqthGRAPQAEVIAPGYKYNLADINAALALVQLGKLK 254
Cdd:cd00616  161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRD---------RDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 255 EANRRRQEIAERYLRELADTPFqpLTIPSWP--HVHAWHLFIIRVDEArCGISRDNLMAALKEKGIGTGLHFRAAHTQKY 332
Cdd:cd00616  232 EIIARRREIAERYKELLADLPG--IRLPDVPpgVKHSYHLYVIRLDPE-AGESRDELIEALKEAGIETRVHYPPLHHQPP 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 556424614 333 YRER--FPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITALH 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 ...
 5-373 2.75e-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: 365.88  E-value: 2.75e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614    5 LPFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWV 84
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   85 STLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAIT----PRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  161 TYYKNRHVG---WKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDAYDRQTHGRAP-QAEVIAPGYKY 236
Cdd:TIGR03588 161 AEYGGKPVGncrYADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEKQDEGPwYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  237 NLADINAALALVQLGKLKEANRRRQEIAERYLRELADTP-FQPLTIPSwPHVHAWHLFIIRVDeARCGISRDNLMAALKE 315
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPyFTPLTIPL-GSKSAWHLYPILLD-QEFGCTRKEVFEALRA 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 556424614  316 KGIGTGLHFRAAHTQKYYRERFPDVSLPNSEWNSARICSLPLFPDMTHDDTTRVITAL 373
Cdd:TIGR03588 319 AGIGVQVHYIPVHLQPYYRQGFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETL 376
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 6-375 1.45e-87

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 269.40  E-value: 1.45e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   6 PFSRPSMGAEEIAALQDVLMSGWIT-TGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALDIGPGDEVITPSQTWV 84
Cdd:PRK11706   3 PFNKPPVVGTELDYIQQAMSSGKLCgDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYTFV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  85 STLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAHAAGTYYK 164
Cdd:PRK11706  83 STANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 165 NRHVGWKGT-AIFSFHAIKNMTCAEGGLVVTDNAQLAQR--I-------RSLKFHGLgVDAYDRQthgrapqaEViapGY 234
Cdd:PRK11706 163 GRALGTIGHiGCFSFHETKNYTAGEGGALLINDPALIERaeIirekgtnRSQFFRGQ-VDKYTWV--------DI---GS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 235 KYNLADINAALALVQLGKLKEANRRRQEIAERYLRELAdtPFQP---LTIPSWPH--VHAWHLFIIRV-DEARcgisRDN 308
Cdd:PRK11706 231 SYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALA--PLAEagrIELPSIPDdcKHNAHMFYIKLrDLED----RSA 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556424614 309 LMAALKEKGIGTGLHFRAAHTQKYYRE--RFPDvSLPNSEWNSARICSLPLFPDMTHDDTTRVITALHQ 375
Cdd:PRK11706 305 LINFLKEAGIMAVFHYIPLHSSPAGERfgRFHG-EDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILE 372
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 6-378 9.36e-54

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 183.55  E-value: 9.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   6 PFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALD--------IGPGDEVI 77
Cdd:PRK15407  36 PPSGKVIDAKELQNLVDASLDFWLTTGRFNDAFEKKLAEFLGVRYALLVNSGSSANLLAFSALTspklgdraLKPGDEVI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  78 TPSQTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGERHGIPVIEDAAH 157
Cdd:PRK15407 116 TVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCD 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 158 AAGTYYKNRHVG-WKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGL------GVD-----AYDRQtHGRAP 225
Cdd:PRK15407 196 ALGSTYDGRMTGtFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRdcwcapGCDntcgkRFGWQ-LGELP 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 226 QaeviapGYK---------YNL--ADINAALALVQLGKLKE-ANRRRQEIAerYLRE-LADtpFQPLTI---------PS 283
Cdd:PRK15407 275 F------GYDhkytyshlgYNLkiTDMQAAIGLAQLEKLPGfIEARKANFA--YLKEgLAS--LEDFLIlpeatpnsdPS 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 284 wphvhaWHLFIIRVDEArCGISRDNLMAALKEKGIGTGLHFRAAHT-QKYYRERFPDV--SLPNSE-------Wnsaric 353
Cdd:PRK15407 345 ------WFGFPITVKED-AGFTRVELVKYLEENKIGTRLLFAGNLTrQPYFKGVKYRVvgELTNTDrimndtfW------ 411

                        410       420
                 ....*....|....*....|....*
gi 556424614 354 sLPLFPDMTHDDTTRVITALHQLAG 378
Cdd:PRK15407 412 -IGVYPGLTEEMLDYVIEKIEEFFG 435
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 34-195 2.18e-25

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: 100.92  E-value: 2.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  34 KNQELEEAFCQLT--GNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLN-MIVLLGATPVMIDVDKDTLMVT 110
Cdd:cd01494    1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWvAAELAGAKPVPVPVDDAGYGGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 111 P--EAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGE---RHGIPVIEDAAHAAGTYYKN---RHVGWKGTAIFSFHaiK 182
Cdd:cd01494   80 DvaILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKiakEYGILLLVDAASAGGASPAPgvlIPEGGADVVTFSLH--K 157

                        170
                 ....*....|...
gi 556424614 183 NMTCAEGGLVVTD 195
Cdd:cd01494  158 NLGGEGGGVVIVK 170
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 37-154 2.67e-19

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 88.26  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  37 ELEEAFCQLTGNQHAIAVCSA----TAG----MHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDT-L 107
Cdd:PRK05764  72 ELREAIAAKLKRDNGLDYDPSqvivTTGakqaLYNAFMAL-LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgF 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556424614 108 MVTPEAVEAAITPRTKAII---PVHYAGA---PCEIDAIHAIGERHGIPVIED 154
Cdd:PRK05764 151 KLTVEQLEAAITPKTKALIlnsPSNPTGAvysPEELEAIADVAVEHDIWVLSD 203
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 37-168 1.48e-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: 86.34  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  37 ELEEAFCQLTGNQHAIAV--------CSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDT-L 107
Cdd:COG0436   71 ELREAIAAYYKRRYGVDLdpdeilvtNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgF 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 108 MVTPEAVEAAITPRTKAII------PvhyAGA---PCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHV 168
Cdd:COG0436  150 LPDPEALEAAITPRTKAIVlnspnnP---TGAvysREELEALAELAREHDLLVISDEIYEELVYDGAEHV 216
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 6-318 1.09e-17

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: 83.16  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   6 PFSRPSMGAEEIAALQDVLMSGWITTGPKNQELEEAFCQLTGNQHA-------IAVCS-ATAGMHVTLMALdIGPGDEVI 77
Cdd:cd00609    9 DFPPPPEVLEALAAAALRAGLLGYYPDPGLPELREAIAEWLGRRGGvdvppeeIVVTNgAQEALSLLLRAL-LNPGDEVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  78 TPSQTWVSTLNMIVLLGATPVMIDVDKD-TLMVTPEAVEAAITPRTKAIIpVHYAGAPC-------EIDAIHAIGERHGI 149
Cdd:cd00609   88 VPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLY-LNNPNNPTgavlseeELEELAELAKKHGI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 150 PVIEDAAHAAGTYYKNRH-----VGWKGTAI----FSfhaiKNMtcAEGGL----VVTDNAQLAQRIRSLKFHGLGVDAy 216
Cdd:cd00609  167 LIISDEAYAELVYDGEPPpalalLDAYERVIvlrsFS----KTF--GLPGLrigyLIAPPEELLERLKKLLPYTTSGPS- 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 217 drqthgrAPQAEVIAPGYKYNLADINaalalvqlgKLKEANRRRQEIAERYLRELadtPFQPLTIPSwphvHAWHLFiIR 296
Cdd:cd00609  240 -------TLSQAAAAAALDDGEEHLE---------ELRERYRRRRDALLEALKEL---GPLVVVKPS----GGFFLW-LD 295

                        330       340
                 ....*....|....*....|..
gi 556424614 297 VDEarcGISRDNLMAALKEKGI 318
Cdd:cd00609  296 LPE---GDDEEFLERLLLEAGV 314
PRK07682 PRK07682
aminotransferase;
67-184 3.71e-14

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 73.23  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  67 ALDIG------PGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDT-LMVTPEAVEAAITPRTKAII---PVHYAGA--- 133
Cdd:PRK07682  93 ALDVAmraiinPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPTGAvln 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556424614 134 PCEIDAIHAIGERHGIPVIEDAAHAAGTYYKnrhvgwkgtAIFSFHAIKNM 184
Cdd:PRK07682 173 KSELEEIAVIVEKHDLIVLSDEIYAELTYDE---------AYTSFASIKGM 214
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
36-296 3.31e-12

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 66.47  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   36 QELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVIT--PSQTWVSTLNMIVLL-GATPVMIDVDKDTLMvTPE 112
Cdd:pfam01212  35 NRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICgePAHIHFDETGGHAELgGVQPRPLDGDEAGNM-DLE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  113 AVEAAITPRTKAIIP----------VHYAGAPC----EIDAIHAIGERHGIPVIEDAA---HAAgtyyknRHVG------ 169
Cdd:pfam01212 113 DLEAAIREVGADIFPptglislentHNSAGGQVvsleNLREIAALAREHGIPVHLDGArfaNAA------VALGvivkei 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  170 WKGTAIFSFHAIKNMTCAEGGLVVTDNAQLAQRIRSLKFHGLGVDaydrqthgrapQAEVIAPGYKYNLaDINAALalvq 249
Cdd:pfam01212 187 TSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIRQRKYLGGGLR-----------QAGVLAAAGLRAL-EEGVAR---- 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 556424614  250 lgkLKEANRRRQEIAERyLRELadtpfqPLTIPSWPHVHAwHLFIIR 296
Cdd:pfam01212 251 ---LARDHATARRLAEG-LELL------RLAIPRRVYTNT-HMVYVA 286
PRK06107 PRK06107
aspartate transaminase;
57-147 3.56e-11

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 63.99  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  57 ATAGMHVTLMAlDIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDT-LMVTPEAVEAAITPRTKAII---PVHYAG 132
Cdd:PRK06107 102 AKQAIFLALMA-TLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVACPEEQgFKLTPEALEAAITPRTRWLIlnaPSNPTG 180

                         90
                 ....*....|....*...
gi 556424614 133 APCEIDAIHAIGE---RH 147
Cdd:PRK06107 181 AVYSRAELRALADvllRH 198
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 31-154 1.04e-10

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 62.81  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  31 TGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVL----LGATPVMIDVDKdt 106
Cdd:PRK05994  61 TNPTNAVLEERVAALEGGTAALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHafksFGWQVRWADADD-- 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556424614 107 lmvtPEAVEAAITPRTKAIIPVHYA---GAPCEIDAIHAIGERHGIPVIED 154
Cdd:PRK05994 138 ----PASFERAITPRTKAIFIESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
37-154 1.79e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 61.88  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  37 ELEEA--------FCQLTGNQHaIAVCSAtaGMHVTLMALDI--GPGDEVITPSQTWVSTLNMIVLLGATPVMI--DVDK 104
Cdd:PRK06108  65 ELREAlaryvsrlHGVATPPER-IAVTSS--GVQALMLAAQAlvGPGDEVVAVTPLWPNLVAAPKILGARVVCVplDFGG 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556424614 105 DTLMVTPEAVEAAITPRTKAII------PVHYAGAPCEIDAIHAIGERHGIPVIED 154
Cdd:PRK06108 142 GGWTLDLDRLLAAITPRTRALFinspnnPTGWTASRDDLRAILAHCRRHGLWIVAD 197
PRK07683 PRK07683
aminotransferase A; Validated
 37-191 6.21e-10

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 60.12  E-value: 6.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  37 ELEEAFCQL---------TGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDTL 107
Cdd:PRK07683  69 ELRKAACNFvkdkydlhySPESEIIVTIGASEAIDIAFRTI-LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGF 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 108 MVTPEAVEAAITPRTKAII---PVHYAGAPC---EIDAIHAIGERHGIPVIEDAAHAAGTyYKNRHVgwkgtAIFSFHAI 181
Cdd:PRK07683 148 RLTAEALENAITEKTRCVVlpyPSNPTGVTLskeELQDIADVLKDKNIFVLSDEIYSELV-YEQPHT-----SIAHFPEM 221

                        170
                 ....*....|
gi 556424614 182 KNMTCAEGGL 191
Cdd:PRK07683 222 REKTIVINGL 231
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
53-163 6.87e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 60.12  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  53 AVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMID-VDKDTLMVTPEAVEAAITPRTKAII---PV 128
Cdd:PRK06348  94 ATVGACHGMYLALQSI-LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPN 172

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 556424614 129 HYAGA---PCEIDAIHAIGERHGIPVIEDAAHAAGTYY 163
Cdd:PRK06348 173 NPTGAvfsKETLEEIAKIAIEYDLFIISDEVYDGFSFY 210
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
49-126 7.22e-10

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 60.21  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  49 QHAIAVCSATAGMHVTLMALdIGPGDEVITPS------QTWVSTLnmivllGATPVMIDVDKDTLMVTPEAVEAAITPRT 122
Cdd:PRK06836  97 DHIVMTCGAAGALNVALKAI-LNPGDEVIVFApyfveyRFYVDNH------GGKLVVVPTDTDTFQPDLDALEAAITPKT 169


                 ....
gi 556424614 123 KAII 126
Cdd:PRK06836 170 KAVI 173
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
57-168 1.18e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 59.35  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  57 ATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPR---TKAIIpVHYAGA 133
Cdd:PRK07309 100 ATEALSASLTAI-LEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILEQgdkLKAVI-LNYPAN 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 556424614 134 PC-------EIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHV 168
Cdd:PRK07309 178 PTgvtysreQIKALADVLKKYDIFVISDEVYSELTYTGEPHV 219
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
37-162 2.10e-09

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 58.47  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614   37 ELEEAFCQLTGNQH--------AIAVCSATAGMHVTLMALDIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDK-DTL 107
Cdd:pfam00155  43 ELREALAKFLGRSPvlkldreaAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYDsNDF 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556424614  108 MVTPEAVEAAITPRTKAIIpVHYAGAPC-------EIDAIHAIGERHGIPVIEDAAHAAGTY 162
Cdd:pfam00155 123 HLDFDALEAALKEKPKVVL-HTSPHNPTgtvatleELEKLLDLAKEHNILLLVDEAYAGFVF 183
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
48-168 6.43e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 57.00  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  48 NQHAIAVcsaTAGMHVTLM--ALDI-GPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDkDTLMVTPEAVEAAITPRTKA 124
Cdd:PRK05957  88 NEQAIVV---TAGSNMAFMnaILAItDPGDEIILNTPYYFNHEMAITMAGCQPILVPTD-DNYQLQPEAIEQAITPKTRA 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556424614 125 II---PVHYAGAP-CEID--AIHAIGERHGIPVIEDAAHAAGTYYKNRHV 168
Cdd:PRK05957 164 IVtisPNNPTGVVyPEALlrAVNQICAEHGIYHISDEAYEYFTYDGVKHF 213
PRK07550 PRK07550
aminotransferase;
18-154 1.12e-08

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 56.51  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  18 AALQDVLMSGWittGP--KNQELEEAFCQLTGNQHAIAVcsATAGMHVT----------LMALdIGPGDEVITPS----- 80
Cdd:PRK07550  53 EAAADPAAHLY---GPveGLPELREAYAAHYSRLYGAAI--SPEQVHITsgcnqafwaaMVTL-AGAGDEVILPLpwyfn 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  81 -QTWvstLNMivlLGATPVMIDVD-KDTLMVTPEAVEAAITPRTKAII---PVHYAGA---PCEIDAIHAIGERHGIPVI 152
Cdd:PRK07550 127 hKMW---LDM---LGIRPVYLPCDeGPGLLPDPAAAEALITPRTRAIAlvtPNNPTGVvypPELLHELYDLARRHGIALI 200


                 ..
gi 556424614 153 ED 154
Cdd:PRK07550 201 LD 202
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 33-164 8.49e-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: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  33 PKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMI-VLLGATPVMID-VDKDTlmvt 110
Cdd:cd00614   40 PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLYGGTYRLFeRLLPKLGIEVTfVDPDD---- 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556424614 111 PEAVEAAITPRTKAIipvhYAGAP-------CEIDAIHAIGERHGIPVIEDAAHAAGTYYK 164
Cdd:cd00614  115 PEALEAAIKPETKLV----YVESPtnptlkvVDIEAIAELAHEHGALLVVDNTFATPYLQR 171
PRK12414 PRK12414
putative aminotransferase; Provisional
 54-126 1.46e-07

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 52.87  E-value: 1.46e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556424614  54 VCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAII 126
Cdd:PRK12414  96 IASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 36-280 2.50e-07

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


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 51.95  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  36 QELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLN---MIVLLGATPVMIDVDKDTLmvTPE 112
Cdd:cd06502   35 AKLEARAAELFGKEAALFVPSGTAANQLALAAH-TQPGGSVICHETAHIYTDEagaPEFLSGVKLLPVPGENGKL--TPE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 113 AVEAAIT-------PRTKAI---IPVHYAG--APCEIDAIHAIGERHGIPVIEDAAH--AAGTYYKNRHVGWK-GTAIFS 177
Cdd:cd06502  112 DLEAAIRprddihfPPPSLVsleNTTEGGTvyPLDELKAISALAKENGLPLHLDGARlaNAAAALGVALKTYKsGVDSVS 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 178 FHAIKNMtCAEGGLVVTDNAQLAQRIRSLKfhglgvdaydRQTHGRAPQAEVIAPGYKYNLADInaalalVQLGKLKEAN 257
Cdd:cd06502  192 FCLSKGG-GAPVGAVVVGNRDFIARARRRR----------KQAGGGMRQSGFLAAAGLAALEND------LWLRRLRHDH 254

                        250       260
                 ....*....|....*....|...
gi 556424614 258 RRRQEIAErYLRELADTPFQPLT 280
Cdd:cd06502  255 EMARRLAE-ALEELGGLESEVQT 276
PRK08248 PRK08248
homocysteine synthase;
33-154 7.93e-07

homocysteine synthase;


Pssm-ID: 236201 [Multi-domain]  Cd Length: 431  Bit Score: 50.61  E-value: 7.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  33 PKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVL----LGATPVMIDVDKdtlm 108
Cdd:PRK08248  64 PTTDVFEKRIAALEGGIGALAVSSGQAAITYSILNI-ASAGDEIVSSSSLYGGTYNLFAHtlpkLGITVKFVDPSD---- 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556424614 109 vtPEAVEAAITPRTKAIIpVHYAGAP----CEIDAIHAIGERHGIPVIED 154
Cdd:PRK08248 139 --PENFEAAITDKTKALF-AETIGNPkgdvLDIEAVAAIAHEHGIPLIVD 185
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
30-154 3.23e-06

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 48.55  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  30 TTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHvTLMALdIGPGDEVITPSQtwvstlnmivLLGATPVMIDVDKDTLMV 109
Cdd:PRK08247  49 TGNPTRGVLEQAIADLEGGDQGFACSSGMAAIQ-LVMSL-FRSGDELIVSSD----------LYGGTYRLFEEHWKKWNV 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556424614 110 TP--------EAVEAAITPRTKAII---PVHYAGAPCEIDAIHAIGERHGIPVIED 154
Cdd:PRK08247 117 RFvyvntaslKAIEQAITPNTKAIFietPTNPLMQETDIAAIAKIAKKHGLLLIVD 172
PRK08912 PRK08912
aminotransferase;
13-126 7.19e-06

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 47.66  E-value: 7.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  13 GAEEI-AALQDVLMSGWittgpkNQ--------ELEEAFCQLTGNQHAIA--------VCS-ATAGMHVTLMALdIGPGD 74
Cdd:PRK08912  40 GPEDVrRAAADALLDGS------NQyppmmglpELRQAVAAHYARFQGLDldpetevmVTSgATEALAAALLAL-VEPGD 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556424614  75 EVITPSQTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAII 126
Cdd:PRK08912 113 EVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVL 164
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 16-159 1.40e-05

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: 46.47  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  16 EIAALQDVLmsgwITTGPKnQELEEAFCQLTGNQHA-IAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLG 94
Cdd:cd00615   47 ELTGLDDLL----DPTGPI-KEAQELAARAFGAKHTfFLVNGTSSSNKAVILAV-CGPGDKILIDRNCHKSVINGLVLSG 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556424614  95 ATPVMIDVDKDTLM-----VTPEAVEAAIT--PRTKAII---PVHYaGAPCEIDAIHAIGERHGIPVIEDAAHAA 159
Cdd:cd00615  121 AVPVYLKPERNPYYgiaggIPPETFKKALIehPDAKAAVitnPTYY-GICYNLRKIVEEAHHRGLPVLVDEAHGA 194
PRK07811 PRK07811
cystathionine gamma-synthase; Provisional
 30-154 1.41e-05

cystathionine gamma-synthase; Provisional


Pssm-ID: 236104 [Multi-domain]  Cd Length: 388  Bit Score: 46.56  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  30 TTGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMI--VL----LGATPVMidvd 103
Cdd:PRK07811  58 TGNPTRTALEEQLAALEGGAYGRAFSSGMAATDCLLRAV-LRPGDHIVIPNDAYGGTFRLIdkVFtrwgVEYTPVD---- 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556424614 104 kdtlMVTPEAVEAAITPRTKAI---IPVHYAGAPCEIDAIHAIGERHGIPVIED 154
Cdd:PRK07811 133 ----LSDLDAVRAAITPRTKLIwveTPTNPLLSITDIAALAELAHDAGAKVVVD 182
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
57-168 1.62e-05

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 46.57  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  57 ATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGAT--PVMIDVDKDTLMVTPEAVEAAITPRTKAII---PVHYA 131
Cdd:PRK07777  94 ATEAIAAAVLGL-VEPGDEVLLIEPYYDSYAAVIAMAGAHrvPVPLVPDGRGFALDLDALRAAVTPRTRALIvnsPHNPT 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556424614 132 GA---PCEIDAIHAIGERHGIPVIEDAAHAAGTYYKNRHV 168
Cdd:PRK07777 173 GTvltAAELAAIAELAVEHDLLVITDEVYEHLVFDGARHL 212
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
69-160 1.66e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 46.29  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  69 DIGPGDEVITPSQTWVSTLNMIVLL----GATPVMIDVDkDTLMVTPEAVEAAITPRTK------------AIIPVHyag 132
Cdd:COG0520   99 RLKPGDEILITEMEHHSNIVPWQELaertGAEVRVIPLD-EDGELDLEALEALLTPRTKlvavthvsnvtgTVNPVK--- 174

                         90       100
                 ....*....|....*....|....*...
gi 556424614 133 apceidAIHAIGERHGIPVIEDAAHAAG 160
Cdd:COG0520  175 ------EIAALAHAHGALVLVDGAQSVP 196
SelA COG1921
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
38-156 6.93e-05

Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441524  Cd Length: 399  Bit Score: 44.34  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  38 LEEAFCQLTGNQHAIAVCSATAGMHVTLMALdiGPGDEVItpsqtwVST--L----------NMIVLLGATPVMIDVdkd 105
Cdd:COG1921   70 VEELLCELTGAEAALVVNNNAAAVLLALAAL--AAGKEVI------VSRgeLveiggsfripDVMALSGAKLVEVGT--- 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556424614 106 TLMVTPEAVEAAITPRTKAIIPVH---YA--GAPCEID--AIHAIGERHGIPVIEDAA 156
Cdd:COG1921  139 TNRTHLRDYEAAITENTAALLKVHtsnYRivGFTEEVSlaELAELAHEHGLPVIVDLG 196
PRK06176 PRK06176
cystathionine gamma-synthase;
33-203 7.53e-05

cystathionine gamma-synthase;


Pssm-ID: 180443 [Multi-domain]  Cd Length: 380  Bit Score: 44.50  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  33 PKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdiGPGDEVITPSQTWVSTLNMI--VLLGATPVMIDVDKDTLmvt 110
Cdd:PRK06176  50 PTRFALEELIADLEGGVKGFAFASGLAGIHAVFSLF--QSGDHVLLGDDVYGGTFRLFdkVLVKNGLSCTIIDTSDL--- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614 111 pEAVEAAITPRTKAIipvhYAGAPC-------EIDAIHAIGERHGIPVIEDAAHAAgTYYKNRHVgwKGTAIFSFHAIKN 183
Cdd:PRK06176 125 -SQIKKAIKPNTKAL----YLETPSnpllkitDLAQCASVAKDHGLLTIVDNTFAT-PYYQNPLL--LGADIVVHSGTKY 196

                        170       180
                 ....*....|....*....|...
gi 556424614 184 M---TCAEGGLVVTDNAQLAQRI 203
Cdd:PRK06176 197 LgghSDVVAGLVTTNNEALAQEI 219
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 67-160 1.01e-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: 43.99  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  67 ALDIGPGDEVITpsqtwvSTL----NMIVLL------GATPVMIDVDKDTLmVTPEAVEAAITPRTKAIIPVHYAGAPCE 136
Cdd:cd06453   82 GRANKPGDEIVT------SVMehhsNIVPWQqlaertGAKLKVVPVDDDGQ-LDLEALEKLLTERTKLVAVTHVSNVLGT 154

                         90       100
                 ....*....|....*....|....*..
gi 556424614 137 IDAIHAIGE---RHGIPVIEDAAHAAG 160
Cdd:cd06453  155 INPVKEIGEiahEAGVPVLVDGAQSAG 181
PRK08363 PRK08363
alanine aminotransferase; Validated
 58-169 2.30e-04

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 42.87  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  58 TAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMID-VDKDTLMVTPEAVEAAITPRTKAII---PVHYAGA 133
Cdd:PRK08363 103 TEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAvinPNNPTGA 181

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556424614 134 PCE---IDAIHAIGERHGIPVIEDAAHAAGTyYKNRHVG 169
Cdd:PRK08363 182 LYEkktLKEILDIAGEHDLPVISDEIYDLMT-YEGKHVS 219
PRK09082 PRK09082
methionine aminotransferase; Validated
 57-126 3.21e-04

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 42.60  E-value: 3.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  57 ATAGMHVTLMALdIGPGDEVITPSQTWVSTLNMIVLLGATPVMIDVDKDTLMVTPEAVEAAITPRTKAII 126
Cdd:PRK09082 100 ATEALFAAILAL-VRPGDEVIVFDPSYDSYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLII 168
PRK05613 PRK05613
O-acetylhomoserine/O-acetylserine sulfhydrylase;
31-160 9.96e-04

O-acetylhomoserine/O-acetylserine sulfhydrylase;


Pssm-ID: 168128 [Multi-domain]  Cd Length: 437  Bit Score: 41.01  E-value: 9.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  31 TGPKNQELEEAFCQLTGNQHAIAVCSATAGMHVTLMALdIGPGDEVITPSQTW--VSTLNMIVL--LGATPVMIDVDKDt 106
Cdd:PRK05613  67 TNPTVEALENRIASLEGGVHAVAFASGQAAETAAILNL-AGAGDHIVTSPRLYggTETLFLVTLnrLGIEVTFVENPDD- 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556424614 107 lmvtPEAVEAAITPRTKAIIPVHYAGAPCEIDAIHAIGE---RHGIPVIEDAAHAAG 160
Cdd:PRK05613 145 ----PESWQAAVQPNTKAFFGETFANPQADVLDIPAVAEvahRNQVPLIVDNTIATA 197
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 93-160 1.30e-03

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 40.42  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556424614  93 LGATPVMIDVDKDTLmVTPEAVEAAITPRTkAIIPVHYA----GA--PceIDAIHAIGERHGIPVIEDAAHAAG 160
Cdd:COG1104  113 EGFEVTYLPVDEDGR-VDLEALEAALRPDT-ALVSVMHAnnetGTiqP--IAEIAEIAKEHGVLFHTDAVQAVG 182
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
72-154 1.66e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 40.22  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556424614  72 PGDEVITPSQTWVSTLNMIVLLGAT--PVMIDVDKDTLMVTPEAVEAAITPRTKAII------PVHYAGAPCEIDAIHAI 143
Cdd:PRK07568 111 PGDEILVPEPFYANYNGFATSAGVKivPVTTKIEEGFHLPSKEEIEKLITPKTKAILisnpgnPTGVVYTKEELEMLAEI 190

                         90
                 ....*....|.
gi 556424614 144 GERHGIPVIED 154
Cdd:PRK07568 191 AKKHDLFLISD 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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