|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
10-282 |
5.12e-116 |
|
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.
Pssm-ID: 238799 [Multi-domain] Cd Length: 270 Bit Score: 334.57 E-value: 5.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNHVMPEDCEPTAFAYAQPARLPTAEQRHHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAG 169
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 170 ALETLLFR-DGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSAT 248
Cdd:cd01558 161 ADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|....
gi 1596252157 249 KEILPVTTLDHEPVGHgalrGKPGPVYARLYEAY 282
Cdd:cd01558 241 AEVMPVVEIDGRPIGD----GKPGPVTKRLREAY 270
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
9-286 |
6.16e-97 |
|
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439885 [Multi-domain] Cd Length: 285 Bit Score: 286.70 E-value: 6.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 9 CYLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGV 88
Cdd:COG0115 3 IWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 89 EDQWVYLQITRGPAPRNHvMPEDCEPTAFAYAQPARLPTAEQRHHGVACVSARDFRWE---RGDIKSTSLLGNVLARQIS 165
Cdd:COG0115 83 EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAApggLGGIKTGNYLNNVLAKQEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 166 ADAGALETLLFR-DGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILI 244
Cdd:COG0115 162 KEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1596252157 245 SSATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAYQRAK 286
Cdd:COG0115 242 TGTAAEVTPVTEIDGRPIGD----GKPGPVTRRLRELYTDIV 279
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
10-282 |
3.72e-81 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 246.38 E-value: 3.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:PRK06680 6 YVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNHVMP-EDCEPTAFAYAQPARLPTAEQR-HHGVACVSARDFRWERGDIKSTSLLGNVLARQISAD 167
Cdd:PRK06680 86 EGLVYLQVTRGVARRDHVFPaADVKPSVVVFAKSVDFARPAAAaETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 168 AGALETLLFRDGHLTEASASNVWIV-KEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISS 246
Cdd:PRK06680 166 AGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITA 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1596252157 247 ATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAY 282
Cdd:PRK06680 246 ASSFVFPVVQIDGKQIGN----GKPGPIAKRLREAY 277
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
12-283 |
1.65e-78 |
|
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130191 Cd Length: 276 Bit Score: 239.64 E-value: 1.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 12 NGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQ 91
Cdd:TIGR01121 5 NGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNLNTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 92 WVYLQITRGPAPRNHVMPEDC-EPTAFAYAQPARLPTAEQRhHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAGA 170
Cdd:TIGR01121 85 HVYFQVTRGVAPRNHQFPAGTvKPVITAYTKEVPRPEENLE-KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 171 LETLLFRDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKE 250
Cdd:TIGR01121 164 YEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVSSTTAE 243
|
250 260 270
....*....|....*....|....*....|...
gi 1596252157 251 ILPVTTLDHEPVGHgalrGKPGPVYARLYEAYQ 283
Cdd:TIGR01121 244 ITPVIEIDGQQIGD----GKPGPWTRQLQKAFE 272
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
35-255 |
1.03e-48 |
|
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Pssm-ID: 395844 [Multi-domain] Cd Length: 221 Bit Score: 161.37 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 35 GVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQWVYLQITRGPAPRNHvmpEDCEP 114
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGL---PTSDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 115 TAFAYAQPARLPTAEQRHHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAGALETLLF-RDGHLTEASASNVWIVK 193
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLVK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596252157 194 EGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVT 255
Cdd:pfam01063 158 GGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVS 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
10-282 |
5.12e-116 |
|
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.
Pssm-ID: 238799 [Multi-domain] Cd Length: 270 Bit Score: 334.57 E-value: 5.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNHVMPEDCEPTAFAYAQPARLPTAEQRHHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAG 169
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 170 ALETLLFR-DGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSAT 248
Cdd:cd01558 161 ADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|....
gi 1596252157 249 KEILPVTTLDHEPVGHgalrGKPGPVYARLYEAY 282
Cdd:cd01558 241 AEVMPVVEIDGRPIGD----GKPGPVTKRLREAY 270
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
9-286 |
6.16e-97 |
|
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439885 [Multi-domain] Cd Length: 285 Bit Score: 286.70 E-value: 6.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 9 CYLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGV 88
Cdd:COG0115 3 IWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 89 EDQWVYLQITRGPAPRNHvMPEDCEPTAFAYAQPARLPTAEQRHHGVACVSARDFRWE---RGDIKSTSLLGNVLARQIS 165
Cdd:COG0115 83 EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAApggLGGIKTGNYLNNVLAKQEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 166 ADAGALETLLFR-DGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILI 244
Cdd:COG0115 162 KEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1596252157 245 SSATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAYQRAK 286
Cdd:COG0115 242 TGTAAEVTPVTEIDGRPIGD----GKPGPVTRRLRELYTDIV 279
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
10-282 |
3.72e-81 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 246.38 E-value: 3.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:PRK06680 6 YVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNHVMP-EDCEPTAFAYAQPARLPTAEQR-HHGVACVSARDFRWERGDIKSTSLLGNVLARQISAD 167
Cdd:PRK06680 86 EGLVYLQVTRGVARRDHVFPaADVKPSVVVFAKSVDFARPAAAaETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 168 AGALETLLFRDGHLTEASASNVWIV-KEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISS 246
Cdd:PRK06680 166 AGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITA 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1596252157 247 ATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAY 282
Cdd:PRK06680 246 ASSFVFPVVQIDGKQIGN----GKPGPIAKRLREAY 277
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
12-283 |
1.65e-78 |
|
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130191 Cd Length: 276 Bit Score: 239.64 E-value: 1.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 12 NGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQ 91
Cdd:TIGR01121 5 NGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNLNTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 92 WVYLQITRGPAPRNHVMPEDC-EPTAFAYAQPARLPTAEQRhHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAGA 170
Cdd:TIGR01121 85 HVYFQVTRGVAPRNHQFPAGTvKPVITAYTKEVPRPEENLE-KGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEKGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 171 LETLLFRDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKE 250
Cdd:TIGR01121 164 YEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVSSTTAE 243
|
250 260 270
....*....|....*....|....*....|...
gi 1596252157 251 ILPVTTLDHEPVGHgalrGKPGPVYARLYEAYQ 283
Cdd:TIGR01121 244 ITPVIEIDGQQIGD----GKPGPWTRQLQKAFE 272
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
27-282 |
2.28e-74 |
|
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.
Pssm-ID: 238254 [Multi-domain] Cd Length: 256 Bit Score: 228.25 E-value: 2.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 27 DRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQWVYLQITRGPAPRNH 106
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 107 VMPEDCEPTAFAYAQPArLPTAEQRHHGVACVSARDFR----WERGDIKSTSLLGNVLARQISADAGALETLLFRD-GHL 181
Cdd:cd00449 81 APPPSPEPTFVVFASPV-GAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDnGYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 182 TEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVTTLDHEP 261
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRG 239
|
250 260
....*....|....*....|.
gi 1596252157 262 VGHgalrGKPGPVYARLYEAY 282
Cdd:cd00449 240 IGD----GKPGPVTRKLRELL 256
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
35-255 |
1.03e-48 |
|
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Pssm-ID: 395844 [Multi-domain] Cd Length: 221 Bit Score: 161.37 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 35 GVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQWVYLQITRGPAPRNHvmpEDCEP 114
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGL---PTSDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 115 TAFAYAQPARLPTAEQRHHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAGALETLLF-RDGHLTEASASNVWIVK 193
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLVK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596252157 194 EGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVT 255
Cdd:pfam01063 158 GGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVS 219
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
6-284 |
1.10e-47 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 160.81 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 6 ELQCYLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIAD 85
Cdd:PRK08320 2 EQLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 86 LGVEDQWVYLQITRGPA-----PRNhvmpedC-EPTAFAYAQP-ARLP-----------TAEQRHHGVACVSARdfrwer 147
Cdd:PRK08320 82 NNLRDAYIRLVVSRGVGdlgldPRK------CpKPTVVCIAEPiGLYPgelyekglkviTVSTRRNRPDALSPQ------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 148 gdIKSTSLLGNVLARQISADAGALETLLF-RDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAF 226
Cdd:PRK08320 150 --VKSLNYLNNILAKIEANLAGVDEAIMLnDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1596252157 227 NLRPIAESEVFTADEILISSATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAYQR 284
Cdd:PRK08320 228 REELFTLHDLYTADEVFLTGTAAEVIPVVKVDGRVIGD----GKPGPITKKLLEEFRE 281
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
10-284 |
3.81e-47 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 159.73 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:PRK12479 7 YMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNEYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNhVMPEDCE-PTAFAYAQPARLPTAEQRHHGVACVSARDfRWERGD-----IKSTSLLGNVLARQ 163
Cdd:PRK12479 87 DAYIRLIVSRGKGDLG-LDPRSCVkPSVIIIAEQLKLFPQEFYDNGLSVVSVAS-RRNTPDaldprIKSMNYLNNVLVKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 164 ISADAGALETLLF-RDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEI 242
Cdd:PRK12479 165 EAAQAGVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1596252157 243 LISSATKEILPVTTLDHEPVGhgalRGKPGPVYARLYEAYQR 284
Cdd:PRK12479 245 FLTGTAAELIPVVKVDSREIG----DGKPGSVTKQLTEEFKK 282
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
20-285 |
2.80e-45 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 154.79 E-value: 2.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 20 EAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGV-EDQWVYLQIT 98
Cdd:PRK12400 20 KTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFhEDGTIYLQVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 99 RGPAPRNHVMPEDCEPTAFAYAQPARLPtAEQRHHGVACVSARDFRWERGDIKSTSLLGNVLARQISADAGALETLLFRD 178
Cdd:PRK12400 100 RGVQARTHTFSYDVPPTIYAYITKKERP-ALWIEYGVRAISEPDTRWLRCDIKSLNLLPNILAATKAERKGCKEALFVRN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 179 GHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVTTLD 258
Cdd:PRK12400 179 GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 258
|
250 260
....*....|....*....|....*..
gi 1596252157 259 hepvGHGALRGKPGPVYARLYEAYQRA 285
Cdd:PRK12400 259 ----GTAIQDGQVGPITKMLQRSFSQS 281
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
27-282 |
9.48e-42 |
|
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.
Pssm-ID: 238800 [Multi-domain] Cd Length: 249 Bit Score: 144.37 E-value: 9.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 27 DRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPlSRDQWLAVCRRLIADLGVEDQWVYLQITRGPAPRNH 106
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEP-DLPRLRAALESLLAANDIDEGRIRLILSRGPGGRGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 107 VMPEDCEPTAFAYAQPArlpTAEQRHHGVACVSARdfrWERGD------IKSTSLLGNVLARQISADAGALETLLFR-DG 179
Cdd:cd01559 80 APSVCPGPALYVSVIPL---PPAWRQDGVRLITCP---VRLGEqpllagLKHLNYLENVLAKREARDRGADEALFLDtDG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 180 HLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVTTLDh 259
Cdd:cd01559 154 RVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAID- 232
|
250 260
....*....|....*....|...
gi 1596252157 260 epvghgALRGKPGPVYARLYEAY 282
Cdd:cd01559 233 ------DHDGPPGPLTRALRELL 249
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
10-284 |
1.11e-31 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 118.92 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:PRK07650 3 YVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNGLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGPAPRNHVMPEDCEPTAFAYAQPARLPTAEQRHHGVACVSAR-----DFRwergdIKSTSLLGNVLA-RQ 163
Cdd:PRK07650 83 NAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRntpegAFR-----LKSHHYLNNILGkRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 164 ISADAGALETLLFRDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEVFTADEIL 243
Cdd:PRK07650 158 IGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1596252157 244 ISSATKEILPVTTLDHEPvghgaLRGKPGPVYARLYEAYQR 284
Cdd:PRK07650 238 VTNSIQEIVPLTRIEERD-----FPGKVGMVTKRLQNLYEM 273
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
10-282 |
1.95e-24 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 99.84 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVY----ARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIAD 85
Cdd:PRK06606 10 WFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYdtpkGPAIFRLREHTKRLFNSAKILRMEIPYSVDELMEAQREVVRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 86 LGVEDqwVYLqitR--------GPAPRNHvmpeDCEPTAFAYAQP--ARLPTaEQRHHGV-ACVSardfRWERGDIKSTS 154
Cdd:PRK06606 90 NNLKS--AYI---RplvfvgdeGLGVRPH----GLPTDVAIAAWPwgAYLGE-EALEKGIrVKVS----SWTRHAPNSIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 155 LL----GN----VLARQISADAGALETLLF-RDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIA 225
Cdd:PRK06606 156 TRakasGNylnsILAKTEARRNGYDEALLLdVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1596252157 226 FNLRPIAESEVFTADEILISSATKEILPVTTLDHEPVGHgalrGKPGPVYARLYEAY 282
Cdd:PRK06606 236 VIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGN----GKRGPITEKLQSAY 288
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
21-259 |
4.96e-19 |
|
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 132501 Cd Length: 261 Bit Score: 84.18 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 21 AKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSR--DQWLAvcrrlIADLGVEDQWVYLQIT 98
Cdd:TIGR03461 8 TQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDalREEMA-----QLAAGYSLGVLKVIIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 99 RGPAPRNHVMPEDCEPT----AFAY-AQPARLptaeqRHHGVAcVSARDFRWER----GDIKSTSLLGNVLARQISADAG 169
Cdd:TIGR03461 83 RGSGGRGYSPPGCSDPTriisVSPYpAHYSAW-----QQQGIR-LGVSPVRLGRnpllAGIKHLNRLEQVLIKAELENSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 170 ALETL-LFRDGHLTEASASNVWIVKEGALL-------GVpkseqvlEGIRVELLRELCEDCGIAFNLRPIAESEVFTADE 241
Cdd:TIGR03461 157 ADEALvLDTDGNVVECTAANIFWRKGNQVFtpdlsycGV-------AGVMRQHVLALLPALGYEIEEVKAGLEELLSADE 229
|
250
....*....|....*...
gi 1596252157 242 ILISSATKEILPVTTLDH 259
Cdd:TIGR03461 230 VFITNSLMGVVPVNAIGE 247
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
23-278 |
7.40e-18 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 81.04 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 23 VSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPlsrdQWLAVCRRLI-ADLGVEDQWVYLQITRGP 101
Cdd:PRK06092 12 LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLD----DWAQLEQEMKqLAAELENGVLKVIISRGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 102 APRNHVMPEDCEPT----AFAY-AQPARlptaeQRHHGVaCVSARDFRWER-----GdIKSTSLLGNVLARQISADAGAL 171
Cdd:PRK06092 88 GGRGYSPAGCAAPTrilsVSPYpAHYSR-----WREQGI-TLALCPTRLGRnpllaG-IKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 172 ETLLF-RDGHLTEASASNVWIVKEGALL-------GVpkseqvlEGI-RVELLRELcEDCGIAFNLRPIAESEVFTADEI 242
Cdd:PRK06092 161 EALVLdSEGWVIECCAANLFWRKGGVVYtpdldqcGV-------AGVmRQFILELL-AQSGYPVVEVDASLEELLQADEV 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 1596252157 243 LISSATKEILPVTTLdhepvghGALRGKPGPVYARL 278
Cdd:PRK06092 233 FICNSLMPVWPVRAI-------GETSYSSGTLTRYL 261
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
22-282 |
2.85e-16 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 76.85 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 22 KVSVMDRGFIFGDGVYEMIPVYAR-----RLFRFAQHMDRLDRSLSKLRIsNPLSRDQWLAVCRRLIAdlgVEDQWV--- 93
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTpdgkiVLFRPDENAERLNRSARRLGL-PPFSVEEFIDAIKELVK---LDADWVpyg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 94 -----YL---QITRGPaprnHVMPEDCEPTAFA-YAQP--ARLPTAEQrhhGV-ACVSARDFRWER--GDIKSTSLLGN- 158
Cdd:cd01557 77 ggaslYIrpfIFGTDP----QLGVSPALEYLFAvFASPvgAYFKGGEK---GVsALVSSFRRAAPGgpGAAKAGGNYAAs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 159 VLARQISADAGALETLLF--RDGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDCGIAFNLRPIAESEV 236
Cdd:cd01557 150 LLAQKEAAEKGYDQALWLdgAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDEL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1596252157 237 FTADEILISSATKEILPVTTLDHEPVGHGAlrGKPGPVYARLYEAY 282
Cdd:cd01557 230 YEADEVFATGTAAVVTPVGEIDYRGKEPGE--GEVGPVTKKLYDLL 273
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
27-281 |
8.43e-14 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 70.43 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 27 DRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVEDQWVYLQITRGPAPRNH 106
Cdd:PLN02845 61 DHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGSLRYWLSAGPGGFSL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 107 VmPEDCEPTAFaYAQPARLPTAEQRHHGVACVSAR------DFrwerGDIKSTSLLGNVLARQISADAGALETL-LFRDG 179
Cdd:PLN02845 141 S-PSGCSEPAF-YAVVIEDTYAQDRPEGVKVVTSSvpikppQF----ATVKSVNYLPNALSQMEAEERGAFAGIwLDEEG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 180 HLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELCEDC---GI--AFNLRPIAESEVFTADEILISSATKEILPV 254
Cdd:PLN02845 215 FVAEGPNMNVAFLTNDGELVLPPFDKILSGCTARRVLELAPRLvspGDlrGVKQRKISVEEAKAADEMMLIGSGVPVLPI 294
|
250 260
....*....|....*....|....*..
gi 1596252157 255 TTLDHEPVGHgalrGKPGPVYARLYEA 281
Cdd:PLN02845 295 VSWDGQPIGD----GKVGPITLALHDL 317
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
10-287 |
4.11e-12 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 65.00 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVE 89
Cdd:PRK07544 12 WMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 90 DQWVYLQITRGP------APRN--HVMPEDCE-PTAFAYAQP---ARLPTAEqrhhgvacvsardfrWERGD---IKSTS 154
Cdd:PRK07544 92 DAYVRPVAWRGSemmgvsAQQNkiHLAIAAWEwPSYFDPEAKmkgIRLDIAK---------------WRRPDpetAPSAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 155 -LLGNVLARQIS---ADAGALETLLFRD--GHLTEASASNVWIVKEGAlLGVPKSEQVLEGIRVELLRELCEDCGIAFNL 228
Cdd:PRK07544 157 kAAGLYMICTISkhaAEAKGYADALMLDyrGYVAEATGANIFFVKDGV-IHTPTPDCFLDGITRQTVIELAKRRGIEVVE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1596252157 229 RPIAESEVFTADEILISSATKEILPVTTLdhepvghGALRGKPGPVYARLYEAYQ---RAKP 287
Cdd:PRK07544 236 RHIMPEELAGFSECFLTGTAAEVTPVSEI-------GEYRFTPGAITRDLMDDYEalvRPRA 290
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
33-268 |
8.16e-10 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 58.43 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 33 GDGVYEMIPVYARRLFRFAQHMDRLDRSLSKLRISNPlSRDQWlavcRRLIaDLGVED----------QWVYlqiTRGPA 102
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEP-DLDRW----RRAV-ELAIEEwrapedeaalRLVY---SRGRE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 103 PrnhvmpeDCEPTAFAYAQPARLPTAEQRHHGVACVSA-RDFR--------WERGDIKSTSLLGNVLARQISADAGALET 173
Cdd:PRK07849 109 S-------GGAPTAWVTVSPVPERVARARREGVSVITLdRGYPsdaaerapWLLAGAKTLSYAVNMAALRYAARRGADDV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 174 LLFR-DGHLTEASASNVWIVKEGALLGVPKSEQVLEGIRV----ELLRELCEDCGiafnLRPIAESEVFTADEI-LISSA 247
Cdd:PRK07849 182 IFTStDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQaalfEVAREKGWDCE----YRALRPADLFAADGVwLVSSV 257
|
250 260
....*....|....*....|.
gi 1596252157 248 TKeILPVTTLDHEPVGHGALR 268
Cdd:PRK07849 258 RL-AARVHTLDGRPLPRDPLA 277
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
10-260 |
8.43e-07 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 49.72 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 10 YLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYARR-----LFRFAQHMDRLDRSLSKLRISNPlSRDQWL-AVCRRLI 83
Cdd:PLN02259 82 FTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKEngkllLFRPDHNAIRMKLGAERMLMPSP-SVDQFVnAVKQTAL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 84 ADlgveDQWV--------YLQ---------ITRGPAPrnhvmpedcEPTAFAYAQParlpTAEQRHHGVACVS------- 139
Cdd:PLN02259 161 AN----KRWVppagkgtlYIRpllmgsgpiLGLGPAP---------EYTFIVYASP----VGNYFKEGMAALNlyveeey 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 140 ARDFRWERGDIKSTSLLGNVLARQISADAGALETLLFRDG----HLTEASASNVWIVKeGALLGVPKSE-QVLEGIRVEL 214
Cdd:PLN02259 224 VRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvkkkYLEEASSCNVFVVK-GRTISTPATNgTILEGITRKS 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1596252157 215 LRELCEDCGIAFNLRPIAESEVFTADEILISSATKEILPVTTLDHE 260
Cdd:PLN02259 303 VMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQ 348
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
8-257 |
1.17e-06 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 49.16 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 8 QCYLNGEYAPLAEAKVSVMDRGFIFGDGVYEMIPVYAR-----RLFRFAQHMDRLDRSLSKLRISNPlSRDQWL-AVCRR 81
Cdd:PLN03117 44 ESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTedgriTLFRPDQNALRMQTGADRLCMTPP-SLEQFVeAVKQT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 82 LIADlgveDQWV--------YLQ-ITRGPAPRNHVMPEDcEPTAFAYAQP-ARLPTA--------EQRHHgvacvsaRDF 143
Cdd:PLN03117 123 VLAN----KKWVpppgkgtlYIRpLLIGSGAVLGVAPAP-EYTFLIYASPvGNYHKAssglnlkvDHKHR-------RAH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 144 RWERGDIKSTSLLGNVLARQISADAGALETLLFRDG----HLTEASASNVWIVKEGALLGVPKSEQVLEGIRVELLRELC 219
Cdd:PLN03117 191 SGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAatgkNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELA 270
|
250 260 270
....*....|....*....|....*....|....*...
gi 1596252157 220 EDCGIAFNLRPIAESEVFTADEILISSATKEILPVTTL 257
Cdd:PLN03117 271 RDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETV 308
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
53-282 |
3.71e-05 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 44.18 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 53 HMDRLDRSLSKLRISNPLSRDQWLAVCRRLIADLGVeDQWVYL----------QITRGPAPR---------NHVMPEdce 113
Cdd:PRK13356 53 HCARVNRSAEALGLKPTVSAEEIEALAREGLKRFDP-DTALYIrpmywaedgfASGVAPDPEstrfalcleEAPMPE--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 114 PTAFAYA-QPARLPTAEqrhhgVACVSArdfrwergdiKSTSLLGNVlARQIS-ADAGALETLLFRD--GHLTEASASNV 189
Cdd:PRK13356 129 PTGFSLTlSPFRRPTLE-----MAPTDA----------KAGCLYPNN-ARALReARSRGFDNALVLDmlGNVAETATSNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596252157 190 WIVKEGALLGVPKSEQVLEGI---RV-ELLRElcedCGIAFNLRPIAESEVFTADEILISSATKEILPVTTLDHEPVghg 265
Cdd:PRK13356 193 FMVKDGVVFTPVPNGTFLNGItrqRViALLRE----DGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL--- 265
|
250
....*....|....*..
gi 1596252157 266 alrgKPGPVYARLYEAY 282
Cdd:PRK13356 266 ----QPGPVTRRARELY 278
|
|
| CHD |
cd07302 |
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ... |
239-280 |
5.55e-03 |
|
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.
Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 36.79 E-value: 5.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1596252157 239 ADEILISSATKEILPVTTLDHEPVGHGALRGKPGPVyaRLYE 280
Cdd:cd07302 137 PGQILVSEATYELLGDAGFEFEELGEVELKGKSGPV--RVYR 176
|
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