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Conserved domains on  [gi|2212027142|ref|WP_242309297|]
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UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase [Bacillus cereus group sp. BfR-BA-01524]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 10001360)

DegT/DnrJ/EryC1/StrS family aminotransferase such as Bacillus subtilis 3-oxo-glucose-6-phosphate:glutamate aminotransferase and Saccharopolyspora erythraea erythromycin biosynthesis sensory transduction protein EryC1

CATH:  3.40.640.10|3.90.1150.10
EC:  2.6.1.-
Gene Ontology:  GO:0008483
PubMed:  17109392
SCOP:  4000675

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
19-393 0e+00

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 533.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  19 LPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFV 98
Cdd:COG0399     2 IPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  99 ASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYK 178
Cdd:COG0399    82 ATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 179 NKKIGSIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKkllenhgpwyYEMQFLGYNYRITDIQA 258
Cdd:COG0399   162 GKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK----------YEHVELGYNYRMDELQA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 259 ALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTkllKCNRKEFYEALQRENIGVNVH 338
Cdd:COG0399   232 AIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE---GEDRDELIAALKARGIGTRVH 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2212027142 339 Y-IPVHLQPFYQKLGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:COG0399   309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
19-393 0e+00

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 533.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  19 LPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFV 98
Cdd:COG0399     2 IPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  99 ASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYK 178
Cdd:COG0399    82 ATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 179 NKKIGSIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKkllenhgpwyYEMQFLGYNYRITDIQA 258
Cdd:COG0399   162 GKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK----------YEHVELGYNYRMDELQA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 259 ALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTkllKCNRKEFYEALQRENIGVNVH 338
Cdd:COG0399   232 AIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE---GEDRDELIAALKARGIGTRVH 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2212027142 339 Y-IPVHLQPFYQKLGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:COG0399   309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 19-393 0e+00

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: 516.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  19 LPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFV 98
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  99 ASANCILYQGAKPVFADIDNETYNISPKSIEEKITN----KTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALG 174
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 175 ATYKNKKIGSI--GDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKKLL-ENHGPWYYEMQFLGYNY 251
Cdd:TIGR03588 161 AEYGGKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEkQDEGPWYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 252 RITDIQAALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTKlLKCNRKEFYEALQRE 331
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQE-FGCTRKEVFEALRAA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212027142 332 NIGVNVHYIPVHLQPFYQKlGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 30-390 5.70e-168

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: 473.95  E-value: 5.70e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  30 DIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFVASANCILYQGA 109
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 110 KPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYKNKKIGSIGDMT 189
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 190 MFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNskkllenhgPWYYEMQFLGYNYRITDIQAALGLSQLSKLD 269
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRD---------RFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 270 SFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTKlLKCNRKEFYEALQRENIGVNVHYIPVHLQPFYQ 349
Cdd:cd00616   232 EIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPE-AGESRDELIEALKEAGIETRVHYPPLHHQPPYK 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2212027142 350 K-LGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVR 390
Cdd:cd00616   311 KlLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 24-390 1.96e-151

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: 432.48  E-value: 1.96e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  24 QQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFVASANC 103
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 104 ILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYKNKKIG 183
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 184 SIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKKllenhgPWYYEMqfLGYNYRITDIQAALGLS 263
Cdd:pfam01041 161 TLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADK------RYWHEV--LGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 264 QLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSS-SWHLYIIRLNTKllKCNRKEFYEALQRENIGVNVHY-IP 341
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVhAWHLFPILVPEE--AINRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2212027142 342 VHLQPFYQKL-GYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVR 390
Cdd:pfam01041 311 LHLQPYYRDLfGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
18-393 2.28e-96

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 292.70  E-value: 2.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  18 YLPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTF 97
Cdd:PRK11658    4 FLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTW 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  98 VASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATY 177
Cdd:PRK11658   84 VSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 178 KNKKIGSIGdMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGI-----ERNSkkllenHG--PwYYEMQFLGYN 250
Cdd:PRK11658  164 KGRHIGARG-TAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafDRQT------QGraP-QAEVLTPGYK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 251 YRITDIQAALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSeiIIPKQLPQTSS--SWHLYIIRLNTKLLKCNRKEFYEAL 328
Cdd:PRK11658  236 YNLADINAAIALVQLAKLEALNARRREIAARYLQALADLP--FQPLSLPAWPHqhAWHLFIIRVDEERCGISRDALMEAL 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212027142 329 QRENIGVNVHYIPVHLQPFYQKlGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:PRK11658  314 KERGIGTGLHFRAAHTQKYYRE-RFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
19-393 0e+00

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 533.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  19 LPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFV 98
Cdd:COG0399     2 IPLSRPSIGEEEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFTFV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  99 ASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYK 178
Cdd:COG0399    82 ATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 179 NKKIGSIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKkllenhgpwyYEMQFLGYNYRITDIQA 258
Cdd:COG0399   162 GKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDAK----------YEHVELGYNYRMDELQA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 259 ALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTkllKCNRKEFYEALQRENIGVNVH 338
Cdd:COG0399   232 AIGLAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRLDE---GEDRDELIAALKARGIGTRVH 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2212027142 339 Y-IPVHLQPFYQKLGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:COG0399   309 YpIPLHLQPAYRDLGYRPGDLPVAERLAERVLSLPLHPGLTEEDVDRVIEAIREFL 364
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 19-393 0e+00

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: 516.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  19 LPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFV 98
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFLTQGPTVPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTPITFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  99 ASANCILYQGAKPVFADIDNETYNISPKSIEEKITN----KTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALG 174
Cdd:TIGR03588  81 ATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDASHALG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 175 ATYKNKKIGSI--GDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKKLL-ENHGPWYYEMQFLGYNY 251
Cdd:TIGR03588 161 AEYGGKPVGNCryADATVFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKDPLLFEkQDEGPWYYEQQELGFNY 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 252 RITDIQAALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTKlLKCNRKEFYEALQRE 331
Cdd:TIGR03588 241 RMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQE-FGCTRKEVFEALRAA 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212027142 332 NIGVNVHYIPVHLQPFYQKlGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:TIGR03588 320 GIGVQVHYIPVHLQPYYRQ-GFGDGDLPSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 30-390 5.70e-168

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: 473.95  E-value: 5.70e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  30 DIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFVASANCILYQGA 109
Cdd:cd00616     1 ELEAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 110 KPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYKNKKIGSIGDMT 189
Cdd:cd00616    81 TPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 190 MFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNskkllenhgPWYYEMQFLGYNYRITDIQAALGLSQLSKLD 269
Cdd:cd00616   161 AFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRD---------RFKYEHEILGYNYRLSEIQAAIGLAQLEKLD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 270 SFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSSSWHLYIIRLNTKlLKCNRKEFYEALQRENIGVNVHYIPVHLQPFYQ 349
Cdd:cd00616   232 EIIARRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPE-AGESRDELIEALKEAGIETRVHYPPLHHQPPYK 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2212027142 350 K-LGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVR 390
Cdd:cd00616   311 KlLGYPPGDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEALR 352
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 24-390 1.96e-151

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: 432.48  E-value: 1.96e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  24 QQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFVASANC 103
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATANA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 104 ILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATYKNKKIG 183
Cdd:pfam01041  81 ALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 184 SIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNSKKllenhgPWYYEMqfLGYNYRITDIQAALGLS 263
Cdd:pfam01041 161 TLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADK------RYWHEV--LGYNYRMTEIQAAIGLA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 264 QLSKLDSFIKIRKKYVDIYSKEFSCLSEIIIPKQLPQTSS-SWHLYIIRLNTKllKCNRKEFYEALQRENIGVNVHY-IP 341
Cdd:pfam01041 233 QLERLDEFIARRREIAALYQTLLADLPGFTPLTTPPEADVhAWHLFPILVPEE--AINRDELVEALKEAGIGTRVHYpIP 310

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2212027142 342 VHLQPFYQKL-GYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVR 390
Cdd:pfam01041 311 LHLQPYYRDLfGYAPGDLPNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
18-393 2.28e-96

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 292.70  E-value: 2.28e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  18 YLPYGQQQIDEYDIQAVVDVLKGDFLTTGPMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTF 97
Cdd:PRK11658    4 FLPFSRPAMGDEELAAVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLTW 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  98 VASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNLIIIEDAAHALGATY 177
Cdd:PRK11658   84 VSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTYY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 178 KNKKIGSIGdMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGI-----ERNSkkllenHG--PwYYEMQFLGYN 250
Cdd:PRK11658  164 KGRHIGARG-TAIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGLgvdafDRQT------QGraP-QAEVLTPGYK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 251 YRITDIQAALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSeiIIPKQLPQTSS--SWHLYIIRLNTKLLKCNRKEFYEAL 328
Cdd:PRK11658  236 YNLADINAAIALVQLAKLEALNARRREIAARYLQALADLP--FQPLSLPAWPHqhAWHLFIIRVDEERCGISRDALMEAL 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212027142 329 QRENIGVNVHYIPVHLQPFYQKlGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:PRK11658  314 KERGIGTGLHFRAAHTQKYYRE-RFPTLSLPNTEWNSERICSLPLFPDMTDADVDRVITALQQIA 377
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 84-393 2.32e-73

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 233.57  E-value: 2.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITEGDEVITTPMTFVASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNNL 163
Cdd:PRK11706   68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 164 IIIEDAAHALGATYKNKKIGSIGDMTMFSFHPVKHITTGEGGVITTNNPLFYEKLVQFRTHGIERNS-------Kkllen 236
Cdd:PRK11706  148 FVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIERAEIIREKGTNRSQffrgqvdK----- 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 237 hgpwyYEMQFLGYNYRITDIQAALGLSQLSKLDSFIKIRKKYVDIYSKEFSCLSE---IIIPKQLPQTSSSWHLYIIRLN 313
Cdd:PRK11706  223 -----YTWVDIGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLAEagrIELPSIPDDCKHNAHMFYIKLR 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 314 TkllKCNRKEFYEALQRENIGVNVHYIPVHLQPFYQKLGYEKGICPQAENVYEEIITLPLFPKMTEADVWDVIQAVRKVL 393
Cdd:PRK11706  298 D---LEDRSALINFLKEAGIMAVFHYIPLHSSPAGERFGRFHGEDRYTTKESERLLRLPLFYNLTDVEQRTVIDTILEFF 374
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 16-334 1.38e-68

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 223.22  E-value: 1.38e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  16 ETYLPYGQQQIDEYDIQAVVD-VLkgDF-LTTGPMVQQFEEAIAKYVGAKYA-----------VSFSNGTAALHAACYaa 82
Cdd:PRK15407   32 KSPIPPSGKVIDAKELQNLVDaSL--DFwLTTGRFNDAFEKKLAEFLGVRYAllvnsgssanlLAFSALTSPKLGDRA-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  83 gITEGDEVITTPMTFVASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAIIPVHFTGQPVELEAIKKIAKKNN 162
Cdd:PRK15407  108 -LKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHN 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 163 LIIIEDAAHALGATYKNKKIGSIGDMTMFSFHPVKHITTGEGGVITTNNPLFYeKLVQ-FRTHGieRN-----------S 230
Cdd:PRK15407  187 LWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLK-KIIEsFRDWG--RDcwcapgcdntcG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 231 KKLLENHG--PWYYEMQF----LGYNYRITDIQAALGLSQLSKLDSFIKIRKK-YVDIYSKEFSCLSEIIIPKQLPQTSS 303
Cdd:PRK15407  264 KRFGWQLGelPFGYDHKYtyshLGYNLKITDMQAAIGLAQLEKLPGFIEARKAnFAYLKEGLASLEDFLILPEATPNSDP 343

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2212027142 304 SWHLYII--RLNTKLlkcNRKEFYEALQRENIG 334
Cdd:PRK15407  344 SWFGFPItvKEDAGF---TRVELVKYLEENKIG 373
PRK07682 PRK07682
aminotransferase;
54-172 3.53e-13

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 70.15  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  54 EAIAKYVGAKYAVSFSNGTAALHAACYAAGI--------TEGDEVITTPMTFVASANCILYQGAKPVFADIDNET-YNIS 124
Cdd:PRK07682   64 QEIAKYLKKRFAVSYDPNDEIIVTVGASQALdvamraiiNPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQ 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2212027142 125 PKSIEEKITNKTKAII---PVHFTG---QPVELEAIKKIAKKNNLIIIEDAAHA 172
Cdd:PRK07682  144 PAQIEAAITAKTKAILlcsPNNPTGavlNKSELEEIAVIVEKHDLIVLSDEIYA 197
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 86-168 5.60e-13

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 69.77  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  86 EGDEV-ITTPMtFVASANCILYQGAKPVFADIDNET-YNISPKSIEEKITNKTKAII---PVHFTGQ---PVELEAIKKI 157
Cdd:PRK05764  114 PGDEViIPAPY-WVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIlnsPSNPTGAvysPEELEAIADV 192

                          90
                  ....*....|.
gi 2212027142 158 AKKNNLIIIED 168
Cdd:PRK05764  193 AVEHDIWVLSD 203
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 54-168 3.18e-11

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: 64.38  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  54 EAIAKYVGAKYAVSFS-------NGTAALHAACYAAGITEGDEVI-TTPMtFVASANCILYQGAKPVFADIDNET-YNIS 124
Cdd:COG0436    74 EAIAAYYKRRYGVDLDpdeilvtNGAKEALALALLALLNPGDEVLvPDPG-YPSYRAAVRLAGGKPVPVPLDEENgFLPD 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2212027142 125 PKSIEEKITNKTKAII------PvhfTGQ---PVELEAIKKIAKKNNLIIIED 168
Cdd:COG0436   153 PEALEAAITPRTKAIVlnspnnP---TGAvysREELEALAELAREHDLLVISD 202
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
84-202 8.86e-11

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 62.82  E-value: 8.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITEGDEVITTPMTFVASANCILYQGAKPVFAD-IDNETYNISPKSIEEKITNKTKAII---PVHFTG---QPVELEAIKK 156
Cdd:PRK06348  110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGavfSKETLEEIAK 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2212027142 157 IAKKNNLIIIEDAAHAlGATYKNKKIgsigDMTMFSFHPVKHITTG 202
Cdd:PRK06348  190 IAIEYDLFIISDEVYD-GFSFYEDFV----PMATLAGMPERTITFG 230
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 52-172 2.88e-10

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: 61.20  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  52 FEEAIAKYVGAKYA-------VSFSNGTAALHAACYAAGITEGDEVITTPMTFVASANCILYQGAKPVFADIDNE-TYNI 123
Cdd:cd00609    41 LREAIAEWLGRRGGvdvppeeIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLL 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2212027142 124 SPKSIEEKITNKTKAIIPVHF---TGQ---PVELEAIKKIAKKNNLIIIEDAAHA 172
Cdd:cd00609   121 DLELLEAAKTPKTKLLYLNNPnnpTGAvlsEEELEELAELAKKHGILIISDEAYA 175
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
31-175 2.57e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 51.92  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  31 IQAVVDVL-KGDFLTTGPMV--QQFEEAIAKYVG--------AKYAVSFSNGTAALHAACYAAGITEGDEVITTPMTFVA 99
Cdd:pfam00155  20 AKAEKDALaGGTRNLYGPTDghPELREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPAPTYAS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 100 SANCILYQGAKPV-FADIDNETYNISPKSIEEKITNKTKAII---PVHFTGQ---PVELEAIKKIAKKNNLIIIEDAAHA 172
Cdd:pfam00155 100 YIRIARLAGGEVVrYPLYDSNDFHLDFDALEAALKEKPKVVLhtsPHNPTGTvatLEELEKLLDLAKEHNILLLVDEAYA 179


                  ...
gi 2212027142 173 LGA 175
Cdd:pfam00155 180 GFV 182
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 49-210 6.13e-07

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: 48.92  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  49 VQQFEEAIAKY--VGAKYAVSFSNGTAALHAACYAAGITeGDEVITTPMTFVAS-ANCILYQGAKPVFADIDNETYNISP 125
Cdd:cd01494     2 LEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGP-GDEVIVDANGHGSRyWVAAELAGAKPVPVPVDDAGYGGLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 126 KSIEE--KITNKTKAIIPVHFTGQP---VELEAIKKIAKKNNLIIIEDAAHALGATYKNKKIGSIG--DMTMFSFHpvKH 198
Cdd:cd01494    81 VAILEelKAKPNVALIVITPNTTSGgvlVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGgaDVVTFSLH--KN 158

                         170
                  ....*....|..
gi 2212027142 199 ITTGEGGVITTN 210
Cdd:cd01494   159 LGGEGGGVVIVK 170
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
50-174 8.64e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.52  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  50 QQFEEA---IAKYVGAK--YAVSFSNGTaalhaacyaagiTE--------------GDEVITTPM----TFVASANCILY 106
Cdd:COG0520    59 DAYEAArekVARFIGAAspDEIIFTRGT------------TEainlvayglgrlkpGDEILITEMehhsNIVPWQELAER 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2212027142 107 QGAKPVFADIDnETYNISPKSIEEKITNKTKAIIPVH---FTGQPVELEAIKKIAKKNNLIIIEDAAHALG 174
Cdd:COG0520   127 TGAEVRVIPLD-EDGELDLEALEALLTPRTKLVAVTHvsnVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
86-168 9.08e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 50.62  E-value: 9.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  86 EGDEVITtPMTFVASANCIL-YQGAK--PVFADIDNeTYNISPKS-IEEKITNKTKAII---PVHFTG---QPVELEAIK 155
Cdd:PRK07568  111 PGDEILV-PEPFYANYNGFAtSAGVKivPVTTKIEE-GFHLPSKEeIEKLITPKTKAILisnPGNPTGvvyTKEELEMLA 188

                          90
                  ....*....|...
gi 2212027142 156 KIAKKNNLIIIED 168
Cdd:PRK07568  189 EIAKKHDLFLISD 201
PRK07683 PRK07683
aminotransferase A; Validated
 84-168 1.80e-06

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 49.72  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITEGDEVITTPMTFVASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAII---PVHFTGQPVELEAIKKIA-- 158
Cdd:PRK07683  110 LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRCVVlpyPSNPTGVTLSKEELQDIAdv 189

                          90
                  ....*....|.
gi 2212027142 159 -KKNNLIIIED 168
Cdd:PRK07683  190 lKDKNIFVLSD 200
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
41-168 2.12e-06

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 49.32  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  41 DFLTTG-PMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAagITEGDEVIttpmtfvASANciLYQGAKPVFaDIDNE 119
Cdd:PRK08247   45 DYSRTGnPTRGVLEQAIADLEGGDQGFACSSGMAAIQLVMSL--FRSGDELI-------VSSD--LYGGTYRLF-EEHWK 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 120 TYNISP--------KSIEEKITNKTKAII---PVHFTGQPVELEAIKKIAKKNNLIIIED 168
Cdd:PRK08247  113 KWNVRFvyvntaslKAIEQAITPNTKAIFietPTNPLMQETDIAAIAKIAKKHGLLLIVD 172
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 86-174 1.03e-05

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: 47.08  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  86 EGDEVITTPM---------TFVASAncilyQGAKPVFADIDnETYNISPKSIEEKITNKTKAIIPVH---FTG--QPVel 151
Cdd:cd06453    87 PGDEIVTSVMehhsnivpwQQLAER-----TGAKLKVVPVD-DDGQLDLEALEKLLTERTKLVAVTHvsnVLGtiNPV-- 158

                          90       100
                  ....*....|....*....|...
gi 2212027142 152 EAIKKIAKKNNLIIIEDAAHALG 174
Cdd:cd06453   159 KEIGEIAHEAGVPVLVDGAQSAG 181
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
84-171 4.44e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 45.06  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITE-GDEVI-TTPMTF-----VASANCilyqgaKPVFADIDnETYNISPKSIEEKITNKTKAII---PVHFTG---QPVE 150
Cdd:PRK05957  109 ITDpGDEIIlNTPYYFnhemaITMAGC------QPILVPTD-DNYQLQPEAIEQAITPKTRAIVtisPNNPTGvvyPEAL 181

                          90       100
                  ....*....|....*....|.
gi 2212027142 151 LEAIKKIAKKNNLIIIEDAAH 171
Cdd:PRK05957  182 LRAVNQICAEHGIYHISDEAY 202
PRK08363 PRK08363
alanine aminotransferase; Validated
 84-189 1.34e-04

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 43.64  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITEGDEVITTPMTFVASANCILYQGAKPVFAD-IDNETYNISPKSIEEKITNKTKAII---PVHFTGQPVE---LEAIKK 156
Cdd:PRK08363  114 LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRtIEEEGWQPDIDDIRKKITEKTKAIAvinPNNPTGALYEkktLKEILD 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2212027142 157 IAKKNNLIIIEDAAHALgATYKNKKIgSIGDMT 189
Cdd:PRK08363  194 IAGEHDLPVISDEIYDL-MTYEGKHV-SPGSLT 224
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
47-193 1.71e-04

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 42.97  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  47 PMVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAgITEGDEVITTP---MTFVASANCILYQGAKPVFADIDnETYNI 123
Cdd:pfam01212  32 PTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICGEpahIHFDETGGHAELGGVQPRPLDGD-EAGNM 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 124 SPKSIEEKITNKTKAIIP----VHFT-------GQPV---ELEAIKKIAKKNNLIIIED------AAHALGATYknKKIG 183
Cdd:pfam01212 110 DLEDLEAAIREVGADIFPptglISLEnthnsagGQVVsleNLREIAALAREHGIPVHLDgarfanAAVALGVIV--KEIT 187

                         170
                  ....*....|
gi 2212027142 184 SIGDMTMFSF 193
Cdd:pfam01212 188 SYADSVTMCL 197
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 50-174 2.25e-04

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 43.00  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  50 QQFEEA---IAKYVGAKYA--VSFSNGT---AALHAACYAAGITEGDEVITTPM----TFVASANCILYQGAKPVFADID 117
Cdd:pfam00266  43 QAYEEArekVAEFINAPSNdeIIFTSGTteaINLVALSLGRSLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLD 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212027142 118 nETYNISPKSIEEKITNKTKAiipVHFTG--------QPVEleAIKKIAKKNNLIIIEDAAHALG 174
Cdd:pfam00266 123 -EDGLLDLDELEKLITPKTKL---VAITHvsnvtgtiQPVP--EIGKLAHQYGALVLVDAAQAIG 181
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 5-171 4.73e-04

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: 41.85  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142   5 ILGIHGGKPVRETYLPYGQQQIDEYDIQAVVDVlkGDFLT-TGPmVQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAG 83
Cdd:cd00615    19 VPGHKGGRGFRKSFYEFYGENLFKADVTELTGL--DDLLDpTGP-IKEAQELAARAFGAKHTFFLVNGTSSSNKAVILAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  84 ITEGDEVITtpmtfvaSANC-------ILYQGAKPVF--ADIDNET---YNISPKSIEEKITNKTKA----IIPVHFTGQ 147
Cdd:cd00615    96 CGPGDKILI-------DRNChksvingLVLSGAVPVYlkPERNPYYgiaGGIPPETFKKALIEHPDAkaavITNPTYYGI 168

                         170       180
                  ....*....|....*....|....
gi 2212027142 148 PVELEAIKKIAKKNNLIIIEDAAH 171
Cdd:cd00615   169 CYNLRKIVEEAHHRGLPVLVDEAH 192
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
87-159 1.08e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 40.95  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2212027142  87 GDEVITTPMTFVASANCILYQGAKPVFADIDNETYNISPKSIEEKITNKTKAII---PVHFTGQPVELEAIKKIAK 159
Cdd:PRK06836  120 GDEVIVFAPYFVEYRFYVDNHGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVIinsPNNPTGVVYSEETLKALAA 195
PRK13355 PRK13355
bifunctional HTH-domain containing protein/aminotransferase; Provisional
 87-168 1.18e-03

bifunctional HTH-domain containing protein/aminotransferase; Provisional


Pssm-ID: 237361 [Multi-domain]  Cd Length: 517  Bit Score: 40.88  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  87 GDEVITtPMT----FVASANcilYQGAKPV--FADIDNETYnisP--KSIEEKITNKTKAII---PVHFTGQ--PVE-LE 152
Cdd:PRK13355  232 GDEVLI-PSPdyplWTACVN---LAGGTAVhyRCDEQSEWY---PdiDDIRSKITSRTKAIViinPNNPTGAlyPREvLQ 304

                          90
                  ....*....|....*.
gi 2212027142 153 AIKKIAKKNNLIIIED 168
Cdd:PRK13355  305 QIVDIAREHQLIIFSD 320
PRK12414 PRK12414
putative aminotransferase; Provisional
 47-168 1.30e-03

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 40.54  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  47 PM--VQQFEEAIAKYVGAKYAVSFSNGTAALHAACYAAGITE--------GDEVITTPMTFVASANCILYQGAKPVFADI 116
Cdd:PRK12414   64 PMagIAALREALAEKTERLYGARYDPASEVTVIASASEGLYAaisalvhpGDEVIYFEPSFDSYAPIVRLQGATPVAIKL 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2212027142 117 DNETYNISPKSIEEKITNKTKAII---PVHFTGQPV---ELEAIKKIAKKNNLIIIED 168
Cdd:PRK12414  144 SPEDFRVNWDEVAAAITPRTRMIIvntPHNPSATVFsaaDLARLAQLTRNTDIVILSD 201
PRK06290 PRK06290
LL-diaminopimelate aminotransferase;
49-180 1.67e-03

LL-diaminopimelate aminotransferase;


Pssm-ID: 235772  Cd Length: 410  Bit Score: 40.41  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  49 VQQFEEAIAKYVGAKYAVSFSN---------GTAALHAACYAAGITEGDEVI-TTPMTFVASANCILYQGakpvfadidn 118
Cdd:PRK06290   83 IQEFKEAAARYMEKVFGVKDIDpvtevihsiGSKPALAMLPSCFINPGDVTLmTVPGYPVTGTHTKYYGG---------- 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212027142 119 ETYNIS--------P--KSIEEKITNKTKAII---PVHFTGQPVELEAIKK---IAKKNNLIIIEDAAHAlGATYKNK 180
Cdd:PRK06290  153 EVYNLPlleennflPdlDSIPKDIKEKAKLLYlnyPNNPTGAVATKEFYEEvvdFAKENNIIVVQDAAYA-ALTFDGK 229
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 49-168 1.72e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 40.25  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  49 VQQFEEAIAKYVGAKYAVSFS-------NGTAALHAACYAAGITEGDEVITTPMTFVASANCILYQGAKPVFADIDNET- 120
Cdd:PRK08361   72 IPELREAIAEYYKKFYGVDVDvdnvivtAGAYEATYLAFESLLEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENe 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2212027142 121 YNISPKSIEEKITNKTKAII---PVHFTGQPVELE---AIKKIAKKNNLIIIED 168
Cdd:PRK08361  152 FQPDPDELLELITKRTRMIVinyPNNPTGATLDKEvakAIADIAEDYNIYILSD 205
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 47-222 4.34e-03

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: 39.11  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  47 PMVQQFEEAIAKYVGAKYAVSFSNGTaalhaacyaAGIT--------EGDEVittpmtfVASANCilYQGAKPVFADIDN 118
Cdd:cd00614    40 PTVDALEKKLAALEGGEAALAFSSGM---------AAIStvllallkAGDHV-------VASDDL--YGGTYRLFERLLP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142 119 EtYNIS--------PKSIEEKITNKTKAII---PVHFTGQPVELEAIKKIAKKNNLIIIEDAAHA---------LGATY- 177
Cdd:cd00614   102 K-LGIEvtfvdpddPEALEAAIKPETKLVYvesPTNPTLKVVDIEAIAELAHEHGALLVVDNTFAtpylqrpleLGADIv 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2212027142 178 ---KNKKIGSIGDMTmfsfhpvkhittgeGGVITTNNPLFYEKLVQFR 222
Cdd:cd00614   181 vhsATKYIGGHSDVI--------------AGVVVGSGEALIQRLRFLR 214
PRK09265 PRK09265
aminotransferase AlaT; Validated
 87-168 5.70e-03

aminotransferase AlaT; Validated


Pssm-ID: 181738  Cd Length: 404  Bit Score: 38.64  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212027142  87 GDEVITtPM------TFVASANcilyqGAKPV----------FADIDNetynispksIEEKITNKTKAII---PVHFTGQ 147
Cdd:PRK09265  119 GDEVLV-PApdyplwTAAVSLS-----GGKPVhylcdeeagwFPDLDD---------IRSKITPRTKAIViinPNNPTGA 183

                          90       100
                  ....*....|....*....|....
gi 2212027142 148 --PVE-LEAIKKIAKKNNLIIIED 168
Cdd:PRK09265  184 vySKElLEEIVEIARQHNLIIFAD 207
 
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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