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Conserved domains on  [gi|2221393024|gb|UOO12014|]
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DegT/DnrJ/EryC1/StrS family aminotransferase [Synechocystis sp. PCC 6803]

Protein Classification

DegT/DnrJ/EryC1/StrS family aminotransferase( domain architecture ID 11111798)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 11-365 1.37e-174

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: 490.26  E-value: 1.37e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWGDRcYEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTNWIATVA 90
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  91 PIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSVYHGKRA 170
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 171 GSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQTKQFWADMVGFKYKMSNIQAAIGCAQMERIEE 250
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 251 LVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVLFKEANVDARVFFW-PLSSLSMFDD 329
Cdd:pfam01041 240 FIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEAINRDELVEALKEAGIGTRVHYPiPLHLQPYYRD 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2221393024 330 KPTNK-----LAWDIPTRAINLPSYHDLSGKDIKQVIDSMT 365
Cdd:pfam01041 320 LFGYApgdlpNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
 
Name Accession Description Interval E-value
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 11-365 1.37e-174

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: 490.26  E-value: 1.37e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWGDRcYEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTNWIATVA 90
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  91 PIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSVYHGKRA 170
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 171 GSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQTKQFWADMVGFKYKMSNIQAAIGCAQMERIEE 250
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 251 LVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVLFKEANVDARVFFW-PLSSLSMFDD 329
Cdd:pfam01041 240 FIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEAINRDELVEALKEAGIGTRVHYPiPLHLQPYYRD 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2221393024 330 KPTNK-----LAWDIPTRAINLPSYHDLSGKDIKQVIDSMT 365
Cdd:pfam01041 320 LFGYApgdlpNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-363 2.04e-154

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: 438.51  E-value: 2.04e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  17 EVEYATDAARNGW---GdrcyEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTNWIATVAPIV 93
Cdd:cd00616     1 ELEAVEEVLDSGWltlG----PKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  94 HLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSVYHGKRAGSM 173
Cdd:cd00616    77 LLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 174 GKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQtKQFWADMVGFKYKMSNIQAAIGCAQMERIEELVS 253
Cdd:cd00616   157 GDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDR-FKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 254 RKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVLFKEANVDARVFFWPLSSLSMFDDKP-- 331
Cdd:cd00616   236 RRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLgy 315

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2221393024 332 ---TNKLAWDIPTRAINLPSYHDLSGKDIKQVIDS 363
Cdd:cd00616   316 ppgDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEA 350
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-366 8.53e-154

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 437.58  E-value: 8.53e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   5 RIYYTKPSITELEVEYATDAARNGW---GdrcyEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILA 81
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWltlG----PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  82 DTNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAI 161
Cdd:COG0399    77 AFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 162 GSVYHGKRAGSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQtkQFWADMVGFKYKMSNIQAAIG 241
Cdd:COG0399   157 GATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA--KYEHVELGYNYRMDELQAAIG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 242 CAQMERIEELVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFspESGITREKLQVLFKEANVDARV-FFWP 320
Cdd:COG0399   235 LAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRL--DEGEDRDELIAALKARGIGTRVhYPIP 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2221393024 321 LSSLSMFDDKPTNKL----AWDIPTRAINLPSYHDLSGKDIKQVIDSMTD 366
Cdd:COG0399   313 LHLQPAYRDLGYRPGdlpvAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 6-368 3.29e-85

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: 263.42  E-value: 3.29e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   6 IYYTKPSITELEVEYATDAARNGW---GDRcyeyIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILAD 82
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFltqGPT----VPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAIT----PRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAA 158
Cdd:TIGR03588  77 ITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDAS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 159 EAIGSVYHGKRAGSmGKFGS---FSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRAR-------GQTKQFWADMV- 227
Cdd:TIGR03588 157 HALGAEYGGKPVGN-CRYADatvFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdpllfekQDEGPWYYEQQe 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 228 -GFKYKMSNIQAAIGCAQMERIEELVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVL 306
Cdd:TIGR03588 236 lGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEA 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221393024 307 FKEANVDARVFFWPLSSLS----MFDDKPTnKLAWDIPTRAINLPSYHDLSGKDIKQVIDSMTDNL 368
Cdd:TIGR03588 316 LRAAGIGVQVHYIPVHLQPyyrqGFGDGDL-PSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
8-270 4.23e-79

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 247.63  E-value: 4.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   8 YTKPSITELEVEYATDAARNGW---GDRCYEyivrFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTN 84
Cdd:PRK11658    7 FSRPAMGDEELAAVKEVLRSGWittGPKNQA----LEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  85 WIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSV 164
Cdd:PRK11658   83 WVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 165 YHGKRAGSMGKfGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHG--------RARGQTKQfwADMV--GFKYKMS 234
Cdd:PRK11658  163 YKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGlgvdafdrQTQGRAPQ--AEVLtpGYKYNLA 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2221393024 235 NIQAAIGCAQMERIEELVSRKREILSYYKENLESLP 270
Cdd:PRK11658  240 DINAAIALVQLAKLEALNARRREIAARYLQALADLP 275
 
Name Accession Description Interval E-value
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 11-365 1.37e-174

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: 490.26  E-value: 1.37e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWGDRcYEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTNWIATVA 90
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLTT-GPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFVATAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  91 PIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSVYHGKRA 170
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 171 GSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQTKQFWADMVGFKYKMSNIQAAIGCAQMERIEE 250
Cdd:pfam01041 160 GTLGDAATFSFHPTKNLTTGEGGAVVTNDPELAEKARVLRNHGMVRKADKRYWHEVLGYNYRMTEIQAAIGLAQLERLDE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 251 LVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVLFKEANVDARVFFW-PLSSLSMFDD 329
Cdd:pfam01041 240 FIARRREIAALYQTLLADLPGFTPLTTPPEADVHAWHLFPILVPEEAINRDELVEALKEAGIGTRVHYPiPLHLQPYYRD 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2221393024 330 KPTNK-----LAWDIPTRAINLPSYHDLSGKDIKQVIDSMT 365
Cdd:pfam01041 320 LFGYApgdlpNAEDISSRVLSLPLYPGLTDEDVDRVVEAVR 360
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 17-363 2.04e-154

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: 438.51  E-value: 2.04e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  17 EVEYATDAARNGW---GdrcyEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTNWIATVAPIV 93
Cdd:cd00616     1 ELEAVEEVLDSGWltlG----PKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  94 HLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSVYHGKRAGSM 173
Cdd:cd00616    77 LLGATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 174 GKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQtKQFWADMVGFKYKMSNIQAAIGCAQMERIEELVS 253
Cdd:cd00616   157 GDAGAFSFHPTKNLTTGEGGAVVTNDEELAERARLLRNHGRDRDR-FKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 254 RKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVLFKEANVDARVFFWPLSSLSMFDDKP-- 331
Cdd:cd00616   236 RRREIAERYKELLADLPGIRLPDVPPGVKHSYHLYVIRLDPEAGESRDELIEALKEAGIETRVHYPPLHHQPPYKKLLgy 315

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2221393024 332 ---TNKLAWDIPTRAINLPSYHDLSGKDIKQVIDS 363
Cdd:cd00616   316 ppgDLPNAEDLAERVLSLPLHPSLTEEEIDRVIEA 350
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
5-366 8.53e-154

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 437.58  E-value: 8.53e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   5 RIYYTKPSITELEVEYATDAARNGW---GdrcyEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILA 81
Cdd:COG0399     1 MIPLSRPSIGEEEIAAVVEVLRSGWltlG----PEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  82 DTNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAI 161
Cdd:COG0399    77 AFTFVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQAL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 162 GSVYHGKRAGSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRARGQtkQFWADMVGFKYKMSNIQAAIG 241
Cdd:COG0399   157 GATYKGKKVGTFGDAGCFSFYPTKNLTTGEGGAVVTNDEELAERARSLRNHGRDRDA--KYEHVELGYNYRMDELQAAIG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 242 CAQMERIEELVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFspESGITREKLQVLFKEANVDARV-FFWP 320
Cdd:COG0399   235 LAQLKRLDEFIARRRAIAARYREALADLPGLTLPKVPPGAEHVYHLYVIRL--DEGEDRDELIAALKARGIGTRVhYPIP 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2221393024 321 LSSLSMFDDKPTNKL----AWDIPTRAINLPSYHDLSGKDIKQVIDSMTD 366
Cdd:COG0399   313 LHLQPAYRDLGYRPGdlpvAERLAERVLSLPLHPGLTEEDVDRVIEAIRE 362
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 6-368 3.29e-85

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: 263.42  E-value: 3.29e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   6 IYYTKPSITELEVEYATDAARNGW---GDRcyeyIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILAD 82
Cdd:TIGR03588   1 LPYGRQSIDQDDIDAVVEVLKSDFltqGPT----VPAFEEALAEYVGAKYAVAFNSATSALHIACLALGVGPGDRVWTTP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAIT----PRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAA 158
Cdd:TIGR03588  77 ITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAaakgKLPKAIVPVDFAGKSVDMQAIAALAKKHGLKIIEDAS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 159 EAIGSVYHGKRAGSmGKFGS---FSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGRAR-------GQTKQFWADMV- 227
Cdd:TIGR03588 157 HALGAEYGGKPVGN-CRYADatvFSFHPVKIITTAEGGAVTTNDEELAERMRLLRSHGITKdpllfekQDEGPWYYEQQe 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 228 -GFKYKMSNIQAAIGCAQMERIEELVSRKREILSYYKENLESLPGITMNPEPKGMVNGGWMPTAVFSPESGITREKLQVL 306
Cdd:TIGR03588 236 lGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLKDLPYFTPLTIPLGSKSAWHLYPILLDQEFGCTRKEVFEA 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221393024 307 FKEANVDARVFFWPLSSLS----MFDDKPTnKLAWDIPTRAINLPSYHDLSGKDIKQVIDSMTDNL 368
Cdd:TIGR03588 316 LRAAGIGVQVHYIPVHLQPyyrqGFGDGDL-PSAENFYLAEISLPLHPALTLEQQQRVVETLRKVL 380
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
8-270 4.23e-79

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 247.63  E-value: 4.23e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   8 YTKPSITELEVEYATDAARNGW---GDRCYEyivrFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILADTN 84
Cdd:PRK11658    7 FSRPAMGDEELAAVKEVLRSGWittGPKNQA----LEQAFCQLTGNQHAIAVSSATAGMHITLMALGIGPGDEVITPSLT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  85 WIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIGSV 164
Cdd:PRK11658   83 WVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAHAVGTY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 165 YHGKRAGSMGKfGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHG--------RARGQTKQfwADMV--GFKYKMS 234
Cdd:PRK11658  163 YKGRHIGARGT-AIFSFHAIKNITCAEGGLVVTDDDELADRLRSLKFHGlgvdafdrQTQGRAPQ--AEVLtpGYKYNLA 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2221393024 235 NIQAAIGCAQMERIEELVSRKREILSYYKENLESLP 270
Cdd:PRK11658  240 DINAAIALVQLAKLEALNARRREIAARYLQALADLP 275
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 5-366 5.66e-72

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 229.34  E-value: 5.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   5 RIYYTKPSITELEVEYATDAARNG--WGD-----RCyeyivrfEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDE 77
Cdd:PRK11706    1 MIPFNKPPVVGTELDYIQQAMSSGklCGDggftrRC-------QQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  78 VILADTNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDA 157
Cdd:PRK11706   74 VIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 158 AEAIGSVYHGKRAGSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYEtvltlsnhgRA--------------RGQT-KQF 222
Cdd:PRK11706  154 AQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGEGGALLINDPALIE---------RAeiirekgtnrsqffRGQVdKYT 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 223 WADmVGFKYKMSNIQAAIGCAQMERIEELVSRKREILSYYKENLESL--PGITMNPE-PKGMVNGGWMPTAVFSPESgiT 299
Cdd:PRK11706  225 WVD-IGSSYLPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPLaeAGRIELPSiPDDCKHNAHMFYIKLRDLE--D 301

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221393024 300 REKLQVLFKEANVDArVFFW-PLSSLSMF--------DDKPTNKLAWdiptRAINLPSYHDLSGKDIKQVIDSMTD 366
Cdd:PRK11706  302 RSALINFLKEAGIMA-VFHYiPLHSSPAGerfgrfhgEDRYTTKESE----RLLRLPLFYNLTDVEQRTVIDTILE 372
ECA_wecE TIGR02379
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ...
 5-366 1.17e-60

TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of TDP-4-keto-6-deoxy-D-glucose transaminases, the WecE (formerly RffA) protein of enterobacterial common antigen (ECA) biosynthesis, from enterobacteria. It also includes closely matching sequence from species not expected to make ECA, but which contain other genes for the biosynthesis of TDP-4-keto-6-deoxy-D-Glc, an intermediate in the biosynthesis of other compounds as well and the substrate of WecA. This family belongs to the DegT/DnrJ/EryC1/StrS aminotransferase family (pfam01041). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131432  Cd Length: 376  Bit Score: 200.05  E-value: 1.17e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   5 RIYYTKPSITELEVEYATDAARNG--WGDRcyEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGIGPGDEVILAD 82
Cdd:TIGR02379   1 MIPFNKPPVTGTELDYIQEAISSGklSGDG--PFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGIPIIEDAAEAIG 162
Cdd:TIGR02379  79 YTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 163 SVYHGKRAGSMGKFGSFSFHGTKTLTTG-EGGMFVTNDPDLYETVLTLSNHGRARGQ------TKQFWADmVGFKYKMSN 235
Cdd:TIGR02379 159 STYKGRALGSIGHIGTFSFHETKNYTSGgEGGALLINDQAFIERAEIIREKGTNRSQffrgevDKYTWRD-IGSSYLPSE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 236 IQAAIGCAQMERIEELVSRKREILSYYKENLESL--PGITMNPE-PKGMVNGGWMPTAVFSPEsgITREKLQVLFKEANV 312
Cdd:TIGR02379 238 LQAAYLWAQLEQADRINQQRLALWQNYYDALAPLeeKGIIELPSiPDGCQHNAHMFYIKLRDI--DDRSELINFLKEQEI 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221393024 313 DARVFFWPLSS------LSMF--DDKPTNKLAwdipTRAINLPSYHDLSGKDIKQVIDSMTD 366
Cdd:TIGR02379 316 MAVFHYIPLHSspagrhFGRFhgEDIYTTKES----ERLVRLPLFYGLSPEDQRRVIATLCD 373
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 3-318 1.06e-58

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 196.64  E-value: 1.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024   3 KSRIYYTKPSITELEVEYATDAARNGW---GdrcyEYIVRFEEVFKKYLGVEYSIATSSCTGA-LHMGMA----ALG--- 71
Cdd:PRK15407   32 KSPIPPSGKVIDAKELQNLVDASLDFWlttG----RFNDAFEKKLAEFLGVRYALLVNSGSSAnLLAFSAltspKLGdra 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  72 IGPGDEVILADTNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIVATHIYGNLCDMEALLAIEQRHGI 151
Cdd:PRK15407  108 LKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 152 PIIEDAAEAIGSVYHGKRAGSMGKFGSFSFHGTKTLTTGEGGMFVTNDPDLYETVLTLSNHGR----ARGQT----KQFW 223
Cdd:PRK15407  188 WLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAHHITMGEGGAVFTNDPLLKKIIESFRDWGRdcwcAPGCDntcgKRFG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 224 ADM---------------VGFKYKMSNIQAAIGCAQMERIEELVSRKREILSYYKENLES------LPGITMNPEPKgmv 282
Cdd:PRK15407  268 WQLgelpfgydhkytyshLGYNLKITDMQAAIGLAQLEKLPGFIEARKANFAYLKEGLASledfliLPEATPNSDPS--- 344

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2221393024 283 nggW--MPTAVfSPESGITREKLQVLFKEANVDARVFF 318
Cdd:PRK15407  345 ---WfgFPITV-KEDAGFTRVELVKYLEENKIGTRLLF 378
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 44-180 1.02e-16

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: 80.56  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  44 FKKYLGVEYS----IATSSCTGALHMGMAALgIGPGDEVILAD---TNWIATVApivHLGAKPVFVDILP-DSWCIDPVL 115
Cdd:COG0436    80 YKRRYGVDLDpdeiLVTNGAKEALALALLAL-LNPGDEVLVPDpgyPSYRAAVR---LAGGKPVPVPLDEeNGFLPDPEA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 116 AEQAITPRTKAIVathiygnLC-------------DMEALLAIEQRHGIPIIEDAA-EAIgsVYHGKRAGSMGK------ 175
Cdd:COG0436   156 LEAAITPRTKAIV-------LNspnnptgavysreELEALAELAREHDLLVISDEIyEEL--VYDGAEHVSILSlpglkd 226


                  ....*....
gi 2221393024 176 ----FGSFS 180
Cdd:COG0436   227 rtivINSFS 235
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 40-198 1.10e-14

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: 71.26  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  40 FEEVFKKYL--GVEYSIATSSCTGALHMGMAALGiGPGDEVILADTNWIA-TVAPIVHLGAKPVFVDILPDSWCIDPV-- 114
Cdd:cd01494     5 LEEKLARLLqpGNDKAVFVPSGTGANEAALLALL-GPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVDDAGYGGLDVai 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 115 LAEQAITPRTKAIVATHIYGNLCDMEALLAIEQ---RHGIPIIEDAAEAIGSVYHGKRAGSMGKFGSFSFHGTKTLTTGE 191
Cdd:cd01494    84 LEELKAKPNVALIVITPNTTSGGVLVPLKEIRKiakEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEG 163


                  ....*..
gi 2221393024 192 GGMFVTN 198
Cdd:cd01494   164 GGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 11-281 3.97e-14

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 72.76  E-value: 3.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWGDrcYEYIVRFEEVFKKYLGVEYS--------IATSSCTGALHMGMAALgIGPGDEVILAD 82
Cdd:cd00609    14 PEVLEALAAAALRAGLLGYYP--DPGLPELREAIAEWLGRRGGvdvppeeiVVTNGAQEALSLLLRAL-LNPGDEVLVPD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWIATVAPIVHLGAKPVFVDILPD-SWCIDPVLAEQAITPRTKAIVathiygnLC-------------DMEALLAIEQR 148
Cdd:cd00609    91 PTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKLLY-------LNnpnnptgavlseeELEELAELAKK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 149 HGIPIIEDaaEA-IGSVYHGKRAGSMGK---------FGSFSfhgtKTL-TTGE-GGMFVTNDPDLYEtvltlsnhgrar 216
Cdd:cd00609   164 HGILIISD--EAyAELVYDGEPPPALALldayervivLRSFS----KTFgLPGLrIGYLIAPPEELLE------------ 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 217 gqtkqFWADMVGFKYKMSNIQAAIGCAQM-----ERIEELVSRKREILSYYKENLESLPGITMNPEPKGM 281
Cdd:cd00609   226 -----RLKKLLPYTTSGPSTLSQAAAAAAlddgeEHLEELRERYRRRRDALLEALKELGPLVVVKPSGGF 290
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 44-174 1.73e-12

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 68.23  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  44 FKKYLGVEYS----IATSSCTGALHMGMAALgIGPGDEVILADTNWiATVAPIVHL-GAKPVFVDILPD-SWCIDPVLAE 117
Cdd:PRK05764   81 LKRDNGLDYDpsqvIVTTGAKQALYNAFMAL-LDPGDEVIIPAPYW-VSYPEMVKLaGGVPVFVPTGEEnGFKLTVEQLE 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2221393024 118 QAITPRTKAIVAT-------HIYgNLCDMEALLAIEQRHGIPIIEDaaEaI--GSVYHGKRAGSMG 174
Cdd:PRK05764  159 AAITPKTKALILNspsnptgAVY-SPEELEAIADVAVEHDIWVLSD--E-IyeKLVYDGAEFTSIA 220
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
44-156 4.13e-12

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 66.89  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  44 FKKYLGVEYSIATSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVHLGAKPVFVDILP--DSWCIDPVLAEQAIT 121
Cdd:PRK06108   78 HGVATPPERIAVTSSGVQALMLAAQAL-VGPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFggGGWTLDLDRLLAAIT 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2221393024 122 PRTKAI-----------VATHiygnlCDMEALLAIEQRHGIPIIED 156
Cdd:PRK06108  157 PRTRALfinspnnptgwTASR-----DDLRAILAHCRRHGLWIVAD 197
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
39-273 5.25e-12

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 66.70  E-value: 5.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  39 RFEEV---FKKYLGV--EYSIA-TSSCTGALHMGMAALG-IGPGDEVILADTNWIATVAPIVHL----GAKPVFVDILPD 107
Cdd:COG0520    60 AYEAArekVARFIGAasPDEIIfTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQELaertGAEVRVIPLDED 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 108 sWCIDPVLAEQAITPRTKAIVATHI---YGNLCDMEALLAIEQRHGIPIIEDAAEAIGsvyHGK---RAgsMGK-FGSFS 180
Cdd:COG0520   140 -GELDLEALEALLTPRTKLVAVTHVsnvTGTVNPVKEIAALAHAHGALVLVDGAQSVP---HLPvdvQA--LGCdFYAFS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 181 FHgtKTL-TTGEGGMFVtnDPDLYETVL-TLSNHGRARgqtkqfWADMVGFKYK---------MSNIQAAIGCAQ----- 244
Cdd:COG0520   214 GH--KLYgPTGIGVLYG--KRELLEALPpFLGGGGMIE------WVSFDGTTYAdlprrfeagTPNIAGAIGLGAaidyl 283

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2221393024 245 ----MERIEElvsRKREILSYYKENLESLPGIT 273
Cdd:COG0520   284 eaigMEAIEA---RERELTAYALEGLAAIPGVR 313
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 41-283 2.10e-09

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: 58.41  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  41 EEVFKKYLGVEYS---IATSSCTGALHM--GMAALGIGPGDEVILADTNWIATVAPIVHL----GAKPVFVDILPDsWCI 111
Cdd:pfam00266  49 REKVAEFINAPSNdeiIFTSGTTEAINLvaLSLGRSLKPGDEIVITEMEHHANLVPWQELakrtGARVRVLPLDED-GLL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 112 DPVLAEQAITPRTKAIVATH---IYGNLCDMEALLAIEQRHGIPIIEDAAEAIgsvyhGKRAGSMGKFGS--FSFHGTKT 186
Cdd:pfam00266 128 DLDELEKLITPKTKLVAITHvsnVTGTIQPVPEIGKLAHQYGALVLVDAAQAI-----GHRPIDVQKLGVdfLAFSGHKL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 187 L-TTGEGGMFVTND------PDLY--ETVLTLSNHGraRGQTKQFWadmvGFKYKMSNIQAAIGCAQ---------MERI 248
Cdd:pfam00266 203 YgPTGIGVLYGRRDllekmpPLLGggGMIETVSLQE--STFADAPW----KFEAGTPNIAGIIGLGAaleylseigLEAI 276

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2221393024 249 EElvsRKREILSYYKENLESLPGITMN--PEPKGMVN 283
Cdd:pfam00266 277 EK---HEHELAQYLYERLLSLPGIRLYgpERRASIIS 310
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 54-162 1.94e-08

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: 55.55  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  54 IATSSCTGALHMGMAALG--IGPGDEVILA----DTNWIatvaPIVHL----GAKPVFVDILPDSwCIDPVLAEQAITPR 123
Cdd:cd06453    65 IFTRNTTEAINLVAYGLGraNKPGDEIVTSvmehHSNIV----PWQQLaertGAKLKVVPVDDDG-QLDLEALEKLLTER 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221393024 124 TKAIVATHI---YGNLCDMEALLAIEQRHGIPIIEDAAEAIG 162
Cdd:cd06453   140 TKLVAVTHVsnvLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
PRK07682 PRK07682
aminotransferase;
12-156 1.05e-07

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 53.20  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  12 SITELEVEYATDAARNGwgdrcyeyIVRFEEVFKKYL----GVEYS-----IATSSCTGALHMGMAALgIGPGDEVILAD 82
Cdd:PRK07682   42 SIRSLEQGYTSYTANAG--------LLELRQEIAKYLkkrfAVSYDpndeiIVTVGASQALDVAMRAI-INPGDEVLIVE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWIAtVAPIVHL-GAKPVFVDI-LPDSWCIDPVLAEQAITPRTKAIV------ATHIYGNLCDMEALLAIEQRHGIPII 154
Cdd:PRK07682  113 PSFVS-YAPLVTLaGGVPVPVATtLENEFKVQPAQIEAAITAKTKAILlcspnnPTGAVLNKSELEEIAVIVEKHDLIVL 191


                  ..
gi 2221393024 155 ED 156
Cdd:PRK07682  192 SD 193
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
39-199 2.83e-07

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 51.45  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  39 RFEEVFKKYLGVEYSIATSSCTGALHMGMAALgIGPGDEVILADTNWI---ATVAPIVHLGAKPVFVDIlPDSWCIDPVL 115
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAH-CQRGDEVICGEPAHIhfdETGGHAELGGVQPRPLDG-DEAGNMDLED 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 116 AEQAIT-------PRTKAI---VATHIYG----NLCDMEALLAIEQRHGIPIIEDAA---EAigSVYHGKRAGSMGKFG- 177
Cdd:pfam01212 114 LEAAIRevgadifPPTGLIsleNTHNSAGgqvvSLENLREIAALAREHGIPVHLDGArfaNA--AVALGVIVKEITSYAd 191

                         170       180
                  ....*....|....*....|..
gi 2221393024 178 SFSFHGTKTLTTGEGGMFVTND 199
Cdd:pfam01212 192 SVTMCLSKGLGAPVGSVLAGSD 213
PRK08912 PRK08912
aminotransferase;
56-206 3.22e-07

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 51.90  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  56 TSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVHLGAKPVFVDILPDSWCIDPVLAEQAITPRTKAIV------- 128
Cdd:PRK08912   93 TSGATEALAAALLAL-VEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnplnp 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 129 ATHIYGnLCDMEALLAIEQRHGIPIIEDAA-EAIgsVYHGK----------------RAGSMGKfgSFSFHGTKtltTGe 191
Cdd:PRK08912  172 AGKVFP-REELALLAEFCQRHDAVAICDEVwEHV--VFDGRrhiplmtlpgmrertvKIGSAGK--IFSLTGWK---VG- 242

                         170
                  ....*....|....*
gi 2221393024 192 ggmFVTNDPDLYETV 206
Cdd:PRK08912  243 ---FVCAAPPLLRVL 254
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 53-156 4.00e-07

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 51.64  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  53 SIATSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVH----LGAKPVFVDilPDswciDPVLAEQAITPRTKAIV 128
Cdd:PRK05994   81 ALAVASGHAAQFLVFHTL-LQPGDEFIAARKLYGGSINQFGHafksFGWQVRWAD--AD----DPASFERAITPRTKAIF 153

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2221393024 129 ATHIY---GNLCDMEALLAIEQRHGIPIIED 156
Cdd:PRK05994  154 IESIAnpgGTVTDIAAIAEVAHRAGLPLIVD 184
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 39-156 4.53e-07

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: 51.43  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  39 RFEEVFKKYLGVEYSIATSSCTGALHMGMAALgIGPGDEVILADT------NWIATVAPIvhLGAKPVFVDilPDswciD 112
Cdd:cd00614    44 ALEKKLAALEGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDlyggtyRLFERLLPK--LGIEVTFVD--PD----D 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221393024 113 PVLAEQAITPRTKAIVA---THIYGNLCDMEALLAIEQRHGIPIIED 156
Cdd:cd00614   115 PEALEAAIKPETKLVYVespTNPTLKVVDIEAIAELAHEHGALLVVD 161
PRK08248 PRK08248
homocysteine synthase;
42-156 2.18e-06

homocysteine synthase;


Pssm-ID: 236201 [Multi-domain]  Cd Length: 431  Bit Score: 49.46  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  42 EVFKKYL----GVEYSIATSSCTGALHMGMAALGiGPGDEVILADTNWIATVAPIVH----LGAKPVFVDilpdswCIDP 113
Cdd:PRK08248   67 DVFEKRIaaleGGIGALAVSSGQAAITYSILNIA-SAGDEIVSSSSLYGGTYNLFAHtlpkLGITVKFVD------PSDP 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2221393024 114 VLAEQAITPRTKAIVATHI---YGNLCDMEALLAIEQRHGIPIIED 156
Cdd:PRK08248  140 ENFEAAITDKTKALFAETIgnpKGDVLDIEAVAAIAHEHGIPLIVD 185
PRK12414 PRK12414
putative aminotransferase; Provisional
 49-173 2.19e-06

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 49.02  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  49 GVEYSIATSSCTGaLHMGMAALgIGPGDEVILADTNWiATVAPIVHL-GAKPVFVDILPDSWCIDPVLAEQAITPRTKAI 127
Cdd:PRK12414   90 ASEVTVIASASEG-LYAAISAL-VHPGDEVIYFEPSF-DSYAPIVRLqGATPVAIKLSPEDFRVNWDEVAAAITPRTRMI 166

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2221393024 128 V-------ATHIYGNlCDMEALLAIEQRHGIPIIEDAA-EAIgsVYHGKRAGSM 173
Cdd:PRK12414  167 IvntphnpSATVFSA-ADLARLAQLTRNTDIVILSDEVyEHV--VFDGARHHSM 217
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 54-178 2.60e-06

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 48.88  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  54 IATSSCTGALHMGMAALGIgPGDEVILADTNW--IATVAPIVHLGAKPVfvDILPD-SWCIDPVLAEQAITPRTKAIVAT 130
Cdd:TIGR01265 100 VLTSGCSQAIEICIEALAN-PGANILVPRPGFplYDTRAAFSGLEVRLY--DLLPEkDWEIDLDGLESLADEKTVAIVVI 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2221393024 131 HIyGNLC-------DMEALLAIEQRHGIPIIEDAAEAiGSVYHGKRAGSMGKFGS 178
Cdd:TIGR01265 177 NP-SNPCgsvfsrdHLQKIAEVAEKLGIPIIADEIYG-HMVFGDAPFIPMASFAS 229
PRK08363 PRK08363
alanine aminotransferase; Validated
 35-280 3.93e-06

alanine aminotransferase; Validated


Pssm-ID: 181402  Cd Length: 398  Bit Score: 48.27  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  35 EYIVRFEevfKKYLGVEYS----IATSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVHLGAKPVFVDILP-DSW 109
Cdd:PRK08363   77 EAIVKRE---KRKNGVDITpddvRVTAAVTEALQLIFGAL-LDPGDEILIPGPSYPPYTGLVKFYGGVPVEYRTIEeEGW 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 110 CIDPVLAEQAITPRTKAIVA------THIYGNLCDMEALLAIEQRHGIPIIEDAA-EAIgsVYHGKRA--GSMGK----- 175
Cdd:PRK08363  153 QPDIDDIRKKITEKTKAIAVinpnnpTGALYEKKTLKEILDIAGEHDLPVISDEIyDLM--TYEGKHVspGSLTKdvpvi 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 176 -FGSFSfhgtKT-LTTGE--GGM-FVTNDPDLYETVLTLSNHGRARGQTK---QFWAdmvgfkykmsnIQAAIGcaQMER 247
Cdd:PRK08363  231 vMNGLS----KVyFATGWrlGYIyFVDPEGKLAEVREAIDKLARIRLCPNtpaQFAA-----------IAGLTG--PMDY 293

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2221393024 248 IEELVSRKREILSYYKENLESLPGITmNPEPKG 280
Cdd:PRK08363  294 LEEYMKKLKERRDYIYKRLNEIPGIS-TTKPQG 325
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
11-172 8.86e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 47.30  E-value: 8.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWGDrcYEYIVRFEEVFKKYLG--------VEYSIATSSCTGALHMGMAALGIGPGDEVILAD 82
Cdd:pfam00155  17 PAVAKAEKDALAGGTRNLYGP--TDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEALIFLLANPGDAILVPA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  83 TNWiATVAPIVHL-GAKPVFVDIL-PDSWCIDPVLAEQAITPRTKAIVATHIY---G---NLCDMEALLAIEQRHGIPII 154
Cdd:pfam00155  95 PTY-ASYIRIARLaGGEVVRYPLYdSNDFHLDFDALEAALKEKPKVVLHTSPHnptGtvaTLEELEKLLDLAKEHNILLL 173

                         170
                  ....*....|....*...
gi 2221393024 155 EDAAEAIGsVYHGKRAGS 172
Cdd:pfam00155 174 VDEAYAGF-VFGSPDAVA 190
PRK07550 PRK07550
aminotransferase;
11-156 1.40e-05

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 46.49  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  11 PSITELEVEYATDAARNGWG------DRCYEYIVRFEEVFKKYLGVEYSIATSSCTGALHMGMAALGiGPGDEVILadTN 84
Cdd:PRK07550   45 PELLRALAEAAADPAAHLYGpveglpELREAYAAHYSRLYGAAISPEQVHITSGCNQAFWAAMVTLA-GAGDEVIL--PL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  85 --------WIATvapivhLGAKPVFVDILPDSWCI-DPVLAEQAITPRTKAIV--------ATHIYGNLcdMEALLAIEQ 147
Cdd:PRK07550  122 pwyfnhkmWLDM------LGIRPVYLPCDEGPGLLpDPAAAEALITPRTRAIAlvtpnnptGVVYPPEL--LHELYDLAR 193


                  ....*....
gi 2221393024 148 RHGIPIIED 156
Cdd:PRK07550  194 RHGIALILD 202
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
 54-156 2.40e-05

tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273529 [Multi-domain]  Cd Length: 401  Bit Score: 45.93  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  54 IATSSCTGALHMGMAALGiGPGDEVILADTNW--IATVAPIVHLGAKPVfvDILPD-SWCIDPVLAEQAITPRTKAIVAT 130
Cdd:TIGR01264  99 VLCSGCSHAIEMCIAALA-NAGQNILVPRPGFplYETLAESMGIEVKLY--NLLPDkSWEIDLKQLESLIDEKTAALIVN 175

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2221393024 131 HIyGNLC-------DMEALLAIEQRHGIPIIED 156
Cdd:TIGR01264 176 NP-SNPCgsvfsrqHLEEILAVAERQCLPIIAD 207
PRK07683 PRK07683
aminotransferase A; Validated
 45-128 2.83e-05

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 45.87  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  45 KKYlGVEYS-----IATSSCTGALHMGMAALgIGPGDEVILAdtnwiATV----APIVHL-GAKPVFVDILPDSWCIDPV 114
Cdd:PRK07683   80 DKY-DLHYSpeseiIVTIGASEAIDIAFRTI-LEPGTEVILP-----APIypgyEPIIRLcGAKPVFIDTRSTGFRLTAE 152

                          90
                  ....*....|....
gi 2221393024 115 LAEQAITPRTKAIV 128
Cdd:PRK07683  153 ALENAITEKTRCVV 166
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
41-128 3.40e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 45.48  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  41 EEVFKKYL-GVEYSIATSSC---TGALH-MGMAALGI-GPGDEVILADTNWIATVAPIVHLGAKPVFVDILP-DSWCIDP 113
Cdd:PRK06348   73 EEIIKYYSkNYDLSFKRNEImatVGACHgMYLALQSIlDPGDEVIIHEPYFTPYKDQIEMVGGKPIILETYEeDGFQINV 152

                          90
                  ....*....|....*
gi 2221393024 114 VLAEQAITPRTKAIV 128
Cdd:PRK06348  153 KKLEALITSKTKAII 167
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 56-190 3.88e-05

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 45.59  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  56 TSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVHLGAKPVFVDILPDSWCIDpVLAEQAITPRTKAIVAT--HIY 133
Cdd:COG1167   176 TSGAQQALDLALRAL-LRPGDTVAVESPTYPGALAALRAAGLRLVPVPVDEDGLDLD-ALEAALRRHRPRAVYVTpsHQN 253

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2221393024 134 --GNLCDME---ALLAIEQRHGIPIIEDAAEAiGSVYHGKRAGSMGKF---------GSFSfhgtKTLTTG 190
Cdd:COG1167   254 ptGATMSLErrrALLELARRHGVPIIEDDYDS-ELRYDGRPPPPLAALdapgrviyiGSFS----KTLAPG 319
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
49-153 9.35e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 44.03  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  49 GVEYS----IATSSCTGALHMGMAALgIGPGDEVIladtnwiaTVAP--------IVHLGAKPVFVDILPDSWCIDPVLA 116
Cdd:PRK06836   91 GTPLTadhiVMTCGAAGALNVALKAI-LNPGDEVI--------VFAPyfveyrfyVDNHGGKLVVVPTDTDTFQPDLDAL 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2221393024 117 EQAITPRTKAIVATH-------IYG--NLCDMEALL-AIEQRHGIPI 153
Cdd:PRK06836  162 EAAITPKTKAVIINSpnnptgvVYSeeTLKALAALLeEKSKEYGRPI 208
PRK09082 PRK09082
methionine aminotransferase; Validated
 56-156 2.24e-04

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 42.98  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  56 TSSCTGALHMGMAALgIGPGDEVILADTNWiATVAPIVHL-GAKPVFVDILPDSWCIDPVLAEQAITPRTKAIV------ 128
Cdd:PRK09082   97 TAGATEALFAAILAL-VRPGDEVIVFDPSY-DSYAPAIELaGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIlntphn 174

                          90       100       110
                  ....*....|....*....|....*....|
gi 2221393024 129 --ATHIYGNlcDMEALLAIEQRHGIPIIED 156
Cdd:PRK09082  175 psGTVWSAA--DMRALWQLIAGTDIYVLSD 202
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
68-158 3.29e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 42.37  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  68 AALGI-GPGDEVILADTNWIATVAPIVHLGAKPVFVDIlPDSWCIDPVLAEQAITPRTKAIVATH-------IYGnlcdm 139
Cdd:PRK05957  105 AILAItDPGDEIILNTPYYFNHEMAITMAGCQPILVPT-DDNYQLQPEAIEQAITPKTRAIVTISpnnptgvVYP----- 178

                          90       100
                  ....*....|....*....|...
gi 2221393024 140 EALLA----IEQRHGIPIIEDAA 158
Cdd:PRK05957  179 EALLRavnqICAEHGIYHISDEA 201
am_tr_V_VC1184 TIGR01976
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ...
 71-160 4.68e-04

cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273906 [Multi-domain]  Cd Length: 397  Bit Score: 42.05  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  71 GIGPGDEVILADTNWIATVAPIVHL----GAKPVFVDILPDSWCIDPVLAEQAITPRTKAI---VATHIYGNLCDMEALL 143
Cdd:TIGR01976 100 RWGPGDEVIVTRLDHEANISPWLQAaeraGAKVKWARVDEATGELHPDDLASLLSPRTRLVavtAASNTLGSIVDLAAIT 179

                          90
                  ....*....|....*..
gi 2221393024 144 AIEQRHGIPIIEDAAEA 160
Cdd:TIGR01976 180 ELVHAAGALVVVDAVHY 196
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
35-176 3.23e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 39.45  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  35 EYIVRFEEVFKKYlGVEYS----IATSSCTGALHMGMAALgIGPGDEVIL-----ADTNWIATVApivhlGAK--PVFVD 103
Cdd:PRK07568   70 ELREAFAKYYKKW-GIDVEpdeiLITNGGSEAILFAMMAI-CDPGDEILVpepfyANYNGFATSA-----GVKivPVTTK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024 104 I-----LPDSWCIdpvlaEQAITPRTKAIvathIYGNLC----------DMEALLAIEQRHGIPIIEDAA--EAigsVYH 166
Cdd:PRK07568  143 IeegfhLPSKEEI-----EKLITPKTKAI----LISNPGnptgvvytkeELEMLAEIAKKHDLFLISDEVyrEF---VYD 210

                         170
                  ....*....|
gi 2221393024 167 GKRAGSMGKF 176
Cdd:PRK07568  211 GLKYTSALSL 220
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
62-156 3.87e-03

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 38.92  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  62 ALHMGMAALGI-----GPGDEVI-----------LADTNWiatvapiVHLGAKPVFVDIlPDSWCIdpvlaEQAITPRTK 125
Cdd:PRK08247   72 ACSSGMAAIQLvmslfRSGDELIvssdlyggtyrLFEEHW-------KKWNVRFVYVNT-ASLKAI-----EQAITPNTK 138

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2221393024 126 AI---VATHIYGNLCDMEALLAIEQRHGIPIIED 156
Cdd:PRK08247  139 AIfieTPTNPLMQETDIAAIAKIAKKHGLLLIVD 172
SelA COG1921
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
117-158 4.49e-03

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


Pssm-ID: 441524  Cd Length: 399  Bit Score: 38.95  E-value: 4.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2221393024 117 EQAITPRTKAIVATH-----IYGNLC--DMEALLAIEQRHGIPIIEDAA 158
Cdd:COG1921   148 EAAITENTAALLKVHtsnyrIVGFTEevSLAELAELAHEHGLPVIVDLG 196
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
45-128 4.55e-03

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 38.87  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221393024  45 KKYLGVEYS-----IATSSCTGALHMGMAALgIGPGDEVILADTNWIATVAPIVHLGAKPVFVDILPDS--WCIDPVLAE 117
Cdd:PRK07777   75 RRRYGLEYDpdtevLVTVGATEAIAAAVLGL-VEPGDEVLLIEPYYDSYAAVIAMAGAHRVPVPLVPDGrgFALDLDALR 153

                          90
                  ....*....|.
gi 2221393024 118 QAITPRTKAIV 128
Cdd:PRK07777  154 AAVTPRTRALI 164
 
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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