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Conserved domains on  [gi|1189018068|gb|ARN64691|]
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Aminotransferase [Vibrio vulnificus]

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];
17-358 3.26e-153

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


:

Pssm-ID: 440168  Cd Length: 364  Bit Score: 435.65  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  17 ELQEACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAWkELGKlddGDEVIVQANTYIASILAI 96
Cdd:COG0399    12 EEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRAL-GIGP---GDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  97 TENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGS 176
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 177 WGHAGAFSFYPGKNLGAlGDAGAITTNDDTLAHVIRALGNYGS--HVKYENIYRGVNSRLDEMQAALLRVKLKYLDFETS 254
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRdrDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 255 IRKSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVI---ETNSRGEFQKYLESHGVQTLIHYPIPPHKQAAYREFV--N 328
Cdd:COG0399   247 RRRAIAARYREALADlPGLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGyrP 326

                         330       340       350
                  ....*....|....*....|....*....|
gi 1189018068 329 YELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRV 356
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
17-358 3.26e-153

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 435.65  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  17 ELQEACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAWkELGKlddGDEVIVQANTYIASILAI 96
Cdd:COG0399    12 EEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRAL-GIGP---GDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  97 TENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGS 176
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 177 WGHAGAFSFYPGKNLGAlGDAGAITTNDDTLAHVIRALGNYGS--HVKYENIYRGVNSRLDEMQAALLRVKLKYLDFETS 254
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRdrDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 255 IRKSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVI---ETNSRGEFQKYLESHGVQTLIHYPIPPHKQAAYREFV--N 328
Cdd:COG0399   247 RRRAIAARYREALADlPGLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGyrP 326

                         330       340       350
                  ....*....|....*....|....*....|
gi 1189018068 329 YELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRV 356
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 20-358 3.76e-129

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: 374.18  E-value: 3.76e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  20 EACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAwkeLGkLDDGDEVIVQANTYIASILAITEN 99
Cdd:cd00616     3 EAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRA---LG-IGPGDEVIVPSFTFVATANAILLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 100 NLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGSWGH 179
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 180 AGAFSFYPGKNLGAlGDAGAITTNDDTLAHVIRALGNYG---SHVKYENIYRGVNSRLDEMQAALLRVKLKYLDFETSIR 256
Cdd:cd00616   159 AGAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGrdrDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 257 KSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVIETN-----SRGEFQKYLESHGVQTLIHYPiPPHKQAAYREFVNY- 329
Cdd:cd00616   238 REIAERYKELLADlPGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYP-PLHHQPPYKKLLGYp 316

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1189018068 330 --ELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:cd00616   317 pgDLPNAEDLAERVLSLPLHPSLTEEEIDRV 347
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 15-358 2.24e-117

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: 344.65  E-value: 2.24e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  15 EKELQEACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAwkeLGkLDDGDEVIVQANTYIASIL 94
Cdd:pfam01041   4 DEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRA---LG-VGPGDEVITPSFTFVATAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  95 AITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRV 174
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 175 GSWGHAGAFSFYPGKNLgALGDAGAITTNDDTLAHVIRALGNYGSHV----KYENIYRGVNSRLDEMQAALLRVKLKYLD 250
Cdd:pfam01041 160 GTLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVRkadkRYWHEVLGYNYRMTEIQAAIGLAQLERLD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 251 FETSIRKSIADCYyskiTNPIIKLPNKS------NSEQHVYHLFVI----ETNSRGEFQKYLESHGVQTLIHYPIPPHKQ 320
Cdd:pfam01041 239 EFIARRREIAALY----QTLLADLPGFTplttppEADVHAWHLFPIlvpeEAINRDELVEALKEAGIGTRVHYPIPLHLQ 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1189018068 321 AAYREFVNY---ELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:pfam01041 315 PYYRDLFGYapgDLPNAEDISSRVLSLPLYPGLTDEDVDRV 355
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 79-358 4.57e-52

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 176.95  E-value: 4.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  79 GDEVIVQANTYIASILAITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVL 158
Cdd:PRK11706   71 GDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 159 EDCAQAHGAAINGKRVGSWGHAGAFSFYPGKNLGAlGDAGAITTNDDTL---AHVIRALGNYGSHV------KYEniYRG 229
Cdd:PRK11706  151 EDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALierAEIIREKGTNRSQFfrgqvdKYT--WVD 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 230 VNSR--LDEMQAALLRVKLKYLDFETSIRKSIADCYYSKITN----PIIKLPNKSNSEQHVYHLFVIETNS---RGEFQK 300
Cdd:PRK11706  228 IGSSylPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPlaeaGRIELPSIPDDCKHNAHMFYIKLRDledRSALIN 307

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 301 YLESHGVQTLIHYpIPPHKQAAYREF--VNYELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:PRK11706  308 FLKEAGIMAVFHY-IPLHSSPAGERFgrFHGEDRYTTKESERLLRLPLFYNLTDVEQRTV 366
 
Name Accession Description Interval E-value
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
17-358 3.26e-153

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 435.65  E-value: 3.26e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  17 ELQEACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAWkELGKlddGDEVIVQANTYIASILAI 96
Cdd:COG0399    12 EEIAAVVEVLRSGWLTLGPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRAL-GIGP---GDEVITPAFTFVATANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  97 TENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGS 176
Cdd:COG0399    88 LYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGATYKGKKVGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 177 WGHAGAFSFYPGKNLGAlGDAGAITTNDDTLAHVIRALGNYGS--HVKYENIYRGVNSRLDEMQAALLRVKLKYLDFETS 254
Cdd:COG0399   168 FGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRdrDAKYEHVELGYNYRMDELQAAIGLAQLKRLDEFIA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 255 IRKSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVI---ETNSRGEFQKYLESHGVQTLIHYPIPPHKQAAYREFV--N 328
Cdd:COG0399   247 RRRAIAARYREALADlPGLTLPKVPPGAEHVYHLYVIrldEGEDRDELIAALKARGIGTRVHYPIPLHLQPAYRDLGyrP 326

                         330       340       350
                  ....*....|....*....|....*....|
gi 1189018068 329 YELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:COG0399   327 GDLPVAERLAERVLSLPLHPGLTEEDVDRV 356
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 20-358 3.76e-129

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: 374.18  E-value: 3.76e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  20 EACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAwkeLGkLDDGDEVIVQANTYIASILAITEN 99
Cdd:cd00616     3 EAVEEVLDSGWLTLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRA---LG-IGPGDEVIVPSFTFVATANAILLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 100 NLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGSWGH 179
Cdd:cd00616    79 GATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 180 AGAFSFYPGKNLGAlGDAGAITTNDDTLAHVIRALGNYG---SHVKYENIYRGVNSRLDEMQAALLRVKLKYLDFETSIR 256
Cdd:cd00616   159 AGAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGrdrDRFKYEHEILGYNYRLSEIQAAIGLAQLEKLDEIIARR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 257 KSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVIETN-----SRGEFQKYLESHGVQTLIHYPiPPHKQAAYREFVNY- 329
Cdd:cd00616   238 REIAERYKELLADlPGIRLPDVPPGVKHSYHLYVIRLDpeageSRDELIEALKEAGIETRVHYP-PLHHQPPYKKLLGYp 316

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1189018068 330 --ELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:cd00616   317 pgDLPNAEDLAERVLSLPLHPSLTEEEIDRV 347
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 15-358 2.24e-117

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: 344.65  E-value: 2.24e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  15 EKELQEACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAwkeLGkLDDGDEVIVQANTYIASIL 94
Cdd:pfam01041   4 DEEELAAVREVLKSGWLTTGPYVREFERAFAAYLGVKHAIAVSSGTAALHLALRA---LG-VGPGDEVITPSFTFVATAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  95 AITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRV 174
Cdd:pfam01041  80 AALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 175 GSWGHAGAFSFYPGKNLgALGDAGAITTNDDTLAHVIRALGNYGSHV----KYENIYRGVNSRLDEMQAALLRVKLKYLD 250
Cdd:pfam01041 160 GTLGDAATFSFHPTKNL-TTGEGGAVVTNDPELAEKARVLRNHGMVRkadkRYWHEVLGYNYRMTEIQAAIGLAQLERLD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 251 FETSIRKSIADCYyskiTNPIIKLPNKS------NSEQHVYHLFVI----ETNSRGEFQKYLESHGVQTLIHYPIPPHKQ 320
Cdd:pfam01041 239 EFIARRREIAALY----QTLLADLPGFTplttppEADVHAWHLFPIlvpeEAINRDELVEALKEAGIGTRVHYPIPLHLQ 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1189018068 321 AAYREFVNY---ELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:pfam01041 315 PYYRDLFGYapgDLPNAEDISSRVLSLPLYPGLTDEDVDRV 355
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 79-358 4.57e-52

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 176.95  E-value: 4.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  79 GDEVIVQANTYIASILAITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVL 158
Cdd:PRK11706   71 GDEVIMPSYTFVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVV 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 159 EDCAQAHGAAINGKRVGSWGHAGAFSFYPGKNLGAlGDAGAITTNDDTL---AHVIRALGNYGSHV------KYEniYRG 229
Cdd:PRK11706  151 EDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALierAEIIREKGTNRSQFfrgqvdKYT--WVD 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 230 VNSR--LDEMQAALLRVKLKYLDFETSIRKSIADCYYSKITN----PIIKLPNKSNSEQHVYHLFVIETNS---RGEFQK 300
Cdd:PRK11706  228 IGSSylPSELQAAYLWAQLEAADRINQRRLALWQRYYDALAPlaeaGRIELPSIPDDCKHNAHMFYIKLRDledRSALIN 307

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 301 YLESHGVQTLIHYpIPPHKQAAYREF--VNYELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:PRK11706  308 FLKEAGIMAVFHY-IPLHSSPAGERFgrFHGEDRYTTKESERLLRLPLFYNLTDVEQRTV 366
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
1-351 3.19e-51

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 175.21  E-value: 3.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068   1 MISFLDLKRiNNLHEKELQeACERVIKSGWYISGEENQQFSKEFARYCGVNNCIGVANGLDALSLTLRAwkeLGkLDDGD 80
Cdd:PRK11658    1 MSDFLPFSR-PAMGDEELA-AVKEVLRSGWITTGPKNQALEQAFCQLTGNQHAIAVSSATAGMHITLMA---LG-IGPGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  81 EVIVQANTYIASILAITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLED 160
Cdd:PRK11658   75 EVITPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIED 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 161 CAQAHGAAINGKRVGSWGHAgAFSFYPGKNLgALGDAGAITTNDDTLAHVIRALGNYGSHV------------KYENIYR 228
Cdd:PRK11658  155 AAHAVGTYYKGRHIGARGTA-IFSFHAIKNI-TCAEGGLVVTDDDELADRLRSLKFHGLGVdafdrqtqgrapQAEVLTP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 229 GVNSRLDEMQAALLRVKLKYLDFETSIRKSIADCYYSKITN-PIIKLPNKSNSEQHVYHLFVIETN------SRGEFQKY 301
Cdd:PRK11658  233 GYKYNLADINAAIALVQLAKLEALNARRREIAARYLQALADlPFQPLSLPAWPHQHAWHLFIIRVDeercgiSRDALMEA 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1189018068 302 LESHGVQTLIHYpIPPHKQAAYRE-FVNYELPITENIHNNILSLPISPVMT 351
Cdd:PRK11658  313 LKERGIGTGLHF-RAAHTQKYYRErFPTLSLPNTEWNSERICSLPLFPDMT 362
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 29-358 5.48e-39

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 143.87  E-value: 5.48e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  29 GWYISGEENQQFSKEFARYCGVNNCIGVANG----LDALSlTLRAWKeLGK--LDDGDEVIVQANTYIASILAITENNLV 102
Cdd:PRK15407   57 FWLTTGRFNDAFEKKLAEFLGVRYALLVNSGssanLLAFS-ALTSPK-LGDraLKPGDEVITVAAGFPTTVNPIIQNGLV 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 103 PVLVEPSSETYNLTTCSIESAITAKTKVILPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGSWGHAGA 182
Cdd:PRK15407  135 PVFVDVELPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIAT 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 183 FSFYPGKNLgALGDAGAITTNDDTLAHVIRALGNYG----------------------------SHvKYenIY--RGVNS 232
Cdd:PRK15407  215 LSFYPAHHI-TMGEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdntcgkrfgwqlgelpfgyDH-KY--TYshLGYNL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068 233 RLDEMQAALLRVKLKYLD---------FETsIRKSIADCyyskitNPIIKLPN---KSNSEQHVYHLFVIETN--SRGEF 298
Cdd:PRK15407  291 KITDMQAAIGLAQLEKLPgfiearkanFAY-LKEGLASL------EDFLILPEatpNSDPSWFGFPITVKEDAgfTRVEL 363

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189018068 299 QKYLESHGVQT-------LIHYPIppHKQAAYRefVNYELPITENIHNNILSLPISPVMTIEEANYI 358
Cdd:PRK15407  364 VKYLEENKIGTrllfagnLTRQPY--FKGVKYR--VVGELTNTDRIMNDTFWIGVYPGLTEEMLDYV 426
PRK07682 PRK07682
aminotransferase;
62-160 1.17e-08

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 56.28  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  62 ALSLTLRAwkelgKLDDGDEVIVQANTYIASILAITENNLVPVLVEPSSET-YNLTTCSIESAITAKTKVIL---PVHLY 137
Cdd:PRK07682   93 ALDVAMRA-----IINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQIEAAITAKTKAILlcsPNNPT 167

                          90       100
                  ....*....|....*....|....*.
gi 1189018068 138 GRI---SPMDEIMVLAEKYELLVLED 160
Cdd:PRK07682  168 GAVlnkSELEEIAVIVEKHDLIVLSD 193
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
77-142 4.36e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 48.14  E-value: 4.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189018068  77 DDGDEVIVQANTYIASILAITENNLVPVLVePSSETYNLTTCSIESAITAKTKVILPvhlygrISP 142
Cdd:PRK05957  111 DPGDEIILNTPYYFNHEMAITMAGCQPILV-PTDDNYQLQPEAIEQAITPKTRAIVT------ISP 169
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 58-203 5.69e-06

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: 46.22  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  58 NGLDALSLTLRAWkelgklddGDEVIVQANTYIASILAITE-NNLVPVLVEPSSETYNLTTCSI--ESAITAKTKVI--- 131
Cdd:cd01494    28 GANEAALLALLGP--------GDEVIVDANGHGSRYWVAAElAGAKPVPVPVDDAGYGGLDVAIleELKAKPNVALIvit 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189018068 132 LPVHLYGRISPMDEIMVLAEKYELLVLEDCAQAHGAAINGKRVGSWGHAGAFSFYPGKNLGALGdAGAITTN 203
Cdd:cd01494   100 PNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEG-GGVVIVK 170
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 38-160 6.17e-06

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: 47.82  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  38 QQFSKEFARYCGVN---NCIGVANGL-DALSLTLRAWkelgkLDDGDEVIVQA---NTYIASILAiteNNLVPVLVEPSS 110
Cdd:COG0436    74 EAIAAYYKRRYGVDldpDEILVTNGAkEALALALLAL-----LNPGDEVLVPDpgyPSYRAAVRL---AGGKPVPVPLDE 145

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189018068 111 ET-YNLTTCSIESAITAKTKVILpvhLygrISP------------MDEIMVLAEKYELLVLED 160
Cdd:COG0436   146 ENgFLPDPEALEAAITPRTKAIV---L---NSPnnptgavysreeLEALAELAREHDLLVISD 202
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 38-160 1.29e-05

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: 46.57  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  38 QQFSKEFARYCGVN---NCIGVANGLD-ALSLTLRAWkelgkLDDGDEVIVQANTYIASILAITENNLVPVLVEPSSE-T 112
Cdd:cd00609    43 EAIAEWLGRRGGVDvppEEIVVTNGAQeALSLLLRAL-----LNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEgG 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189018068 113 YNLTTCSIESAITAKTKVIL------PVhlyGRISPMDE---IMVLAEKYELLVLED 160
Cdd:cd00609   118 FLLDLELLEAAKTPKTKLLYlnnpnnPT---GAVLSEEEleeLAELAKKHGILIISD 171
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
62-169 4.44e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 45.18  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  62 ALSLTLRAWkelgkLDDGDEVIVQA------NTYIasilaitEN-NLVPVLVEPSSETYNLTTCSIESAITAKTKVIL-- 132
Cdd:PRK06836  108 ALNVALKAI-----LNPGDEVIVFApyfveyRFYV-------DNhGGKLVVVPTDTDTFQPDLDALEAAITPKTKAVIin 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1189018068 133 ----PVhlyGRISPMDEIMVLAEkyellVLEDCAQAHGAAI 169
Cdd:PRK06836  176 spnnPT---GVVYSEETLKALAA-----LLEEKSKEYGRPI 208
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
61-164 2.44e-04

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.82  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  61 DALSLTLRAWKELGKlddGDEVIVQANTYIASILA---ITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVILPVHL- 136
Cdd:COG0520    88 EAINLVAYGLGRLKP---GDEILITEMEHHSNIVPwqeLAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVs 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 1189018068 137 --YGRISPMDEIMVLAEKYELLVLEDCAQA 164
Cdd:COG0520   165 nvTGTVNPVKEIAALAHAHGALVLVDGAQS 194
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 76-160 2.95e-04

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 42.42  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  76 LDDGDEVIVQANTYIASILAITENNLVPVLVEPSSET-YNLTTCSIESAITAKTKVIL------PV-HLYGRISpMDEIM 147
Cdd:PRK05764  112 LDPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgFKLTVEQLEAAITPKTKALIlnspsnPTgAVYSPEE-LEAIA 190

                          90
                  ....*....|...
gi 1189018068 148 VLAEKYELLVLED 160
Cdd:PRK05764  191 DVAVEHDIWVLSD 203
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
40-160 1.26e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 40.47  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  40 FSKEFARYCGVNNCIGVANGLDALSLTLRAWkelgkLDDGDEVIVQANTYIASILAITENNLVPVLVEPSSET-YNLTTC 118
Cdd:PRK06348   79 YSKNYDLSFKRNEIMATVGACHGMYLALQSI-----LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILETYEEDgFQINVK 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1189018068 119 SIESAITAKTKVIL------PVHLYGRISPMDEIMVLAEKYELLVLED 160
Cdd:PRK06348  154 KLEALITSKTKAIIlnspnnPTGAVFSKETLEEIAKIAIEYDLFIISD 201
PRK06107 PRK06107
aspartate transaminase;
38-165 1.97e-03

aspartate transaminase;


Pssm-ID: 180403  Cd Length: 402  Bit Score: 39.72  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  38 QQFSKEFARYCGVN---NCIGVANGL-DALSLTLRAwkelgKLDDGDEVIVQANTYIASILAITENNLVPVLVE-PSSET 112
Cdd:PRK06107   77 KAIIAKLERRNGLHyadNEITVGGGAkQAIFLALMA-----TLEAGDEVIIPAPYWVSYPDMVLANDGTPVIVAcPEEQG 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189018068 113 YNLTTCSIESAITAKTK-VIL--PVHLYGRISPMDEIMVLAEkyellVLEDCAQAH 165
Cdd:PRK06107  152 FKLTPEALEAAITPRTRwLILnaPSNPTGAVYSRAELRALAD-----VLLRHPHVL 202
PRK08912 PRK08912
aminotransferase;
73-151 2.01e-03

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 39.96  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  73 LGKLDDGDEVIVQANTYIASILAITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVIL---PVHLYGRISPMDEIMVL 149
Cdd:PRK08912  105 LALVEPGDEVVLFQPLYDAYLPLIRRAGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVLlnnPLNPAGKVFPREELALL 184


                  ..
gi 1189018068 150 AE 151
Cdd:PRK08912  185 AE 186
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
73-160 2.78e-03

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 39.25  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189018068  73 LGKLDDGDEVIV---QANTYIASIlAITENNLVPVLVEPSSETYNLTTCSIESAITAKTKVIL---PVHLYGRISPMDEI 146
Cdd:PRK07777  103 LGLVEPGDEVLLiepYYDSYAAVI-AMAGAHRVPVPLVPDGRGFALDLDALRAAVTPRTRALIvnsPHNPTGTVLTAAEL 181

                          90
                  ....*....|....*..
gi 1189018068 147 MVLAE---KYELLVLED 160
Cdd:PRK07777  182 AAIAElavEHDLLVITD 198
PRK07683 PRK07683
aminotransferase A; Validated
 62-133 3.45e-03

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 38.94  E-value: 3.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189018068  62 ALSLTLRAWkelgkLDDGDEVIVQANTYIASILAITENNLVPVLVEPSSETYNLTTCSIESAITAKTK-VILP 133
Cdd:PRK07683  101 AIDIAFRTI-----LEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEALENAITEKTRcVVLP 168
 
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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