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Conserved domains on  [gi|148194|gb|AAA67591|]
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unknown [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

dTDP-4-amino-4,6-dideoxygalactose transaminase( domain architecture ID 10714244)

dTDP-4-amino-4,6-dideoxygalactose transaminase catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 1-276 0e+00

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


:

Pssm-ID: 183283  Cd Length: 375  Bit Score: 662.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706   1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:PRK11706  81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148194    241 AYLWAQLEAADRINQQRLALWQNYYDALRLWRKPGV 276
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGR 275
 
Name Accession Description Interval E-value
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 1-276 0e+00

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 662.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706   1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:PRK11706  81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148194    241 AYLWAQLEAADRINQQRLALWQNYYDALRLWRKPGV 276
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGR 275
ECA_wecE TIGR02379
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ...
 1-276 0e+00

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: 589.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194       1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:TIGR02379   1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:TIGR02379  81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148194     241 AYLWAQLEAADRINQQRLALWQNYYDALRLWRKPGV 276
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGI 276
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-269 7.42e-129

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 370.94  E-value: 7.42e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     1 MIPFNAPPVVGTELDYMQSAMGSGKLCGdGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:COG0399   1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:COG0399  80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194   161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQffrgqvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231

                       250       260
                ....*....|....*....|....*....
gi 148194   241 AYLWAQLEAADRINQQRLALWQNYYDALR 269
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALA 260
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 13-269 8.76e-122

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: 352.61  E-value: 8.76e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    13 ELDYMQSAMGSGKLcGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92
Cdd:cd00616   1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    93 AKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616  80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194   173 GCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvdKYTWRDIGSSYLMSDLQAAYLWAQLEAADR 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232

                       250
                ....*....|....*..
gi 148194   253 INQQRLALWQNYYDALR 269
Cdd:cd00616 233 IIARRREIAERYKELLA 249
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 7-269 1.29e-84

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: 258.37  E-value: 1.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194       7 PPVVGTELDYMQSAMGSGKLCgDGGFTRRcqqwLEQRF----GSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFV 82
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLT-TGPYVRE----FERAFaaylGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      83 STANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162
Cdd:pfam01041  76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     163 GRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvDKYTWRDIGSSYLMSDLQAAY 242
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAI 229

                         250       260
                  ....*....|....*....|....*..
gi 148194     243 LWAQLEAADRINQQRLALWQNYYDALR 269
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTLLA 256
 
Name Accession Description Interval E-value
PRK11706 PRK11706
TDP-4-oxo-6-deoxy-D-glucose transaminase; Provisional
 1-276 0e+00

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


Pssm-ID: 183283  Cd Length: 375  Bit Score: 662.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:PRK11706   1 MIPFNKPPVVGTELDYIQQAMSSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:PRK11706  81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITPKTRAIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:PRK11706 161 YKGRALGTIGHIGCFSFHETKNYTA-GEGGALLINDPALIERAEIIREKGTNRSQFFRGQVDKYTWVDIGSSYLPSELQA 239

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 148194    241 AYLWAQLEAADRINQQRLALWQNYYDALRLWRKPGV 276
Cdd:PRK11706 240 AYLWAQLEAADRINQRRLALWQRYYDALAPLAEAGR 275
ECA_wecE TIGR02379
TDP-4-keto-6-deoxy-D-glucose transaminase; This family consists of ...
 1-276 0e+00

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: 589.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194       1 MIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:TIGR02379   1 MIPFNKPPVTGTELDYIQEAISSGKLSGDGPFTRRCEQWLEQRTGTKKALLTPSCTAALEMAALLLDIQPGDEVIMPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:TIGR02379  81 FVSTANAFVLRGAKIVFVDIRPDTMNIDETLIEAAITDRTKAIVPVHYAGVACDMDTIMALANKHNLFVIEDAAQGVMST 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     161 YKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKALIERAEIIREKGTNRSQFFRGQVDKYTWRDIGSSYLMSDLQA 240
Cdd:TIGR02379 161 YKGRALGSIGHIGTFSFHETKNYTSGGEGGALLINDQAFIERAEIIREKGTNRSQFFRGEVDKYTWRDIGSSYLPSELQA 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 148194     241 AYLWAQLEAADRINQQRLALWQNYYDALRLWRKPGV 276
Cdd:TIGR02379 241 AYLWAQLEQADRINQQRLALWQNYYDALAPLEEKGI 276
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
1-269 7.42e-129

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 370.94  E-value: 7.42e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     1 MIPFNAPPVVGTELDYMQSAMGSGKLCGdGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYT 80
Cdd:COG0399   1 MIPLSRPSIGEEEIAAVVEVLRSGWLTL-GPEVKEFEEEFAAYLGVKHAVAVSSGTAALHLALRALGIGPGDEVITPAFT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    81 FVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMST 160
Cdd:COG0399  80 FVATANAILYVGATPVFVDIDPDTYNIDPEALEAAITPRTKAIIPVHLYGQPADMDAIMAIAKKHGLKVIEDAAQALGAT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194   161 YKGRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQffrgqvdKYTWRDIGSSYLMSDLQA 240
Cdd:COG0399 160 YKGKKVGTFGDAGCFSFYPTKNLTT-GEGGAVVTNDEELAERARSLRNHGRDRDA-------KYEHVELGYNYRMDELQA 231

                       250       260
                ....*....|....*....|....*....
gi 148194   241 AYLWAQLEAADRINQQRLALWQNYYDALR 269
Cdd:COG0399 232 AIGLAQLKRLDEFIARRRAIAARYREALA 260
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
 13-269 8.76e-122

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: 352.61  E-value: 8.76e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    13 ELDYMQSAMGSGKLcGDGGFTRRCQQWLEQRFGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRG 92
Cdd:cd00616   1 ELEAVEEVLDSGWL-TLGPKVREFEKAFAEYLGVKYAVAVSSGTAALHLALRALGIGPGDEVIVPSFTFVATANAILLLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    93 AKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHI 172
Cdd:cd00616  80 ATPVFVDIDPDTYNIDPELIEAAITPRTKAIIPVHLYGNPADMDAIMAIAKRHGLPVIEDAAQALGATYKGRKVGTFGDA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194   173 GCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvdKYTWRDIGSSYLMSDLQAAYLWAQLEAADR 252
Cdd:cd00616 160 GAFSFHPTKNLTT-GEGGAVVTNDEELAERARLLRNHGRDRDRF------KYEHEILGYNYRLSEIQAAIGLAQLEKLDE 232

                       250
                ....*....|....*..
gi 148194   253 INQQRLALWQNYYDALR 269
Cdd:cd00616 233 IIARRREIAERYKELLA 249
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 7-269 1.29e-84

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: 258.37  E-value: 1.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194       7 PPVVGTELDYMQSAMGSGKLCgDGGFTRRcqqwLEQRF----GSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFV 82
Cdd:pfam01041   1 PDIDEEELAAVREVLKSGWLT-TGPYVRE----FERAFaaylGVKHAIAVSSGTAALHLALRALGVGPGDEVITPSFTFV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      83 STANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYK 162
Cdd:pfam01041  76 ATANAALRLGAKPVFVDIDPDTYNIDPEAIEAAITPRTKAIIPVHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     163 GRALGTIGHIGCFSFHETKNYTAgGEGGATLINDKALIERAEIIREKGTNRSQFfrgqvDKYTWRDIGSSYLMSDLQAAY 242
Cdd:pfam01041 156 GKKVGTLGDAATFSFHPTKNLTT-GEGGAVVTNDPELAEKARVLRNHGMVRKAD-----KRYWHEVLGYNYRMTEIQAAI 229

                         250       260
                  ....*....|....*....|....*..
gi 148194     243 LWAQLEAADRINQQRLALWQNYYDALR 269
Cdd:pfam01041 230 GLAQLERLDEFIARRREIAALYQTLLA 256
PRK11658 PRK11658
UDP-4-amino-4-deoxy-L-arabinose aminotransferase;
2-268 9.45e-59

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


Pssm-ID: 183263  Cd Length: 379  Bit Score: 192.55  E-value: 9.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      2 IPFNAPPVVGTELDYMQSAMGSGKLcgdggfTR--RCQQwLEQRF----GSAKVLLTPSCTASLEMAALLLDIQPGDEVI 75
Cdd:PRK11658   5 LPFSRPAMGDEELAAVKEVLRSGWI------TTgpKNQA-LEQAFcqltGNQHAIAVSSATAGMHITLMALGIGPGDEVI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     76 MPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQ 155
Cdd:PRK11658  78 TPSLTWVSTLNMIVLLGATPVMVDVDRDTLMVTPEAIEAAITPRTKAIIPVHYAGAPADLDAIRAIGERYGIPVIEDAAH 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    156 GVMSTYKGRALGTIGhIGCFSFHETKNYTAgGEGGATLINDKALIERAeiirekgtnRSQFFRG-QVDKYTwRDI----- 229
Cdd:PRK11658 158 AVGTYYKGRHIGARG-TAIFSFHAIKNITC-AEGGLVVTDDDELADRL---------RSLKFHGlGVDAFD-RQTqgrap 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 148194    230 -------GSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDAL 268
Cdd:PRK11658 226 qaevltpGYKYNLADINAAIALVQLAKLEALNARRREIAARYLQAL 271
PseC TIGR03588
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase; This family of enzymes are ...
 54-269 7.74e-56

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: 184.84  E-value: 7.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      54 SCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITD----KTRVIVPVHYA 129
Cdd:TIGR03588  52 SATSALHIACLALGVGPGDRVWTTPITFVATANCALYCGAKVDFVDIDPDTGNIDEDALEKKLAAakgkLPKAIVPVDFA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     130 GVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGH--IGCFSFHETKNYTAgGEGGATLINDKALIERAEIIR 207
Cdd:TIGR03588 132 GKSVDMQAIAALAKKHGLKIIEDASHALGAEYGGKPVGNCRYadATVFSFHPVKIITT-AEGGAVTTNDEELAERMRLLR 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148194     208 EKGTNRSQFFRGQVDKYTW----RDIGSSYLMSDLQAAYLWAQLEAADRINQQRLALWQNYYDALR 269
Cdd:TIGR03588 211 SHGITKDPLLFEKQDEGPWyyeqQELGFNYRMTDIQAALGLSQLKKLDRFVAKRREIAARYDRLLK 276
PRK15407 PRK15407
lipopolysaccharide biosynthesis protein RfbH; Provisional
 30-269 1.43e-41

lipopolysaccharide biosynthesis protein RfbH; Provisional


Pssm-ID: 237960  Cd Length: 438  Bit Score: 148.88  E-value: 1.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     30 GGFTRRCQQWLEQRFGSAKVLLTPSCTAS--LEMAAL----LLD--IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVR 101
Cdd:PRK15407  62 GRFNDAFEKKLAEFLGVRYALLVNSGSSAnlLAFSALtspkLGDraLKPGDEVITVAAGFPTTVNPIIQNGLVPVFVDVE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    102 PDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETK 181
Cdd:PRK15407 142 LPTYNIDASLLEAAVSPKTKAIMIAHTLGNPFDLAAVKAFCDKHNLWLIEDNCDALGSTYDGRMTGTFGDIATLSFYPAH 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    182 NYTAgGEGGATLINDKALIERAEIIREKG-----------TNRSQFF-------RGQVDKYTWRDIGSSYLMSDLQAAYL 243
Cdd:PRK15407 222 HITM-GEGGAVFTNDPLLKKIIESFRDWGrdcwcapgcdnTCGKRFGwqlgelpFGYDHKYTYSHLGYNLKITDMQAAIG 300

                        250       260
                 ....*....|....*....|....*.
gi 148194    244 WAQLEAADRINQQRLALWQNYYDALR 269
Cdd:PRK15407 301 LAQLEKLPGFIEARKANFAYLKEGLA 326
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 3-206 1.33e-18

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: 84.70  E-value: 1.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     3 PFNAPPVVGTELDYMQSAMGSGKLCGDGG---FTRRCQQWLEQRFGSAK----VLLTPSCTASLEMAALLLdIQPGDEVI 75
Cdd:cd00609   9 DFPPPPEVLEALAAAALRAGLLGYYPDPGlpeLREAIAEWLGRRGGVDVppeeIVVTNGAQEALSLLLRAL-LNPGDEVL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    76 MPSYTFVSTANAFVLRGAKIVFVDVRPDTMN-IDETLIEAAITDKTRVIVpVHYA----GV---ACEMDTIMALAKKHNL 147
Cdd:cd00609  88 VPDPTYPGYEAAARLAGAEVVPVPLDEEGGFlLDLELLEAAKTPKTKLLY-LNNPnnptGAvlsEEELEELAELAKKHGI 166

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148194   148 FVVEDAA-QG-VMSTYKGRALGTIGH----IGCFSFheTKNYTAGGE-GGATLINDKALIERAEII 206
Cdd:cd00609 167 LIISDEAyAElVYDGEPPPALALLDAyervIVLRSF--SKTFGLPGLrIGYLIAPPEELLERLKKL 230
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 38-152 1.07e-15

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: 76.32  E-value: 1.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    38 QWLEQRFG---SAK-VLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT-MNIDETLI 112
Cdd:COG0436  78 AYYKRRYGvdlDPDeILVTNGAKEALALALLAL-LNPGDEVLVPDPGYPSYRAAVRLAGGKPVPVPLDEENgFLPDPEAL 156

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 148194   113 EAAITDKTRVIV------PvhyAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:COG0436 157 EAAITPRTKAIVlnspnnP---TGAVYsreELEALAELAREHDLLVISD 202
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 48-190 1.54e-15

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: 72.80  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLR-GAKIVFVDVRPDTMNIDE--TLIEAAITDKTRVIV 124
Cdd:cd01494  19 KAVFVPSGTGANEAALLAL-LGPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGGLDvaILEELKAKPNVALIV 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148194   125 PVHYA---GVACEMDTIMALAKKHNLFVVEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGG 190
Cdd:cd01494  98 ITPNTtsgGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNLGGEGGGV 166
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 61-152 5.51e-13

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 68.61  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     61 MAALLldiQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT---MNIDEtlIEAAITDKTRVIV---PVHYAGVAC- 133
Cdd:PRK05764 108 FMALL---DPGDEVIIPAPYWVSYPEMVKLAGGVPVFVPTGEENgfkLTVEQ--LEAAITPKTKALIlnsPSNPTGAVYs 182

                         90       100
                 ....*....|....*....|.
gi 148194    134 --EMDTIMALAKKHNLFVVED 152
Cdd:PRK05764 183 peELEAIADVAVEHDIWVLSD 203
PRK07683 PRK07683
aminotransferase A; Validated
 37-152 1.35e-11

aminotransferase A; Validated


Pssm-ID: 236075  Cd Length: 387  Bit Score: 64.36  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     37 QQWLEQRFG-----SAKVLLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETL 111
Cdd:PRK07683  75 CNFVKDKYDlhyspESEIIVTIGASEAID-IAFRTILEPGTEVILPAPIYPGYEPIIRLCGAKPVFIDTRSTGFRLTAEA 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 148194    112 IEAAITDKTRVIV---PVHYAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:PRK07683 154 LENAITEKTRCVVlpyPSNPTGVTLskeELQDIADVLKDKNIFVLSD 200
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
49-206 1.15e-10

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 61.55  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      49 VLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVR-PDTMNIDETLIEAAITDKTRVIV--- 124
Cdd:pfam00155  66 VVFGSGAGANIEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPLYdSNDFHLDFDALEAALKEKPKVVLhts 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     125 PVHYAGVAC---EMDTIMALAKKHNLFVVEDAAQGVM----STYKGRALGTIGHIGCF---SFheTKNYTAGGE-GGATL 193
Cdd:pfam00155 145 PHNPTGTVAtleELEKLLDLAKEHNILLLVDEAYAGFvfgsPDAVATRALLAEGPNLLvvgSF--SKAFGLAGWrVGYIL 222

                         170
                  ....*....|...
gi 148194     194 INDkALIERAEII 206
Cdd:pfam00155 223 GNA-AVISQLRKL 234
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 48-159 8.16e-10

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: 58.80  E-value: 8.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      48 KVLLTPSCTASLEMAA--LLLDIQPGDEVIMPSY----TFVSTANAFVLRGAKIVFVDVRPDTmNIDETLIEAAITDKTR 121
Cdd:pfam00266  63 EIIFTSGTTEAINLVAlsLGRSLKPGDEIVITEMehhaNLVPWQELAKRTGARVRVLPLDEDG-LLDLDELEKLITPKTK 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 148194     122 VivpVHYA------GVACEMDTIMALAKKHNLFVVEDAAQGVMS 159
Cdd:pfam00266 142 L---VAIThvsnvtGTIQPVPEIGKLAHQYGALVLVDAAQAIGH 182
PRK07682 PRK07682
aminotransferase;
39-152 1.06e-09

aminotransferase;


Pssm-ID: 181082 [Multi-domain]  Cd Length: 378  Bit Score: 58.59  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     39 WLEQRFG-----SAKVLLTPSCTASLEMAaLLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT-MNIDETLI 112
Cdd:PRK07682  69 YLKKRFAvsydpNDEIIVTVGASQALDVA-MRAIINPGDEVLIVEPSFVSYAPLVTLAGGVPVPVATTLENeFKVQPAQI 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 148194    113 EAAITDKTRVIV---PVHYAGVAC---EMDTIMALAKKHNLFVVED 152
Cdd:PRK07682 148 EAAITAKTKAILlcsPNNPTGAVLnksELEEIAVIVEKHDLIVLSD 193
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
49-178 1.63e-09

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 58.23  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    49 VLLTPSCTASLEMAALLLD-IQPGDEVIMPSYTFVSTANAFVL----RGAKIVFVDVRPD-TMNIDEtlIEAAITDKTRV 122
Cdd:COG0520  80 IIFTRGTTEAINLVAYGLGrLKPGDEILITEMEHHSNIVPWQElaerTGAEVRVIPLDEDgELDLEA--LEALLTPRTKL 157

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148194   123 ------------IVPVHyagvacemdTIMALAKKHNLFVVEDAAQGVmstykgralgtiGH-------IGC----FSFH 178
Cdd:COG0520 158 vavthvsnvtgtVNPVK---------EIAALAHAHGALVLVDGAQSV------------PHlpvdvqaLGCdfyaFSGH 215
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
70-152 4.05e-09

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 56.78  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     70 PGDEVIMPSyTFVSTANAFvlrgAKIVFVDVRPDTMNIDETL-------IEAAITDKTRVIV------PVHYAGVACEMD 136
Cdd:PRK07568 111 PGDEILVPE-PFYANYNGF----ATSAGVKIVPVTTKIEEGFhlpskeeIEKLITPKTKAILisnpgnPTGVVYTKEELE 185

                         90
                 ....*....|....*.
gi 148194    137 TIMALAKKHNLFVVED 152
Cdd:PRK07568 186 MLAEIAKKHDLFLISD 201
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 48-157 5.52e-09

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: 56.32  E-value: 5.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    48 KVLLTPSCTASLEMAA--LLLDIQPGDEVImpsytfVSTA--NAFVL--------RGAKIVFVDVRPDTmNIDETLIEAA 115
Cdd:cd06453  63 EIIFTRNTTEAINLVAygLGRANKPGDEIV------TSVMehHSNIVpwqqlaerTGAKLKVVPVDDDG-QLDLEALEKL 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 148194   116 ITDKTRVIVPVHYAGVaceMDTIM------ALAKKHNLFVVEDAAQGV 157
Cdd:cd06453 136 LTERTKLVAVTHVSNV---LGTINpvkeigEIAHEAGVPVLVDGAQSA 180
PRK09082 PRK09082
methionine aminotransferase; Validated
 49-152 1.73e-08

methionine aminotransferase; Validated


Pssm-ID: 181642 [Multi-domain]  Cd Length: 386  Bit Score: 54.92  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     49 VLLTPSCTASLeMAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV-- 124
Cdd:PRK09082  94 ITVTAGATEAL-FAAILALVRPGDEVIVfdPSYD--SYAPAIELAGGRAVRVALQPPDFRVDWQRFAAAISPRTRLIIln 170

                         90       100       110
                 ....*....|....*....|....*....|..
gi 148194    125 -PVHYAGV---ACEMDTIMALAKKHNLFVVED 152
Cdd:PRK09082 171 tPHNPSGTvwsAADMRALWQLIAGTDIYVLSD 202
PRK06348 PRK06348
pyridoxal phosphate-dependent aminotransferase;
68-208 1.76e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180537  Cd Length: 384  Bit Score: 55.11  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD-VRPDTMNIDETLIEAAITDKTRVIV---PVHYAGVACEMDT---IMA 140
Cdd:PRK06348 110 LDPGDEVIIHEPYFTPYKDQIEMVGGKPIILEtYEEDGFQINVKKLEALITSKTKAIIlnsPNNPTGAVFSKETleeIAK 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148194    141 LAKKHNLFVVEDAAQGV---------MSTYKGRALGTIGhIGCFSfhetKNYTAGGEGGATLINDKALIERAEIIRE 208
Cdd:PRK06348 190 IAIEYDLFIISDEVYDGfsfyedfvpMATLAGMPERTIT-FGSFS----KDFAMTGWRIGYVIAPDYIIETAKIINE 261
PRK07309 PRK07309
pyridoxal phosphate-dependent aminotransferase;
49-170 6.31e-08

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235985  Cd Length: 391  Bit Score: 53.19  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     49 VLLTPSCTASLEmAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAIT---DKTRVIV- 124
Cdd:PRK07309  94 ILVTIGATEALS-ASLTAILEPGDKVLLPAPAYPGYEPIVNLVGAEIVEIDTTENDFVLTPEMLEKAILeqgDKLKAVIl 172

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148194    125 --PVHYAGVACEMDTIMALA---KKHNLFVVEDAaqgVMS--TYKGRALGTIG 170
Cdd:PRK07309 173 nyPANPTGVTYSREQIKALAdvlKKYDIFVISDE---VYSelTYTGEPHVSIA 222
PLN00175 PLN00175
aminotransferase family protein; Provisional
 48-152 6.58e-08

aminotransferase family protein; Provisional


Pssm-ID: 215089 [Multi-domain]  Cd Length: 413  Bit Score: 53.33  E-value: 6.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     48 KVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV--- 124
Cdd:PLN00175 117 EVTVTSGCTEAIAATILGL-INPGDEVILFAPFYDSYEATLSMAGAKIKTVTLRPPDFAVPEDELKAAFTSKTRAILint 195

                         90       100       110
                 ....*....|....*....|....*....|.
gi 148194    125 ---PVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PLN00175 196 phnPTGKMFTREELELIASLCKENDVLAFTD 226
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
49-152 1.12e-07

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 52.35  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     49 VLLTPSCTASLEmAALLLDIQPGDEVIM--PSYTfvSTANAFVLRGAKIVFVDVRPD----TMNIDEtlIEAAITDKTRV 122
Cdd:PRK07777  88 VLVTVGATEAIA-AAVLGLVEPGDEVLLiePYYD--SYAAVIAMAGAHRVPVPLVPDgrgfALDLDA--LRAAVTPRTRA 162

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 148194    123 IV------PVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PRK07777 163 LIvnsphnPTGTVLTAAELAAIAELAVEHDLLVITD 198
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
61-184 1.65e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 52.00  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     61 MAALLLDIQPGDEVIMPS-YTFvstaNAFVlrgaKIVFVDVRPDTMNIDET------LIEAAITDKTRVIV---PVHYAG 130
Cdd:PRK05957 103 MNAILAITDPGDEIILNTpYYF----NHEM----AITMAGCQPILVPTDDNyqlqpeAIEQAITPKTRAIVtisPNNPTG 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 148194    131 VACEMDTIMA---LAKKHNLFVVEDAAqgvmstYKGRALGTIGHIGCFSFHETKNYT 184
Cdd:PRK05957 175 VVYPEALLRAvnqICAEHGIYHISDEA------YEYFTYDGVKHFSPGSIPGSGNHT 225
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
33-154 2.08e-07

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 51.45  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      33 TRRCQQWLEQRFGSAKVLLTPSCTASlEMAALLLDIQPGDEVIM--PSYTFVSTA-NAFVLRGAKIVFVDVRPD-TMNID 108
Cdd:pfam01212  34 VNRLEDRVAELFGKEAALFVPSGTAA-NQLALMAHCQRGDEVICgePAHIHFDETgGHAELGGVQPRPLDGDEAgNMDLE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     109 EtlIEAAIT-------DKTRVI---VPVHYAGVAC----EMDTIMALAKKHNLFVVEDAA 154
Cdd:pfam01212 113 D--LEAAIRevgadifPPTGLIsleNTHNSAGGQVvsleNLREIAALAREHGIPVHLDGA 170
PRK06836 PRK06836
pyridoxal phosphate-dependent aminotransferase;
40-152 4.02e-07

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180720  Cd Length: 394  Bit Score: 50.96  E-value: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     40 LEQRFGSA----KVLLTPSCTASLEMA--ALLldiQPGDEVIMPSYTFVS----TANAfvlrGAKIVFVDVRPDTMNIDE 109
Cdd:PRK06836  86 LNRRFGTPltadHIVMTCGAAGALNVAlkAIL---NPGDEVIVFAPYFVEyrfyVDNH----GGKLVVVPTDTDTFQPDL 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148194    110 TLIEAAITDKTRVIV---PVHYAGVACEMDTIMALAK---------KHNLFVVED 152
Cdd:PRK06836 159 DALEAAITPKTKAVIinsPNNPTGVVYSEETLKALAAlleekskeyGRPIYLISD 213
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 28-203 1.11e-06

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


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 49.25  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    28 GDGGF-----TRRCQQWLEQRFGSAKVLLTPSCTA--SLEMAALLldiQPGDEVIMPS----YTFVSTANAFvLRGAKIV 96
Cdd:cd06502  24 GDDVYgedptTAKLEARAAELFGKEAALFVPSGTAanQLALAAHT---QPGGSVICHEtahiYTDEAGAPEF-LSGVKLL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    97 FVDvrpdtmNIDETLIEAAITDKTRVIVPVHYAGVAC----------------EMDTIMALAKKHNLFVVEDAAQ-GVMS 159
Cdd:cd06502 100 PVP------GENGKLTPEDLEAAIRPRDDIHFPPPSLvslentteggtvypldELKAISALAKENGLPLHLDGARlANAA 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 148194   160 TYKGRALGTIG-HIGCFSFHETKNYTAggEGGATLINDKALIERA 203
Cdd:cd06502 174 AALGVALKTYKsGVDSVSFCLSKGGGA--PVGAVVVGNRDFIARA 216
PRK06108 PRK06108
pyridoxal phosphate-dependent aminotransferase;
61-152 1.29e-06

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180404  Cd Length: 382  Bit Score: 49.17  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     61 MAALLLDIQ----PGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPD----TMNIDEtlIEAAITDKTRVIV------PV 126
Cdd:PRK06108  94 VQALMLAAQalvgPGDEVVAVTPLWPNLVAAPKILGARVVCVPLDFGgggwTLDLDR--LLAAITPRTRALFinspnnPT 171

                         90       100
                 ....*....|....*....|....*.
gi 148194    127 HYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:PRK06108 172 GWTASRDDLRAILAHCRRHGLWIVAD 197
PRK08912 PRK08912
aminotransferase;
49-152 7.64e-06

aminotransferase;


Pssm-ID: 181580  Cd Length: 387  Bit Score: 46.89  E-value: 7.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     49 VLLTPSCTASLEmAALLLDIQPGDEVIM--PSYtfvsTANAFVLR--GAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV 124
Cdd:PRK08912  90 VMVTSGATEALA-AALLALVEPGDEVVLfqPLY----DAYLPLIRraGGVPRLVRLEPPHWRLPRAALAAAFSPRTKAVL 164

                         90       100       110
                 ....*....|....*....|....*....|....
gi 148194    125 ---PVHYAGV---ACEMDTIMALAKKHNLFVVED 152
Cdd:PRK08912 165 lnnPLNPAGKvfpREELALLAEFCQRHDAVAICD 198
PLN02855 PLN02855
Bifunctional selenocysteine lyase/cysteine desulfurase
 65-157 1.71e-05

Bifunctional selenocysteine lyase/cysteine desulfurase


Pssm-ID: 215460 [Multi-domain]  Cd Length: 424  Bit Score: 45.89  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     65 LLDIQPGDEVIMP---------SYTFVSTANAFVLRgakivFVDVRPDTmNIDETLIEAAITDKTRVIVPVHYAGV-ACE 134
Cdd:PLN02855 116 LANLKPGDEVILSvaehhsnivPWQLVAQKTGAVLK-----FVGLTPDE-VLDVEQLKELLSEKTKLVATHHVSNVlGSI 189

                         90       100
                 ....*....|....*....|....*
gi 148194    135 MDT--IMALAKKHNLFVVEDAAQGV 157
Cdd:PLN02855 190 LPVedIVHWAHAVGAKVLVDACQSV 214
PRK07337 PRK07337
pyridoxal phosphate-dependent aminotransferase;
4-121 3.20e-05

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 180937  Cd Length: 388  Bit Score: 45.05  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194      4 FNAPPVVgteLDYMQSAMGSG--KLCGDGGFT---RRCQQWLEQRFG----SAKVLLTPSCTASLEMAALLLdIQPGDEV 74
Cdd:PRK07337  42 FTAPEPV---VEAAARALRRGvtQYTSALGLAplrEAIAAWYARRFGldvaPERIVVTAGASAALLLACLAL-VERGDEV 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148194     75 IM--PSYT----FVSTAnafvlrGAKIVFVDVRPDT-MNIDETLIEAAITDKTR 121
Cdd:PRK07337 118 LMpdPSYPcnrhFVAAA------EGRPVLVPSGPAErFQLTAADVEAAWGERTR 165
PRK12414 PRK12414
putative aminotransferase; Provisional
 46-124 3.78e-05

putative aminotransferase; Provisional


Pssm-ID: 183514  Cd Length: 384  Bit Score: 44.78  E-value: 3.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148194     46 SAKVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMNIDETLIEAAITDKTRVIV 124
Cdd:PRK12414  90 ASEVTVIASASEGLYAAISAL-VHPGDEVIYFEPSFDSYAPIVRLQGATPVAIKLSPEDFRVNWDEVAAAITPRTRMII 167
PRK08247 PRK08247
methionine biosynthesis PLP-dependent protein;
61-152 1.74e-04

methionine biosynthesis PLP-dependent protein;


Pssm-ID: 181320 [Multi-domain]  Cd Length: 366  Bit Score: 42.77  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     61 MAALLLDI---QPGDEVIMPSYTFVST----ANAFVLRGAKIVFVDVRpdtmniDETLIEAAITDKTRVI---VPVHYAG 130
Cdd:PRK08247  77 MAAIQLVMslfRSGDELIVSSDLYGGTyrlfEEHWKKWNVRFVYVNTA------SLKAIEQAITPNTKAIfieTPTNPLM 150

                         90       100
                 ....*....|....*....|..
gi 148194    131 VACEMDTIMALAKKHNLFVVED 152
Cdd:PRK08247 151 QETDIAAIAKIAKKHGLLLIVD 172
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 40-152 2.59e-04

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: 42.19  E-value: 2.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    40 LEQRF----GSAKVLLTPSCTASLEMAALLLdIQPGDEVIMPSYTFvSTANAFVLRGAKIVFVDVRP-DTMNIDEtlIEA 114
Cdd:cd00614  45 LEKKLaaleGGEAALAFSSGMAAISTVLLAL-LKAGDHVVASDDLY-GGTYRLFERLLPKLGIEVTFvDPDDPEA--LEA 120

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 148194   115 AITDKTRVI---VPVHYAGVACEMDTIMALAKKHNLFVVED 152
Cdd:cd00614 121 AIKPETKLVyveSPTNPTLKVVDIEAIAELAHEHGALLVVD 161
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 68-152 5.58e-04

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 41.02  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194     68 IQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDT---MNIDEtLIEaAITDKTRVIV---PVHYAGVACEMDTIMA- 140
Cdd:PRK08361 114 LEEGDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENefqPDPDE-LLE-LITKRTRMIVinyPNNPTGATLDKEVAKAi 191

                         90
                 ....*....|....
gi 148194    141 --LAKKHNLFVVED 152
Cdd:PRK08361 192 adIAEDYNIYILSD 205
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 44-156 1.91e-03

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 39.15  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    44 FGSAKVLLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVDVRPDTMN----------IDETLIE 113
Cdd:cd00615  72 FGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPERNPYYgiaggippetFKKALIE 151

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 148194   114 ------AAITDKTrvivpvhYAGVACEMDTIMALAKKHNLFVVEDAAQG 156
Cdd:cd00615 152 hpdakaAVITNPT-------YYGICYNLRKIVEEAHHRGLPVLVDEAHG 193
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 40-152 1.93e-03

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 39.26  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194    40 LEQRF----GSAKVLLTPS----CTASLeMAALlldiQPGDEVIMP------SYTFVSTanafVLR--GAKIVFVDvrpd 103
Cdd:COG0626  63 LEEALaaleGGEAALAFASgmaaISAVL-LALL----KAGDHVVASddlyggTRRLLDK----VLArfGIEVTFVD---- 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148194   104 TMNIDEtlIEAAITDKTRVIVpvhyagvaCE-----------MDTIMALAKKHNLFVVED 152
Cdd:COG0626 130 PTDLAA--VEAAIRPNTKLVF--------LEtpsnptlevvdIAAIAAIAHAAGALLVVD 179
 
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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