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Conserved domains on  [gi|504291509|ref|WP_014478611|]
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MULTISPECIES: aminodeoxychorismate lyase [Bacillus]

Protein Classification

aminodeoxychorismate lyase( domain architecture ID 10012954)

aminodeoxychorismate lyase catalyzes the production of 4-aminobenzoate (PABA) from 4-amino-4-deoxychorismate in the folate biosynthesis pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 1-280 0e+00

4-amino-4-deoxychorismate lyase; Provisional


:

Pssm-ID: 181067  Cd Length: 283  Bit Score: 534.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:PRK07650   1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IkdGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREI 160
Cdd:PRK07650  81 L--ENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILGKREI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 161 GNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWM 240
Cdd:PRK07650 159 GNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 504291509 241 TNSVLEIIPFTKIEEVNYGSQSGEATSALQLLYKKEIKNM 280
Cdd:PRK07650 239 TNSIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKL 278
 
Name Accession Description Interval E-value
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 1-280 0e+00

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 534.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:PRK07650   1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IkdGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREI 160
Cdd:PRK07650  81 L--ENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILGKREI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 161 GNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWM 240
Cdd:PRK07650 159 GNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 504291509 241 TNSVLEIIPFTKIEEVNYGSQSGEATSALQLLYKKEIKNM 280
Cdd:PRK07650 239 TNSIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKL 278
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 20-273 1.54e-99

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 291.91  E-value: 1.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  20 DHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEyTVSKHEILEMLDKLLKLNDIKDGnaRVRLNISAGISDK 99
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIP-EPDLPRLRAALESLLAANDIDEG--RIRLILSRGPGGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 100 GFVAQTYDKPTVLCFVNQLKPEslPLQKEGKVLSIRRNTPE--GSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAV 177
Cdd:cd01559   78 GYAPSVCPGPALYVSVIPLPPA--WRQDGVRLITCPVRLGEqpLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 178 AEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEvn 257
Cdd:cd01559  156 IEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD-- 233

                        250
                 ....*....|....*.
gi 504291509 258 YGSQSGEATSALQLLY 273
Cdd:cd01559  234 HDGPPGPLTRALRELL 249
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 1-279 2.47e-91

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 272.45  E-value: 2.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:COG0115    2 LIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IKDGnaRVRLNISAGISDKGFVAQTYdKPTVLCFVNQLKPESLPLQKEG---KVLSIRRNTPEGSFRLKSHHYLNNMYAK 157
Cdd:COG0115   82 LEDG--YIRPQVTRGVGGRGVFAEEY-EPTVIIIASPLPAYPAEAYEKGvrvITSPYRRAAPGGLGGIKTGNYLNNVLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 158 REI---GNDprvEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLT 234
Cdd:COG0115  159 QEAkeaGAD---EALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYT 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 504291509 235 ADEAWMTNSVLEIIPFTKIEEVNYGS-QSGEATSALQLLYKKEIKN 279
Cdd:COG0115  236 ADEVFLTGTAAEVTPVTEIDGRPIGDgKPGPVTRRLRELYTDIVRG 281
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 28-253 4.05e-62

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 195.65  E-value: 4.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   28 GVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDikDGNARVRLNISAGISDKGFVAQTyd 107
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANG--LGVGRLRLTVSRGPGGFGLPTSD-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  108 kPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFW 187
Cdd:pfam01063  77 -PTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVFL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504291509  188 RKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKI 253
Cdd:pfam01063 156 VKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 4-270 1.01e-39

aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 132501  Cd Length: 261  Bit Score: 139.26  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509    4 VNGRYMEEkdavLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYtVSKHEILEMLDKLLKlndiKD 83
Cdd:TIGR03461   2 VNGVLQTQ----ISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPL-PDWDALREEMAQLAA----GY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   84 GNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEG---KVLSIR--RNTpegsfRLKSHHYLNNM---Y 155
Cdd:TIGR03461  73 SLGVLKVIISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGirlGVSPVRlgRNP-----LLAGIKHLNRLeqvL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  156 AKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTA 235
Cdd:TIGR03461 148 IKAELENSEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSA 227

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 504291509  236 DEAWMTNSVLEIIPFTKIEEVNYgsQSGEATSALQ 270
Cdd:TIGR03461 228 DEVFITNSLMGVVPVNAIGETSY--PSRTLTRLLQ 260
 
Name Accession Description Interval E-value
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 1-280 0e+00

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 534.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:PRK07650   1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IkdGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREI 160
Cdd:PRK07650  81 L--ENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILGKREI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 161 GNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWM 240
Cdd:PRK07650 159 GNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFV 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 504291509 241 TNSVLEIIPFTKIEEVNYGSQSGEATSALQLLYKKEIKNM 280
Cdd:PRK07650 239 TNSIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKL 278
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
 20-273 1.54e-99

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 291.91  E-value: 1.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  20 DHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEyTVSKHEILEMLDKLLKLNDIKDGnaRVRLNISAGISDK 99
Cdd:cd01559    1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIP-EPDLPRLRAALESLLAANDIDEG--RIRLILSRGPGGR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 100 GFVAQTYDKPTVLCFVNQLKPEslPLQKEGKVLSIRRNTPE--GSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAV 177
Cdd:cd01559   78 GYAPSVCPGPALYVSVIPLPPA--WRQDGVRLITCPVRLGEqpLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 178 AEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEvn 257
Cdd:cd01559  156 IEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD-- 233

                        250
                 ....*....|....*.
gi 504291509 258 YGSQSGEATSALQLLY 273
Cdd:cd01559  234 HDGPPGPLTRALRELL 249
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 1-279 2.47e-91

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 272.45  E-value: 2.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:COG0115    2 LIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IKDGnaRVRLNISAGISDKGFVAQTYdKPTVLCFVNQLKPESLPLQKEG---KVLSIRRNTPEGSFRLKSHHYLNNMYAK 157
Cdd:COG0115   82 LEDG--YIRPQVTRGVGGRGVFAEEY-EPTVIIIASPLPAYPAEAYEKGvrvITSPYRRAAPGGLGGIKTGNYLNNVLAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 158 REI---GNDprvEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLT 234
Cdd:COG0115  159 QEAkeaGAD---EALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYT 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 504291509 235 ADEAWMTNSVLEIIPFTKIEEVNYGS-QSGEATSALQLLYKKEIKN 279
Cdd:COG0115  236 ADEVFLTGTAAEVTPVTEIDGRPIGDgKPGPVTRRLRELYTDIVRG 281
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 20-273 1.03e-75

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 231.72  E-value: 1.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  20 DHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDIKDGnaRVRLNISAGISDK 99
Cdd:cd00449    1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASL--YIRPLLTRGVGGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 100 GFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLS---IRRNTPEGSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGA 176
Cdd:cd00449   79 GVAPPPSPEPTFVVFASPVGAYAKGGEKGVRLITspdRRRAAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNGY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 177 VAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEV 256
Cdd:cd00449  159 VTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGR 238

                        250
                 ....*....|....*...
gi 504291509 257 NYG-SQSGEATSALQLLY 273
Cdd:cd00449  239 GIGdGKPGPVTRKLRELL 256
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 28-253 4.05e-62

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 195.65  E-value: 4.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   28 GVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDikDGNARVRLNISAGISDKGFVAQTyd 107
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANG--LGVGRLRLTVSRGPGGFGLPTSD-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  108 kPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFW 187
Cdd:pfam01063  77 -PTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVFL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504291509  188 RKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKI 253
Cdd:pfam01063 156 VKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 3-273 2.42e-60

D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.


Pssm-ID: 238799 [Multi-domain]  Cd Length: 270  Bit Score: 192.81  E-value: 2.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   3 YVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDIK 82
Cdd:cd01558    1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  83 DGNARVRlnISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSI---RRNtpeGSFRLKSHHYLNNMYAKRE 159
Cdd:cd01558   81 EGDVYIQ--VTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITvpdIRW---LRCDIKSLNLLNNVLAKQE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 160 IGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAW 239
Cdd:cd01558  156 AKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVF 235

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 504291509 240 MTNSVLEIIPFTKIEEVNYGS-QSGEATSALQLLY 273
Cdd:cd01558  236 LTSTTAEVMPVVEIDGRPIGDgKPGPVTKRLREAY 270
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 2-253 1.79e-56

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 183.53  E-value: 1.79e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   2 IYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDI 81
Cdd:PRK08320   5 IYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  82 KDgnARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEG-KVL--SIRRNTPEG-SFRLKSHHYLNNMYAK 157
Cdd:PRK08320  85 RD--AYIRLVVSRGVGDLGLDPRKCPKPTVVCIAEPIGLYPGELYEKGlKVItvSTRRNRPDAlSPQVKSLNYLNNILAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 158 REIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADE 237
Cdd:PRK08320 163 IEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADE 242

                        250
                 ....*....|....*.
gi 504291509 238 AWMTNSVLEIIPFTKI 253
Cdd:PRK08320 243 VFLTGTAAEVIPVVKV 258
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
1-293 1.20e-46

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 158.58  E-value: 1.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLND 80
Cdd:PRK12479   5 YIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  81 IKDgnARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEG-KVLSI--RRNTPEG-SFRLKSHHYLNNMYA 156
Cdd:PRK12479  85 YAD--AYIRLIVSRGKGDLGLDPRSCVKPSVIIIAEQLKLFPQEFYDNGlSVVSVasRRNTPDAlDPRIKSMNYLNNVLV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 157 KREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTAD 236
Cdd:PRK12479 163 KIEAAQAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVAD 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504291509 237 EAWMTNSVLEIIPFTKIEEVNYG-SQSGEATSALQllykKEIKNMIHEKGGRAWRSTQ 293
Cdd:PRK12479 243 EVFLTGTAAELIPVVKVDSREIGdGKPGSVTKQLT----EEFKKLTRERGVRVPGLAE 296
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 1-270 4.98e-42

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 145.37  E-value: 4.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEkdavLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQI---EYTVSKHEILEMLDKLlk 77
Cdd:PRK06092   1 MFWINGQPQES----LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIpldDWAQLEQEMKQLAAEL-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  78 lndikdGNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRnTPEG-SFRLKSHHYLNNM-- 154
Cdd:PRK06092  75 ------ENGVLKVIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCP-TRLGrNPLLAGIKHLNRLeq 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 155 -YAKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALL 233
Cdd:PRK06092 148 vLIRAELEQTEADEALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELL 227

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 504291509 234 TADEAWMTNSVLEIIPFTKIEEVNYgsQSGEATSALQ 270
Cdd:PRK06092 228 QADEVFICNSLMPVWPVRAIGETSY--SSGTLTRYLQ 262
pabC_Proteo TIGR03461
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ...
 4-270 1.01e-39

aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]


Pssm-ID: 132501  Cd Length: 261  Bit Score: 139.26  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509    4 VNGRYMEEkdavLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYtVSKHEILEMLDKLLKlndiKD 83
Cdd:TIGR03461   2 VNGVLQTQ----ISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPL-PDWDALREEMAQLAA----GY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   84 GNARVRLNISAGISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEG---KVLSIR--RNTpegsfRLKSHHYLNNM---Y 155
Cdd:TIGR03461  73 SLGVLKVIISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGirlGVSPVRlgRNP-----LLAGIKHLNRLeqvL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  156 AKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTA 235
Cdd:TIGR03461 148 IKAELENSEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSA 227

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 504291509  236 DEAWMTNSVLEIIPFTKIEEVNYgsQSGEATSALQ 270
Cdd:TIGR03461 228 DEVFITNSLMGVVPVNAIGETSY--PSRTLTRLLQ 260
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 2-273 4.85e-38

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 135.83  E-value: 4.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   2 IYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDI 81
Cdd:PRK06680   5 AYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  82 KDGNarVRLNISAGISDKGFVAQTYD-KPTVLCFVNQLKPE-SLPLQKEG-KVLSIRRNtpegsfR-----LKSHHYLNN 153
Cdd:PRK06680  85 REGL--VYLQVTRGVARRDHVFPAADvKPSVVVFAKSVDFArPAAAAETGiKVITVPDN------RwkrcdIKSVGLLPN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 154 MYAKREIGNDPRVEGIFLtEDGAVAEGIISNVF--WRKGRCIyTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEA 231
Cdd:PRK06680 157 VLAKQAAKEAGAQEAWMV-DDGFVTEGASSNAWivTKDGKLV-TRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQE 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 504291509 232 LLTADEAWMTNSVLEIIPFTKIEEVNYGS-QSGEATSALQLLY 273
Cdd:PRK06680 235 AYAAREAFITAASSFVFPVVQIDGKQIGNgKPGPIAKRLREAY 277
PRK06606 PRK06606
branched-chain amino acid transaminase;
2-273 3.65e-31

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 117.94  E-value: 3.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   2 IYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEG----CPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLK 77
Cdd:PRK06606   9 IWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTpkgpAIFRLREHTKRLFNSAKILRMEIPYSVDELMEAQREVVR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  78 LNDIKDGNAR-------VRLNISA-GISDKGFVA----QTYdkptvlcfvnqLKPESLplqKEG---KVLSIRRNTPEGS 142
Cdd:PRK06606  89 KNNLKSAYIRplvfvgdEGLGVRPhGLPTDVAIAawpwGAY-----------LGEEAL---EKGirvKVSSWTRHAPNSI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 143 F-RLK-SHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGL 220
Cdd:PRK06606 155 PtRAKaSGNYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGI 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504291509 221 ELKTGRYELEALLTADEAWMTNSVLEIIPFTKIEEVNYGSQS-GEATSALQLLY 273
Cdd:PRK06606 235 EVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGKrGPITEKLQSAY 288
PRK07849 PRK07849
aminodeoxychorismate lyase;
15-253 1.53e-26

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 105.43  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  15 VLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLER--ALKDLQ----------IEYTVSKHeilemldkllklnDIK 82
Cdd:PRK07849  27 LLHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARsaALLDLPepdldrwrraVELAIEEW-------------RAP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  83 DGNARVRLNISAGISDKGfvaqtydKPTVLCFVNQLKPESLPLQKEG-KVLSIRRNTPEGSFRL--------KSHHYLNN 153
Cdd:PRK07849  94 EDEAALRLVYSRGRESGG-------APTAWVTVSPVPERVARARREGvSVITLDRGYPSDAAERapwllagaKTLSYAVN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 154 M----YAKREiGNDprvEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYEL 229
Cdd:PRK07849 167 MaalrYAARR-GAD---DVIFTSTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRP 242

                        250       260
                 ....*....|....*....|....
gi 504291509 230 EALLTADEAWMTNSVLEIIPFTKI 253
Cdd:PRK07849 243 ADLFAADGVWLVSSVRLAARVHTL 266
PRK12400 PRK12400
D-amino acid aminotransferase; Reviewed
 20-281 1.80e-24

D-amino acid aminotransferase; Reviewed


Pssm-ID: 171470  Cd Length: 290  Bit Score: 99.71  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  20 DHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDI-KDGNarVRLNISAGISD 98
Cdd:PRK12400  27 ERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFhEDGT--IYLQVSRGVQA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  99 KGFvAQTYD-KPTVLCFVNQLKPESLPLQKEGKVLSirrnTPEGSF---RLKSHHYLNNMYAKREIGNDPRVEGIFLtED 174
Cdd:PRK12400 105 RTH-TFSYDvPPTIYAYITKKERPALWIEYGVRAIS----EPDTRWlrcDIKSLNLLPNILAATKAERKGCKEALFV-RN 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 175 GAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKIE 254
Cdd:PRK12400 179 GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 258

                        250       260
                 ....*....|....*....|....*..
gi 504291509 255 evNYGSQSGEATSALQLLYKKEIKNMI 281
Cdd:PRK12400 259 --GTAIQDGQVGPITKMLQRSFSQSLL 283
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 1-278 7.40e-20

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 87.34  E-value: 7.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   1 MIYVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERA--LKDLQIEYTVSkhEILEMLDKLLKL 78
Cdd:PRK07544  10 FIWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSaeLLDFEIPYSVA--EIDAAKKETLAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  79 NDIKDgnARVRLNISAGISDKGFVAQ---------TYDKPtvlcfvNQLKPEslpLQKEGKVLSI---RRNTPEGS-FRL 145
Cdd:PRK07544  88 NGLTD--AYVRPVAWRGSEMMGVSAQqnkihlaiaAWEWP------SYFDPE---AKMKGIRLDIakwRRPDPETApSAA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 146 K-SHHYLNNMYAKREIGNDPRVEGIFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTgILDGVTRRFIIENAKNIGLELKT 224
Cdd:PRK07544 157 KaAGLYMICTISKHAAEAKGYADALMLDYRGYVAEATGANIFFVKDGVIHTPTPDC-FLDGITRQTVIELAKRRGIEVVE 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504291509 225 GRYELEALLTADEAWMTNSVLEIIPFTKIEEVNYgsQSGEATSALQLLYKKEIK 278
Cdd:PRK07544 236 RHIMPEELAGFSECFLTGTAAEVTPVSEIGEYRF--TPGAITRDLMDDYEALVR 287
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 16-273 4.68e-17

BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.


Pssm-ID: 238798  Cd Length: 279  Bit Score: 79.16  E-value: 4.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  16 LSPFDHGFLYGIGVFETFRLYEGCP-----FLLDWHIERLERALKDLQIEyTVSKHEILEMLDKLLKLNDI-----KDGN 85
Cdd:cd01557    2 LHPATHALHYGQAVFEGLKAYRTPDgkivlFRPDENAERLNRSARRLGLP-PFSVEEFIDAIKELVKLDADwvpygGGAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  86 ARVR---------LNISAGISDKGFVAQ----TYDKPtvlcfvnQLKPESLplqkegKVLSIRRNTPEGSFRLK-SHHYL 151
Cdd:cd01557   81 LYIRpfifgtdpqLGVSPALEYLFAVFAspvgAYFKG-------GEKGVSA------LVSSFRRAAPGGPGAAKaGGNYA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 152 NNMYAKREI---GNDprvEGIFL-TEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRY 227
Cdd:cd01557  148 ASLLAQKEAaekGYD---QALWLdGAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPI 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 504291509 228 ELEALLTADEAWMTNSVLEIIPFTKIE---EVNYGSQSGEATSALQLLY 273
Cdd:cd01557  225 TRDELYEADEVFATGTAAVVTPVGEIDyrgKEPGEGEVGPVTKKLYDLL 273
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 15-269 1.45e-12

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 66.96  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  15 VLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEMLDKLLKLNDIKDGNarVRLNISA 94
Cdd:PLN02845  56 VIPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGS--LRYWLSA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  95 GISDKGFVAQTYDKPTVLCFVNQLKPESLPLQKEGKVLSIRRNTPEGSFRLKSHHYLNNMYAKRE-IGNDPRVeGIFLTE 173
Cdd:PLN02845 134 GPGGFSLSPSGCSEPAFYAVVIEDTYAQDRPEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEaEERGAFA-GIWLDE 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 174 DGAVAEGIISNV-FWRKGRCIYTPSLDTgILDGVTRRFIIENA-----KNIGLELKTGRYELEALLTADEAWMTNSVLEI 247
Cdd:PLN02845 213 EGFVAEGPNMNVaFLTNDGELVLPPFDK-ILSGCTARRVLELAprlvsPGDLRGVKQRKISVEEAKAADEMMLIGSGVPV 291

                        250       260
                 ....*....|....*....|...
gi 504291509 248 IPFTKIEEVNYGS-QSGEATSAL 269
Cdd:PLN02845 292 LPIVSWDGQPIGDgKVGPITLAL 314
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
3-273 2.20e-11

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 63.05  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509   3 YVNGRYMEEKDAVLSPFDHGFLYGIGVFETFRLYEGCPFLLDWHIERLERALKDLQIEYTVSKHEILEM-LDKLLKLNdi 81
Cdd:PRK13356  10 FFDGEWHEGNVPIMGPADHAAWLGSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLKPTVSAEEIEALaREGLKRFD-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509  82 KDGNARVRLNISAGISDKGFVAQTYDKPT-VLCFvnqlkpESLPLQKEGK----VLSIRRNTPE--------GSFrlksh 148
Cdd:PRK13356  88 PDTALYIRPMYWAEDGFASGVAPDPESTRfALCL------EEAPMPEPTGfsltLSPFRRPTLEmaptdakaGCL----- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 149 hYLNNMYAKREigndPRVEG----IFLTEDGAVAEGIISNVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKT 224
Cdd:PRK13356 157 -YPNNARALRE----ARSRGfdnaLVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVE 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 504291509 225 GRYELEALLTADEAWMTNSVLEIIPFTKIEEVNYgsQSGEATSALQLLY 273
Cdd:PRK13356 232 TTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL--QPGPVTRRARELY 278
PRK07546 PRK07546
hypothetical protein; Provisional
 167-249 6.80e-09

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 54.98  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 167 EGIFLTEDGAVAEGIISNVFW-RKGRCIYTPSLDTGILDGVTRRFIIENAKnigleLKTGRYELEALLTADEAWMTNSVL 245
Cdd:PRK07546 127 EVILLNERGEVCEGTITNVFLdRGGGMLTTPPLSCGLLPGVLRAELLDAGR-----AREAVLTVDDLKSARAIWVGNSLR 201


                 ....
gi 504291509 246 EIIP 249
Cdd:PRK07546 202 GLIR 205
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 184-271 4.72e-07

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 50.31  E-value: 4.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 184 NVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIipfTKIEEVNY----- 258
Cdd:PLN03117 239 NIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVV---KAVETVTFhdkkv 315

                         90
                 ....*....|...
gi 504291509 259 GSQSGEATSALQL 271
Cdd:PLN03117 316 KYRTGEEALSTKL 328
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 184-273 1.96e-06

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 48.69  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 184 NVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKI----EEVNYG 259
Cdd:PLN02782 290 NIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSItykgKRVSYG 369

                         90
                 ....*....|....
gi 504291509 260 SQSGEATSalQLLY 273
Cdd:PLN02782 370 EGGFGTVS--QQLY 381
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 184-253 4.34e-06

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 47.41  E-value: 4.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 184 NVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEAWMTNSVLEIIPFTKI 253
Cdd:PLN02259 276 NVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTI 345
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 129-243 1.28e-04

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 43.17  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504291509 129 GKVLSIRRntpegsfRLKSHHYLNNMYAKREIGNDprvegifltedgaVAEGIISNVFWRKGRCIYTPSLDTGILDGVTR 208
Cdd:PLN02883 237 GPVLEVMR-------RAKSRGFSDVLYLDADTGKN-------------IEEVSAANIFLVKGNIIVTPATSGTILGGITR 296

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504291509 209 RFIIENAKNIGLELKTGRYELEALLTADEAWMTNS 243
Cdd:PLN02883 297 KSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGT 331
PRK13357 PRK13357
branched-chain amino acid aminotransferase; Provisional
 184-238 6.73e-03

branched-chain amino acid aminotransferase; Provisional


Pssm-ID: 237363  Cd Length: 356  Bit Score: 37.43  E-value: 6.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504291509 184 NVFWRKGRCIYTPSLDTGILDGVTRRFIIENAKNIGLELKTGRYELEALLTADEA 238
Cdd:PRK13357 237 NFFFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAAS 291
 
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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