NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489933842|ref|WP_003837154|]
View 

MULTISPECIES: tyrosine phenol-lyase [Citrobacter]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
5-454 0e+00

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).


The actual alignment was detected with superfamily member TIGR02618:

Pssm-ID: 450240  Cd Length: 450  Bit Score: 932.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842    5 AEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTV 84
Cdd:TIGR02618   1 AEPYKIKAVEPISMTTREEREKKMQEAGYNTFLLNSEDVYIDLLTDSGTNAMSDKQWAGLMMGDEAYAGSRNFYHLERTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   85 QELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQ 164
Cdd:TIGR02618  81 RELYGFKYVVPTHQGRGAENLLSQIAIKPGDYVPGNMYFTTTRYHQEKNGATFVDIIIDEAHDAQLNIPFKGNVDLKKLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  165 KLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEM 244
Cdd:TIGR02618 161 KLIDEVGADKIPYICLAVTVNLAGGQPVSMANMREVRELCEAHGIKVFYDATRCVENAYFIKEREQGYEDKSIAEILKEM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  245 FSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRY 324
Cdd:TIGR02618 241 MSYADGCTMSGKKDCLVNIGGFLCMNDDEMFQSAKELVVVFEGMPSYGGLAGRDMEAMAIGIREAVDYEYIEHRVKQVRY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  325 LGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVR 404
Cdd:TIGR02618 321 LGDKLKAAGVPIVEPVGGHAVFLDARRFLPHIPQDQFPAQSLAASIYVETGVRSMERGIVSAGRNNVTGEHHRPKLELVR 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 489933842  405 LTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFD 454
Cdd:TIGR02618 401 LTIPRRVYTYAHMDVVADGIIKLYKHRDDIRGLKMVYEPKQLRFFTARFE 450
 
Name Accession Description Interval E-value
tyr_phenol_ly TIGR02618
tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) ...
5-454 0e+00

tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) (beta-tyrosinase), a pyridoxal-phosphate enzyme closely related to tryptophanase (4.1.99.1) (see model TIGR02617). Both belong to the beta-eliminating lyase family (pfam01212) [Energy metabolism, Amino acids and amines]


Pssm-ID: 131667  Cd Length: 450  Bit Score: 932.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842    5 AEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTV 84
Cdd:TIGR02618   1 AEPYKIKAVEPISMTTREEREKKMQEAGYNTFLLNSEDVYIDLLTDSGTNAMSDKQWAGLMMGDEAYAGSRNFYHLERTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   85 QELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQ 164
Cdd:TIGR02618  81 RELYGFKYVVPTHQGRGAENLLSQIAIKPGDYVPGNMYFTTTRYHQEKNGATFVDIIIDEAHDAQLNIPFKGNVDLKKLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  165 KLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEM 244
Cdd:TIGR02618 161 KLIDEVGADKIPYICLAVTVNLAGGQPVSMANMREVRELCEAHGIKVFYDATRCVENAYFIKEREQGYEDKSIAEILKEM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  245 FSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRY 324
Cdd:TIGR02618 241 MSYADGCTMSGKKDCLVNIGGFLCMNDDEMFQSAKELVVVFEGMPSYGGLAGRDMEAMAIGIREAVDYEYIEHRVKQVRY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  325 LGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVR 404
Cdd:TIGR02618 321 LGDKLKAAGVPIVEPVGGHAVFLDARRFLPHIPQDQFPAQSLAASIYVETGVRSMERGIVSAGRNNVTGEHHRPKLELVR 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 489933842  405 LTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFD 454
Cdd:TIGR02618 401 LTIPRRVYTYAHMDVVADGIIKLYKHRDDIRGLKMVYEPKQLRFFTARFE 450
TnaA COG3033
Tryptophanase [Amino acid transport and metabolism];
1-456 0e+00

Tryptophanase [Amino acid transport and metabolism];


Pssm-ID: 442268  Cd Length: 460  Bit Score: 859.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   1 MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHL 80
Cdd:COG3033    3 MKTPAEPFRIKMVEPIRMTTREERERALKEAGYNTFLLRSEDVYIDLLTDSGTGAMSDRQWAAMMLGDESYAGSRSFYRL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  81 ERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDL 160
Cdd:COG3033   83 EDAVRDIFGFKYVLPTHQGRAAENILFPVLVKPGDVVPSNMHFDTTRAHIELAGARAVDLVIDEALDPESDHPFKGNMDL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 161 KKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEI 240
Cdd:COG3033  163 DKLEALIEEVGAENIPFVMMTITNNSAGGQPVSMANIREVRELADKYGIPLVLDAARFAENAYFIKQREEGYADKSIKEI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 241 VHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVK 320
Cdd:COG3033  243 VREMFSYADGFTMSAKKDGLVNIGGFLALRDEELFEKARNLVILYEGFPTYGGLAGRDMEALAVGLYEGLDEDYLRYRIG 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 321 QVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKL 400
Cdd:COG3033  323 QVEYLGEKLDEAGVPVVTPAGGHAVFVDAKRFLPHIPQEQFPAQALAAALYLESGIRGVEIGSLSLGRDPDTGEQVPAPL 402
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489933842 401 ETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFDYI 456
Cdd:COG3033  403 ELVRLAIPRRVYTQSHMDYVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPV 458
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
23-453 0e+00

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 798.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  23 ERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGA 102
Cdd:cd00617    1 ERERALKEAGYNVFLLRSEDVYIDLLTDSGTGAMSDYQWAAMMLGDEAYAGSKSFYDLEDAVQDLFGFKHIIPTHQGRGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 103 ENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQKLIDEKGAENIAYICLAV 182
Cdd:cd00617   81 ENILFSILLKPGRTVPSNMHFDTTRGHIEANGAVPVDLVIDEAHDAQELIPFKGNIDVAKLEKLIDEVGAENIPYIVLTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 183 TVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGCTMSGKKDCLVN 262
Cdd:cd00617  161 TNNTAGGQPVSMANLREVRELAHKYGIPVVLDAARFAENAYFIKEREEGYRDKSIAEIAREMFSYADGCTMSAKKDGLVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 263 IGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGG 342
Cdd:cd00617  241 IGGFLALRDDELYEEARQRVVLYEGFVTYGGMAGRDMEALAQGLREAVEEDYLRHRVEQVRYLGDRLDEAGVPIVEPAGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 343 HAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVRLTIPRRVYTYAHMDVVAD 422
Cdd:cd00617  321 HAVFIDAREFLPHIPQEQFPAQALAAELYLEAGVRAVELGIFSAGRDPNTGENKYPELELVRLAIPRRVYTQDHMDYVAA 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 489933842 423 GIIKLYQHKEDIRGLKFIYEPKQLRFFTARF 453
Cdd:cd00617  401 AVIALYERREDIRGLRIVYEPKLLRHFTARL 431
tnaA PRK13238
tryptophanase;
1-454 0e+00

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 736.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   1 MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHL 80
Cdd:PRK13238   4 MKHLPEPFRIKMVEPIRLTTREERERALAEAGYNPFLLKSEDVFIDLLTDSGTGAMSDRQWAAMMRGDEAYAGSRSYYRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  81 ERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDL 160
Cdd:PRK13238  84 EDAVKDIFGYPYTIPTHQGRAAEQILFPVLIKKGDVVPSNYHFDTTRAHIELNGATAVDLVIDEALDTGSRHPFKGNFDL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 161 KKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEI 240
Cdd:PRK13238 164 EKLEALIEEVGAENVPFIVMTITNNSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARFAENAYFIKQREPGYKDKSIKEI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 241 VHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVK 320
Cdd:PRK13238 244 AREMFSYADGLTMSAKKDAMVNIGGLLCFRDEDLFTECRTLCILYEGFPTYGGLAGRDMEALAVGLYEGMDEDYLAYRIG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 321 QVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKL 400
Cdd:PRK13238 324 QVEYLGEGLEEAGVPIQTPAGGHAVFVDAGKFLPHIPAEQFPAQALACELYLEAGIRGVEIGSLLLGRDPKTGEQLPAPA 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489933842 401 ETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFD 454
Cdd:PRK13238 404 ELLRLAIPRRVYTQSHMDYVAEALKAVKENRESIKGLRFTYEPPVLRHFTARLK 457
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
46-422 7.04e-101

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 302.98  E-value: 7.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   46 DLLTDS---GTNAMSDKQwAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYV----A 118
Cdd:pfam01212   1 DLRSDTvtgPTPAMREAM-AAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVicgeP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  119 GNMYFTTTRYHQEKNGAVFVDIVRDEAhdaglniafkGDIDLKKLQKLIDEKGA---ENIAYICLAVTVNLAGGQPVSMA 195
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDEA----------GNMDLEDLEAAIREVGAdifPPTGLISLENTHNSAGGQVVSLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  196 NMRAVRELTEAHGIKVFYDATRCVENAyfikeqeqgfenKSIAEIVHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDemf 275
Cdd:pfam01212 150 NLREIAALAREHGIPVHLDGARFANAA------------VALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDD--- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  276 ssakelvvvyegmpsygglagrdmeamaiglreamqyeYIEHRVKQVRYLGDKLKAAGVPIvepvgghavfldarrfceh 355
Cdd:pfam01212 215 --------------------------------------FIAKAIRQRKYLGGGLRQAGVLA------------------- 237
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489933842  356 ltqdefpaqslAAsiyvetGVRSMERGIISAGRNNVTGEHHRPKLETVRLTIPRRVYTYAHMDVVAD 422
Cdd:pfam01212 238 -----------AA------GLRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAA 287
 
Name Accession Description Interval E-value
tyr_phenol_ly TIGR02618
tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) ...
5-454 0e+00

tyrosine phenol-lyase; This model describes a group of tyrosine phenol-lyase (4.1.99.2) (beta-tyrosinase), a pyridoxal-phosphate enzyme closely related to tryptophanase (4.1.99.1) (see model TIGR02617). Both belong to the beta-eliminating lyase family (pfam01212) [Energy metabolism, Amino acids and amines]


Pssm-ID: 131667  Cd Length: 450  Bit Score: 932.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842    5 AEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTV 84
Cdd:TIGR02618   1 AEPYKIKAVEPISMTTREEREKKMQEAGYNTFLLNSEDVYIDLLTDSGTNAMSDKQWAGLMMGDEAYAGSRNFYHLERTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   85 QELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQ 164
Cdd:TIGR02618  81 RELYGFKYVVPTHQGRGAENLLSQIAIKPGDYVPGNMYFTTTRYHQEKNGATFVDIIIDEAHDAQLNIPFKGNVDLKKLQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  165 KLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEM 244
Cdd:TIGR02618 161 KLIDEVGADKIPYICLAVTVNLAGGQPVSMANMREVRELCEAHGIKVFYDATRCVENAYFIKEREQGYEDKSIAEILKEM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  245 FSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRY 324
Cdd:TIGR02618 241 MSYADGCTMSGKKDCLVNIGGFLCMNDDEMFQSAKELVVVFEGMPSYGGLAGRDMEAMAIGIREAVDYEYIEHRVKQVRY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  325 LGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVR 404
Cdd:TIGR02618 321 LGDKLKAAGVPIVEPVGGHAVFLDARRFLPHIPQDQFPAQSLAASIYVETGVRSMERGIVSAGRNNVTGEHHRPKLELVR 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 489933842  405 LTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFD 454
Cdd:TIGR02618 401 LTIPRRVYTYAHMDVVADGIIKLYKHRDDIRGLKMVYEPKQLRFFTARFE 450
TnaA COG3033
Tryptophanase [Amino acid transport and metabolism];
1-456 0e+00

Tryptophanase [Amino acid transport and metabolism];


Pssm-ID: 442268  Cd Length: 460  Bit Score: 859.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   1 MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHL 80
Cdd:COG3033    3 MKTPAEPFRIKMVEPIRMTTREERERALKEAGYNTFLLRSEDVYIDLLTDSGTGAMSDRQWAAMMLGDESYAGSRSFYRL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  81 ERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDL 160
Cdd:COG3033   83 EDAVRDIFGFKYVLPTHQGRAAENILFPVLVKPGDVVPSNMHFDTTRAHIELAGARAVDLVIDEALDPESDHPFKGNMDL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 161 KKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEI 240
Cdd:COG3033  163 DKLEALIEEVGAENIPFVMMTITNNSAGGQPVSMANIREVRELADKYGIPLVLDAARFAENAYFIKQREEGYADKSIKEI 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 241 VHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVK 320
Cdd:COG3033  243 VREMFSYADGFTMSAKKDGLVNIGGFLALRDEELFEKARNLVILYEGFPTYGGLAGRDMEALAVGLYEGLDEDYLRYRIG 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 321 QVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKL 400
Cdd:COG3033  323 QVEYLGEKLDEAGVPVVTPAGGHAVFVDAKRFLPHIPQEQFPAQALAAALYLESGIRGVEIGSLSLGRDPDTGEQVPAPL 402
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489933842 401 ETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFDYI 456
Cdd:COG3033  403 ELVRLAIPRRVYTQSHMDYVAEALIELYERRESIKGLRIVYEPPVLRHFTARLEPV 458
Tnase_like cd00617
Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent ...
23-453 0e+00

Tryptophanase family (Tnase). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to tryptophanase (Tnase) and tyrosine phenol-lyase (TPL). Tnase and TPL are active as tetramers and catalyze beta-elimination reactions. Tnase catalyzes degradation of L-tryptophan to yield indole, pyruvate and ammonia and TPL catalyzes degradation of L-tyrosine to yield phenol, pyruvate and ammonia.


Pssm-ID: 99741  Cd Length: 431  Bit Score: 798.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  23 ERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGA 102
Cdd:cd00617    1 ERERALKEAGYNVFLLRSEDVYIDLLTDSGTGAMSDYQWAAMMLGDEAYAGSKSFYDLEDAVQDLFGFKHIIPTHQGRGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 103 ENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDLKKLQKLIDEKGAENIAYICLAV 182
Cdd:cd00617   81 ENILFSILLKPGRTVPSNMHFDTTRGHIEANGAVPVDLVIDEAHDAQELIPFKGNIDVAKLEKLIDEVGAENIPYIVLTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 183 TVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEIVHEMFSYADGCTMSGKKDCLVN 262
Cdd:cd00617  161 TNNTAGGQPVSMANLREVRELAHKYGIPVVLDAARFAENAYFIKEREEGYRDKSIAEIAREMFSYADGCTMSAKKDGLVN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 263 IGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVKQVRYLGDKLKAAGVPIVEPVGG 342
Cdd:cd00617  241 IGGFLALRDDELYEEARQRVVLYEGFVTYGGMAGRDMEALAQGLREAVEEDYLRHRVEQVRYLGDRLDEAGVPIVEPAGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 343 HAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKLETVRLTIPRRVYTYAHMDVVAD 422
Cdd:cd00617  321 HAVFIDAREFLPHIPQEQFPAQALAAELYLEAGVRAVELGIFSAGRDPNTGENKYPELELVRLAIPRRVYTQDHMDYVAA 400
                        410       420       430
                 ....*....|....*....|....*....|.
gi 489933842 423 GIIKLYQHKEDIRGLKFIYEPKQLRFFTARF 453
Cdd:cd00617  401 AVIALYERREDIRGLRIVYEPKLLRHFTARL 431
tnaA PRK13238
tryptophanase;
1-454 0e+00

tryptophanase;


Pssm-ID: 237314  Cd Length: 460  Bit Score: 736.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   1 MNYPAEPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHL 80
Cdd:PRK13238   4 MKHLPEPFRIKMVEPIRLTTREERERALAEAGYNPFLLKSEDVFIDLLTDSGTGAMSDRQWAAMMRGDEAYAGSRSYYRL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  81 ERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFKGDIDL 160
Cdd:PRK13238  84 EDAVKDIFGYPYTIPTHQGRAAEQILFPVLIKKGDVVPSNYHFDTTRAHIELNGATAVDLVIDEALDTGSRHPFKGNFDL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 161 KKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENKSIAEI 240
Cdd:PRK13238 164 EKLEALIEEVGAENVPFIVMTITNNSAGGQPVSMANLRAVYEIAKKYGIPVVIDAARFAENAYFIKQREPGYKDKSIKEI 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 241 VHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDEMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQYEYIEHRVK 320
Cdd:PRK13238 244 AREMFSYADGLTMSAKKDAMVNIGGLLCFRDEDLFTECRTLCILYEGFPTYGGLAGRDMEALAVGLYEGMDEDYLAYRIG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 321 QVRYLGDKLKAAGVPIVEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVTGEHHRPKL 400
Cdd:PRK13238 324 QVEYLGEGLEEAGVPIQTPAGGHAVFVDAGKFLPHIPAEQFPAQALACELYLEAGIRGVEIGSLLLGRDPKTGEQLPAPA 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489933842 401 ETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARFD 454
Cdd:PRK13238 404 ELLRLAIPRRVYTQSHMDYVAEALKAVKENRESIKGLRFTYEPPVLRHFTARLK 457
tnaA_trp_ase TIGR02617
tryptophanase, leader peptide-associated; Members of this family belong to the ...
6-453 0e+00

tryptophanase, leader peptide-associated; Members of this family belong to the beta-eliminating lyase family (pfam01212) and act as tryptophanase (L-tryptophan indole-lyase). The tryptophanases of this family, as a rule, are found with a tryptophanase leader peptide (TnaC) encoded upstream. Both tryptophanases (4.1.99.1) and tyrosine phenol-lyases (EC 4.1.99.2) are found between trusted and noise cutoffs, but this model captures nearly all tryptophanases for which the leader peptide gene tnaC can be found upstream. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131666  Cd Length: 467  Bit Score: 515.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842    6 EPFRIKSVETVSMIPRDERLKKMQEAGYNTFLLNSKDIYIDLLTDSGTNAMSDKQWAGMMMGDEAYAGSENFYHLERTVQ 85
Cdd:TIGR02617   5 EPFRIRVIEPVKRTTRAYREKAIIKAGMNPFLLDSEDVFIDLLTDSGTGAVTQSMQAAMMRGDEAYSGSRSYYALAESVK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   86 ELFGFKHIVPTHQGRGAENLLSQLAIK----------PGQYVAGNMYFTTTRYHQEKNGAVFVDIVRDEAHDAGLNIAFK 155
Cdd:TIGR02617  85 NIFGYQYTIPTHQGRGAEQIYIPVLIKkreqekgldrSKMVAFSNYFFDTTQGHSQINGCTARNVYTKEAFDTGVRYDFK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  156 GDIDLKKLQKLIDEKGAENIAYICLAVTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATRCVENAYFIKEQEQGFENK 235
Cdd:TIGR02617 165 GNFDLEGLERGIEEVGPNNVPYIVATITCNSAGGQPVSLANLKAVYEIAKKYDIPVVMDSARFAENAYFIKQREAEYKNW 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  236 SIAEIVHEMFSYADGCTMSGKKDCLVNIGGFLCMNDD---EMFSSAKELVVVYEGMPSYGGLAGRDMEAMAIGLREAMQY 312
Cdd:TIGR02617 245 SIEQITRETYKYADMLAMSAKKDAMVPMGGLLCFKDDsffDVYTECRTLCVVQEGFPTYGGLEGGAMERLAVGLYDGMNL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  313 EYIEHRVKQVRYLGDKLKAAGVPIvEPVGGHAVFLDARRFCEHLTQDEFPAQSLAASIYVETGVRSMERGIISAGRNNVT 392
Cdd:TIGR02617 325 DWLAYRINQVQYLVNGLEEIGVVC-QQAGGHAAFVDAGKLLPHIPADQFPAHALACELYKVAGIRAVEIGSLLLGRDPKT 403
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489933842  393 GEHHRPKLETVRLTIPRRVYTYAHMDVVADGIIKLYQHKEDIRGLKFIYEPKQLRFFTARF 453
Cdd:TIGR02617 404 GKQLPCPAELLRLTIPRATYTQTHMDFIIEAFKHVKENAPNIKGLTFTYEPKVLRHFTARL 464
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
46-422 7.04e-101

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 302.98  E-value: 7.04e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842   46 DLLTDS---GTNAMSDKQwAGMMMGDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGAENLLSQLAIKPGQYV----A 118
Cdd:pfam01212   1 DLRSDTvtgPTPAMREAM-AAAMVGDEVYGGDPTVNRLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVicgeP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  119 GNMYFTTTRYHQEKNGAVFVDIVRDEAhdaglniafkGDIDLKKLQKLIDEKGA---ENIAYICLAVTVNLAGGQPVSMA 195
Cdd:pfam01212  80 AHIHFDETGGHAELGGVQPRPLDGDEA----------GNMDLEDLEAAIREVGAdifPPTGLISLENTHNSAGGQVVSLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  196 NMRAVRELTEAHGIKVFYDATRCVENAyfikeqeqgfenKSIAEIVHEMFSYADGCTMSGKKDCLVNIGGFLCMNDDemf 275
Cdd:pfam01212 150 NLREIAALAREHGIPVHLDGARFANAA------------VALGVIVKEITSYADSVTMCLSKGLGAPVGSVLAGSDD--- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  276 ssakelvvvyegmpsygglagrdmeamaiglreamqyeYIEHRVKQVRYLGDKLKAAGVPIvepvgghavfldarrfceh 355
Cdd:pfam01212 215 --------------------------------------FIAKAIRQRKYLGGGLRQAGVLA------------------- 237
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489933842  356 ltqdefpaqslAAsiyvetGVRSMERGIISAGRNNVTGEHHRPKLETVRLTIPRRVYTYAHMDVVAD 422
Cdd:pfam01212 238 -----------AA------GLRALEEGVARLARDHATARRLAEGLELLRLAIPRRVYTNTHMVYVAA 287
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
76-270 5.66e-32

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: 119.79  E-value: 5.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  76 NFYHLERTVQELF--GFKHIVPTHQGRGAENLLSQLAIKPGQYVAGNMYFTTTRY--HQEKNGAVFVDIVRDEAHDAGLN 151
Cdd:cd01494    1 KLEELEEKLARLLqpGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYwvAAELAGAKPVPVPVDDAGYGGLD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 152 IafkgdidlkklQKLIDEKGAENIAYICLAVTVNLAGGQPVSmanmRAVRELTEAHGIKVFYDATRCVENAYFIKeqeqg 231
Cdd:cd01494   81 V-----------AILEELKAKPNVALIVITPNTTSGGVLVPL----KEIRKIAKEYGILLLVDAASAGGASPAPG----- 140
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 489933842 232 fenksiaeiVHEMFSYADGCTMSGKKDCLVNIGGFLCMN 270
Cdd:cd01494  141 ---------VLIPEGGADVVTFSLHKNLGGEGGGVVIVK 170
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
80-215 9.81e-05

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


Pssm-ID: 440168  Cd Length: 364  Bit Score: 44.29  E-value: 9.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  80 LERTVQELFGFKHIVPTHQGRGAeNLLSQLA--IKPGQYV--AGNMYFTTT---RYhqekNGA--VFVDIvrDEAHdagL 150
Cdd:COG0399   35 FEEEFAAYLGVKHAVAVSSGTAA-LHLALRAlgIGPGDEVitPAFTFVATAnaiLY----VGAtpVFVDI--DPDT---Y 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489933842 151 NIafkgdiDLKKLQKLIDEKgaenIAYIclaVTVNLAGgQPvsmANMRAVRELTEAHGIKVFYDA 215
Cdd:COG0399  105 NI------DPEALEAAITPR----TKAI---IPVHLYG-QP---ADMDAIMAIAKKHGLKVIEDA 152
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
67-361 2.06e-04

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: 43.09  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  67 GDEAYAGSENFYHLERTVQELFGFKHIVPTHQGRGAeNLLSQLAIkpgqyvagnmyftTTRYHqekngAVFVD----IVR 142
Cdd:cd06502   24 GDDVYGEDPTTAKLEARAAELFGKEAALFVPSGTAA-NQLALAAH-------------TQPGG-----SVICHetahIYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 143 DEA----HDAGLN-IAFKGDIDLKKLQKLIDEKGAENIAY------ICLAVTVNLAGGQPVsmANMRAVRELTEAHGIKV 211
Cdd:cd06502   85 DEAgapeFLSGVKlLPVPGENGKLTPEDLEAAIRPRDDIHfpppslVSLENTTEGGTVYPL--DELKAISALAKENGLPL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 212 FYDATRcvenayfikeqeqgFENKSIAEIVHEM--FSYADGCTMSGKKDCLVNIGGFLCMNDD--EMFSSAKELvvvyeg 287
Cdd:cd06502  163 HLDGAR--------------LANAAAALGVALKtyKSGVDSVSFCLSKGGGAPVGAVVVGNRDfiARARRRRKQ------ 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 288 mpsYGGLAgRDMEAMAIGLREAMQYEYIEHRVKQV----RYLGDKLKAAG---------VPIVEPVGGHAVFLDARRFCE 354
Cdd:cd06502  223 ---AGGGM-RQSGFLAAAGLAALENDLWLRRLRHDhemaRRLAEALEELGglesevqtnIVLLDPVEANAVFVELSKEAI 298

                 ....*..
gi 489933842 355 HLTQDEF 361
Cdd:cd06502  299 ERRGEGV 305
AHBA_syn cd00616
3-amino-5-hydroxybenzoic acid synthase family (AHBA_syn). AHBA_syn family belongs to pyridoxal ...
80-215 1.28e-03

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: 40.99  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  80 LERTVQELFGFKHIVPTHQGRGAeNLLSQLA--IKPGQYV--AGNMYFTTTryhqekN-----GA--VFVDIvrDEAHda 148
Cdd:cd00616   23 FEKAFAEYLGVKYAVAVSSGTAA-LHLALRAlgIGPGDEVivPSFTFVATA------NailllGAtpVFVDI--DPDT-- 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489933842 149 gLNIafkgdiDLKKLQKLIDEKgaenIAYIclaVTVNLAGgqpvSMANMRAVRELTEAHGIKVFYDA 215
Cdd:cd00616   92 -YNI------DPELIEAAITPR----TKAI---IPVHLYG----NPADMDAIMAIAKRHGLPVIEDA 140
PLN02721 PLN02721
threonine aldolase
45-217 6.85e-03

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 38.52  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842  45 IDLLTDSGTNAmSDKQWAGMM---MGDEAYAGSENFYHLERTVQELFGFKH--IVPT-----------H-QGRGAENLL- 106
Cdd:PLN02721   8 VDLRSDTVTKP-TDAMRAAMAnaeVDDDVLGYDPTALRLEEEMAKIFGKEAalFVPSgtmgnlisvlvHcDVRGSEVILg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489933842 107 --SQLAIkpgqYVAGNMYFtttryhqekNGAVFVDIVRDEAhdaglniafKGDIDLKKLQKLIDEKGAENIA---YICLA 181
Cdd:PLN02721  87 dnSHIHL----YENGGIST---------LGGVHPRTVKNNE---------DGTMDLDAIEAAIRPKGDDHFPttrLICLE 144
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489933842 182 VTVNLAGGQPVSMANMRAVRELTEAHGIKVFYDATR 217
Cdd:PLN02721 145 NTHANCGGRCLSVEYTDKVGELAKRHGLKLHIDGAR 180
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH