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Conserved domains on  [gi|1489134502|ref|NP_417511|]
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4,5-DOPA dioxygenase extradiol [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

dioxygenase( domain architecture ID 10793431)

dioxygenase similar to 4,5-DOPA extradiol dioxygenase, which opens the cyclic ring of 4,5-dihydroxy-phenylalanine (DOPA) to form betalamic acid

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK10628 PRK10628
LigB family dioxygenase; Provisional
26-271 0e+00

LigB family dioxygenase; Provisional


:

Pssm-ID: 182598  Cd Length: 246  Bit Score: 528.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  26 MNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 105
Cdd:PRK10628    1 MNVLEDNLYTRAWRTLGETLPRPKAIVVVSAHWYTRGTGVTAMETPRTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 106 APIPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 185
Cdd:PRK10628   81 APVPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSTKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 186 GDSSPYPWATSFNEYVKANLTWQGPVEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPITIPVEGIEMGSLSM 265
Cdd:PRK10628  161 GDSSPYPWAESFNQFVKANLTWQGPVEQHPLVNYLQHEGGALSNPTPEHYLPLLYVLGAWDGKEPISIPVDGIEMGSLSM 240

                  ....*.
gi 1489134502 266 LSVQIG 271
Cdd:PRK10628  241 LSVQVG 246
 
Name Accession Description Interval E-value
PRK10628 PRK10628
LigB family dioxygenase; Provisional
26-271 0e+00

LigB family dioxygenase; Provisional


Pssm-ID: 182598  Cd Length: 246  Bit Score: 528.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  26 MNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 105
Cdd:PRK10628    1 MNVLEDNLYTRAWRTLGETLPRPKAIVVVSAHWYTRGTGVTAMETPRTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 106 APIPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 185
Cdd:PRK10628   81 APVPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSTKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 186 GDSSPYPWATSFNEYVKANLTWQGPVEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPITIPVEGIEMGSLSM 265
Cdd:PRK10628  161 GDSSPYPWAESFNQFVKANLTWQGPVEQHPLVNYLQHEGGALSNPTPEHYLPLLYVLGAWDGKEPISIPVDGIEMGSLSM 240

                  ....*.
gi 1489134502 266 LSVQIG 271
Cdd:PRK10628  241 LSVQVG 246
LigB COG3384
Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites ...
13-271 6.11e-132

Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442611  Cd Length: 260  Bit Score: 373.74  E-value: 6.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  13 TRMPALFLGHGSPMNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAP 92
Cdd:COG3384     2 GRLPALFISHGSPMNALEDGALTAALRRLGRRLPRPDAILVVSAHWETRGTTVTAAARPETIYDFYGFPPELYELQYPAP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  93 GSPALAQRLVELLAP--IPVTLDkEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLV 170
Cdd:COG3384    82 GDPELAERVAELLAAagLPVRLD-PERGLDHGTWVPLRLMYPDADIPVVQLSLDPTLDPAEHYALGRALAPLRDEGVLII 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 171 ASGNVVHNLRTVKWHGDSS-PYPWATSFNEYVKANLTWQgpvEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQE 249
Cdd:COG3384   161 GSGSLVHNLRALRWGPGDAiPSPWAEEFDDWLLEALAAG---DHDALLDYRPAPYARLAHPTEEHLLPLLVALGAAGDDA 237
                         250       260
                  ....*....|....*....|..
gi 1489134502 250 PITIPVEGIEMGSLSMLSVQIG 271
Cdd:COG3384   238 KARVFHDGVEYGSLSMRSVQFG 259
45_DOPA_Dioxygenase cd07363
The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both ...
16-270 1.57e-121

The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine; This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153375  Cd Length: 253  Bit Score: 347.21  E-value: 1.57e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  16 PALFLGHGSPMNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSP 95
Cdd:cd07363     1 PVLFISHGSPMLALEDNPATAFLRELGKELPKPKAILVISAHWETRGPTVTASARPETIYDFYGFPPELYEIQYPAPGSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  96 ALAQRLVELL--APIPVTLDKEaWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASG 173
Cdd:cd07363    81 ELAERVAELLkaAGIPARLDPE-RGLDHGAWVPLKLMYPDADIPVVQLSLPASLDPAEHYALGRALAPLRDEGVLIIGSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 174 NVVHNLRTVKWHGDSSPYPWATSFNEYVKANLTWQGPVEQhpLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPiTI 253
Cdd:cd07363   160 SSVHNLRALRWGGPAPPPPWALEFDDWLKDALTAGDLDAL--LDYWEKAPHARRAHPTEEHLLPLLVALGAAGGDEA-RR 236
                         250
                  ....*....|....*..
gi 1489134502 254 PVEGIEMGSLSMLSVQI 270
Cdd:cd07363   237 LHDSIEYGSLSMSSYRF 253
LigB pfam02900
Catalytic LigB subunit of aromatic ring-opening dioxygenase;
17-251 1.11e-19

Catalytic LigB subunit of aromatic ring-opening dioxygenase;


Pssm-ID: 397167 [Multi-domain]  Cd Length: 260  Bit Score: 85.48  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  17 ALFLGHGSPMNVLEDN------------LYTRSWQKLGMTLPRpqAIVVVSAHWFTRGTGVTAM---ETPPTIHDFGGfp 81
Cdd:pfam02900   1 ALKLSHVPPILAAVDGgsqegcwqpvikGYEEIRRRIKEKGPD--TIIVFSPHWLTAINPVFAIgcaEEFPGAYDGFG-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  82 qalYDTHYPAPGSPALAQRLVELL--APIPVTLDKEAwGFDHGSWGVLIKMYPDADIPMVQLSIDSSK----PAAWHFEM 155
Cdd:pfam02900  77 ---PRPEYEVPGNPELAEHIAELLiqDGIDLTVSNSM-GLDHGTLVPLRFMNPEAPVPVIPVSSNTVQypvpSFERCYRL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 156 GRKLAALR---DEGIMLVASGNVVHNLRtvkwhgDSSPYPWATSFNEYVKANLTwQGPVEQhpLVNYLDHEGGTLSNPTP 232
Cdd:pfam02900 153 GRALRRAVeeeDLNVLILGSGGLSHQLQ------GPRAGPFNEEFDNEFLDLLK-EGRVEE--LCKMLHEYPYRAAGHGE 223
                         250
                  ....*....|....*....
gi 1489134502 233 EHYLPLLYVLGAWDGQEPI 251
Cdd:pfam02900 224 GELVPWLVALGALGWGAES 242
 
Name Accession Description Interval E-value
PRK10628 PRK10628
LigB family dioxygenase; Provisional
26-271 0e+00

LigB family dioxygenase; Provisional


Pssm-ID: 182598  Cd Length: 246  Bit Score: 528.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  26 MNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 105
Cdd:PRK10628    1 MNVLEDNLYTRAWRTLGETLPRPKAIVVVSAHWYTRGTGVTAMETPRTIHDFGGFPQALYDTHYPAPGSPALAQRLVELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 106 APIPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 185
Cdd:PRK10628   81 APVPVTLDKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSTKPAAWHFEMGRKLAALRDEGIMLVASGNVVHNLRTVKWH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 186 GDSSPYPWATSFNEYVKANLTWQGPVEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPITIPVEGIEMGSLSM 265
Cdd:PRK10628  161 GDSSPYPWAESFNQFVKANLTWQGPVEQHPLVNYLQHEGGALSNPTPEHYLPLLYVLGAWDGKEPISIPVDGIEMGSLSM 240

                  ....*.
gi 1489134502 266 LSVQIG 271
Cdd:PRK10628  241 LSVQVG 246
LigB COG3384
Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites ...
13-271 6.11e-132

Aromatic ring-opening dioxygenase, catalytic subunit, LigB family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442611  Cd Length: 260  Bit Score: 373.74  E-value: 6.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  13 TRMPALFLGHGSPMNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAP 92
Cdd:COG3384     2 GRLPALFISHGSPMNALEDGALTAALRRLGRRLPRPDAILVVSAHWETRGTTVTAAARPETIYDFYGFPPELYELQYPAP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  93 GSPALAQRLVELLAP--IPVTLDkEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLV 170
Cdd:COG3384    82 GDPELAERVAELLAAagLPVRLD-PERGLDHGTWVPLRLMYPDADIPVVQLSLDPTLDPAEHYALGRALAPLRDEGVLII 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 171 ASGNVVHNLRTVKWHGDSS-PYPWATSFNEYVKANLTWQgpvEQHPLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQE 249
Cdd:COG3384   161 GSGSLVHNLRALRWGPGDAiPSPWAEEFDDWLLEALAAG---DHDALLDYRPAPYARLAHPTEEHLLPLLVALGAAGDDA 237
                         250       260
                  ....*....|....*....|..
gi 1489134502 250 PITIPVEGIEMGSLSMLSVQIG 271
Cdd:COG3384   238 KARVFHDGVEYGSLSMRSVQFG 259
45_DOPA_Dioxygenase cd07363
The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both ...
16-270 1.57e-121

The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine; This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153375  Cd Length: 253  Bit Score: 347.21  E-value: 1.57e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  16 PALFLGHGSPMNVLEDNLYTRSWQKLGMTLPRPQAIVVVSAHWFTRGTGVTAMETPPTIHDFGGFPQALYDTHYPAPGSP 95
Cdd:cd07363     1 PVLFISHGSPMLALEDNPATAFLRELGKELPKPKAILVISAHWETRGPTVTASARPETIYDFYGFPPELYEIQYPAPGSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  96 ALAQRLVELL--APIPVTLDKEaWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKPAAWHFEMGRKLAALRDEGIMLVASG 173
Cdd:cd07363    81 ELAERVAELLkaAGIPARLDPE-RGLDHGAWVPLKLMYPDADIPVVQLSLPASLDPAEHYALGRALAPLRDEGVLIIGSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 174 NVVHNLRTVKWHGDSSPYPWATSFNEYVKANLTWQGPVEQhpLVNYLDHEGGTLSNPTPEHYLPLLYVLGAWDGQEPiTI 253
Cdd:cd07363   160 SSVHNLRALRWGGPAPPPPWALEFDDWLKDALTAGDLDAL--LDYWEKAPHARRAHPTEEHLLPLLVALGAAGGDEA-RR 236
                         250
                  ....*....|....*..
gi 1489134502 254 PVEGIEMGSLSMLSVQI 270
Cdd:cd07363   237 LHDSIEYGSLSMSSYRF 253
Extradiol_Dioxygenase_3B_like cd07320
Subunit B of Class III Extradiol ring-cleavage dioxygenases; Dioxygenases catalyze the ...
16-270 1.67e-91

Subunit B of Class III Extradiol ring-cleavage dioxygenases; Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4,5-dioxygenase (LigAB), 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB), 4,5-DOPA Dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, and 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity.


Pssm-ID: 153371 [Multi-domain]  Cd Length: 260  Bit Score: 271.29  E-value: 1.67e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  16 PALFLGHGSPMNVLEDNLYTR-----SWQKLGMTLPRPQAIVVVSAHWF--TRGTGVTAMETPPTIHDFggfpQALYDTH 88
Cdd:cd07320     1 LAIIIPHGPALYAAEDTGKTRndyqpIEISKRIKEKRPDTIIVVSPHHLviISATAITCAETFETADSG----QWGRRPV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  89 YPAPGSPALAQRLVELLA-PIPVTLDKEAWGFDHGSWGVLIKMYPD-ADIPMVQLSIDSSK-PAAWHFEMGRKLAALR-- 163
Cdd:cd07320    77 YDVKGDPDLAWEIAEELIkEIPVTIVNEMDGLDHGTLVPLSYIFGDpWDFKVIPLSVGVLVpPFAKLFEFGKAIRAAVep 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 164 -DEGIMLVASGNVVHNLRTVKWHGDSSPYPWATSFNEYVKANLTWQGPVEQHPLvnyldHEGGTLSNPTPEHYLPLLYVL 242
Cdd:cd07320   157 sDLRVHVVASGDLSHQLQGDRPSSQSGYYPIAEEFDKYVIDNLEELDPVEFKNM-----HQYLTISNATPCGFHPLLILL 231
                         250       260
                  ....*....|....*....|....*....
gi 1489134502 243 GAWDGQEP-ITIPVEGIEMGSLSMLSVQI 270
Cdd:cd07320   232 GALDGKERkDLFTVYGIPSSSTGYAAAIL 260
LigB pfam02900
Catalytic LigB subunit of aromatic ring-opening dioxygenase;
17-251 1.11e-19

Catalytic LigB subunit of aromatic ring-opening dioxygenase;


Pssm-ID: 397167 [Multi-domain]  Cd Length: 260  Bit Score: 85.48  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  17 ALFLGHGSPMNVLEDN------------LYTRSWQKLGMTLPRpqAIVVVSAHWFTRGTGVTAM---ETPPTIHDFGGfp 81
Cdd:pfam02900   1 ALKLSHVPPILAAVDGgsqegcwqpvikGYEEIRRRIKEKGPD--TIIVFSPHWLTAINPVFAIgcaEEFPGAYDGFG-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  82 qalYDTHYPAPGSPALAQRLVELL--APIPVTLDKEAwGFDHGSWGVLIKMYPDADIPMVQLSIDSSK----PAAWHFEM 155
Cdd:pfam02900  77 ---PRPEYEVPGNPELAEHIAELLiqDGIDLTVSNSM-GLDHGTLVPLRFMNPEAPVPVIPVSSNTVQypvpSFERCYRL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 156 GRKLAALR---DEGIMLVASGNVVHNLRtvkwhgDSSPYPWATSFNEYVKANLTwQGPVEQhpLVNYLDHEGGTLSNPTP 232
Cdd:pfam02900 153 GRALRRAVeeeDLNVLILGSGGLSHQLQ------GPRAGPFNEEFDNEFLDLLK-EGRVEE--LCKMLHEYPYRAAGHGE 223
                         250
                  ....*....|....*....
gi 1489134502 233 EHYLPLLYVLGAWDGQEPI 251
Cdd:pfam02900 224 GELVPWLVALGALGWGAES 242
HPCD_like cd07362
Class III extradiol dioxygenases with similarity to homoprotocatechuate 2,3-dioxygenase, which ...
47-179 1.23e-07

Class III extradiol dioxygenases with similarity to homoprotocatechuate 2,3-dioxygenase, which catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate; This subfamily of class III extradiol dioxygenases consists of two types of proteins with known enzymatic activities; 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD) and 2-amino-5-chlorophenol 1,6-dioxygenase. HPCD catalyzes the key ring cleavage step in the metabolism of homoprotocatechuate (hpca), a central intermediate in the bacterial degradation of aromatic compounds. The enzyme incorporates both atoms of molecular oxygen into hpca, resulting in aromatic ring-opening to yield the product alpha-hydroxy-delta-carboxymethyl cis-muconic semialdehyde. 2-amino-5-chlorophenol 1,6-dioxygenase catalyzes the oxidization and subsequent ring-opening of 2-amino-5-chlorophenol, which is an intermediate during p-chloronitrobenzene degradation. The enzyme is probably a heterotetramer composed of two alpha and two beta subunits. Alpha and beta subunits share significant sequence similarity and both belong to this family. Like all Class III extradiol dioxygenases, these enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.


Pssm-ID: 153374  Cd Length: 272  Bit Score: 51.75  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  47 RPQAIVVVSAHWFT-----------RGTGVTAMETPPTIHDFggfpqalydtHYPAPGSPALAQRLVE--LLAPIP-VTL 112
Cdd:cd07362    43 KPDVILVISCHWMSssfhhfvdatpRHGGLTAVECPDLISDV----------PYDYPGDPELGRLLVEegQEAGLRvKAV 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489134502 113 DKEAWGFDHGSWGVLIKMYPDADIPMVQLSIDSSkpaAWHFEMGRKLA-----ALR--DEGIMLVASGNVVHNL 179
Cdd:cd07362   113 NDPTYIWDYGTVVPLRYLNPNKDIPVVSISACWT---AASLEESYTWGevigkALLesDKRVVFLASGSLSHNL 183
ED_3B_N_AMMECR1 cd07951
The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown ...
47-180 1.34e-04

The N-terminal domain, an extradiol dioxygenase class III subunit B-like domain, of unknown proteins containing a C-terminal AMMECR1 domain; This subfamily is composed of uncharacterized proteins containing an N-terminal domain with similarity to the catalytic B subunit of class III extradiol dioxygenases and a C-terminal AMMECR1-like domain. This model represents the N-terminal domain. Class III extradiol dioxygenases use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon, however, proteins in this subfamily do not contain a potential metal binding site and may not exhibit class III extradiol dioxygenase-like activity. The AMMECR1 protein was proposed to be a regulatory factor that is potentially involved in the development of AMME contiguous gene deletion syndrome.


Pssm-ID: 153388 [Multi-domain]  Cd Length: 256  Bit Score: 42.26  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  47 RPQAIVVVSAHWFTRGTGVtAMETPPTIH-DFGGF--PQALYDTHYPAPGSPALAQRLVELLAPIpVTLDKEAWGFDHGs 123
Cdd:cd07951    38 RPDTIVVVSPHAPVFRDAF-AISTGGTLRgDFSRFgaPEVSFGVDLDLELVEEIAGEADKEGLPV-GALGERIPELDHG- 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1489134502 124 WGV----LIKMYPDADIPMVQLSIdssKPAAWHFEMGRKLA-ALRDEG--IMLVASGNVVHNLR 180
Cdd:cd07951   115 TLVplyfLRKAGSDGKLVRIGLSG---LSPEELYAFGRALAaAAEELGrrVALIASGDLSHRLT 175
PCA_45_Doxase_B_like cd07359
Subunit B of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and simlar ...
47-187 4.42e-03

Subunit B of the Class III Extradiol dioxygenase, Protocatechuate 4,5-dioxygenase, and simlar enzymes; This subfamily of class III extradiol dioxygenases consists of a number of proteins with known enzymatic activities: Protocatechuate (PCA) 4,5-dioxygenase (LigAB), 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB), 3-O-Methylgallate Dioxygenase, 2-aminophenol 1,6-dioxygenase, as well as proteins without any known enzymatic activity. These proteins play essential roles in the degradation of aromatic compounds by catalyzing the incorporation of both atoms of molecular oxygen into their preferred substrates. As members of the Class III extradiol dioxygenase family, the enzymes use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon. LigAB-like class III enzymes are usually composed of two subunits, designated A and B, which form a tetramer composed of two copies of each subunit. This model represents the catalytic subunit, B.


Pssm-ID: 153372 [Multi-domain]  Cd Length: 271  Bit Score: 37.64  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502  47 RPQAIVVVSAHWFTrgtgvtametpptIHDFGGFPQ---ALYDTH------------YPAPGSPALAQRLVE--LLAPIP 109
Cdd:cd07359    44 RPDVVVVVGNDHFT-------------NFFLDNMPAfaiGIADSYegpdegwlgiprAPVPGDADLARHLLAglVEDGFD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489134502 110 VTLDKEaWGFDHGSWGVLIKMYPDADIPMVQLSIDSSKP----AAWHFEMGRKLAA-----LRDEGIMLVASGNVVHNLr 180
Cdd:cd07359   111 VAFSYE-LRLDHGITVPLHFLDPDNDVPVVPVLVNCVTPplpsLRRCYALGRALRRaiesfPGDLRVAVLGTGGLSHWP- 188

                  ....*..
gi 1489134502 181 TVKWHGD 187
Cdd:cd07359   189 GGPRHGE 195
 
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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